Entry
stringlengths 6
10
| Entry Name
stringlengths 5
11
| Sequence
stringlengths 2
35.2k
| EC number
stringlengths 7
118
⌀ | Cofactor
stringlengths 38
1.77k
⌀ | Gene Ontology (biological process)
stringlengths 18
11.3k
⌀ | Gene Ontology (cellular component)
stringlengths 17
1.75k
⌀ | Gene Ontology (molecular function)
stringlengths 24
2.09k
⌀ | Pfam
stringlengths 8
232
⌀ | Gene3D
stringlengths 10
250
⌀ | Protein families
stringlengths 9
237
⌀ | Post-translational modification
stringlengths 16
8.52k
⌀ | Subcellular location [CC]
stringlengths 29
6.18k
⌀ | Catalytic activity
stringlengths 64
35.7k
⌀ | Kinetics
stringlengths 69
11.7k
⌀ | Pathway
stringlengths 27
908
⌀ | pH dependence
stringlengths 64
955
⌀ | Temperature dependence
stringlengths 70
1.16k
⌀ | Function [CC]
stringlengths 17
15.3k
⌀ | Organism
stringlengths 8
196
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O95238
|
SPDEF_HUMAN
|
MGSASPGLSSVSPSHLLLPPDTVSRTGLEKAAAGAVGLERRDWSPSPPATPEQGLSAFYLSYFDMLYPEDSSWAAKAPGASSREEPPEEPEQCPVIDSQAPAGSLDLVPGGLTLEEHSLEQVQSMVVGEVLKDIETACKLLNITADPMDWSPSNVQKWLLWTEHQYRLPPMGKAFQELAGKELCAMSEEQFRQRSPLGGDVLHAHLDIWKSAAWMKERTSPGAIHYCASTSEESWTDSEVDSSCSGQPIHLWQFLKELLLKPHSYGRFIRWLNKEKGIFKIEDSAQVARLWGIRKNRPAMNYDKLSRSIRQYYKKGIIRKPDISQRLVYQFVHPI
| null | null |
epithelial cell fate commitment [GO:0072148]; glandular epithelial cell development [GO:0002068]; intestinal epithelial cell development [GO:0060576]; lung goblet cell differentiation [GO:0060480]; negative regulation of cell fate commitment [GO:0010454]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell fate commitment [GO:0010455]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription by RNA polymerase II [GO:0006366]
|
chromatin [GO:0000785]; nucleus [GO:0005634]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00178;PF02198;
|
1.10.150.50;1.10.10.10;
|
ETS family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: May function as an androgen-independent transactivator of the prostate-specific antigen (PSA) promoter. Binds to 5'-GGAT-3' DNA sequences. May play a role in the regulation of the prostate gland and/or prostate cancer development. Acts as a transcriptional activator for SERPINB5 promoter. {ECO:0000269|PubMed:10625666}.
|
Homo sapiens (Human)
|
O95239
|
KIF4A_HUMAN
|
MKEEVKGIPVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGAYTAEQENEPTVGVIPRVIQLLFKEIDKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVNIDPQTAELNHLKQQVQQLQVLLLQAHGGTLPGSITVEPSENLQSLMEKNQSLVEENEKLSRGLSEAAGQTAQMLERIILTEQANEKMNAKLEELRQHAACKLDLQKLVETLEDQELKENVEIICNLQQLITQLSDETVACMAAAIDTAVEQEAQVETSPETSRSSDAFTTQHALRQAQMSKELVELNKALALKEALARKMTQNDSQLQPIQYQYQDNIKELELEVINLQKEKEELVLELQTAKKDANQAKLSERRRKRLQELEGQIADLKKKLNEQSKLLKLKESTERTVSKLNQEIRMMKNQRVQLMRQMKEDAEKFRQWKQKKDKEVIQLKERDRKRQYELLKLERNFQKQSNVLRRKTEEAAAANKRLKDALQKQREVADKRKETQSRGMEGTAARVKNWLGNEIEVMVSTEEAKRHLNDLLEDRKILAQDVAQLKEKKESGENPPPKLRRRTFSLTEVRGQVSESEDSITKQIESLETEMEFRSAQIADLQQKLLDAESEDRPKQRWENIATILEAKCALKYLIGELVSSKIQVSKLESSLKQSKTSCADMQKMLFEERNHFAEIETELQAELVRMEQQHQEKVLYLLSQLQQSQMAEKQLEESVSEKEQQLLSTLKCQDEELEKMREVCEQNQQLLRENEIIKQKLTLLQVASRQKHLPKDTLLSPDSSFEYVPPKPKPSRVKEKFLEQSMDIEDLKYCSEHSVNEHEDGDGDDDEGDDEEWKPTKLVKVSRKNIQGCSCKGWCGNKQCGCRKQKSDCGVDCCCDPTKCRNRQQGKDSLGTVERTQDSEGSFKLEDPTEVTPGLSFFNPVCATPNSKILKEMCDVEQVLSKKTPPAPSPFDLPELKHVATEYQENKAPGKKKKRALASNTSFFSGCSPIEEEAH
| null |
COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:29848660}; Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:29848660}; Note=Binds 1 [4Fe-4S] cluster (PubMed:29848660). In the presence of oxygen, the [4Fe-4S] cluster may be converted to [2Fe-2S] (PubMed:29848660). {ECO:0000269|PubMed:29848660};
|
anterograde axonal transport [GO:0008089]; mitotic cytokinesis [GO:0000281]; mitotic spindle midzone assembly [GO:0051256]; mitotic spindle organization [GO:0007052]; organelle organization [GO:0006996]; spindle elongation [GO:0051231]
|
axon cytoplasm [GO:1904115]; chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; microtubule associated complex [GO:0005875]; midbody [GO:0030496]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; spindle microtubule [GO:0005876]
|
ATP binding [GO:0005524]; DNA binding [GO:0003677]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]
|
PF00225;
|
3.40.850.10;
|
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Chromokinesin subfamily
| null |
SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:11736643}. Cytoplasm {ECO:0000269|PubMed:11736643}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:29848660}. Midbody {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:29848660}. Chromosome {ECO:0000269|PubMed:11736643, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:29848660}. Note=Associates with chromosomes at all stage of mitosis (PubMed:11736643, PubMed:15297875, PubMed:15625105). Chromatin localization is dependent on iron-sulfur cluster binding (PubMed:29848660). In anaphase, associates with the mitotic spindle midzone (PubMed:15297875). In telophase and cytokinesis, co-localizes with CIAO2B at the spindle midzone and midbody (PubMed:15297875, PubMed:29848660). Co-localizes with PRC1 in early mitosis and at the spindle midzone from anaphase B to telophase (PubMed:15297875, PubMed:15625105). Does not localize to the nucleolus (PubMed:11736643). {ECO:0000269|PubMed:11736643, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:29848660}.
| null | null | null | null | null |
FUNCTION: Iron-sulfur (Fe-S) cluster binding motor protein that has a role in chromosome segregation during mitosis (PubMed:29848660). Translocates PRC1 to the plus ends of interdigitating spindle microtubules during the metaphase to anaphase transition, an essential step for the formation of an organized central spindle midzone and midbody and for successful cytokinesis (PubMed:15297875, PubMed:15625105). May play a role in mitotic chromosomal positioning and bipolar spindle stabilization (By similarity). {ECO:0000250|UniProtKB:P33174, ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:29848660}.
|
Homo sapiens (Human)
|
O95243
|
MBD4_HUMAN
|
MGTTGLESLSLGDRGAAPTVTSSERLVPDPPNDLRKEDVAMELERVGEDEEQMMIKRSSECNPLLQEPIASAQFGATAGTECRKSVPCGWERVVKQRLFGKTAGRFDVYFISPQGLKFRSKSSLANYLHKNGETSLKPEDFDFTVLSKRGIKSRYKDCSMAALTSHLQNQSNNSNWNLRTRSKCKKDVFMPPSSSSELQESRGLSNFTSTHLLLKEDEGVDDVNFRKVRKPKGKVTILKGIPIKKTKKGCRKSCSGFVQSDSKRESVCNKADAESEPVAQKSQLDRTVCISDAGACGETLSVTSEENSLVKKKERSLSSGSNFCSEQKTSGIINKFCSAKDSEHNEKYEDTFLESEEIGTKVEVVERKEHLHTDILKRGSEMDNNCSPTRKDFTGEKIFQEDTIPRTQIERRKTSLYFSSKYNKEALSPPRRKAFKKWTPPRSPFNLVQETLFHDPWKLLIATIFLNRTSGKMAIPVLWKFLEKYPSAEVARTADWRDVSELLKPLGLYDLRAKTIVKFSDEYLTKQWKYPIELHGIGKYGNDSYRIFCVNEWKQVHPEDHKLNKYHDWLWENHEKLSLS
|
3.2.2.-
| null |
depyrimidination [GO:0045008]; DNA repair [GO:0006281]; response to estradiol [GO:0032355]
|
nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; DNA endonuclease activity [GO:0004520]; DNA N-glycosylase activity [GO:0019104]; pyrimidine-specific mismatch base pair DNA N-glycosylase activity [GO:0008263]; satellite DNA binding [GO:0003696]
|
PF01429;
| null | null | null |
SUBCELLULAR LOCATION: Nucleus.
| null | null | null | null | null |
FUNCTION: Mismatch-specific DNA N-glycosylase involved in DNA repair. Has thymine glycosylase activity and is specific for G:T mismatches within methylated and unmethylated CpG sites. Can also remove uracil or 5-fluorouracil in G:U mismatches. Has no lyase activity. Was first identified as methyl-CpG-binding protein. {ECO:0000269|PubMed:10097147, ECO:0000269|PubMed:10930409}.
|
Homo sapiens (Human)
|
O95248
|
MTMR5_HUMAN
|
MARLADYFVLVAFGPHPRGSGEGQGQILQRFPEKDWEDNPFPQGIELFCQPSGWQLCPERNPPTFFVAVLTDINSERHYCACLTFWEPAEPSQQETTRVEDATEREEEGDEGGQTHLSPTAPAPSAQLFAPKTLVLVSRLDHTEVFRNSLGLIYAIHVEGLNVCLENVIGNLLTCTVPLAGGSQRTISLGAGDRQVIQTPLADSLPVSRCSVALLFRQLGITNVLSLFCAALTEHKVLFLSRSYQRLADACRGLLALLFPLRYSFTYVPILPAQLLEVLSTPTPFIIGVNAAFQAETQELLDVIVADLDGGTVTIPECVHIPPLPEPLQSQTHSVLSMVLDPELELADLAFPPPTTSTSSLKMQDKELRAVFLRLFAQLLQGYRWCLHVVRIHPEPVIRFHKAAFLGQRGLVEDDFLMKVLEGMAFAGFVSERGVPYRPTDLFDELVAHEVARMRADENHPQRVLRHVQELAEQLYKNENPYPAVAMHKVQRPGESSHLRRVPRPFPRLDEGTVQWIVDQAAAKMQGAPPAVKAERRTTVPSGPPMTAILERCSGLHVNSARRLEVVRNCISYVFEGKMLEAKKLLPAVLRALKGRAARRCLAQELHLHVQQNRAVLDHQQFDFVVRMMNCCLQDCTSLDEHGIAAALLPLVTAFCRKLSPGVTQFAYSCVQEHVVWSTPQFWEAMFYGDVQTHIRALYLEPTEDLAPAQEVGEAPSQEDERSALDVASEQRRLWPTLSREKQQELVQKEESTVFSQAIHYANRMSYLLLPLDSSKSRLLRERAGLGDLESASNSLVTNSMAGSVAESYDTESGFEDAETCDVAGAVVRFINRFVDKVCTESGVTSDHLKGLHVMVPDIVQMHIETLEAVQRESRRLPPIQKPKLLRPRLLPGEECVLDGLRVYLLPDGREEGAGGSAGGPALLPAEGAVFLTTYRVIFTGMPTDPLVGEQVVVRSFPVAALTKEKRISVQTPVDQLLQDGLQLRSCTFQLLKMAFDEEVGSDSAELFRKQLHKLRYPPDIRATFAFTLGSAHTPGRPPRVTKDKGPSLRTLSRNLVKNAKKTIGRQHVTRKKYNPPSWEHRGQPPPEDQEDEISVSEELEPSTLTPSSALKPSDRMTMSSLVERACCRDYQRLGLGTLSSSLSRAKSEPFRISPVNRMYAICRSYPGLLIVPQSVQDNALQRVSRCYRQNRFPVVCWRSGRSKAVLLRSGGLHGKGVVGLFKAQNAPSPGQSQADSSSLEQEKYLQAVVSSMPRYADASGRNTLSGFSSAHMGSHGKWGSVRTSGRSSGLGTDVGSRLAGRDALAPPQANGGPPDPGFLRPQRAALYILGDKAQLKGVRSDPLQQWELVPIEVFEARQVKASFKKLLKACVPGCPAAEPSPASFLRSLEDSEWLIQIHKLLQVSVLVVELLDSGSSVLVGLEDGWDITTQVVSLVQLLSDPFYRTLEGFRLLVEKEWLSFGHRFSHRGAHTLAGQSSGFTPVFLQFLDCVHQVHLQFPMEFEFSQFYLKFLGYHHVSRRFRTFLLDSDYERIELGLLYEEKGERRGQVPCRSVWEYVDRLSKRTPVFHNYMYAPEDAEVLRPYSNVSNLKVWDFYTEETLAEGPPYDWELAQGPPEPPEEERSDGGAPQSRRRVVWPCYDSCPRAQPDAISRLLEELQRLETELGQPAERWKDTWDRVKAAQRLEGRPDGRGTPSSLLVSTAPHHRRSLGVYLQEGPVGSTLSLSLDSDQSSGSTTSGSRQAARRSTSTLYSQFQTAESENRSYEGTLYKKGAFMKPWKARWFVLDKTKHQLRYYDHRVDTECKGVIDLAEVEAVAPGTPTMGAPKTVDEKAFFDVKTTRRVYNFCAQDVPSAQQWVDRIQSCLSDA
| null | null |
protein dephosphorylation [GO:0006470]; spermatid development [GO:0007286]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nuclear body [GO:0016604]; perinuclear region of cytoplasm [GO:0048471]
|
guanyl-nucleotide exchange factor activity [GO:0005085]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]
|
PF02141;PF02893;PF06602;PF00169;PF12335;PF03456;
|
3.30.450.200;3.40.50.11500;2.30.29.30;
|
Protein-tyrosine phosphatase family, Non-receptor class myotubularin subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:20937701}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:12668758}.
| null | null | null | null | null |
FUNCTION: Acts as an adapter for the phosphatase MTMR2 to regulate MTMR2 catalytic activity and subcellular location (PubMed:12668758). May function as a guanine nucleotide exchange factor (GEF) activating RAB28 (PubMed:20937701). Promotes the exchange of GDP to GTP, converting inactive GDP-bound Rab proteins into their active GTP-bound form (PubMed:20937701). Inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts (PubMed:9537414). {ECO:0000269|PubMed:12668758, ECO:0000269|PubMed:20937701, ECO:0000269|PubMed:9537414}.
|
Homo sapiens (Human)
|
O95249
|
GOSR1_HUMAN
|
MAAGTSSYWEDLRKQARQLENELDLKLVSFSKLCTSYSHSSTRDGRRDRYSSDTTPLLNGSSQDRMFETMAIEIEQLLARLTGVNDKMAEYTNSAGVPSLNAALMHTLQRHRDILQDYTHEFHKTKANFMAIRERENLMGSVRKDIESYKSGSGVNNRRTELFLKEHDHLRNSDRLIEETISIAMATKENMTSQRGMLKSIHSKMNTLANRFPAVNSLIQRINLRKRRDSLILGGVIGICTILLLLYAFH
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; inter-Golgi cisterna vesicle-mediated transport [GO:0048219]; intra-Golgi vesicle-mediated transport [GO:0006891]; protein transport [GO:0015031]; retrograde transport, endosome to Golgi [GO:0042147]; vesicle fusion [GO:0006906]
|
cis-Golgi network [GO:0005801]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi medial cisterna [GO:0005797]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; SNARE complex [GO:0031201]; transport vesicle [GO:0030133]
|
SNAP receptor activity [GO:0005484]
|
PF12352;
| null |
GOSR1 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:15728195, ECO:0000269|PubMed:17274796, ECO:0000269|PubMed:17337506, ECO:0000269|PubMed:21669198}; Single-pass type IV membrane protein {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:15728195, ECO:0000269|PubMed:17274796, ECO:0000269|PubMed:17337506, ECO:0000269|PubMed:21669198}. Note=Localizes throughout the Golgi apparatus, with lowest levels in the trans-Golgi network (By similarity). Enriched on vesicular components at the terminal rims of the Golgi. Found in Golgi microtubules at low temperature (15 degrees Celsius). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Involved in transport from the ER to the Golgi apparatus as well as in intra-Golgi transport. It belongs to a super-family of proteins called t-SNAREs or soluble NSF (N-ethylmaleimide-sensitive factor) attachment protein receptor. May play a protective role against hydrogen peroxide induced cytotoxicity under glutathione depleted conditions in neuronal cells by regulating the intracellular ROS levels via inhibition of p38 MAPK (MAPK11, MAPK12, MAPK13 and MAPK14). Participates in docking and fusion stage of ER to cis-Golgi transport. Plays an important physiological role in VLDL-transport vesicle-Golgi fusion and thus in VLDL delivery to the hepatic cis-Golgi. {ECO:0000269|PubMed:15215310, ECO:0000269|PubMed:21860593}.
|
Homo sapiens (Human)
|
O95251
|
KAT7_HUMAN
|
MPRRKRNAGSSSDGTEDSDFSTDLEHTDSSESDGTSRRSARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQVVDFSDRETKNTADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSLKDSGSDLSHRPKRRRFHESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHNLSADECKVRAQSRDKQIEERMLSHRQDDNNRHATRHQAPTERQLRYKEKVAELRKKRNSGLSKEQKEKYMEHRQTYGNTREPLLENLTSEYDLDLFRRAQARASEDLEKLRLQGQITEGSNMIKTIAFGRYELDTWYHSPYPEEYARLGRLYMCEFCLKYMKSQTILRRHMAKCVWKHPPGDEIYRKGSISVFEVDGKKNKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVMTEADNTGCHLIGYFSKEKNSFLNYNVSCILTMPQYMRQGYGKMLIDFSYLLSKVEEKVGSPERPLSDLGLISYRSYWKEVLLRYLHNFQGKEISIKEISQETAVNPVDIVSTLQALQMLKYWKGKHLVLKRQDLIDEWIAKEAKRSNSNKTMDPSCLKWTPPKGT
|
2.3.1.48
| null |
DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication-dependent chromatin disassembly [GO:0140889]; internal peptidyl-lysine acetylation [GO:0018393]; natural killer cell differentiation [GO:0001779]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA replication [GO:0045740]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; positive regulation of hematopoietic stem cell proliferation [GO:1902035]; positive regulation of protein localization to nucleus [GO:1900182]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell cycle [GO:0051726]; regulation of cell growth [GO:0001558]; regulation of DNA biosynthetic process [GO:2000278]; regulation of DNA replication [GO:0006275]; regulation of DNA-templated DNA replication initiation [GO:0030174]; regulation of DNA-templated transcription [GO:0006355]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357]; response to actinomycin D [GO:0072716]; response to anisomycin [GO:0072739]; response to dithiothreitol [GO:0072720]; response to hydroxyurea [GO:0072710]; response to sorbitol [GO:0072708]; stress-activated protein kinase signaling cascade [GO:0031098]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; cytosol [GO:0005829]; histone acetyltransferase complex [GO:0000123]; histone H3-K14 acetyltransferase complex [GO:0036409]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; site of DNA damage [GO:0090734]
|
chromatin binding [GO:0003682]; DNA replication origin binding [GO:0003688]; histone acetyltransferase activity [GO:0004402]; histone H3 acetyltransferase activity [GO:0010484]; histone H3K14 acetyltransferase activity [GO:0036408]; histone H3K23 acetyltransferase activity [GO:0043994]; histone H3K4 acetyltransferase activity [GO:0044016]; histone H4 acetyltransferase activity [GO:0010485]; histone H4K12 acetyltransferase activity [GO:0043997]; histone H4K5 acetyltransferase activity [GO:0043995]; histone H4K8 acetyltransferase activity [GO:0043996]; transcription coregulator activity [GO:0003712]; zinc ion binding [GO:0008270]
|
PF01853;PF01530;PF17772;
|
3.40.630.30;4.10.320.30;3.30.60.60;1.10.10.10;
|
MYST (SAS/MOZ) family
|
PTM: Phosphorylated at Ser-50 and Ser-53 by ATR in response to DNA damage, promoting its ubiquitination by the CRL4(DDB2) complex and subsequent degradation (PubMed:26572825). Phosphorylation at Ser-50 and Ser-53 by ATR in response to ultraviolet-induced DNA, promotes localization to DNA damage sites (PubMed:28719581). Phosphorylation at Ser-57 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior phosphorylation at Thr-85 and Thr-88 by CDK1 (PubMed:18250300). Phosphorylated by MAP2K1, which accelerates its degradation (By similarity). {ECO:0000250|UniProtKB:Q5SVQ0, ECO:0000269|PubMed:18250300, ECO:0000269|PubMed:26572825, ECO:0000269|PubMed:28719581}.; PTM: Ubiquitinated at Lys-338, leading to proteasomal degradation (PubMed:23319590). Ubiquitinated by the CRL4(DDB2) complex following phosphorylation by ATR, leading to its subsequent degradation (PubMed:26572825). {ECO:0000269|PubMed:23319590, ECO:0000269|PubMed:26572825}.; PTM: Autoacetylation at Lys-432 is required for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10930412, ECO:0000269|PubMed:11278932, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:28719581}. Chromosome {ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:19187766, ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:28719581}. Chromosome, centromere {ECO:0000269|PubMed:27270040}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5SVQ0}. Note=Associates with replication origins specifically during the G1 phase of the cell cycle (PubMed:18832067, PubMed:20129055). Localizes to transcription start sites (PubMed:21753189, PubMed:24065767). Localizes to ultraviolet-induced DNA damage sites following phosphorylation by ATR (PubMed:28719581). Localizes to centromeres in G1 phase (PubMed:27270040). {ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:27270040, ECO:0000269|PubMed:28719581}.
|
CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:17954561, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, ECO:0000269|PubMed:31827282}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:17954561, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, ECO:0000269|PubMed:31827282};
| null | null | null | null |
FUNCTION: Catalytic subunit of histone acetyltransferase HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance and embryonic development (PubMed:16387653, PubMed:21753189, PubMed:24065767, PubMed:26620551, PubMed:31767635, PubMed:31827282). Some complexes also catalyze acetylation of histone H4 at 'Lys-5', 'Lys-8' and 'Lys-12' (H4K5ac, H4K8ac and H4K12ac, respectively), regulating DNA replication initiation, regulating DNA replication initiation (PubMed:10438470, PubMed:19187766, PubMed:20129055, PubMed:24065767). Specificity of the HBO1 complexes is determined by the scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE (JADE1, JADE2 and JADE3) scaffold direct KAT7/HBO1 specificity towards histone H4 (PubMed:19187766, PubMed:20129055, PubMed:24065767, PubMed:26620551). H3K14ac promotes transcriptional elongation by facilitating the processivity of RNA polymerase II (PubMed:31827282). Acts as a key regulator of hematopoiesis by forming a complex with BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and promoting erythroid differentiation (PubMed:21753189). H3K14ac is also required for T-cell development (By similarity). KAT7/HBO1-mediated acetylation facilitates two consecutive steps, licensing and activation, in DNA replication initiation: H3K14ac facilitates the activation of replication origins, and histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes, promoting DNA replication licensing (PubMed:10438470, PubMed:11278932, PubMed:18832067, PubMed:19187766, PubMed:20129055, PubMed:21856198, PubMed:24065767, PubMed:26620551). Acts as a positive regulator of centromeric CENPA assembly: recruited to centromeres and mediates histone acetylation, thereby preventing centromere inactivation mediated by SUV39H1, possibly by increasing histone turnover/exchange (PubMed:27270040). Involved in nucleotide excision repair: phosphorylation by ATR in response to ultraviolet irradiation promotes its localization to DNA damage sites, where it mediates histone acetylation to facilitate recruitment of XPC at the damaged DNA sites (PubMed:28719581). Acts as an inhibitor of NF-kappa-B independently of its histone acetyltransferase activity (PubMed:16997280). {ECO:0000250|UniProtKB:Q5SVQ0, ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:11278932, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:16997280, ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:19187766, ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:21856198, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, ECO:0000269|PubMed:27270040, ECO:0000269|PubMed:28719581, ECO:0000269|PubMed:31767635, ECO:0000269|PubMed:31827282}.; FUNCTION: Plays a central role in the maintenance of leukemia stem cells in acute myeloid leukemia (AML) (PubMed:31827282). Acts by mediating acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby facilitating the processivity of RNA polymerase II to maintain the high expression of key genes, such as HOXA9 and HOXA10 that help to sustain the functional properties of leukemia stem cells (PubMed:31827282). {ECO:0000269|PubMed:31827282}.
|
Homo sapiens (Human)
|
O95255
|
MRP6_HUMAN
|
MAAPAEPCAGQGVWNQTEPEPAATSLLSLCFLRTAGVWVPPMYLWVLGPIYLLFIHHHGRGYLRMSPLFKAKMVLGFALIVLCTSSVAVALWKIQQGTPEAPEFLIHPTVWLTTMSFAVFLIHTERKKGVQSSGVLFGYWLLCFVLPATNAAQQASGAGFQSDPVRHLSTYLCLSLVVAQFVLSCLADQPPFFPEDPQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARRHNKAIAFKRKGGSGMKAPETEPFLRQEGSQWRPLLKAIWQVFHSTFLLGTLSLIISDVFRFTVPKLLSLFLEFIGDPKPPAWKGYLLAVLMFLSACLQTLFEQQNMYRLKVLQMRLRSAITGLVYRKVLALSSGSRKASAVGDVVNLVSVDVQRLTESVLYLNGLWLPLVWIVVCFVYLWQLLGPSALTAIAVFLSLLPLNFFISKKRNHHQEEQMRQKDSRARLTSSILRNSKTIKFHGWEGAFLDRVLGIRGQELGALRTSGLLFSVSLVSFQVSTFLVALVVFAVHTLVAENAMNAEKAFVTLTVLNILNKAQAFLPFSIHSLVQARVSFDRLVTFLCLEEVDPGVVDSSSSGSAAGKDCITIHSATFAWSQESPPCLHRINLTVPQGCLLAVVGPVGAGKSSLLSALLGELSKVEGFVSIEGAVAYVPQEAWVQNTSVVENVCFGQELDPPWLERVLEACALQPDVDSFPEGIHTSIGEQGMNLSGGQKQRLSLARAVYRKAAVYLLDDPLAALDAHVGQHVFNQVIGPGGLLQGTTRILVTHALHILPQADWIIVLANGAIAEMGSYQELLQRKGALMCLLDQARQPGDRGEGETEPGTSTKDPRGTSAGRRPELRRERSIKSVPEKDRTTSEAQTEVPLDDPDRAGWPAGKDSIQYGRVKATVHLAYLRAVGTPLCLYALFLFLCQQVASFCRGYWLSLWADDPAVGGQQTQAALRGGIFGLLGCLQAIGLFASMAAVLLGGARASRLLFQRLLWDVVRSPISFFERTPIGHLLNRFSKETDTVDVDIPDKLRSLLMYAFGLLEVSLVVAVATPLATVAILPLFLLYAGFQSLYVVSSCQLRRLESASYSSVCSHMAETFQGSTVVRAFRTQAPFVAQNNARVDESQRISFPRLVADRWLAANVELLGNGLVFAAATCAVLSKAHLSAGLVGFSVSAALQVTQTLQWVVRNWTDLENSIVSVERMQDYAWTPKEAPWRLPTCAAQPPWPQGGQIEFRDFGLRYRPELPLAVQGVSFKIHAGEKVGIVGRTGAGKSSLASGLLRLQEAAEGGIWIDGVPIAHVGLHTLRSRISIIPQDPILFPGSLRMNLDLLQEHSDEAIWAALETVQLKALVASLPGQLQYKCADRGEDLSVGQKQLLCLARALLRKTQILILDEATAAVDPGTELQMQAMLGSWFAQCTVLLIAHRLRSVMDCARVLVMDKGQVAESGSPAQLLAQKGLFYRLAQESGLV
|
7.6.2.-; 7.6.2.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11880368, ECO:0000269|PubMed:12414644};
|
ATP metabolic process [GO:0046034]; ATP transport [GO:0015867]; calcium ion homeostasis [GO:0055074]; gene expression [GO:0010467]; inhibition of non-skeletal tissue mineralization [GO:0140928]; inorganic diphosphate transport [GO:0030505]; intracellular phosphate ion homeostasis [GO:0030643]; leukotriene transport [GO:0071716]; phosphate ion homeostasis [GO:0055062]; response to magnesium ion [GO:0032026]; response to sodium phosphate [GO:1904383]; response to xenobiotic stimulus [GO:0009410]; transmembrane transport [GO:0055085]; visual perception [GO:0007601]
|
basal plasma membrane [GO:0009925]; basolateral plasma membrane [GO:0016323]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
ABC-type glutathione S-conjugate transporter activity [GO:0015431]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled inorganic anion transmembrane transporter activity [GO:0043225]; ATPase-coupled transmembrane transporter activity [GO:0042626]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCC family, Conjugate transporter (TC 3.A.1.208) subfamily
|
PTM: Glycosylated. {ECO:0000269|PubMed:30154241}.
|
SUBCELLULAR LOCATION: Basal cell membrane {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein {ECO:0000255}. Note=Localized to the basal membrane of Sertoli cells. {ECO:0000269|PubMed:35307651}.; SUBCELLULAR LOCATION: [Isoform 1]: Basolateral cell membrane {ECO:0000269|PubMed:12901863, ECO:0000269|PubMed:23625951}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23912081}; Single-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: [Isoform 1]: Reaction=an S-substituted glutathione(in) + ATP + H2O = ADP + an S-substituted glutathione(out) + H(+) + phosphate; Xref=Rhea:RHEA:19121, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:90779, ChEBI:CHEBI:456216; EC=7.6.2.3; Evidence={ECO:0000269|PubMed:11880368, ECO:0000269|PubMed:12414644}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19122; Evidence={ECO:0000305|PubMed:11880368, ECO:0000305|PubMed:12414644}; CATALYTIC ACTIVITY: [Isoform 1]: Reaction=ATP + H2O + leukotriene C4(in) = ADP + H(+) + leukotriene C4(out) + phosphate; Xref=Rhea:RHEA:38963, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57973, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:11880368, ECO:0000269|PubMed:12414644}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38964; Evidence={ECO:0000305|PubMed:11880368, ECO:0000305|PubMed:12414644};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=600 nM for LTC4 {ECO:0000269|PubMed:11880368}; KM=282 uM for N-ethylmaleimide S-glutathione {ECO:0000269|PubMed:11880368}; Vmax=106 pmol/min/mg enzyme for N-ethylmaleimide S-glutathione transport {ECO:0000269|PubMed:11880368}; Vmax=50 pmol/min/mg enzyme for LTC4 transport {ECO:0000269|PubMed:11880368};
| null | null | null |
FUNCTION: [Isoform 1]: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Mediates ATP-dependent transport of glutathione conjugates such as leukotriene-c4 (LTC4) and N-ethylmaleimide S-glutathione (NEM-GS) (in vitro), and an anionic cyclopentapeptide endothelin antagonist, BQ-123 (PubMed:11880368, PubMed:12414644). May contribute to regulate the transport of organic compounds in testes across the blood-testis-barrier (Probable). Does not appear to actively transport drugs outside the cell. Confers low levels of cellular resistance to etoposide, teniposide, anthracyclines and cisplatin (PubMed:12414644). {ECO:0000269|PubMed:11880368, ECO:0000269|PubMed:12414644, ECO:0000305|PubMed:35307651}.; FUNCTION: [Isoform 1]: Mediates the release of nucleoside triphosphates, predominantly ATP, into the circulation, where it is rapidly converted into AMP and the mineralization inhibitor inorganic pyrophosphate (PPi) by the ecto-enzyme ectonucleotide pyrophosphatase phosphodiesterase 1 (ENPP1), therefore playing a role in PPi homeostasis. {ECO:0000269|PubMed:24277820, ECO:0000269|PubMed:24969777}.; FUNCTION: [Isoform 2]: Inhibits TNF-alpha-mediated apoptosis through blocking one or more caspases. {ECO:0000269|PubMed:23912081}.
|
Homo sapiens (Human)
|
O95256
|
I18RA_HUMAN
|
MLCLGWIFLWLVAGERIKGFNISGCSTKKLLWTYSTRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPEHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLTPGVNNSGSYICRPKMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDLLLGSTGSISCPSLSCQSDAQSPAVTWYKNGKLLSVERSNRIVVDEVYDYHQGTYVCDYTQSDTVSSWTVRAVVQVRTIVGDTKLKPDILDPVEDTLEVELGKPLTISCKARFGFERVFNPVIKWYIKDSDLEWEVSVPEAKSIKSTLKDEIIERNIILEKVTQRDLRRKFVCFVQNSIGNTTQSVQLKEKRGVVLLYILLGTIGTLVAVLAASALLYRHWIEIVLLYRTYQSKDQTLGDKKDFDAFVSYAKWSSFPSEATSSLSEEHLALSLFPDVLENKYGYSLCLLERDVAPGGVYAEDIVSIIKRSRRGIFILSPNYVNGPSIFELQAAVNLALDDQTLKLILIKFCYFQEPESLPHLVKKALRVLPTVTWRGLKSVPPNSRFWAKMRYHMPVKNSQGFTWNQLRITSRIFQWKGLSRTETTGRSSQPKEW
|
3.2.2.6
| null |
cell population proliferation [GO:0008283]; cellular response to hydrogen peroxide [GO:0070301]; immune response [GO:0006955]; inflammatory response [GO:0006954]; interleukin-18-mediated signaling pathway [GO:0035655]; neutrophil activation [GO:0042119]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]
|
interleukin-18 receptor complex [GO:0045092]; plasma membrane [GO:0005886]
|
coreceptor activity [GO:0015026]; interleukin-18 receptor activity [GO:0042008]; NAD+ nucleosidase activity [GO:0003953]; NAD+ nucleotidase, cyclic ADP-ribose generating [GO:0061809]
|
PF18452;PF01582;
|
2.60.40.10;3.40.50.10140;
|
Interleukin-1 receptor family
|
PTM: N-glycosylated. {ECO:0000269|PubMed:25500532}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14528293}; Single-pass type I membrane protein {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide; Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302; Evidence={ECO:0000255|PROSITE-ProRule:PRU00204};
| null | null | null | null |
FUNCTION: Within the IL18 receptor complex, does not mediate IL18-binding, but involved in IL18-dependent signal transduction, leading to NF-kappa-B and JNK activation (PubMed:14528293, PubMed:25500532, PubMed:9792649). May play a role in IL18-mediated IFNG synthesis from T-helper 1 (Th1) cells (Probable). {ECO:0000269|PubMed:14528293, ECO:0000269|PubMed:25500532, ECO:0000269|PubMed:9792649, ECO:0000305|PubMed:10653850}.
|
Homo sapiens (Human)
|
O95257
|
GA45G_HUMAN
|
MTLEEVRGQDTVPESTARMQGAGKALHELLLSAQRQGCLTAGVYESAKVLNVDPDNVTFCVLAAGEEDEGDIALQIHFTLIQAFCCENDIDIVRVGDVQRLAAIVGAGEEAGAPGDLHCILISNPNEDAWKDPALEKLSLFCEESRSVNDWVPSITLPE
| null | null |
apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cold-induced thermogenesis [GO:0120162]; positive regulation of JNK cascade [GO:0046330]; positive regulation of p38MAPK cascade [GO:1900745]; regulation of cell cycle [GO:0051726]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
| null |
PF01248;
|
3.30.1330.30;
|
GADD45 family
| null | null | null | null | null | null | null |
FUNCTION: Involved in the regulation of growth and apoptosis. Mediates activation of stress-responsive MTK1/MEKK4 MAPKKK.
|
Homo sapiens (Human)
|
O95258
|
UCP5_HUMAN
|
MGIFPGIILIFLRVKFATAAVIVSGHQKSTTVSHEMSGLNWKPFVYGGLASIVAEFGTFPVDLTKTRLQVQGQSIDARFKEIKYRGMFHALFRICKEEGVLALYSGIAPALLRQASYGTIKIGIYQSLKRLFVERLEDETLLINMICGVVSGVISSTIANPTDVLKIRMQAQGSLFQGSMIGSFIDIYQQEGTRGLWRGVVPTAQRAAIVVGVELPVYDITKKHLILSGMMGDTILTHFVSSFTCGLAGALASNPVDVVRTRMMNQRAIVGHVDLYKGTVDGILKMWKHEGFFALYKGFWPNWLRLGPWNIIFFITYEQLKRLQI
| null | null |
aerobic respiration [GO:0009060]; inorganic anion transport [GO:0015698]; regulation of cellular response to oxidative stress [GO:1900407]
|
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
chloride transmembrane transporter activity [GO:0015108]; protein homodimerization activity [GO:0042803]; proton transmembrane transporter activity [GO:0015078]; solute:inorganic anion antiporter activity [GO:0005452]; transmembrane transporter activity [GO:0022857]
|
PF00153;
|
1.50.40.10;
|
Mitochondrial carrier (TC 2.A.29) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:20600837}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=sulfate(out) + sulfite(in) = sulfate(in) + sulfite(out); Xref=Rhea:RHEA:73207, ChEBI:CHEBI:16189, ChEBI:CHEBI:17359; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=sulfate(out) + thiosulfate(in) = sulfate(in) + thiosulfate(out); Xref=Rhea:RHEA:73215, ChEBI:CHEBI:16189, ChEBI:CHEBI:33542; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=phosphate(in) + sulfate(out) = phosphate(out) + sulfate(in); Xref=Rhea:RHEA:71631, ChEBI:CHEBI:16189, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=oxalate(in) + sulfate(out) = oxalate(out) + sulfate(in); Xref=Rhea:RHEA:72275, ChEBI:CHEBI:16189, ChEBI:CHEBI:30623; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=malonate(in) + sulfate(out) = malonate(out) + sulfate(in); Xref=Rhea:RHEA:73195, ChEBI:CHEBI:15792, ChEBI:CHEBI:16189; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=maleate(in) + sulfate(out) = maleate(out) + sulfate(in); Xref=Rhea:RHEA:73199, ChEBI:CHEBI:16189, ChEBI:CHEBI:30780; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=(S)-malate(in) + sulfate(out) = (S)-malate(out) + sulfate(in); Xref=Rhea:RHEA:71615, ChEBI:CHEBI:15589, ChEBI:CHEBI:16189; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=(3S)-citramalate(in) + sulfate(out) = (3S)-citramalate(out) + sulfate(in); Xref=Rhea:RHEA:73223, ChEBI:CHEBI:16189, ChEBI:CHEBI:30936; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=(3R)-citramalate(in) + sulfate(out) = (3R)-citramalate(out) + sulfate(in); Xref=Rhea:RHEA:73227, ChEBI:CHEBI:16189, ChEBI:CHEBI:30934; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=succinate(in) + sulfate(out) = succinate(out) + sulfate(in); Xref=Rhea:RHEA:73411, ChEBI:CHEBI:16189, ChEBI:CHEBI:30031; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=(S,S)-tartrate(in) + sulfate(out) = (S,S)-tartrate(out) + sulfate(in); Xref=Rhea:RHEA:73407, ChEBI:CHEBI:16189, ChEBI:CHEBI:30927; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=(2R,3R)-tartrate(in) + sulfate(out) = (2R,3R)-tartrate(out) + sulfate(in); Xref=Rhea:RHEA:73403, ChEBI:CHEBI:16189, ChEBI:CHEBI:30924; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=D-aspartate(in) + sulfate(out) = D-aspartate(out) + sulfate(in); Xref=Rhea:RHEA:73399, ChEBI:CHEBI:16189, ChEBI:CHEBI:29990; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=L-aspartate(in) + sulfate(out) = L-aspartate(out) + sulfate(in); Xref=Rhea:RHEA:73395, ChEBI:CHEBI:16189, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=sulfate(in) = sulfate(out); Xref=Rhea:RHEA:34983, ChEBI:CHEBI:16189; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=(S)-malate(out) = (S)-malate(in); Xref=Rhea:RHEA:74555, ChEBI:CHEBI:15589; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=citrate(in) = citrate(out); Xref=Rhea:RHEA:33183, ChEBI:CHEBI:16947; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=L-aspartate(out) = L-aspartate(in); Xref=Rhea:RHEA:66332, ChEBI:CHEBI:29991; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336, ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:31356773}; CATALYTIC ACTIVITY: Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:22524567, ECO:0000269|PubMed:26182433}; CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:22524567, ECO:0000269|PubMed:26182433};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 mM for sulfate {ECO:0000269|PubMed:31356773}; KM=1.3 mM for thiosulfate {ECO:0000269|PubMed:31356773}; Vmax=4.7 mmol/min/g protein toward sulfate {ECO:0000269|PubMed:31356773};
| null | null | null |
FUNCTION: Transports inorganic anions (sulfate, sulfite, thiosulfate and phosphate) and, to a lesser extent, a variety of dicarboxylates (e.g. malonate, malate and citramalate) and, even more so, aspartate and glutamate and tricarboxylates (PubMed:31356773). May catalyze the export of sulfite and thiosulfate (the hydrogen sulfide degradation products) from the mitochondria, thereby modulating the level of the hydrogen sulfide (Probable). Also can mediate a very low unidirectional transport of anions including sulfate, phosphate, (S)-malate, citrate, L-aspartate and L-glutamate (PubMed:31356773). Maintains oxidative balance (through uncoupling activities) and ATP production (by modifying mitochondrial membrane potential) (PubMed:20600837). Is able to transport protons across lipid membranes (PubMed:22524567, PubMed:26182433). Also exhibits transmembrane chloride transport activity to a lesser extent (PubMed:22524567, PubMed:26182433). May modify mitochondrial respiratory efficiency and mitochondrial oxidant production (By similarity). {ECO:0000250|UniProtKB:Q9Z2B2, ECO:0000269|PubMed:20600837, ECO:0000269|PubMed:22524567, ECO:0000269|PubMed:31356773, ECO:0000305|PubMed:31356773}.
|
Homo sapiens (Human)
|
O95259
|
KCNH1_HUMAN
|
MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSAFMGDPGKIGFADQIPPPLEGRESQGISSLFSSLKVVRLLRLGRVARKLDHYIEYGAAVLVLLVCVFGLAAHWMACIWYSIGDYEIFDEDTKTIRNNSWLYQLAMDIGTPYQFNGSGSGKWEGGPSKNSVYISSLYFTMTSLTSVGFGNIAPSTDIEKIFAVAIMMIGSLLYATIFGNVTTIFQQMYANTNRYHEMLNSVRDFLKLYQVPKGLSERVMDYIVSTWSMSRGIDTEKVLQICPKDMRADICVHLNRKVFKEHPAFRLASDGCLRALAMEFQTVHCAPGDLIYHAGESVDSLCFVVSGSLEVIQDDEVVAILGKGDVFGDVFWKEATLAQSCANVRALTYCDLHVIKRDALQKVLEFYTAFSHSFSRNLILTYNLRKRIVFRKISDVKREEEERMKRKNEAPLILPPDHPVRRLFQRFRQQKEARLAAERGGRDLDDLDVEKGNVLTEHASANHSLVKASVVTVRESPATPVSFQAASTSGVPDHAKLQAPGSECLGPKGGGGDCAKRKSWARFKDACGKSEDWNKVSKAESMETLPERTKASGEATLKKTDSCDSGITKSDLRLDNVGEARSPQDRSPILAEVKHSFYPIPEQTLQATVLEVRHELKEDIKALNAKMTNIEKQLSEILRILTSRRSSQSPQELFEISRPQSPESERDIFGAS
| null | null |
cellular response to calcium ion [GO:0071277]; myoblast fusion [GO:0007520]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of cell population proliferation [GO:0042127]; regulation of membrane potential [GO:0042391]
|
axon [GO:0030424]; dendrite [GO:0030425]; early endosome membrane [GO:0031901]; intracellular membrane-bounded organelle [GO:0043231]; nuclear inner membrane [GO:0005637]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; presynaptic membrane [GO:0042734]; voltage-gated potassium channel complex [GO:0008076]
|
calmodulin binding [GO:0005516]; delayed rectifier potassium channel activity [GO:0005251]; phosphatidylinositol bisphosphate binding [GO:1902936]
|
PF00027;PF00520;PF13426;
|
1.10.1200.260;1.10.287.70;2.60.120.10;3.30.450.20;
|
Potassium channel family, H (Eag) (TC 1.A.1.20) subfamily, Kv10.1/KCNH1 sub-subfamily
|
PTM: Channel activity is regulated via tyrosine phosphorylation/dephosphorylation by SRC and PTPN6 (PubMed:24587194). {ECO:0000269|PubMed:24587194}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:21559285, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:9738473}; Multi-pass membrane protein {ECO:0000269|PubMed:21559285}. Nucleus inner membrane {ECO:0000269|PubMed:21559285}; Multi-pass membrane protein {ECO:0000269|PubMed:21559285}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon {ECO:0000250|UniProtKB:Q63472}. Presynaptic cell membrane {ECO:0000250|UniProtKB:Q63472}. Perikaryon {ECO:0000250|UniProtKB:Q63472}. Postsynaptic density membrane {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane {ECO:0000269|PubMed:22841712}. Note=Perinuclear KCNH1 is located to NPC-free islands.
| null | null | null | null | null |
FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed rectifier potassium channel (PubMed:10880439, PubMed:11943152, PubMed:22732247, PubMed:25556795, PubMed:27005320, PubMed:27325704, PubMed:27618660, PubMed:9738473). Channel properties are modulated by subunit assembly (PubMed:11943152). Mediates IK(NI) current in myoblasts (PubMed:9738473). Involved in the regulation of cell proliferation and differentiation, in particular adipogenic and osteogenic differentiation in bone marrow-derived mesenchymal stem cells (MSCs) (PubMed:23881642). {ECO:0000269|PubMed:10880439, ECO:0000269|PubMed:11943152, ECO:0000269|PubMed:22732247, ECO:0000269|PubMed:23881642, ECO:0000269|PubMed:25556795, ECO:0000269|PubMed:27005320, ECO:0000269|PubMed:27325704, ECO:0000269|PubMed:27618660, ECO:0000269|PubMed:9738473}.
|
Homo sapiens (Human)
|
O95263
|
PDE8B_HUMAN
|
MGCAPSIHVSQSGVIYCRDSDESSSPRQTTSVSQGPAAPLPGLFVQTDAADAIPPSRASGPPSVARVRRARTELGSGSSAGSAAPAATTSRGRRRHCCSSAEAETQTCYTSVKQVSSAEVRIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKSDKNRADLLDTINTCIKKGKEWQGVYYARRKSGDSIQQHVKITPVIGQGGKIRHFVSLKKLCCTTDNNKQIHKIHRDSGDNSQTEPHSFRYKNRRKESIDVKSISSRGSDAPSLQNRRYPSMARIHSMTIEAPITKVINIINAAQENSPVTVAEALDRVLEILRTTELYSPQLGTKDEDPHTSDLVGGLMTDGLRRLSGNEYVFTKNVHQSHSHLAMPITINDVPPCISQLLDNEESWDFNIFELEAITHKRPLVYLGLKVFSRFGVCEFLNCSETTLRAWFQVIEANYHSSNAYHNSTHAADVLHATAFFLGKERVKGSLDQLDEVAALIAATVHDVDHPGRTNSFLCNAGSELAVLYNDTAVLESHHTALAFQLTVKDTKCNIFKNIDRNHYRTLRQAIIDMVLATEMTKHFEHVNKFVNSINKPMAAEIEGSDCECNPAGKNFPENQILIKRMMIKCADVANPCRPLDLCIEWAGRISEEYFAQTDEEKRQGLPVVMPVFDRNTCSIPKSQISFIDYFITDMFDAWDAFAHLPALMQHLADNYKHWKTLDDLKCKSLRLPSDS
|
3.1.4.53
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000250}; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions. {ECO:0000250};
|
behavioral fear response [GO:0001662]; cAMP catabolic process [GO:0006198]; cAMP-mediated signaling [GO:0019933]; negative regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0061179]; negative regulation of steroid hormone biosynthetic process [GO:0090032]; neuromuscular process controlling balance [GO:0050885]; operant conditioning [GO:0035106]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; visual learning [GO:0008542]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]
|
3',5'-cyclic-AMP phosphodiesterase activity [GO:0004115]; 3',5'-cyclic-GMP phosphodiesterase activity [GO:0047555]; metal ion binding [GO:0046872]
|
PF13426;PF08629;PF00233;
|
1.10.1300.10;3.30.450.20;
|
Cyclic nucleotide phosphodiesterase family, PDE8 subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53; Evidence={ECO:0000269|PubMed:12681444};
| null |
PATHWAY: Purine metabolism; 3',5'-cyclic AMP degradation; AMP from 3',5'-cyclic AMP: step 1/1.
| null | null |
FUNCTION: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May be involved in specific signaling in the thyroid gland.
|
Homo sapiens (Human)
|
O95264
|
5HT3B_HUMAN
|
MLSSVMAPLWACILVAAGILATDTHHPQDSALYHLSKQLLQKYHKEVRPVYNWTKATTVYLDLFVHAILDVDAENQILKTSVWYQEVWNDEFLSWNSSMFDEIREISLPLSAIWAPDIIINEFVDIERYPDLPYVYVNSSGTIENYKPIQVVSACSLETYAFPFDVQNCSLTFKSILHTVEDVDLAFLRSPEDIQHDKKAFLNDSEWELLSVSSTYSILQSSAGGFAQIQFNVVMRRHPLVYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTSVLVGYTVFRVNMSNQVPRSVGSTPLIGHFFTICMAFLVLSLAKSIVLVKFLHDEQRGGQEQPFLCLRGDTDADRPRVEPRAQRAVVTESSLYGEHLAQPGTLKEVWSQLQSISNYLQTQDQTDQQEAEWLVLLSRFDRLLFQSYLFMLGIYTITLCSLWALWGGV
| null | null |
inorganic cation transmembrane transport [GO:0098662]; serotonin receptor signaling pathway [GO:0007210]
|
cell surface [GO:0009986]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; serotonin-activated cation-selective channel complex [GO:1904602]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495]
|
acetylcholine-gated monoatomic cation-selective channel activity [GO:0022848]; excitatory extracellular ligand-gated monoatomic ion channel activity [GO:0005231]; serotonin-gated monoatomic cation channel activity [GO:0022850]; transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential [GO:1904315]
|
PF02931;PF02932;
|
2.70.170.10;1.20.58.390;
|
Ligand-gated ion channel (TC 1.A.9) family, 5-hydroxytryptamine receptor (TC 1.A.9.2) subfamily, HTR3B sub-subfamily
|
PTM: N-glycosylation required for membrane localization. {ECO:0000269|PubMed:21138434}.
|
SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000305|PubMed:9950429}; Multi-pass membrane protein {ECO:0000269|PubMed:21138434}. Cell membrane {ECO:0000269|PubMed:21138434}; Multi-pass membrane protein {ECO:0000269|PubMed:21138434}. Note=Presumably retained within the endoplasmic reticulum unless complexed with HTR3A. {ECO:0000269|PubMed:21138434}.
|
CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:9950429}; CATALYTIC ACTIVITY: Reaction=K(+)(in) = K(+)(out); Xref=Rhea:RHEA:29463, ChEBI:CHEBI:29103; Evidence={ECO:0000269|PubMed:9950429}; CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10521471, ECO:0000269|PubMed:17392525, ECO:0000269|PubMed:9950429};
| null | null | null | null |
FUNCTION: Forms serotonin (5-hydroxytryptamine/5-HT3)-activated cation-selective channel complexes, which when activated cause fast, depolarizing responses in neurons. {ECO:0000269|PubMed:10521471, ECO:0000269|PubMed:12867984, ECO:0000269|PubMed:17392525, ECO:0000269|PubMed:9950429}.
|
Homo sapiens (Human)
|
O95267
|
GRP1_HUMAN
|
MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEINKVLGEMTELLSSSRNYDNYRRAYGECTDFKIPILGVHLKDLISLYEAMPDYLEDGKVNVHKLLALYNHISELVQLQEVAPPLEANKDLVHLLTLSLDLYYTEDEIYELSYAREPRNHRAPPLTPSKPPVVVDWASGVSPKPDPKTISKHVQRMVDSVFKNYDHDQDGYISQEEFEKIAASFPFSFCVMDKDREGLISRDEITAYFMRASSIYSKLGLGFPHNFQETTYLKPTFCDNCAGFLWGVIKQGYRCKDCGMNCHKQCKDLVVFECKKRAKNPVAPTENNTSVGPVSNLCSLGAKDLLHAPEEGPFTFPNGEAVEHGEESKDRTIMLMGVSSQKISLRLKRAVAHKATQTESQPWIGSEGPSGPFVLSSPRKTAQDTLYVLPSPTSPCPSPVLVRKRAFVKWENKDSLIKSKEELRHLRLPTYQELEQEINTLKADNDALKIQLKYAQKKIESLQLEKSNHVLAQMEQGDCS
| null | null |
activation of GTPase activity [GO:0090630]; B cell activation [GO:0042113]; B cell proliferation [GO:0042100]; cell differentiation [GO:0030154]; inflammatory response to antigenic stimulus [GO:0002437]; mast cell degranulation [GO:0043303]; natural killer cell activation [GO:0030101]; positive regulation of ERK1 and ERK2 cascade [GO:0070374]; positive regulation of granulocyte macrophage colony-stimulating factor production [GO:0032725]; positive regulation of GTPase activity [GO:0043547]; positive regulation of JNK cascade [GO:0046330]; positive regulation of MAP kinase activity [GO:0043406]; positive regulation of natural killer cell differentiation [GO:0032825]; positive regulation of natural killer cell mediated cytotoxicity [GO:0045954]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of Ras protein signal transduction [GO:0046579]; positive regulation of T cell differentiation in thymus [GO:0033089]; positive regulation of tumor necrosis factor production [GO:0032760]; positive regulation of type II interferon production [GO:0032729]; Ras protein signal transduction [GO:0007265]; regulation of ERK1 and ERK2 cascade [GO:0070372]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; secretory granule localization [GO:0032252]; signal transduction [GO:0007165]; T cell activation [GO:0042110]; T cell proliferation [GO:0042098]; vesicle transport along microtubule [GO:0047496]
|
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
calcium ion binding [GO:0005509]; diacylglycerol binding [GO:0019992]; guanyl-nucleotide exchange factor activity [GO:0005085]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; phosphatidylcholine binding [GO:0031210]; zinc ion binding [GO:0008270]
|
PF00130;PF00617;PF00618;
|
3.30.60.20;6.10.250.2730;1.10.238.10;1.10.840.10;1.20.870.10;
|
RASGRP family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cell membrane; Peripheral membrane protein. Golgi apparatus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Found both in the cytosol and associated with membranes. Relocalization to the cell membrane upon activation is F-actin-dependent. Translocates to the Golgi in response to phorbol ester or nerve growth factor. Localizes to somata and dendrites but not to axons of hippocampal pyramidal cells (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Functions as a calcium- and diacylglycerol (DAG)-regulated nucleotide exchange factor specifically activating Ras through the exchange of bound GDP for GTP (PubMed:15899849, PubMed:23908768, PubMed:27776107, PubMed:29155103). Activates the Erk/MAP kinase cascade (PubMed:15899849). Regulates T-cell/B-cell development, homeostasis and differentiation by coupling T-lymphocyte/B-lymphocyte antigen receptors to Ras (PubMed:10807788, PubMed:12839994, PubMed:27776107, PubMed:29155103). Regulates NK cell cytotoxicity and ITAM-dependent cytokine production by activation of Ras-mediated ERK and JNK pathways (PubMed:19933860). Functions in mast cell degranulation and cytokine secretion, regulating FcERI-evoked allergic responses. May also function in differentiation of other cell types (PubMed:12845332). {ECO:0000250|UniProtKB:Q9Z1S3, ECO:0000269|PubMed:10807788, ECO:0000269|PubMed:12782630, ECO:0000269|PubMed:12839994, ECO:0000269|PubMed:12845332, ECO:0000269|PubMed:15060167, ECO:0000269|PubMed:15184873, ECO:0000269|PubMed:15899849, ECO:0000269|PubMed:19933860, ECO:0000269|PubMed:23908768, ECO:0000269|PubMed:27776107, ECO:0000269|PubMed:29155103}.
|
Homo sapiens (Human)
|
O95271
|
TNKS1_HUMAN
|
MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALDLADPSAKAVLTGEYKKDELLEAARSGNEEKLMALLTPLNVNCHASDGRKSTPLHLAAGYNRVRIVQLLLQHGADVHAKDKGGLVPLHNACSYGHYEVTELLLKHGACVNAMDLWQFTPLHEAASKNRVEVCSLLLSHGADPTLVNCHGKSAVDMAPTPELRERLTYEFKGHSLLQAAREADLAKVKKTLALEIINFKQPQSHETALHCAVASLHPKRKQVTELLLRKGANVNEKNKDFMTPLHVAAERAHNDVMEVLHKHGAKMNALDTLGQTALHRAALAGHLQTCRLLLSYGSDPSIISLQGFTAAQMGNEAVQQILSESTPIRTSDVDYRLLEASKAGDLETVKQLCSSQNVNCRDLEGRHSTPLHFAAGYNRVSVVEYLLHHGADVHAKDKGGLVPLHNACSYGHYEVAELLVRHGASVNVADLWKFTPLHEAAAKGKYEICKLLLKHGADPTKKNRDGNTPLDLVKEGDTDIQDLLRGDAALLDAAKKGCLARVQKLCTPENINCRDTQGRNSTPLHLAAGYNNLEVAEYLLEHGADVNAQDKGGLIPLHNAASYGHVDIAALLIKYNTCVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTMKNQEGQTPLDLATADDIRALLIDAMPPEALPTCFKPQATVVSASLISPASTPSCLSAASSIDNLTGPLAELAVGGASNAGDGAAGTERKEGEVAGLDMNISQFLKSLGLEHLRDIFETEQITLDVLADMGHEELKEIGINAYGHRHKLIKGVERLLGGQQGTNPYLTFHCVNQGTILLDLAPEDKEYQSVEEEMQSTIREHRDGGNAGGIFNRYNVIRIQKVVNKKLRERFCHRQKEVSEENHNHHNERMLFHGSPFINAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPTHKDRSCYICHRQMLFCRVTLGKSFLQFSTMKMAHAPPGHHSVIGRPSVNGLAYAEYVIYRGEQAYPEYLITYQIMKPEAPSQTATAAEQKT
|
2.4.2.-; 2.4.2.30
| null |
cell division [GO:0051301]; mitotic spindle organization [GO:0007052]; mRNA transport [GO:0051028]; negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric [GO:1904908]; negative regulation of telomere maintenance via telomere lengthening [GO:1904357]; negative regulation of telomeric DNA binding [GO:1904743]; peptidyl-serine phosphorylation [GO:0018105]; peptidyl-threonine phosphorylation [GO:0018107]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of telomerase activity [GO:0051973]; positive regulation of telomere capping [GO:1904355]; positive regulation of telomere maintenance via telomerase [GO:0032212]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein auto-ADP-ribosylation [GO:0070213]; protein localization to chromosome, telomeric region [GO:0070198]; protein poly-ADP-ribosylation [GO:0070212]; protein polyubiquitination [GO:0000209]; protein transport [GO:0015031]; regulation of telomere maintenance via telomerase [GO:0032210]; spindle assembly [GO:0051225]; Wnt signaling pathway [GO:0016055]
|
chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; mitotic spindle pole [GO:0097431]; nuclear body [GO:0016604]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentriolar material [GO:0000242]
|
histone binding [GO:0042393]; NAD+ ADP-ribosyltransferase activity [GO:0003950]; NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; nucleotidyltransferase activity [GO:0016779]; zinc ion binding [GO:0008270]
|
PF00023;PF12796;PF13637;PF00644;PF07647;
|
3.90.228.10;6.20.320.10;1.25.40.20;1.10.150.50;
|
ARTD/PARP family
|
PTM: Phosphorylated on serine residues by MAPK kinases upon insulin stimulation. Phosphorylated during mitosis. {ECO:0000269|PubMed:10988299}.; PTM: Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation. Deubiquitinated by USP25; leading to stabilization (PubMed:28619731). {ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:28619731}.; PTM: ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination. {ECO:0000269|PubMed:21478859}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:21799911, ECO:0000269|PubMed:22864114}. Golgi apparatus membrane {ECO:0000269|PubMed:22864114}; Peripheral membrane protein {ECO:0000269|PubMed:22864114}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:21799911}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:10523501}. Chromosome, telomere {ECO:0000305|PubMed:9822378}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16076287}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles (PubMed:22864114). A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres (PubMed:10523501). During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1 (PubMed:12768206). Localizes to spindle poles at mitosis onset via interaction with NUMA1 (PubMed:12080061). {ECO:0000269|PubMed:10523501, ECO:0000269|PubMed:12080061, ECO:0000269|PubMed:12768206, ECO:0000269|PubMed:22864114}.
|
CATALYTIC ACTIVITY: Reaction=NAD(+) + (ADP-D-ribosyl)n-acceptor = nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H(+).; EC=2.4.2.30; Evidence={ECO:0000269|PubMed:19759537}; CATALYTIC ACTIVITY: Reaction=L-aspartyl-[protein] + NAD(+) = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide; Xref=Rhea:RHEA:54424, Rhea:RHEA-COMP:9867, Rhea:RHEA-COMP:13832, ChEBI:CHEBI:17154, ChEBI:CHEBI:29961, ChEBI:CHEBI:57540, ChEBI:CHEBI:138102; Evidence={ECO:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54425; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reaction=L-glutamyl-[protein] + NAD(+) = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58224, Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:15089, ChEBI:CHEBI:17154, ChEBI:CHEBI:29973, ChEBI:CHEBI:57540, ChEBI:CHEBI:142540; Evidence={ECO:0000305}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58225; Evidence={ECO:0000305};
| null | null | null | null |
FUNCTION: Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking (PubMed:10988299, PubMed:11739745, PubMed:16076287, PubMed:19759537, PubMed:21478859, PubMed:22864114, PubMed:23622245, PubMed:25043379, PubMed:28619731). Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation (PubMed:19759537, PubMed:21478859). Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination (PubMed:21478859). Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length (PubMed:11739745). Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI (PubMed:22864114). May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles (PubMed:10988299). May be involved in spindle pole assembly through PARsylation of NUMA1 (PubMed:16076287). Stimulates 26S proteasome activity (PubMed:23622245). {ECO:0000269|PubMed:10988299, ECO:0000269|PubMed:11739745, ECO:0000269|PubMed:16076287, ECO:0000269|PubMed:19759537, ECO:0000269|PubMed:21478859, ECO:0000269|PubMed:22864114, ECO:0000269|PubMed:23622245, ECO:0000269|PubMed:25043379, ECO:0000269|PubMed:28619731}.
|
Homo sapiens (Human)
|
O95273
|
CCDB1_HUMAN
|
MASATAPAAAVPTLASPLEQLRHLAEELRLLLPRVRVGEAQETTEEFNREMFWRRLNEAAVTVSREATTLTIVFSQLPLPSPQETQKFCEQVHAAIKAFIAVYYLLPKDQGITLRKLVRGATLDIVDGMAQLMEVLSVTPTQSPENNDLISYNSVWVACQQMPQIPRDNKAAALLMLTKNVDFVKDAHEEMEQAVEECDPYSGLLNDTEENNSDNHNHEDDVLGFPSNQDLYWSEDDQELIIPCLALVRASKACLKKIRMLVAENGKKDQVAQLDDIVDISDEISPSVDDLALSIYPPMCHLTVRINSAKLVSVLKKALEITKASHVTPQPEDSWIPLLINAIDHCMNRIKELTQSELEL
| null | null |
cell cycle [GO:0007049]; regulation of cell cycle [GO:0051726]
|
cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
| null |
PF20936;PF13324;
|
1.20.1410.10;1.20.1420.10;
|
CCNDBP1 family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:10854051}.
|
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
| null | null | null | null | null |
FUNCTION: May negatively regulate cell cycle progression. May act at least in part via inhibition of the cyclin-D1/CDK4 complex, thereby preventing phosphorylation of RB1 and blocking E2F-dependent transcription. {ECO:0000269|PubMed:10801854}.
|
Homo sapiens (Human)
|
O95274
|
LYPD3_HUMAN
|
MDPARKAGAQAMIWTAGWLLLLLLRGGAQALECYSCVQKADDGCSPNKMKTVKCAPGVDVCTEAVGAVETIHGQFSLAVRGCGSGLPGKNDRGLDLHGLLAFIQLQQCAQDRCNAKLNLTSRALDPAGNESAYPPNGVECYSCVGLSREACQGTSPPVVSCYNASDHVYKGCFDGNVTLTAANVTVSLPVRGCVQDEFCTRDGVTGPGFTLSGSCCQGSRCNSDLRNKTYFSPRIPPLVRLPPPEPTTVASTTSVTTSTSAPVRPTSTTKPMPAPTSQTPRQGVEHEASRDEEPRLTGGAAGHQDRSNSGQYPAKGGPQQPHNKGCVAPTAGLAALLLAVAAGVLL
| null | null |
cell-matrix adhesion [GO:0007160]; negative regulation of smooth muscle cell apoptotic process [GO:0034392]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
laminin binding [GO:0043236]
|
PF00021;
|
2.10.60.10;
| null |
PTM: N-glycosylated and O-glycosylated. {ECO:0000269|PubMed:15012588}.
|
SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor.
| null | null | null | null | null |
FUNCTION: Supports cell migration. May be involved in urothelial cell-matrix interactions. May be involved in tumor progression. {ECO:0000269|PubMed:11179665, ECO:0000269|PubMed:11245483, ECO:0000269|PubMed:12592373, ECO:0000269|PubMed:15012588}.
|
Homo sapiens (Human)
|
O95278
|
EPM2A_HUMAN
|
MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEALARAQEDFFQKFGKVRSSVCSL
|
3.1.3.-; 3.1.3.16; 3.1.3.48
| null |
autophagosome assembly [GO:0000045]; calcium ion transport [GO:0006816]; carbohydrate phosphorylation [GO:0046835]; dephosphorylation [GO:0016311]; glial cell proliferation [GO:0014009]; glycogen biosynthetic process [GO:0005978]; glycogen metabolic process [GO:0005977]; habituation [GO:0046959]; L-glutamate transmembrane transport [GO:0015813]; mitochondrion organization [GO:0007005]; negative regulation of cell cycle [GO:0045786]; negative regulation of dephosphorylation [GO:0035305]; negative regulation of gene expression [GO:0010629]; negative regulation of peptidyl-serine phosphorylation [GO:0033137]; negative regulation of phosphatase activity [GO:0010923]; peptidyl-tyrosine dephosphorylation [GO:0035335]; positive regulation of macroautophagy [GO:0016239]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein dephosphorylation [GO:0006470]; regulation of cell growth [GO:0001558]; regulation of proteasomal protein catabolic process [GO:0061136]; regulation of protein import into nucleus [GO:0042306]; regulation of protein localization to plasma membrane [GO:1903076]; regulation of protein ubiquitination [GO:0031396]; Wnt signaling pathway [GO:0016055]
|
cytoplasm [GO:0005737]; cytoplasmic side of rough endoplasmic reticulum membrane [GO:0098556]; cytosol [GO:0005829]; dendrite [GO:0030425]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]
|
carbohydrate binding [GO:0030246]; carbohydrate phosphatase activity [GO:0019203]; glycogen (starch) synthase activity [GO:0004373]; glycogen binding [GO:2001069]; myosin phosphatase activity [GO:0017018]; phosphatase activity [GO:0016791]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine phosphatase activity [GO:0004725]; protein tyrosine/serine/threonine phosphatase activity [GO:0008138]; starch binding [GO:2001070]
|
PF00686;PF00782;
|
2.60.40.10;3.90.190.10;
|
Protein-tyrosine phosphatase family
|
PTM: Polyubiquitinated by NHLRC1/malin. {ECO:0000269|PubMed:15930137}.; PTM: Phosphorylation on Ser-25 by AMPK affects the phosphatase activity of the enzyme and its ability to homodimerize and interact with NHLRC1, PPP1R3C or PRKAA2. {ECO:0000269|PubMed:21728993}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11220751, ECO:0000269|PubMed:11739371, ECO:0000269|PubMed:15102711, ECO:0000269|PubMed:17908927}. Note=Under glycogenolytic conditions localizes to the nucleus. {ECO:0000269|PubMed:17908927}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11739371, ECO:0000269|PubMed:11883934, ECO:0000269|PubMed:14532330, ECO:0000269|PubMed:18311786, ECO:0000269|PubMed:18617530, ECO:0000269|PubMed:22036712}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:14722920, ECO:0000269|PubMed:18311786}; Peripheral membrane protein {ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:18311786}; Cytoplasmic side {ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:18311786}. Cell membrane {ECO:0000269|PubMed:11220751}. Note=Colocalizes with glycogen synthase in punctate structures in the cytoplasm (PubMed:11739371, PubMed:14532330). Primarily associated with polyribosomes at the rough endoplasmic reticulum, and also detected at the plasma membrane (PubMed:11001928, PubMed:11220751, PubMed:11883934, PubMed:18311786). {ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11220751, ECO:0000269|PubMed:11739371, ECO:0000269|PubMed:11883934, ECO:0000269|PubMed:14532330, ECO:0000269|PubMed:18311786}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:18617530}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:11883934}; Peripheral membrane protein {ECO:0000269|PubMed:11883934}; Cytoplasmic side {ECO:0000269|PubMed:11883934}. Cell membrane {ECO:0000269|PubMed:11883934}. Nucleus {ECO:0000269|PubMed:11883934, ECO:0000269|PubMed:14722920, ECO:0000269|PubMed:18617530}. Note=Also found in the nucleus. {ECO:0000269|PubMed:11883934, ECO:0000269|PubMed:18617530}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:22036712}. Nucleus {ECO:0000269|PubMed:22036712}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm {ECO:0000269|PubMed:22036712}. Nucleus {ECO:0000269|PubMed:22036712}.; SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm {ECO:0000269|PubMed:22036712}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044, ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11220751}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000305|PubMed:11001928}; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16; Evidence={ECO:0000305|PubMed:11001928};
| null | null | null | null |
FUNCTION: Plays an important role in preventing glycogen hyperphosphorylation and the formation of insoluble aggregates, via its activity as glycogen phosphatase, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with the E3 ubiquitin ligase NHLRC1/malin. Shows strong phosphatase activity towards complex carbohydrates in vitro, avoiding glycogen hyperphosphorylation which is associated with reduced branching and formation of insoluble aggregates (PubMed:16901901, PubMed:23922729, PubMed:25538239, PubMed:25544560, PubMed:26231210). Dephosphorylates phosphotyrosine and synthetic substrates, such as para-nitrophenylphosphate (pNPP), and has low activity with phosphoserine and phosphothreonine substrates (in vitro) (PubMed:11001928, PubMed:11220751, PubMed:11739371, PubMed:14532330, PubMed:14722920, PubMed:16971387, PubMed:18617530, PubMed:22036712, PubMed:23922729). Has been shown to dephosphorylate MAPT (By similarity). Forms a complex with NHLRC1/malin and HSP70, which suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Acts as a scaffold protein to facilitate PPP1R3C/PTG ubiquitination by NHLRC1/malin (PubMed:23922729). Also promotes proteasome-independent protein degradation through the macroautophagy pathway (PubMed:20453062). {ECO:0000250|UniProtKB:Q9WUA5, ECO:0000269|PubMed:11001928, ECO:0000269|PubMed:11220751, ECO:0000269|PubMed:11739371, ECO:0000269|PubMed:14532330, ECO:0000269|PubMed:14722920, ECO:0000269|PubMed:16901901, ECO:0000269|PubMed:16971387, ECO:0000269|PubMed:18070875, ECO:0000269|PubMed:18617530, ECO:0000269|PubMed:19036738, ECO:0000269|PubMed:20453062, ECO:0000269|PubMed:22036712, ECO:0000269|PubMed:23624058, ECO:0000269|PubMed:23922729, ECO:0000269|PubMed:25538239, ECO:0000269|PubMed:25544560, ECO:0000269|PubMed:26231210}.; FUNCTION: [Isoform 2]: Does not bind to glycogen (PubMed:18617530). Lacks phosphatase activity and might function as a dominant-negative regulator for the phosphatase activity of isoform 1 and isoform 7 (PubMed:18617530, PubMed:22036712). {ECO:0000269|PubMed:18617530, ECO:0000269|PubMed:22036712}.; FUNCTION: [Isoform 7]: Has phosphatase activity (in vitro). {ECO:0000269|PubMed:22036712}.
|
Homo sapiens (Human)
|
O95279
|
KCNK5_HUMAN
|
MVDRGPLLTSAIIFYLAIGAAIFEVLEEPHWKEAKKNYYTQKLHLLKEFPCLGQEGLDKILEVVSDAAGQGVAITGNQTFNNWNWPNAMIFAATVITTIGYGNVAPKTPAGRLFCVFYGLFGVPLCLTWISALGKFFGGRAKRLGQFLTKRGVSLRKAQITCTVIFIVWGVLVHLVIPPFVFMVTEGWNYIEGLYYSFITISTIGFGDFVAGVNPSANYHALYRYFVELWIYLGLAWLSLFVNWKVSMFVEVHKAIKKRRRRRKESFESSPHSRKALQVKGSTASKDVNIFSFLSKKEETYNDLIKQIGKKAMKTSGGGETGPGPGLGPQGGGLPALPPSLVPLVVYSKNRVPTLEEVSQTLRSKGHVSRSPDEEAVARAPEDSSPAPEVFMNQLDRISEECEPWDAQDYHPLIFQDASITFVNTEAGLSDEETSKSSLEDNLAGEESPQQGAEAKAPLNMGEFPSSSESTFTSTESELSVPYEQLMNEYNKANSPKGT
| null | null |
potassium ion export across plasma membrane [GO:0097623]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; regulation of resting membrane potential [GO:0060075]; stabilization of membrane potential [GO:0030322]
|
monoatomic ion channel complex [GO:0034702]; plasma membrane [GO:0005886]
|
outward rectifier potassium channel activity [GO:0015271]; potassium channel activity [GO:0005267]; potassium ion leak channel activity [GO:0022841]
|
PF07885;
|
1.10.287.70;
|
Two pore domain potassium channel (TC 1.A.1.8) family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: pH-dependent, outwardly rectifying potassium channel (PubMed:9812978). Outward rectification is lost at high external K(+) concentrations (PubMed:9812978). {ECO:0000269|PubMed:9812978}.
|
Homo sapiens (Human)
|
O95292
|
VAPB_HUMAN
|
MAKVEQVLSLEPQHELKFRGPFTDVVTTNLKLGNPTDRNVCFKVKTTAPRRYCVRPNSGIIDAGASINVSVMLQPFDYDPNEKSKHKFMVQSMFAPTDTSDMEAVWKEAKPEDLMDSKLRCVFELPAENDKPHDVEINKIISTTASKTETPIVSKSLSSSLDDTEVKKVMEECKRLQGEVQRLREENKQFKEEDGLRMRKTVQSNSPISALAPTGKEEGLSTRLLALVVLFFIVGVIIGKIAL
| null | null |
cholesterol transport [GO:0030301]; COPII-coated vesicle budding [GO:0090114]; endoplasmic reticulum membrane organization [GO:0090158]; endoplasmic reticulum organization [GO:0007029]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; endoplasmic reticulum unfolded protein response [GO:0030968]; endoplasmic reticulum-plasma membrane tethering [GO:0061817]; intracellular calcium ion homeostasis [GO:0006874]; IRE1-mediated unfolded protein response [GO:0036498]; modulation by host of viral RNA genome replication [GO:0044830]; negative regulation by host of viral genome replication [GO:0044828]; negative regulation by virus of viral protein levels in host cell [GO:0046725]; positive regulation by host of viral genome replication [GO:0044829]; positive regulation of viral genome replication [GO:0045070]; suppression of viral release by host [GO:0044790]; viral release from host cell [GO:0019076]
|
cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]
|
beta-tubulin binding [GO:0048487]; cadherin binding [GO:0045296]; enzyme binding [GO:0019899]; FFAT motif binding [GO:0033149]; microtubule binding [GO:0008017]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]
|
PF00635;
|
2.60.40.10;
|
VAMP-associated protein (VAP) (TC 9.B.17) family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:32344433, ECO:0000269|PubMed:33124732}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:Q9P0L0}. Note=Present in mitochondria-associated membranes that are endoplasmic reticulum membrane regions closely apposed to the outer mitochondrial membrane. {ECO:0000269|PubMed:22131369}.
| null | null | null | null | null |
FUNCTION: Endoplasmic reticulum (ER)-anchored protein that mediates the formation of contact sites between the ER and endosomes via interaction with FFAT motif-containing proteins such as STARD3 or WDR44 (PubMed:32344433, PubMed:33124732). Interacts with STARD3 in a FFAT motif phosphorylation dependent manner (PubMed:33124732). Via interaction with WDR44 participates in neosynthesized protein export (PubMed:32344433). Participates in the endoplasmic reticulum unfolded protein response (UPR) by inducing ERN1/IRE1 activity (PubMed:16891305, PubMed:20940299). Involved in cellular calcium homeostasis regulation (PubMed:22131369). {ECO:0000269|PubMed:16891305, ECO:0000269|PubMed:20940299, ECO:0000269|PubMed:22131369, ECO:0000269|PubMed:32344433, ECO:0000269|PubMed:33124732}.
|
Homo sapiens (Human)
|
O95294
|
RASL1_HUMAN
|
MAKSSSLNVRVVEGRALPAKDVSGSSDPYCLVKVDDEVVARTATVWRSLGPFWGEEYTVHLPLDFHQLAFYVLDEDTVGHDDIIGKISLSREAITADPRGIDSWINLSRVDPDAEVQGEICLSVQMLEDGQGRCLRCHVLQARDLAPRDISGTSDPFARVFWGSQSLETSTIKKTRFPHWDEVLELREMPGAPSPLRVELWDWDMVGKNDFLGMVEFSPKTLQQKPPKGWFRLLPFPRAEEDSGGNLGALRVKVRLIEDRVLPSQCYQPLMELLMESVQGPAEEDTASPLALLEELTLGDCRQDLATKLVKLFLGRGLAGRFLDYLTRREVARTMDPNTLFRSNSLASKSMEQFMKLVGMPYLHEVLKPVISRVFEEKKYMELDPCKMDLGRTRRISFKGALSEEQMRETSLGLLTGYLGPIVDAIVGSVGRCPPAMRLAFKQLHRRVEERFPQAEHQDVKYLAISGFLFLRFFAPAILTPKLFDLRDQHADPQTSRSLLLLAKAVQSIGNLGQQLGQGKELWMAPLHPFLLQCVSRVRDFLDRLVDVDGDEAGVPARALFPPSAIVREGYLLKRKEEPAGLATRFAFKKRYVWLSGETLSFSKSPEWQMCHSIPVSHIRAVERVDEGAFQLPHVMQVVTQDGTGALHTTYLQCKNVNELNQWLSALRKASAPNPNKLAACHPGAFRSARWTCCLQAERSAAGCSRTHSAVTLGDWSDPLDPDAEAQTVYRQLLLGRDQLRLKLLEDSNMDTTLEADTGACPEVLARQRAATARLLEVLADLDRAHEEFQQQERGKAALGPLGP
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
|
cell differentiation [GO:0030154]; cellular response to calcium ion [GO:0071277]; intracellular signal transduction [GO:0035556]; negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of dendrite extension [GO:1903861]; signal transduction [GO:0007165]
|
cytosol [GO:0005829]
|
GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872]; phospholipid binding [GO:0005543]
|
PF00779;PF00168;PF00169;PF00616;
|
2.60.40.150;2.30.29.30;
| null | null | null | null | null | null | null | null |
FUNCTION: Probable inhibitory regulator of the Ras-cyclic AMP pathway (PubMed:9751798). Plays a role in dendrite formation by melanocytes (PubMed:23999003). {ECO:0000269|PubMed:23999003, ECO:0000269|PubMed:9751798}.
|
Homo sapiens (Human)
|
O95295
|
SNAPN_HUMAN
|
MAGAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDNLATELCRINEDQKVALDLDPYVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARRRAMLDSGIYPPGSPGK
| null | null |
anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; autophagosome maturation [GO:0097352]; endosome to lysosome transport [GO:0008333]; intracellular protein transport [GO:0006886]; late endosome to lysosome transport [GO:1902774]; lysosomal lumen acidification [GO:0007042]; lysosome localization [GO:0032418]; lysosome organization [GO:0007040]; melanosome organization [GO:0032438]; negative regulation of neuron projection development [GO:0010977]; neuron cellular homeostasis [GO:0070050]; neuron projection development [GO:0031175]; neurotransmitter secretion [GO:0007269]; organelle transport along microtubule [GO:0072384]; positive regulation of late endosome to lysosome transport [GO:1902824]; protein maturation [GO:0051604]; protein-containing complex localization [GO:0031503]; regulation of endosome size [GO:0051036]; regulation of lysosome size [GO:0062196]; regulation of protein binding [GO:0043393]; regulation of synaptic vesicle exocytosis [GO:2000300]; retrograde axonal transport [GO:0008090]; synaptic vesicle exocytosis [GO:0016079]; synaptic vesicle fusion to presynaptic active zone membrane [GO:0031629]; synaptic vesicle maturation [GO:0016188]; synaptic vesicle transport [GO:0048489]; terminal button organization [GO:0072553]
|
acrosomal vesicle [GO:0001669]; axon cytoplasm [GO:1904115]; BLOC-1 complex [GO:0031083]; BORC complex [GO:0099078]; cytoplasmic side of lysosomal membrane [GO:0098574]; cytosol [GO:0005829]; Golgi membrane [GO:0000139]; manchette [GO:0002177]; microvesicle [GO:1990742]; perinuclear region of cytoplasm [GO:0048471]; secretory granule [GO:0030141]; synapse [GO:0045202]; synaptic vesicle [GO:0008021]; synaptic vesicle membrane [GO:0030672]
|
SNARE binding [GO:0000149]
|
PF14712;
| null |
SNAPIN family
|
PTM: Phosphorylated by CSNK1D/CK1 (By similarity). Phosphorylated by PKD, phosphorylation controls SNAPIN protein stability. {ECO:0000250, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:21102408}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z266}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z266}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21102408}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z266}. Lysosome membrane {ECO:0000305|PubMed:25898167}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:21102408}. Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells. {ECO:0000269|PubMed:19168546}.
| null | null | null | null | null |
FUNCTION: Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells (PubMed:17182842, PubMed:18167355). As part of the BORC complex may play a role in lysosomes movement and localization at the cell periphery. Associated with the cytosolic face of lysosomes, the BORC complex may recruit ARL8B and couple lysosomes to microtubule plus-end-directed kinesin motor (PubMed:25898167). {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:25898167}.
|
Homo sapiens (Human)
|
O95297
|
MPZL1_HUMAN
|
MAASAGAGAVIAAPDSRRWLWSVLAAALGLLTAGVSALEVYTPKEIFVANGTQGKLTCKFKSTSTTGGLTSVSWSFQPEGADTTVSFFHYSQGQVYLGNYPPFKDRISWAGDLDKKDASINIENMQFIHNGTYICDVKNPPDIVVQPGHIRLYVVEKENLPVFPVWVVVGIVTAVVLGLTLLISMILAVLYRRKNSKRDYTGCSTSESLSPVKQAPRKSPSDTEGLVKSLPSGSHQGPVIYAQLDHSGGHHSDKINKSESVVYADIRKN
| null | null |
cell-cell signaling [GO:0007267]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169]
|
cell surface [GO:0009986]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]
|
structural molecule activity [GO:0005198]
|
PF07686;
|
2.60.40.10;
|
Myelin P0 protein family
|
PTM: Phosphorylated on tyrosine residues upon stimulation with pervanadate and concanavalin-A (ConA). Phosphorylation at Tyr-241 and Tyr-263 is required for interaction with PTPN11/SHP-2. Dephosphorylated by PTPN11/SHP-2 (in vitro). {ECO:0000269|PubMed:10681522, ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:9792637}.; PTM: N-glycosylated. N-glycosylation is required for concanavalin A binding (PubMed:30392906). {ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:30392906, ECO:0000269|PubMed:9792637}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Cell surface receptor, which is involved in signal transduction processes. Recruits PTPN11/SHP-2 to the cell membrane and is a putative substrate of PTPN11/SHP-2. Is a major receptor for concanavalin-A (ConA) and is involved in cellular signaling induced by ConA, which probably includes Src family tyrosine-protein kinases. Isoform 3 seems to have a dominant negative role; it blocks tyrosine phosphorylation of MPZL1 induced by ConA. Isoform 1, but not isoform 2 and isoform 3, may be involved in regulation of integrin-mediated cell motility. {ECO:0000269|PubMed:11751924, ECO:0000269|PubMed:12410637}.
|
Homo sapiens (Human)
|
O95298
|
NDUC2_HUMAN
|
MIARRNPEPLRFLPDEARSLPPPKLTDPRLLYIGFLGYCSGLIDNLIRRRPIATAGLHRQLLYITAFFFAGYYLVKREDYLYAVRDREMFGYMKLHPEDFPEEDKKTYGEIFEKFHPIR
| null | null |
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
azurophil granule membrane [GO:0035577]; cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]
|
NADH dehydrogenase (ubiquinone) activity [GO:0008137]
|
PF06374;
| null |
Complex I NDUFC2 subunit family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Single-pass membrane protein {ECO:0000255}; Matrix side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis but required for the complex assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371, ECO:0000269|PubMed:32969598}.
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Homo sapiens (Human)
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O95299
|
NDUAA_HUMAN
|
MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQDKFEVLNYTSIPIFLPEVTIGAHQTDRVLHQFRELPGRKYSPGYNTEVGDKWIWLK
| null |
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.;
|
aerobic respiration [GO:0009060]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; proton motive force-driven mitochondrial ATP synthesis [GO:0042776]
|
cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739]
|
deoxynucleoside kinase activity [GO:0019136]; NADH dehydrogenase (ubiquinone) activity [GO:0008137]
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PF01712;
|
3.40.50.300;
|
Complex I NDUFA10 subunit family
|
PTM: Phosphorylation at Ser-250 by PINK1 is required for the binding and/or reduction of the complex I substrate ubiquinone. {ECO:0000250|UniProtKB:Q99LC3}.
|
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305|PubMed:12611891}.
| null | null | null | null | null |
FUNCTION: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
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Homo sapiens (Human)
|
O95302
|
FKBP9_HUMAN
|
MAFRGWRPPPPPLLLLLLWVTGQAAPVAGLGSDAELQIERRFVPDECPRTVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDIWNSEDQVQIHTYFKPPSCPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLVFDVALLDLHNPKDSISIENKVVPENCERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDEGLLGVCIGEKRRIVVPPHLGYGEEGRGNIPGSAVLVFDIHVIDFHNPSDSISITSHYKPPDCSVLSKKGDYLKYHYNASLLDGTLLDSTWNLGKTYNIVLGSGQVVLGMDMGLREMCVGEKRTVIIPPHLGYGEAGVDGEVPGSAVLVFDIELLELVAGLPEGYMFIWNGEVSPNLFEEIDKDGNGEVLLEEFSEYIHAQVASGKGKLAPGFDAELIVKNMFTNQDRNGDGKVTAEEFKLKDQEAKHDEL
|
5.2.1.8
| null |
protein folding [GO:0006457]
|
endoplasmic reticulum [GO:0005783]
|
calcium ion binding [GO:0005509]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]
|
PF00254;
|
3.10.50.40;1.10.238.10;
| null |
PTM: Phosphorylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138}.
|
CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8;
| null | null | null | null |
FUNCTION: PPIases accelerate the folding of proteins during protein synthesis.
|
Homo sapiens (Human)
|
O95319
|
CELF2_HUMAN
|
MRCPKSAVTMRNEELLLSNGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGMAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGPEGANLFIYHLPQEFGDQDILQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSAQAAIQAMNGFQIGMKRLKVQLKRSKNDSKPY
| null | null |
mRNA splice site recognition [GO:0006376]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of heart contraction [GO:0008016]; RNA processing [GO:0006396]
|
cytoplasm [GO:0005737]; Flemming body [GO:0090543]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]
|
mRNA 3'-UTR binding [GO:0003730]; pre-mRNA binding [GO:0036002]; RNA binding [GO:0003723]
|
PF00076;
|
3.30.70.330;
|
CELF/BRUNOL family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33131106}. Cytoplasm {ECO:0000250|UniProtKB:Q7T2T1, ECO:0000250|UniProtKB:Q9Z0H4}. Note=Accumulates in the cytoplasm after ionizing radiation (By similarity). Colocalizes with APOBEC1 and A1CF. RNA-binding activity is detected in both nuclear and cytoplasmic compartments. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: RNA-binding protein implicated in the regulation of several post-transcriptional events. Involved in pre-mRNA alternative splicing, mRNA translation and stability. Mediates exon inclusion and/or exclusion in pre-mRNA that are subject to tissue-specific and developmentally regulated alternative splicing. Specifically activates exon 5 inclusion of TNNT2 in embryonic, but not adult, skeletal muscle. Activates TNNT2 exon 5 inclusion by antagonizing the repressive effect of PTB. Acts both as an activator and as a repressor of a pair of coregulated exons: promotes inclusion of the smooth muscle (SM) exon but exclusion of the non-muscle (NM) exon in actinin pre-mRNAs. Promotes inclusion of exonS 21 and exclusion of exon 5 of the NMDA receptor R1 pre-mRNA. Involved in the apoB RNA editing activity. Increases COX2 mRNA stability and inhibits COX2 mRNA translation in epithelial cells after radiation injury (By similarity). Modulates the cellular apoptosis program by regulating COX2-mediated prostaglandin E2 (PGE2) expression (By similarity). Binds to (CUG)n triplet repeats in the 3'-UTR of transcripts such as DMPK. Binds to the muscle-specific splicing enhancer (MSE) intronic sites flanking the TNNT2 alternative exon 5. Binds preferentially to UG-rich sequences, in particular UG repeat and UGUU motifs. Binds to apoB mRNA, specifically to AU-rich sequences located immediately upstream of the edited cytidine. Binds AU-rich sequences in the 3'-UTR of COX2 mRNA (By similarity). Binds to an intronic RNA element responsible for the silencing of exon 21 splicing (By similarity). Binds to (CUG)n repeats (By similarity). May be a specific regulator of miRNA biogenesis. Binds to primary microRNA pri-MIR140 and, with CELF1, negatively regulates the processing to mature miRNA (PubMed:28431233). {ECO:0000250|UniProtKB:Q9Z0H4, ECO:0000269|PubMed:11158314, ECO:0000269|PubMed:11577082, ECO:0000269|PubMed:11931771, ECO:0000269|PubMed:12649496, ECO:0000269|PubMed:14973222, ECO:0000269|PubMed:15657417, ECO:0000269|PubMed:15894795, ECO:0000269|PubMed:28431233}.
|
Homo sapiens (Human)
|
O95340
|
PAPS2_HUMAN
|
MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVLPVSAEDKTRLEGCSKFVLAHGGRRVAILRDAEFYEHRKEERCSRVWGTTCTKHPHIKMVMESGDWLVGGDLQVLEKIRWNDGLDQYRLTPLELKQKCKEMNADAVFAFQLRNPVHNGHALLMQDTRRRLLERGYKHPVLLLHPLGGWTKDDDVPLDWRMKQHAAVLEEGVLDPKSTIVAIFPSPMLYAGPTEVQWHCRSRMIAGANFYIVGRDPAGMPHPETKKDLYEPTHGGKVLSMAPGLTSVEIIPFRVAAYNKAKKAMDFYDPARHNEFDFISGTRMRKLAREGENPPDGFMAPKAWKVLTDYYRSLEKN
|
2.7.1.25; 2.7.7.4
| null |
3'-phosphoadenosine 5'-phosphosulfate biosynthetic process [GO:0050428]; blood coagulation [GO:0007596]; bone development [GO:0060348]; hormone metabolic process [GO:0042445]; phosphorylation [GO:0016310]; sulfate assimilation [GO:0000103]
|
cytosol [GO:0005829]
|
adenylylsulfate kinase activity [GO:0004020]; ATP binding [GO:0005524]; nucleotidyltransferase activity [GO:0016779]; sulfate adenylyltransferase (ATP) activity [GO:0004781]
|
PF01583;PF01747;PF14306;
|
3.40.50.620;3.40.50.300;3.10.400.10;
|
APS kinase family; Sulfate adenylyltransferase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate; Xref=Rhea:RHEA:18133, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58243; EC=2.7.7.4; Evidence={ECO:0000305|PubMed:11773860, ECO:0000305|PubMed:19474428, ECO:0000305|PubMed:23824674, ECO:0000305|PubMed:25594860}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18134; Evidence={ECO:0000305|PubMed:19474428}; CATALYTIC ACTIVITY: Reaction=adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+); Xref=Rhea:RHEA:24152, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339, ChEBI:CHEBI:456216; EC=2.7.1.25; Evidence={ECO:0000305|PubMed:11773860, ECO:0000305|PubMed:19474428, ECO:0000305|PubMed:23824674}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24153; Evidence={ECO:0000305|PubMed:19474428};
| null |
PATHWAY: Sulfur metabolism; sulfate assimilation. {ECO:0000269|PubMed:11773860, ECO:0000269|PubMed:19474428, ECO:0000269|PubMed:23824674, ECO:0000269|PubMed:25594860}.
| null | null |
FUNCTION: Bifunctional enzyme with both ATP sulfurylase and APS kinase activity, which mediates two steps in the sulfate activation pathway. The first step is the transfer of a sulfate group to ATP to yield adenosine 5'-phosphosulfate (APS), and the second step is the transfer of a phosphate group from ATP to APS yielding 3'-phosphoadenylylsulfate/PAPS, the activated sulfate donor used by sulfotransferases (PubMed:11773860, PubMed:19474428, PubMed:23824674, PubMed:25594860). In mammals, PAPS is the sole source of sulfate while APS appears to only be an intermediate in the sulfate-activation pathway (PubMed:11773860, PubMed:19474428, PubMed:23824674, PubMed:25594860). Plays indirectly an important role in skeletogenesis during postnatal growth (PubMed:9771708). {ECO:0000269|PubMed:11773860, ECO:0000269|PubMed:19474428, ECO:0000269|PubMed:23824674, ECO:0000269|PubMed:25594860, ECO:0000269|PubMed:9771708}.
|
Homo sapiens (Human)
|
O95342
|
ABCBB_HUMAN
|
MSDSVILRSIKKFGEENDGFESDKSYNNDKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIWLMFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQIPGKACVNNTIVWTNSSLNQNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDEGEYTPGTLVQIFLSVIVGALNLGNASPCLEAFATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQALNEEDIKDATEDDMLARTFSRGSYQDSLRASIRQRSKSQLSYLVHEPPLAVVDHKSTYEEDRKDKDIPVQEEVEPAPVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPISVYNTAGEKWDNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTGSPIS
|
7.6.2.-
| null |
bile acid and bile salt transport [GO:0015721]; bile acid biosynthetic process [GO:0006699]; bile acid metabolic process [GO:0008206]; bile acid signaling pathway [GO:0038183]; canalicular bile acid transport [GO:0015722]; cholesterol homeostasis [GO:0042632]; fatty acid metabolic process [GO:0006631]; lipid homeostasis [GO:0055088]; phospholipid homeostasis [GO:0055091]; positive regulation of bile acid secretion [GO:0120189]; protein ubiquitination [GO:0016567]; regulation of bile acid metabolic process [GO:1904251]; regulation of fatty acid beta-oxidation [GO:0031998]; response to estrogen [GO:0043627]; response to ethanol [GO:0045471]; response to organic cyclic compound [GO:0014070]; response to oxidative stress [GO:0006979]; transmembrane transport [GO:0055085]; xenobiotic export from cell [GO:0046618]; xenobiotic metabolic process [GO:0006805]; xenobiotic transmembrane transport [GO:0006855]
|
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; intercellular canaliculus [GO:0046581]; intracellular canaliculus [GO:0046691]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]
|
ABC-type bile acid transporter activity [GO:0015432]; ABC-type oligopeptide transporter activity [GO:0015421]; ABC-type xenobiotic transporter activity [GO:0008559]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; bile acid transmembrane transporter activity [GO:0015125]; canalicular bile acid transmembrane transporter activity [GO:0015126]; carbohydrate transmembrane transporter activity [GO:0015144]
|
PF00664;PF00005;
|
1.20.1560.10;3.40.50.300;
|
ABC transporter superfamily, ABCB family, Multidrug resistance exporter (TC 3.A.1.201) subfamily
|
PTM: N-glycosylated. {ECO:0000269|PubMed:15791618, ECO:0000269|PubMed:18829893}.; PTM: Ubiquitinated; short-chain ubiquitination regulates cell-Surface expression of ABCB11. {ECO:0000269|PubMed:18829893}.
|
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:15791618, ECO:0000269|PubMed:22262466}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:O70127}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O70127}. Endosome {ECO:0000250|UniProtKB:O70127}. Cell membrane {ECO:0000269|PubMed:20010382, ECO:0000269|PubMed:22262466, ECO:0000269|PubMed:29507376, ECO:0000269|PubMed:30431138}; Multi-pass membrane protein {ECO:0000255}. Note=Internalized at the canalicular membrane through interaction with the adapter protein complex 2 (AP-2) (PubMed:22262466). At steady state, localizes in the canalicular membrane but is also present in recycling endosomes. ABCB11 constantly and rapidly exchanges between the two sites through tubulo-vesicles carriers that move along microtubules. Microtubule-dependent trafficking of ABCB11 is enhanced by taurocholate and cAMP and regulated by STK11 through a PKA-mediated pathway. Trafficking of newly synthesized ABCB11 through endosomal compartment to the bile canalicular membrane is accelerated by cAMP but not by taurocholate (By similarity). Cell membrane expression is up-regulated by short- and medium-chain fatty acids (PubMed:20398791). {ECO:0000250|UniProtKB:O70127, ECO:0000269|PubMed:20398791, ECO:0000269|PubMed:22262466}.
|
CATALYTIC ACTIVITY: Reaction=ATP + cholate(in) + H2O = ADP + cholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50048, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29747, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50049; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurocholate(in) = ADP + H(+) + phosphate + taurocholate(out); Xref=Rhea:RHEA:50052, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36257, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15791618, ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:18985798, ECO:0000269|PubMed:19228692, ECO:0000269|PubMed:20010382, ECO:0000269|PubMed:20398791, ECO:0000269|PubMed:22262466, ECO:0000269|PubMed:24711118, ECO:0000269|PubMed:29507376, ECO:0000269|PubMed:32203132}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50053; Evidence={ECO:0000269|PubMed:15791618, ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:18985798, ECO:0000269|PubMed:19228692, ECO:0000269|PubMed:20010382, ECO:0000269|PubMed:20398791, ECO:0000269|PubMed:22262466, ECO:0000269|PubMed:24711118, ECO:0000269|PubMed:29507376, ECO:0000305|PubMed:32203132}; CATALYTIC ACTIVITY: Reaction=ATP + glycocholate(in) + H2O = ADP + glycocholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50056, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29746, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15791618, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:32203132}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50057; Evidence={ECO:0000269|PubMed:15791618, ECO:0000269|PubMed:16332456, ECO:0000305|PubMed:32203132}; CATALYTIC ACTIVITY: Reaction=ATP + glycochenodeoxycholate(in) + H2O = ADP + glycochenodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50060, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36252, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50061; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurochenodeoxycholate(in) = ADP + H(+) + phosphate + taurochenodeoxycholate(out); Xref=Rhea:RHEA:50064, ChEBI:CHEBI:9407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50065; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + glycoursodeoxycholate(in) + H2O = ADP + glycoursodeoxycholate(out) + H(+) + phosphate; Xref=Rhea:RHEA:50068, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:132030, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50069; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + tauroursodeoxycholate(in) = ADP + H(+) + phosphate + tauroursodeoxycholate(out); Xref=Rhea:RHEA:50072, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:132028, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:32203132}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50073; Evidence={ECO:0000269|PubMed:16332456, ECO:0000305|PubMed:32203132}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurodeoxycholate(in) = ADP + H(+) + phosphate + taurodeoxycholate(out); Xref=Rhea:RHEA:50080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36261, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50081; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + taurolithocholate 3-sulfate(in) = ADP + H(+) + phosphate + taurolithocholate 3-sulfate(out); Xref=Rhea:RHEA:50084, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58301, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:16332456}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:50085; Evidence={ECO:0000269|PubMed:16332456}; CATALYTIC ACTIVITY: Reaction=ATP + H2O + pravastatin(in) = ADP + H(+) + phosphate + pravastatin(out); Xref=Rhea:RHEA:63908, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:63660, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:15901796}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63909; Evidence={ECO:0000305|PubMed:15901796};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30.4 uM for taurocholate {ECO:0000269|PubMed:17264802}; KM=6.2 uM for taurocholate {ECO:0000269|PubMed:16332456}; KM=21.7 uM for glycocholate {ECO:0000269|PubMed:16332456}; KM=6.6 uM for taurochenodeoxycholate {ECO:0000269|PubMed:16332456}; KM=7.5 uM for glycochenodeoxycholate {ECO:0000269|PubMed:16332456}; KM=9.5 uM for taurolithocholate sulfate {ECO:0000269|PubMed:16332456}; KM=4.61 uM for taurocholate {ECO:0000269|PubMed:15791618}; KM=4.64 uM for taurocholate {ECO:0000269|PubMed:15901796}; KM=124 uM for pravastatin {ECO:0000269|PubMed:15901796}; KM=19.9 uM for taurocholate {ECO:0000269|PubMed:18985798}; Vmax=232 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:17264802}; Vmax=2510 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:16332456}; Vmax=2310 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:15791618}; Vmax=4290 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:15901796}; Vmax=1220 pmol/min/mg enzyme for pravastatin transport {ECO:0000269|PubMed:15901796}; Vmax=98.5 pmol/min/mg enzyme for taurocholate transport {ECO:0000269|PubMed:18985798};
| null | null | null |
FUNCTION: Catalyzes the transport of the major hydrophobic bile salts, such as taurine and glycine-conjugated cholic acid across the canalicular membrane of hepatocytes in an ATP-dependent manner, therefore participates in hepatic bile acid homeostasis and consequently to lipid homeostasis through regulation of biliary lipid secretion in a bile salts dependent manner (PubMed:15791618, PubMed:16332456, PubMed:18985798, PubMed:19228692, PubMed:20010382, PubMed:20398791, PubMed:22262466, PubMed:24711118, PubMed:29507376, PubMed:32203132). Transports taurine-conjugated bile salts more rapidly than glycine-conjugated bile salts (PubMed:16332456). Also transports non-bile acid compounds, such as pravastatin and fexofenadine in an ATP-dependent manner and may be involved in their biliary excretion (PubMed:15901796, PubMed:18245269). {ECO:0000269|PubMed:15791618, ECO:0000269|PubMed:15901796, ECO:0000269|PubMed:16332456, ECO:0000269|PubMed:18245269, ECO:0000269|PubMed:18985798, ECO:0000269|PubMed:19228692, ECO:0000269|PubMed:20010382, ECO:0000269|PubMed:20398791, ECO:0000269|PubMed:22262466, ECO:0000269|PubMed:24711118, ECO:0000269|PubMed:29507376, ECO:0000269|PubMed:32203132}.
|
Homo sapiens (Human)
|
O95343
|
SIX3_HUMAN
|
MVFRSPLDLYSSHFLLPNFADSHHRSILLASSGGGNGAGGGGGAGGGSGGGNGAGGGGAGGAGGGGGGGSRAPPEELSMFQLPTLNFSPEQVASVCETLEETGDIERLGRFLWSLPVAPGACEAINKHESILRARAVVAFHTGNFRDLYHILENHKFTKESHGKLQAMWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHQAIGPSGMRSLAEPGCPTHGSAESPSTAASPTTSVSSLTERADTGTSILSVTSSDSECDV
| null | null |
apoptotic process involved in development [GO:1902742]; brain development [GO:0007420]; cell proliferation in forebrain [GO:0021846]; epithelial cell maturation [GO:0002070]; eye development [GO:0001654]; forebrain dorsal/ventral pattern formation [GO:0021798]; lens development in camera-type eye [GO:0002088]; lens fiber cell apoptotic process [GO:1990086]; lens fiber cell differentiation [GO:0070306]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of neuron differentiation [GO:0045665]; neuroblast differentiation [GO:0014016]; neuroblast migration [GO:0097402]; optic vesicle morphogenesis [GO:0003404]; pituitary gland development [GO:0021983]; proximal/distal axis specification [GO:0009946]; regulation of cell cycle phase transition [GO:1901987]; regulation of cell population proliferation [GO:0042127]; regulation of neural precursor cell proliferation [GO:2000177]; regulation of neural retina development [GO:0061074]; regulation of neuroblast proliferation [GO:1902692]; regulation of transcription by RNA polymerase II [GO:0006357]; telencephalon development [GO:0021537]; telencephalon regionalization [GO:0021978]; visual perception [GO:0007601]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
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DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]; signaling receptor binding [GO:0005102]; transcription corepressor binding [GO:0001222]
|
PF00046;PF16878;
|
1.10.10.60;
|
SIX/Sine oculis homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q62233, ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-posterior patterning of the diencephalon and formation of the rostral diencephalon. Acts as a direct upstream activator of SHH expression in the rostral diencephalon ventral midline and that in turn SHH maintains its expression. In addition, Six3 activity is required for the formation of the telencephalon. During postnatal stages of brain development is necessary for ependymal cell maturation by promoting the maturation of radial glia into ependymal cells through regulation of neuroblast proliferation and migration. Acts on the proliferation and differentiation of neural progenitor cells through activating transcription of CCND1 and CCND2. During early lens formation plays a role in lens induction and specification by activating directly PAX6 in the presumptive lens ectoderm. In turn PAX6 activates SIX3 resulting in activation of PDGFRA and CCND1 promoting cell proliferation. Also is required for the neuroretina development by directly suppressing WNT8B expression in the anterior neural plate territory. Its action during retina development and lens morphogenesis is TLE5 and TLE4-dependent manner. Furthermore, during eye development regulates several genes expression. Before and during early lens development represses the CRYGF promoter by binding a SIX repressor element. Directly activates RHO transcription, or cooperates with CRX or NRL. Six3 functions also in the formation of the proximodistal axis of the optic cup, and promotes the formation of optic vesicles-like structures. During pituitary development, acts in parallel or alternatively with HESX1 to control cell proliferation through Wnt/beta-catenin pathway (By similarity). Plays a role in eye development by suppressing WNT1 expression and in dorsal-ventral patterning by repressing BMP signaling pathway. {ECO:0000250|UniProtKB:Q62233, ECO:0000269|PubMed:18791198}.
|
Homo sapiens (Human)
|
O95347
|
SMC2_HUMAN
|
MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGKKLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFVDGVSTVARFTQCQNGKISKEAKSKAKPPKGAHVEV
| null | null |
cell division [GO:0051301]; kinetochore organization [GO:0051383]; meiotic chromosome condensation [GO:0010032]; meiotic chromosome segregation [GO:0045132]; mitotic chromosome condensation [GO:0007076]; positive regulation of chromosome condensation [GO:1905821]; positive regulation of chromosome segregation [GO:0051984]; positive regulation of chromosome separation [GO:1905820]
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chromatin [GO:0000785]; condensed chromosome [GO:0000793]; condensed nuclear chromosome [GO:0000794]; condensin complex [GO:0000796]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
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ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; single-stranded DNA binding [GO:0003697]
|
PF06470;PF02463;
|
1.20.1060.20;3.30.70.1620;3.40.50.300;
|
SMC family, SMC2 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10958694}. Cytoplasm {ECO:0000269|PubMed:10958694}. Chromosome {ECO:0000269|PubMed:10958694}. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, the regulatory subunits of the complex are phosphorylated by CDC2, leading to condensin's association with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
| null | null | null | null | null |
FUNCTION: Central component of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.
|
Homo sapiens (Human)
|
O95352
|
ATG7_HUMAN
|
MAAATGDPGLSKLQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDMSAPTPARCCPAIGTLYNTNTLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGLDQRFSLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVSLLKHYSDFFQGQRTKITIGVYDPCNLAQYPGWPLRNFLVLAAHRWSSSFQSVEVVCFRDRTMQGARDVAHSIIFEVKLPEMAFSPDCPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAESSVDLNLKLMCWRLVPTLDLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLGGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVNFSSVTLEQARRDVEQLEQLIESHDVVFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPKQQGAGDLCPNHPVASADLLGSSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAVIAGALAVELMVSVLQHPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEREGFNFLAKVFNSSHSFLEDLTGLTLLHQETQAAEIWDMSDDETI
| null | null |
autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cellular response to hyperoxia [GO:0071455]; cellular response to nitrogen starvation [GO:0006995]; cellular response to starvation [GO:0009267]; defense response to virus [GO:0051607]; macroautophagy [GO:0016236]; mitophagy [GO:0000423]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of apoptotic process [GO:0043065]; positive regulation of protein catabolic process [GO:0045732]; positive regulation of protein modification process [GO:0031401]; protein lipidation [GO:0006497]; protein modification by small protein conjugation [GO:0032446]; protein transport [GO:0015031]; regulation of circadian rhythm [GO:0042752]; rhythmic process [GO:0048511]
|
axoneme [GO:0005930]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; phagophore assembly site [GO:0000407]; secretory granule lumen [GO:0034774]
|
Atg12 activating enzyme activity [GO:0019778]; Atg8 activating enzyme activity [GO:0019779]; protein homodimerization activity [GO:0042803]
|
PF16420;PF00899;
|
3.40.50.720;3.40.140.100;3.40.140.70;
|
ATG7 family
|
PTM: Acetylated by EP300. {ECO:0000269|PubMed:19124466}.; PTM: Polyubiquitinated on Lys-45 via 'Lys-63'-linked ubiquitin by TRIM32; this modification positiely regulates ATG8 and ATG12 activating enzyme activity leading to initiation of autophagy under metabolic stress. {ECO:0000269|PubMed:37943659}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal structure {ECO:0000250}. Note=Localizes also to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: E1-like activating enzyme involved in the 2 ubiquitin-like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 as well as the ATG8 family proteins for their conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Required for autophagic death induced by caspase-8 inhibition. Facilitates LC3-I lipidation with phosphatidylethanolamine to form LC3-II which is found on autophagosomal membranes (PubMed:34161705). Required for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Modulates p53/TP53 activity to regulate cell cycle and survival during metabolic stress. Also plays a key role in the maintenance of axonal homeostasis, the prevention of axonal degeneration, the maintenance of hematopoietic stem cells, the formation of Paneth cell granules, as well as in adipose differentiation. Plays a role in regulating the liver clock and glucose metabolism by mediating the autophagic degradation of CRY1 (clock repressor) in a time-dependent manner (By similarity). {ECO:0000250|UniProtKB:Q9D906, ECO:0000269|PubMed:11096062, ECO:0000269|PubMed:16303767, ECO:0000269|PubMed:22170151, ECO:0000269|PubMed:34161705}.
|
Homo sapiens (Human)
|
O95359
|
TACC2_HUMAN
|
MGNENSTSDNQRTLSAQTPRSAQPPGNSQNIKRKQQDTPGSPDHRDASSIGSVGLGGFCTASESSASLDPCLVSPEVTEPRKDPQGARGPEGSLLPSPPPSQEREHPSSSMPFAECPPEGCLASPAAAPEDGPQTQSPRREPAPNAPGDIAAAFPAERDSSTPYQEIAAVPSAGRERQPKEEGQKSSFSFSSGIDQSPGMSPVPLREPMKAPLCGEGDQPGGFESQEKEAAGGFPPAESRQGVASVQVTPEAPAAAQQGTESSAVLEKSPLKPMAPIPQDPAPRASDRERGQGEAPPQYLTDDLEFLRACHLPRSNSGAAPEAEVNAASQESCQQPVGAYLPHAELPWGLPSPALVPEAGGSGKEALDTIDVQGHPQTGMRGTKPNQVVCVAAGGQPEGGLPVSPEPSLLTPTEEAHPASSLASFPAAQIPIAVEEPGSSSRESVSKAGMPVSADAAKEVVDAGLVGLERQVSDLGSKGEHPEGDPGEVPAPSPQERGEHLNTEQSHEVQPGVPPPPLPKEQSHEVQPGAPPPPLPKAPSESARGPPGPTDGAKVHEDSTSPAVAKEGSRSPGDSPGGKEEAPEPPDGGDPGNLQGEDSQAFSSKRDPEVGKDELSKPSSDAESRDHPSSHSAQPPRKGGAGHTDGPHSQTAEADASGLPHKLGEEDPVLPPVPDGAGEPTVPEGAIWEGSGLQPKCPDTLQSREGLGRMESFLTLESEKSDFPPTPVAEVAPKAQEGESTLEIRKMGSCDGEGLLTSPDQPRGPACDASRQEFHAGVPHPPQGENLAADLGLTALILDQDQQGIPSCPGEGWIRGAASEWPLLSSEKHLQPSQAQPETSIFDVLKEQAQPPENGKETSPSHPGFKDQGADSSQIHVPVEPQEDNNLPTHGGQEQALGSELQSQLPKGTLSDTPTSSPTDMVWESSLTEESELSAPTRQKLPALGEKRPEGACGDGQSSRVSPPAADVLKDFSLAGNFSRKETCCTGQGPNKSQQALADALEEGSQHEEACQRHPGASEAADGCSPLWGLSKREMASGNTGEAPPCQPDSVALLDAVPCLPALAPASPGVTPTQDAPETEACDETQEGRQQPVPAPQQKMECWATSDAESPKLLASFPSAGEQGGEAGAAETGGSAGAGDPGKQQAPEKPGEATLSCGLLQTEHCLTSGEEASTSALRESCQAEHPMASCQDALLPARELGGIPRSTMDFSTHQAVPDPKELLLSGPPEVAAPDTPYLHVDSAAQRGAEDSGVKAVSSADPRAPGESPCPVGEPPLALENAASLKLFAGSLAPLLQPGAAGGEIPAVQASSGSPKARTTEGPVDSMPCLDRMPLLAKGKQATGEEKAATAPGAGAKASGEGMAGDAAGETEGSMERMGEPSQDPKQGTSGGVDTSSEQIATLTGFPDFREHIAKIFEKPVLGALATPGEKAGAGRSAVGKDLTRPLGPEKLLDGPPGVDVTLLPAPPARLQVEKKQQLAGEAEISHLALQDPASDKLLGPAGLTWERNLPGAGVGKEMAGVPPTLREDERPEGPGAAWPGLEGQAYSQLERSRQELASGLPSPAATQELPVERAAAFQVAPHSHGEEAVAQDRIPSGKQHQETSACDSPHGEDGPGDFAHTGVPGHVPRSTCAPSPQREVLTVPEANSEPWTLDTLGGERRPGVTAGILEMRNALGNQSTPAPPTGEVADTPLEPGKVAGAAGEAEGDITLSTAETQACASGDLPEAGTTRTFSVVAGDLVLPGSCQDPACSDKAPGMEGTAALHGDSPARPQQAKEQPGPERPIPAGDGKVCVSSPPEPDETHDPKLQHLAPEELHTDRESPRPGPSMLPSVPKKDAPRVMDKVTSDETRGAEGTESSPVADDIIQPAAPADLESPTLAASSYHGDVVGQVSTDLIAQSISPAAAHAGLPPSAAEHIVSPSAPAGDRVEASTPSCPDPAKDLSRSSDSEEAFETPESTTPVKAPPAPPPPPPEVIPEPEVSTQPPPEEPGCGSETVPVPDGPRSDSVEGSPFRPPSHSFSAVFDEDKPIASSGTYNLDFDNIELVDTFQTLEPRASDAKNQEGKVNTRRKSTDSVPISKSTLSRSLSLQASDFDGASSSGNPEAVALAPDAYSTGSSSASSTLKRTKKPRPPSLKKKQTTKKPTETPPVKETQQEPDEESLVPSGENLASETKTESAKTEGPSPALLEETPLEPAVGPKAACPLDSESAEGVVPPASGGGRVQNSPPVGRKTLPLTTAPEAGEVTPSDSGGQEDSPAKGLSVRLEFDYSEDKSSWDNQQENPPPTKKIGKKPVAKMPLRRPKMKKTPEKLDNTPASPPRSPAEPNDIPIAKGTYTFDIDKWDDPNFNPFSSTSKMQESPKLPQQSYNFDPDTCDESVDPFKTSSKTPSSPSKSPASFEIPASAMEANGVDGDGLNKPAKKKKTPLKTDTFRVKKSPKRSPLSDPPSQDPTPAATPETPPVISAVVHATDEEKLAVTNQKWTCMTVDLEADKQDYPQPSDLSTFVNETKFSSPTEELDYRNSYEIEYMEKIGSSLPQDDDAPKKQALYLMFDTSQESPVKSSPVRMSESPTPCSGSSFEETEALVNTAAKNQHPVPRGLAPNQESHLQVPEKSSQKELEAMGLGTPSEAIEITAPEGSFASADALLSRLAHPVSLCGALDYLEPDLAEKNPPLFAQKLQEELEFAIMRIEALKLARQIALASRSHQDAKREAAHPTDVSISKTALYSRIGTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKMGKS
| null | null |
cell population proliferation [GO:0008283]; cerebral cortex development [GO:0021987]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle organization [GO:0007052]
|
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
nuclear receptor binding [GO:0016922]
|
PF05010;
|
1.20.5.1700;
|
TACC family
|
PTM: Phosphorylated by TTK; which is required for localization in centrosome. {ECO:0000269|PubMed:15304323}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10749935}. Nucleus {ECO:0000269|PubMed:10749935, ECO:0000269|PubMed:14767476}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:15304323}.
| null | null | null | null | null |
FUNCTION: Plays a role in the microtubule-dependent coupling of the nucleus and the centrosome. Involved in the processes that regulate centrosome-mediated interkinetic nuclear migration (INM) of neural progenitors (By similarity). May play a role in organizing centrosomal microtubules. May act as a tumor suppressor protein. May represent a tumor progression marker. {ECO:0000250, ECO:0000269|PubMed:10749935}.
|
Homo sapiens (Human)
|
O95361
|
TRI16_HUMAN
|
MAELDLMAPGPLPRATAQPPAPLSPDSGSPSPDSGSASPVEEEDVGSSEKLGRETEEQDSDSAEQGDPAGEGKEVLCDFCLDDTRRVKAVKSCLTCMVNYCEEHLQPHQVNIKLQSHLLTEPVKDHNWRYCPAHHSPLSAFCCPDQQCICQDCCQEHSGHTIVSLDAARRDKEAELQCTQLDLERKLKLNENAISRLQANQKSVLVSVSEVKAVAEMQFGELLAAVRKAQANVMLFLEEKEQAALSQANGIKAHLEYRSAEMEKSKQELERMAAISNTVQFLEEYCKFKNTEDITFPSVYVGLKDKLSGIRKVITESTVHLIQLLENYKKKLQEFSKEEEYDIRTQVSAVVQRKYWTSKPEPSTREQFLQYAYDITFDPDTAHKYLRLQEENRKVTNTTPWEHPYPDLPSRFLHWRQVLSQQSLYLHRYYFEVEIFGAGTYVGLTCKGIDRKGEERNSCISGNNFSWSLQWNGKEFTAWYSDMETPLKAGPFRRLGVYIDFPGGILSFYGVEYDTMTLVHKFACKFSEPVYAAFWLSKKENAIRIVDLGEEPEKPAPSLVGTAP
|
2.3.2.27
| null |
positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of interleukin-1 beta production [GO:0032731]; positive regulation of keratinocyte differentiation [GO:0045618]; positive regulation of retinoic acid receptor signaling pathway [GO:0048386]; response to growth hormone [GO:0060416]; response to organophosphorus [GO:0046683]; response to retinoic acid [GO:0032526]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; PML body [GO:0016605]
|
DNA binding [GO:0003677]; interleukin-1 binding [GO:0019966]; NACHT domain binding [GO:0032089]; transferase activity [GO:0016740]; zinc ion binding [GO:0008270]
|
PF13765;PF00622;PF00643;
|
2.60.120.920;4.10.830.40;3.30.160.60;
|
TRIM/RBCC family
|
PTM: Phosphorylated by ULK1. {ECO:0000269|PubMed:27693506}.; PTM: Auto-ubiquitinates via its B-Boxes. {ECO:0000269|PubMed:22629402}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27693506}.
|
CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000269|PubMed:22629402};
| null | null | null | null |
FUNCTION: E3 ubiquitin ligase that plays an essential role in the organization of autophagic response and ubiquitination upon lysosomal and phagosomal damages. Plays a role in the stress-induced biogenesis and degradation of protein aggresomes by regulating the p62-KEAP1-NRF2 signaling and particularly by modulating the ubiquitination levels and thus stability of NRF2. Acts as a scaffold protein and facilitates autophagic degradation of protein aggregates by interacting with p62/SQSTM, ATG16L1 and LC3B/MAP1LC3B. In turn, protects the cell against oxidative stress-induced cell death as a consequence of endomembrane damage. {ECO:0000269|PubMed:22629402, ECO:0000269|PubMed:27693506, ECO:0000269|PubMed:30143514}.
|
Homo sapiens (Human)
|
O95363
|
SYFM_HUMAN
|
MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQDDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVEFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLAMILYDIPDIRLFWCEDERFLKQFCVSNINQKVKFQPLSKYPAVINDISFWLPSENYAENDFYDLVRTIGGDLVEKVDLIDKFVHPKTHKTSHCYRITYRHMERTLSQREVRHIHQALQEAAVQLLGVEGRF
|
6.1.1.20
| null |
phenylalanyl-tRNA aminoacylation [GO:0006432]; tRNA aminoacylation for protein translation [GO:0006418]; tRNA processing [GO:0008033]
|
cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049]
|
PF03147;PF01409;
|
3.30.70.380;
|
Class-II aminoacyl-tRNA synthetase family
| null |
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q6AYQ3}. Mitochondrion {ECO:0000250|UniProtKB:Q6AYQ3}.
|
CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6.1.1.20; Evidence={ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.2 uM for L-phenylalanine {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}; KM=1900 uM for L-tyrosine {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}; KM=11.7 uM for DL-m-tyrosine {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}; KM=7.3 uM for L-phenylalanine {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}; KM=2.9 mM for ATP {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}; KM=1.2 uM for tRNA(Phe) {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}; Note=kcat is 2.8 min(-1), 2.0 min(-1) and 3.1 min(-1) with L-phenylalanine, L-tyrosine and m-tyrosine as substrate, respectively. Thus, the catalytic efficiency of the m-Tyr attachment is only 5-fold lower than that of the correct amino acid, while that of Tyr attachment is 1000-fold lower (PubMed:19549855). {ECO:0000269|PubMed:19549855};
| null | null | null |
FUNCTION: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation. To a lesser extent, also catalyzes direct attachment of m-Tyr (an oxidized version of Phe) to tRNA(Phe), thereby opening the way for delivery of the misacylated tRNA to the ribosome and incorporation of ROS-damaged amino acid into proteins. {ECO:0000269|PubMed:19549855, ECO:0000269|PubMed:22833457}.
|
Homo sapiens (Human)
|
O95365
|
ZBT7A_HUMAN
|
MAGGVDGPIGIPFPDHSSDILSGLNEQRTQGLLCDVVILVEGREFPTHRSVLAACSQYFKKLFTSGAVVDQQNVYEIDFVSAEALTALMDFAYTATLTVSTANVGDILSAARLLEIPAVSHVCADLLDRQILAADAGADAGQLDLVDQIDQRNLLRAKEYLEFFQSNPMNSLPPAAAAAAASFPWSAFGASDDDLDATKEAVAAAVAAVAAGDCNGLDFYGPGPPAERPPTGDGDEGDSNPGLWPERDEDAPTGGLFPPPVAPPAATQNGHYGRGGEEEAASLSEAAPEPGDSPGFLSGAAEGEDGDGPDVDGLAASTLLQQMMSSVGRAGAAAGDSDEESRADDKGVMDYYLKYFSGAHDGDVYPAWSQKVEKKIRAKAFQKCPICEKVIQGAGKLPRHIRTHTGEKPYECNICKVRFTRQDKLKVHMRKHTGEKPYLCQQCGAAFAHNYDLKNHMRVHTGLRPYQCDSCCKTFVRSDHLHRHLKKDGCNGVPSRRGRKPRVRGGAPDPSPGATATPGAPAQPSSPDARRNGQEKHFKDEDEDEDVASPDGLGRLNVAGAGGGGDSGGGPGAATDGNFTAGLA
| null | null |
B cell differentiation [GO:0030183]; chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; DNA-templated transcription [GO:0006351]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; erythrocyte maturation [GO:0043249]; fat cell differentiation [GO:0045444]; negative regulation of androgen receptor signaling pathway [GO:0060766]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of Notch signaling pathway [GO:0045746]; negative regulation of transcription by RNA polymerase II [GO:0000122]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of NF-kappaB transcription factor activity [GO:0051092]; protein localization to nucleus [GO:0034504]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; regulation of apoptotic process [GO:0042981]; regulation of DNA-binding transcription factor activity [GO:0051090]; regulation of glycolytic process [GO:0006110]; regulation of transcription by RNA polymerase II [GO:0006357]; regulation of transcription regulatory region DNA binding [GO:2000677]
|
cytoplasm [GO:0005737]; DNA-dependent protein kinase complex [GO:0070418]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone acetyltransferase binding [GO:0035035]; metal ion binding [GO:0046872]; nuclear androgen receptor binding [GO:0050681]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]; SMAD binding [GO:0046332]; transcription corepressor binding [GO:0001222]
|
PF00651;PF00096;
|
3.30.160.60;
| null |
PTM: Sumoylated. Undergoes sumoylation with SUMO1 that may regulate its transcriptional activity. {ECO:0000269|PubMed:17595526}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17595526, ECO:0000269|PubMed:24514149}. Note=Recruited to double-strand break sites of damaged DNA. {ECO:0000250|UniProtKB:O88939}.
| null | null | null | null | null |
FUNCTION: Transcription factor that represses the transcription of a wide range of genes involved in cell proliferation and differentiation (PubMed:14701838, PubMed:17595526, PubMed:20812024, PubMed:25514493, PubMed:26455326, PubMed:26816381). Directly and specifically binds to the consensus sequence 5'-[GA][CA]GACCCCCCCCC-3' and represses transcription both by regulating the organization of chromatin and through the direct recruitment of transcription factors to gene regulatory regions (PubMed:12004059, PubMed:17595526, PubMed:20812024, PubMed:25514493, PubMed:26816381). Negatively regulates SMAD4 transcriptional activity in the TGF-beta signaling pathway through these two mechanisms (PubMed:25514493). That is, recruits the chromatin regulator HDAC1 to the SMAD4-DNA complex and in parallel prevents the recruitment of the transcriptional activators CREBBP and EP300 (PubMed:25514493). Collaborates with transcription factors like RELA to modify the accessibility of gene transcription regulatory regions to secondary transcription factors (By similarity). Also directly interacts with transcription factors like SP1 to prevent their binding to DNA (PubMed:12004059). Functions as an androgen receptor/AR transcriptional corepressor by recruiting NCOR1 and NCOR2 to the androgen response elements/ARE on target genes (PubMed:20812024). Thereby, negatively regulates androgen receptor signaling and androgen-induced cell proliferation (PubMed:20812024). Involved in the switch between fetal and adult globin expression during erythroid cells maturation (PubMed:26816381). Through its interaction with the NuRD complex regulates chromatin at the fetal globin genes to repress their transcription (PubMed:26816381). Specifically represses the transcription of the tumor suppressor ARF isoform from the CDKN2A gene (By similarity). Efficiently abrogates E2F1-dependent CDKN2A transactivation (By similarity). Regulates chondrogenesis through the transcriptional repression of specific genes via a mechanism that also requires histone deacetylation (By similarity). Regulates cell proliferation through the transcriptional regulation of genes involved in glycolysis (PubMed:26455326). Involved in adipogenesis through the regulation of genes involved in adipocyte differentiation (PubMed:14701838). Plays a key role in the differentiation of lymphoid progenitors into B and T lineages (By similarity). Promotes differentiation towards the B lineage by inhibiting the T-cell instructive Notch signaling pathway through the specific transcriptional repression of Notch downstream target genes (By similarity). Also regulates osteoclast differentiation (By similarity). May also play a role, independently of its transcriptional activity, in double-strand break repair via classical non-homologous end joining/cNHEJ (By similarity). Recruited to double-strand break sites on damage DNA, interacts with the DNA-dependent protein kinase complex and directly regulates its stability and activity in DNA repair (By similarity). May also modulate the splicing activity of KHDRBS1 toward BCL2L1 in a mechanism which is histone deacetylase-dependent and thereby negatively regulates the pro-apoptotic effect of KHDRBS1 (PubMed:24514149). {ECO:0000250|UniProtKB:O88939, ECO:0000250|UniProtKB:Q9QZ48, ECO:0000269|PubMed:12004059, ECO:0000269|PubMed:14701838, ECO:0000269|PubMed:17595526, ECO:0000269|PubMed:20812024, ECO:0000269|PubMed:24514149, ECO:0000269|PubMed:25514493, ECO:0000269|PubMed:26455326, ECO:0000269|PubMed:26816381}.
|
Homo sapiens (Human)
|
O95372
|
LYPA2_HUMAN
|
MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAPRIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGGFSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAILQCHGELDPMVPVRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPPV
|
3.1.2.-; 3.1.2.22
| null |
acylglycerol catabolic process [GO:0046464]; axon guidance [GO:0007411]; fatty acid metabolic process [GO:0006631]; prostaglandin catabolic process [GO:1905344]; protein depalmitoylation [GO:0002084]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; Golgi stack [GO:0005795]; nucleoplasm [GO:0005654]
|
cadherin binding [GO:0045296]; carboxylic ester hydrolase activity [GO:0052689]; lysophospholipase activity [GO:0004622]; palmitoyl-(protein) hydrolase activity [GO:0008474]
|
PF02230;
|
3.40.50.1820;
|
AB hydrolase superfamily, AB hydrolase 2 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25301951}.
|
CATALYTIC ACTIVITY: Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, ChEBI:CHEBI:74151; EC=3.1.2.22; Evidence={ECO:0000269|PubMed:28826475}; CATALYTIC ACTIVITY: Reaction=H2O + prostaglandin E2 1-glyceryl ester = glycerol + H(+) + prostaglandin E2; Xref=Rhea:RHEA:48296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754, ChEBI:CHEBI:90230, ChEBI:CHEBI:606564; Evidence={ECO:0000269|PubMed:25301951}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48297; Evidence={ECO:0000305|PubMed:25301951}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:72998; Evidence={ECO:0000269|PubMed:25301951}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436; Evidence={ECO:0000305|PubMed:25301951}; CATALYTIC ACTIVITY: Reaction=1-octadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) + octadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40887, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:25629, ChEBI:CHEBI:73858; Evidence={ECO:0000269|PubMed:25301951}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40888; Evidence={ECO:0000305|PubMed:25301951}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phosphate + H2O = H(+) + hexadecanoate + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:49092, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:57597; Evidence={ECO:0000269|PubMed:25301951}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49093; Evidence={ECO:0000305|PubMed:25301951}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-sn-glycero-3-phospho-L-serine + H2O = H(+) + hexadecanoate + sn-glycero-3-phospho-L-serine; Xref=Rhea:RHEA:44552, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64765, ChEBI:CHEBI:75020; Evidence={ECO:0000269|PubMed:25301951}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44553; Evidence={ECO:0000305|PubMed:25301951};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=67 uM for prostaglandin D2-glycerol ester (PGD2-G) {ECO:0000269|PubMed:25301951}; KM=13 uM for prostaglandin E2-glycerol ester (PGE2-G) {ECO:0000269|PubMed:25301951}; KM=5 uM for prostaglandin F2-alpha-glycerol ester (PGF2-alpha-G) {ECO:0000269|PubMed:25301951}; KM=8.3 uM for Lyso-PC (C16:0) {ECO:0000269|PubMed:25301951}; KM=7.8 uM for Lyso-PC (C18:0) {ECO:0000269|PubMed:25301951}; KM=40.7 uM for Lyso-PC (C18:1) {ECO:0000269|PubMed:25301951}; KM=11.1 uM for Lyso-PA (C16:0) {ECO:0000269|PubMed:25301951}; KM=13.3 uM for Lyso-PS (C16:0) {ECO:0000269|PubMed:25301951}; KM=7.6 uM for 1-arachidonoylglycerol {ECO:0000269|PubMed:25301951};
| null | null | null |
FUNCTION: Acts as an acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins, GAP43, ZDHHC6 or HRAS (PubMed:21152083, PubMed:28826475). Deacylates GAP43 (PubMed:21152083). Mediates depalmitoylation of ZDHHC6 (PubMed:28826475). Has lysophospholipase activity (PubMed:25301951). Hydrolyzes prostaglandin glycerol esters (PG-Gs) in the following order prostaglandin D2-glycerol ester (PGD2-G) > prostaglandin E2 glycerol ester (PGE2-G) > prostaglandin F2-alpha-glycerol ester (PGF2-alpha-G) (PubMed:25301951). Hydrolyzes 1-arachidonoylglycerol but not 2-arachidonoylglycerol or arachidonoylethanolamide (PubMed:25301951). {ECO:0000269|PubMed:21152083, ECO:0000269|PubMed:25301951, ECO:0000269|PubMed:28826475}.
|
Homo sapiens (Human)
|
O95373
|
IPO7_HUMAN
|
MDPNTIIEALRGTMDPALREAAERQLNEAHKSLNFVSTLLQITMSEQLDLPVRQAGVIYLKNMITQYWPDRETAPGDISPYTIPEEDRHCIRENIVEAIIHSPELIRVQLTTCIHHIIKHDYPSRWTAIVDKIGFYLQSDNSACWLGILLCLYQLVKNYEYKKPEERSPLVAAMQHFLPVLKDRFIQLLSDQSDQSVLIQKQIFKIFYALVQYTLPLELINQQNLTEWIEILKTVVNRDVPNETLQVEEDDRPELPWWKCKKWALHILARLFERYGSPGNVSKEYNEFAEVFLKAFAVGVQQVLLKVLYQYKEKQYMAPRVLQQTLNYINQGVSHALTWKNLKPHIQGIIQDVIFPLMCYTDADEELWQEDPYEYIRMKFDVFEDFISPTTAAQTLLFTACSKRKEVLQKTMGFCYQILTEPNADPRKKDGALHMIGSLAEILLKKKIYKDQMEYMLQNHVFPLFSSELGYMRARACWVLHYFCEVKFKSDQNLQTALELTRRCLIDDREMPVKVEAAIALQVLISNQEKAKEYITPFIRPVMQALLHIIRETENDDLTNVIQKMICEYSEEVTPIAVEMTQHLAMTFNQVIQTGPDEEGSDDKAVTAMGILNTIDTLLSVVEDHKEITQQLEGICLQVIGTVLQQHVLEFYEEIFSLAHSLTCQQVSPQMWQLLPLVFEVFQQDGFDYFTDMMPLLHNYVTVDTDTLLSDTKYLEMIYSMCKKVLTGVAGEDAECHAAKLLEVIILQCKGRGIDQCIPLFVEAALERLTREVKTSELRTMCLQVAIAALYYNPHLLLNTLENLRFPNNVEPVTNHFITQWLNDVDCFLGLHDRKMCVLGLCALIDMEQIPQVLNQVSGQILPAFILLFNGLKRAYACHAEHENDSDDDDEAEDDDETEELGSDEDDIDEDGQEYLEILAKQAGEDGDDEDWEEDDAEETALEGYSTIIDDEDNPVDEYQIFKAIFQTIQNRNPVWYQALTHGLNEEQRKQLQDIATLADQRRAAHESKMIEKHGGYKFSAPVVPSSFNFGGPAPGMN
| null | null |
innate immune response [GO:0045087]; negative regulation of cyclin-dependent protein serine/threonine kinase activity [GO:0045736]; negative regulation of osteoblast differentiation [GO:0045668]; positive regulation of odontoblast differentiation [GO:1901331]; positive regulation of protein localization to nucleus [GO:1900182]; protein import into nucleus [GO:0006606]
|
cytosol [GO:0005829]; membrane [GO:0016020]; nuclear envelope [GO:0005635]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]
|
GTPase regulator activity [GO:0030695]; histone binding [GO:0042393]; SMAD binding [GO:0046332]; small GTPase binding [GO:0031267]
|
PF08506;PF03810;
|
1.25.10.10;
|
Importin beta family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9EPL8}. Nucleus {ECO:0000250|UniProtKB:Q9EPL8}. Note=Localizes to the nucleus in the presence of BMP4. {ECO:0000250|UniProtKB:Q9EPL8}.
| null | null | null | null | null |
FUNCTION: Functions in nuclear protein import, either by acting as autonomous nuclear transport receptor or as an adapter-like protein in association with the importin-beta subunit KPNB1. Acting autonomously, is thought to serve itself as receptor for nuclear localization signals (NLS) and to promote translocation of import substrates through the nuclear pore complex (NPC) by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Mediates autonomously the nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5 (PubMed:11682607). In association with KPNB1 mediates the nuclear import of H1 histone and the Ran-binding site of IPO7 is not required but synergizes with that of KPNB1 in importin/substrate complex dissociation. Promotes odontoblast differentiation via promoting nuclear translocation of DLX3, KLF4, SMAD2, thereby facilitating the transcription of target genes that play a role in odontoblast differentiation (By similarity). Facilitates BMP4-induced translocation of SMAD1 to the nucleus and recruitment to the MSX1 gene promoter, thereby promotes the expression of the odontogenic regulator MSX1 in dental mesenchymal cells (By similarity). Also promotes odontoblast differentiation by facilitating the nuclear translocation of HDAC6 and subsequent repression of RUNX2 expression (By similarity). Inhibits osteoblast differentiation by inhibiting nuclear translocation of RUNX2 and therefore inhibition of RUNX2 target gene transcription (By similarity). In vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. {ECO:0000250|UniProtKB:Q9EPL8, ECO:0000269|PubMed:10228156, ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:9687515}.; FUNCTION: (Microbial infection) Mediates the nuclear import of HIV-1 reverse transcription complex (RTC) integrase. Binds and mediates the nuclear import of HIV-1 Rev. {ECO:0000269|PubMed:12853482, ECO:0000269|PubMed:16704975}.
|
Homo sapiens (Human)
|
O95376
|
ARI2_HUMAN
|
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGVSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQEPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQAREALKKYLFYFERWENHNKSLQLEAQTYQRIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKCRYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAEQRRRTLLKDFHDT
|
2.3.2.31
| null |
developmental cell growth [GO:0048588]; hematopoietic stem cell proliferation [GO:0071425]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein K48-linked ubiquitination [GO:0070936]; protein K63-linked ubiquitination [GO:0070534]; protein polyubiquitination [GO:0000209]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
|
ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270]
|
PF19422;PF01485;
|
1.20.120.1750;2.20.25.20;3.30.40.10;
|
RBR family, Ariadne subfamily
|
PTM: Ubiquitinated. Ubiquitination promotes proteasomal degradation. {ECO:0000269|PubMed:16118314}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16118314}. Cytoplasm {ECO:0000269|PubMed:19340006}.
|
CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000269|PubMed:16118314, ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:19340006};
| null |
PATHWAY: Protein modification; protein ubiquitination.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (PubMed:16118314, PubMed:17646546, PubMed:19340006, PubMed:24076655). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity). The initial ubiquitin is then elongated (By similarity). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex (PubMed:24076655). Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination (PubMed:16118314, PubMed:17646546, PubMed:19340006). May play a role in myelopoiesis (PubMed:19340006). {ECO:0000250|UniProtKB:Q9Y4X5, ECO:0000269|PubMed:16118314, ECO:0000269|PubMed:17646546, ECO:0000269|PubMed:19340006, ECO:0000269|PubMed:24076655}.
|
Homo sapiens (Human)
|
O95377
|
CXB5_HUMAN
|
MNWSIFEGLLSGVNKYSTAFGRIWLSLVFIFRVLVYLVTAERVWSDDHKDFDCNTRQPGCSNVCFDEFFPVSHVRLWALQLILVTCPSLLVVMHVAYREVQEKRHREAHGENSGRLYLNPGKKRGGLWWTYVCSLVFKASVDIAFLYVFHSFYPKYILPPVVKCHADPCPNIVDCFISKPSEKNIFTLFMVATAAICILLNLVELIYLVSKRCHECLAARKAQAMCTGHHPHGTTSSCKQDDLLSGDLIFLGSDSHPPLLPDRPRDHVKKTIL
| null | null |
cell-cell signaling [GO:0007267]; epidermis development [GO:0008544]; epididymis development [GO:1905867]; labyrinthine layer morphogenesis [GO:0060713]; spongiotrophoblast differentiation [GO:0060708]; trophoblast giant cell differentiation [GO:0060707]
|
connexin complex [GO:0005922]
|
gap junction channel activity [GO:0005243]
|
PF00029;
|
1.20.1440.80;
|
Connexin family, Beta-type (group I) subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
| null | null | null | null | null |
FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
|
Homo sapiens (Human)
|
O95379
|
TFIP8_HUMAN
|
MHSEAEESKEVATDVFNSKNLAVQAQKKILGKMVSKSIATTLIDDTSSEVLDELYRVTREYTQNKKEAEKIIKNLIKTVIKLAILYRNNQFNQDELALMEKFKKKVHQLAMTVVSFHQVDYTFDRNVLSRLLNECREMLHQIIQRHLTAKSHGRVNNVFDHFSDCEFLAALYNPFGNFKPHLQKLCDGINKMLDEENI
| null | null |
apoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]; positive regulation of apoptotic process [GO:0043065]
|
cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]
|
cysteine-type endopeptidase inhibitor activity involved in apoptotic process [GO:0043027]
|
PF05527;
|
1.20.1440.160;
|
TNFAIP8 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14724590}.
| null | null | null | null | null |
FUNCTION: Acts as a negative mediator of apoptosis and may play a role in tumor progression. Suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, subsequently resulting in inhibition of BID cleavage and caspase-3 activation. {ECO:0000269|PubMed:10644768, ECO:0000269|PubMed:11346652, ECO:0000269|PubMed:14724590}.
|
Homo sapiens (Human)
|
O95382
|
M3K6_HUMAN
|
MAGPCPRSGAERAGSCWQDPLAVALSRGRQLAAPPGRGCARSRPLSVVYVLTREPQPGLEPREGTEAEPLPLRCLREACAQVPRPRPPPQLRSLPFGTLELGDTAALDAFYNADVVVLEVSSSLVQPSLFYHLGVRESFSMTNNVLLCSQADLPDLQALREDVFQKNSDCVGSYTLIPYVVTATGRVLCGDAGLLRGLADGLVQAGVGTEALLTPLVGRLARLLEATPTDSCGYFRETIRRDIRQARERFSGPQLRQELARLQRRLDSVELLSPDIIMNLLLSYRDVQDYSAIIELVETLQALPTCDVAEQHNVCFHYTFALNRRNRPGDRAKALSVLLPLVQLEGSVAPDLYCMCGRIYKDMFFSSGFQDAGHREQAYHWYRKAFDVEPSLHSGINAAVLLIAAGQHFEDSKELRLIGMKLGCLLARKGCVEKMQYYWDVGFYLGAQILANDPTQVVLAAEQLYKLNAPIWYLVSVMETFLLYQHFRPTPEPPGGPPRRAHFWLHFLLQSCQPFKTACAQGDQCLVLVLEMNKVLLPAKLEVRGTDPVSTVTLSLLEPETQDIPSSWTFPVASICGVSASKRDERCCFLYALPPAQDVQLCFPSVGHCQWFCGLIQAWVTNPDSTAPAEEAEGAGEMLEFDYEYTETGERLVLGKGTYGVVYAGRDRHTRVRIAIKEIPERDSRFSQPLHEEIALHRRLRHKNIVRYLGSASQGGYLKIFMEEVPGGSLSSLLRSVWGPLKDNESTISFYTRQILQGLGYLHDNHIVHRDIKGDNVLINTFSGLLKISDFGTSKRLAGITPCTETFTGTLQYMAPEIIDQGPRGYGKAADIWSLGCTVIEMATGRPPFHELGSPQAAMFQVGMYKVHPPMPSSLSAEAQAFLLRTFEPDPRLRASAQTLLGDPFLQPGKRSRSPSSPRHAPRPSDAPSASPTPSANSTTQSQTFPCPQAPSQHPPSPPKRCLSYGGTSQLRVPEEPAAEEPASPEESSGLSLLHQESKRRAMLAAVLEQELPALAENLHQEQKQEQGARLGRNHVEELLRCLGAHIHTPNRRQLAQELRALQGRLRAQGLGPALLHRPLFAFPDAVKQILRKRQIRPHWMFVLDSLLSRAVRAALGVLGPEVEKEAVSPRSEELSNEGDSQQSPGQQSPLPVEPEQGPAPLMVQLSLLRAETDRLREILAGKEREYQALVQRALQRLNEEARTYVLAPEPPTALSTDQGLVQWLQELNVDSGTIQMLLNHSFTLHTLLTYATRDDLIYTRIRGGMVCRIWRAILAQRAGSTPVTSGP
|
2.7.11.25
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
cellular response to stress [GO:0033554]; protein phosphorylation [GO:0006468]; signal transduction [GO:0007165]
| null |
ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; MAP kinase kinase kinase activity [GO:0004709]; protein serine kinase activity [GO:0106310]
|
PF19039;PF20309;PF20302;PF13281;PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.25; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.25;
| null | null | null | null |
FUNCTION: Component of a protein kinase signal transduction cascade. Activates the JNK, but not ERK or p38 kinase pathways. {ECO:0000269|PubMed:17210579, ECO:0000269|PubMed:9875215}.
|
Homo sapiens (Human)
|
O95388
|
CCN4_HUMAN
|
MRWFLPWTLAAVTAAAASTVLATALSPAPTTMDFTPAPLEDTSSRPQFCKWPCECPPSPPRCPLGVSLITDGCECCKMCAQQLGDNCTEAAICDPHRGLYCDYSGDRPRYAIGVCAQVVGVGCVLDGVRYNNGQSFQPNCKYNCTCIDGAVGCTPLCLRVRPPRLWCPHPRRVSIPGHCCEQWVCEDDAKRPRKTAPRDTGAFDAVGEVEAWHRNCIAYTSPWSPCSTSCGLGVSTRISNVNAQCWPEQESRLCNLRPCDVDIHTLIKAGKKCLAVYQPEASMNFTLAGCISTRSYQPKYCGVCMDNRCCIPYKSKTIDVSFQCPDGLGFSRQVLWINACFCNLSCRNPNDIFADLESYPDFSEIAN
| null | null |
bone development [GO:0060348]; cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; glucose homeostasis [GO:0042593]; negative regulation of chondrocyte differentiation [GO:0032331]; negative regulation of fat cell differentiation [GO:0045599]; osteoblast differentiation [GO:0001649]; osteoclast differentiation [GO:0030316]; positive regulation of cell differentiation [GO:0045597]; positive regulation of inflammatory response [GO:0050729]; positive regulation of osteoblast differentiation [GO:0045669]; positive regulation of smooth muscle cell migration [GO:0014911]; positive regulation of smooth muscle cell proliferation [GO:0048661]; positive regulation of Wnt signaling pathway [GO:0030177]; positive regulation of wound healing [GO:0090303]; regulation of cytokine production [GO:0001817]; signal transduction [GO:0007165]; Wnt signaling pathway [GO:0016055]
|
cytosol [GO:0005829]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]
|
heparin binding [GO:0008201]; integrin binding [GO:0005178]
|
PF00007;PF00219;PF19035;PF00093;
|
2.10.70.10;2.20.100.10;
|
CCN family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Downstream regulator in the Wnt/Frizzled-signaling pathway. Associated with cell survival. Attenuates p53-mediated apoptosis in response to DNA damage through activation of AKT kinase. Up-regulates the anti-apoptotic Bcl-X(L) protein. Adheres to skin and melanoma fibroblasts. In vitro binding to skin fibroblasts occurs through the proteoglycans, decorin and biglycan. {ECO:0000269|PubMed:10716946, ECO:0000269|PubMed:11782444}.
|
Homo sapiens (Human)
|
O95389
|
CCN6_HUMAN
|
MQGLLFSTLLLAGLAQFCCRVQGTGPLDTTPEGRPGEVSDAPQRKQFCHWPCKCPQQKPRCPPGVSLVRDGCGCCKICAKQPGEICNEADLCDPHKGLYCDYSVDRPRYETGVCAYLVAVGCEFNQVHYHNGQVFQPNPLFSCLCVSGAIGCTPLFIPKLAGSHCSGAKGGKKSDQSNCSLEPLLQQLSTSYKTMPAYRNLPLIWKKKCLVQATKWTPCSRTCGMGISNRVTNENSNCEMRKEKRLCYIQPCDSNILKTIKIPKGKTCQPTFQLSKAEKFVFSGCSSTQSYKPTFCGICLDKRCCIPNKSKMITIQFDCPNEGSFKWKMLWITSCVCQRNCREPGDIFSELKIL
| null | null |
cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; negative regulation of angiogenesis [GO:0016525]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of cell differentiation [GO:0045597]; regulation of mitochondrial membrane potential [GO:0051881]; regulation of reactive oxygen species biosynthetic process [GO:1903426]; signal transduction [GO:0007165]
|
extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]
|
growth factor activity [GO:0008083]; heparin binding [GO:0008201]; integrin binding [GO:0005178]
|
PF00007;PF00219;PF19035;
|
2.10.70.10;2.20.100.10;
|
CCN family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27252383}. Mitochondrion {ECO:0000269|PubMed:27252383}. Note=Associated with membranes. {ECO:0000269|PubMed:27252383}.
| null | null | null | null | null |
FUNCTION: Plays a role in mitochondrial electron transport and mitochondrial respiration (PubMed:27252383). Through its regulation of the mitochondrial function may play a role in normal postnatal skeletal growth and cartilage homeostasis (PubMed:10471507, PubMed:27252383). {ECO:0000269|PubMed:10471507, ECO:0000269|PubMed:27252383}.
|
Homo sapiens (Human)
|
O95390
|
GDF11_HUMAN
|
MVLAAPLLLGFLLLALELRPRGEAAEGPAAAAAAAAAAAAAGVGGERSSRPAPSVAPEPDGCPVCVWRQHSRELRLESIKSQILSKLRLKEAPNISREVVKQLLPKAPPLQQILDLHDFQGDALQPEDFLEEDEYHATTETVISMAQETDPAVQTDGSPLCCHFHFSPKVMFTKVLKAQLWVYLRPVPRPATVYLQILRLKPLTGEGTAGGGGGGRRHIRIRSLKIELHSRSGHWQSIDFKQVLHSWFRQPQSNWGIEINAFDPSGTDLAVTSLGPGAEGLHPFMELRVLENTKRSRRNLGLDCDEHSSESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGQCEYMFMQKYPHTHLVQQANPRGSAGPCCTPTKMSPINMLYFNDKQQIIYGKIPGMVVDRCGCS
| null | null |
activin receptor signaling pathway [GO:0032924]; amacrine cell differentiation [GO:0035881]; camera-type eye morphogenesis [GO:0048593]; cell population proliferation [GO:0008283]; mesoderm development [GO:0007498]; metanephros development [GO:0001656]; negative regulation of amacrine cell differentiation [GO:1902870]; negative regulation of cell population proliferation [GO:0008285]; nervous system development [GO:0007399]; positive regulation of SMAD protein signal transduction [GO:0060391]; roof of mouth development [GO:0060021]; skeletal system development [GO:0001501]; SMAD protein signal transduction [GO:0060395]; spinal cord anterior/posterior patterning [GO:0021512]; type B pancreatic cell maturation [GO:0072560]; ureteric bud development [GO:0001657]
|
extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; protein-containing complex [GO:0032991]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
|
PTM: Synthesized as large precursor molecule that undergoes proteolytic cleavage by furin-like proteases (PubMed:31215115). This produces an inactive form consisting of the mature C-terminal portion non-covalently bound to its cleaved N-terminal propeptide. Activation of the mature form requires additional cleavage of the propeptide by a tolloid-like metalloproteinase. {ECO:0000250|UniProtKB:Q9Z1W4, ECO:0000269|PubMed:31215115}.
|
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Secreted signal that acts globally to regulate anterior/posterior axial patterning during development. May play critical roles in patterning both mesodermal and neural tissues (By similarity). It is required for proper vertebral patterning and orofacial development (PubMed:31215115). Signals through activin receptors type-2, ACVR2A and ACVR2B, and activin receptors type-1, ACVR1B, ACVR1C and TGFBR1 leading to the phosphorylation of SMAD2 and SMAD3 (PubMed:28257634). {ECO:0000250|UniProtKB:Q9Z1W4, ECO:0000269|PubMed:28257634, ECO:0000269|PubMed:31215115}.
|
Homo sapiens (Human)
|
O95391
|
SLU7_HUMAN
|
MSATVVDAVNAAPLSGSKEMSLEEPKKMTREDWRKKKELEEQRKLGNAPAEVDEEGKDINPHIPQYISSVPWYIDPSKRPTLKHQRPQPEKQKQFSSSGEWYKRGVKENSIITKYRKGACENCGAMTHKKKDCFERPRRVGAKFTGTNIAPDEHVQPQLMFDYDGKRDRWNGYNPEEHMKIVEEYAKVDLAKRTLKAQKLQEELASGKLVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDMPGQNFDSKRRITVRNLRIREDIAKYLRNLDPNSAYYDPKTRAMRENPYANAGKNPDEVSYAGDNFVRYTGDTISMAQTQLFAWEAYDKGSEVHLQADPTKLELLYKSFKVKKEDFKEQQKESILEKYGGQEHLDAPPAELLLAQTEDYVEYSRHGTVIKGQERAVACSKYEEDVKIHNHTHIWGSYWKEGRWGYKCCHSFFKYSYCTGEAGKEIVNSEECIINEITGEESVKKPQTLMELHQEKLKEEKKKKKKKKKKHRKSSSDSDDEEKKHEKLKKALNAEEARLLHVKETMQIDERKRPYNSMYETREPTEEEMEAYRMKRQRPDDPMASFLGQ
| null | null |
alternative mRNA splicing, via spliceosome [GO:0000380]; cellular response to heat [GO:0034605]; intracellular protein transport [GO:0006886]; mRNA 3'-splice site recognition [GO:0000389]; mRNA splicing, via spliceosome [GO:0000398]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375]
|
catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; small nuclear ribonucleoprotein complex [GO:0030532]; spliceosomal complex [GO:0005681]
|
pre-mRNA 3'-splice site binding [GO:0030628]; second spliceosomal transesterification activity [GO:0000386]; zinc ion binding [GO:0008270]
|
PF11708;
| null |
SLU7 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10197984, ECO:0000269|PubMed:15728250, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:30705154}. Nucleus speckle {ECO:0000269|PubMed:15181151}. Cytoplasm {ECO:0000269|PubMed:15728250}. Note=Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Upon UV-C stress stimulus, the nuclear concentration of the protein decreases, affecting alternative splicing. Translocates from the nucleus to the cytoplasm after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules. {ECO:0000269|PubMed:15728250}.
| null | null | null | null | null |
FUNCTION: Required for pre-mRNA splicing as component of the spliceosome (PubMed:10197984, PubMed:28502770, PubMed:30705154). Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation. {ECO:0000269|PubMed:10197984, ECO:0000269|PubMed:10647016, ECO:0000269|PubMed:12764196, ECO:0000269|PubMed:15181151, ECO:0000269|PubMed:15728250, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:30705154}.
|
Homo sapiens (Human)
|
O95393
|
BMP10_HUMAN
|
MGSLVLTLCALFCLAAYLVSGSPIMNLEQSPLEEDMSLFGDVFSEQDGVDFNTLLQSMKDEFLKTLNLSDIPTQDSAKVDPPEYMLELYNKFATDRTSMPSANIIRSFKNEDLFSQPVSFNGLRKYPLLFNVSIPHHEEVIMAELRLYTLVQRDRMIYDGVDRKITIFEVLESKGDNEGERNMLVLVSGEIYGTNSEWETFDVTDAIRRWQKSGSSTHQLEVHIESKHDEAEDASSGRLEIDTSAQNKHNPLLIVFSDDQSSDKERKEELNEMISHEQLPELDNLGLDSFSSGPGEEALLQMRSNIIYDSTARIRRNAKGNYCKRTPLYIDFKEIGWDSWIIAPPGYEAYECRGVCNYPLAEHLTPTKHAIIQALVHLKNSQKASKACCVPTKLEPISILYLDKGVVTYKFKYEGMAVSECGCR
| null | null |
activin receptor signaling pathway [GO:0032924]; adult heart development [GO:0007512]; atrial cardiac muscle tissue morphogenesis [GO:0055009]; BMP signaling pathway [GO:0030509]; cardiac muscle cell proliferation [GO:0060038]; cell adhesion [GO:0007155]; heart trabecula formation [GO:0060347]; kidney development [GO:0001822]; negative regulation of cardiac muscle hypertrophy [GO:0010614]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of endothelial cell migration [GO:0010596]; positive regulation of cardiac muscle cell proliferation [GO:0060045]; positive regulation of cardiac muscle hypertrophy [GO:0010613]; positive regulation of cartilage development [GO:0061036]; positive regulation of cell proliferation involved in heart morphogenesis [GO:2000138]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of sarcomere organization [GO:0060298]; positive regulation of SMAD protein signal transduction [GO:0060391]; regulation of cardiac muscle contraction [GO:0055117]; regulation of cardiac muscle hypertrophy in response to stress [GO:1903242]; sarcomere organization [GO:0045214]; ventricular cardiac muscle cell development [GO:0055015]; ventricular cardiac muscle tissue morphogenesis [GO:0055010]
|
cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Z disc [GO:0030018]
|
cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; receptor serine/threonine kinase binding [GO:0033612]; telethonin binding [GO:0031433]
|
PF00019;PF00688;
|
2.60.120.970;2.10.90.10;
|
TGF-beta family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines. {ECO:0000269|PubMed:16049014, ECO:0000269|PubMed:17068149, ECO:0000269|PubMed:20608934}.
|
Homo sapiens (Human)
|
O95394
|
AGM1_HUMAN
|
MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRVLIDISEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELLVEIGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKQSAEQLEDKKRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQESADHLAHEVSLAVFQLAGGIGERPQPGF
|
5.4.2.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9P4V2}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9P4V2};
|
carbohydrate metabolic process [GO:0005975]; glucosamine metabolic process [GO:0006041]; hemopoiesis [GO:0030097]; protein N-linked glycosylation [GO:0006487]; protein O-linked glycosylation [GO:0006493]; spermatogenesis [GO:0007283]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]
|
cytosol [GO:0005829]
|
magnesium ion binding [GO:0000287]; phosphoacetylglucosamine mutase activity [GO:0004610]
|
PF21405;PF21404;PF02878;PF00408;
|
3.40.120.10;3.30.310.50;
|
Phosphohexose mutase family
| null | null |
CATALYTIC ACTIVITY: Reaction=N-acetyl-alpha-D-glucosamine 1-phosphate = N-acetyl-D-glucosamine 6-phosphate; Xref=Rhea:RHEA:23804, ChEBI:CHEBI:57513, ChEBI:CHEBI:57776; EC=5.4.2.3; Evidence={ECO:0000269|PubMed:24589341, ECO:0000269|PubMed:24698316, ECO:0000269|PubMed:24931394};
| null |
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route I): step 2/2. {ECO:0000303|PubMed:24589341, ECO:0000303|PubMed:24698316, ECO:0000303|PubMed:24931394}.
| null | null |
FUNCTION: Catalyzes the conversion of GlcNAc-6-P into GlcNAc-1-P during the synthesis of uridine diphosphate/UDP-GlcNAc, a sugar nucleotide critical to multiple glycosylation pathways including protein N- and O-glycosylation. {ECO:0000303|PubMed:24589341, ECO:0000303|PubMed:24698316, ECO:0000303|PubMed:24931394}.
|
Homo sapiens (Human)
|
O95395
|
GCNT3_HUMAN
|
MVQWKRLCQLHYLWALGCYMLLATVALKLSFRLKCDSDHLGLESRESQSQYCRNILYNFLKLPAKRSINCSGVTRGDQEAVLQAILNNLEVKKKREPFTDTHYLSLTRDCEHFKAERKFIQFPLSKEEVEFPIAYSMVIHEKIENFERLLRAVYAPQNIYCVHVDEKSPETFKEAVKAIISCFPNVFIASKLVRVVYASWSRVQADLNCMEDLLQSSVPWKYFLNTCGTDFPIKSNAEMVQALKMLNGRNSMESEVPPKHKETRWKYHFEVVRDTLHLTNKKKDPPPYNLTMFTGNAYIVASRDFVQHVLKNPKSQQLIEWVKDTYSPDEHLWATLQRARWMPGSVPNHPKYDISDMTSIARLVKWQGHEGDIDKGAPYAPCSGIHQRAICVYGAGDLNWMLQNHHLLANKFDPKVDDNALQCLEEYLRYKAIYGTEL
|
2.4.1.102; 2.4.1.148; 2.4.1.150
| null |
carbohydrate metabolic process [GO:0005975]; intestinal absorption [GO:0050892]; kidney morphogenesis [GO:0060993]; O-glycan processing [GO:0016266]; protein O-linked glycosylation [GO:0006493]; tissue morphogenesis [GO:0048729]
|
extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
|
acetylgalactosaminyl-O-glycosyl-seryl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity [GO:0106325]; acetylgalactosaminyl-O-glycosyl-threonyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity [GO:0106326]; acetylglucosaminyltransferase activity [GO:0008375]; beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity [GO:0003829]; N-acetyllactosaminide beta-1,6-N-acetylglucosaminyltransferase activity [GO:0008109]
|
PF02485;
| null |
Glycosyltransferase 14 family
|
PTM: N-glycosylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56212, Rhea:RHEA-COMP:13922, Rhea:RHEA-COMP:14419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137949, ChEBI:CHEBI:139605; EC=2.4.1.102; Evidence={ECO:0000269|PubMed:9915862}; CATALYTIC ACTIVITY: Reaction=O(3)-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56216, Rhea:RHEA-COMP:13923, Rhea:RHEA-COMP:14420, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:137950, ChEBI:CHEBI:139607; EC=2.4.1.102; Evidence={ECO:0000269|PubMed:9915862}; CATALYTIC ACTIVITY: Reaction=a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc derivative + UDP-N-acetyl-alpha-D-glucosamine = a beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-[beta-D-GlcNAc-(1->6)]-beta-D-Gal-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:54820, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:138371, ChEBI:CHEBI:138372; EC=2.4.1.150; Evidence={ECO:0000269|PubMed:9915862}; CATALYTIC ACTIVITY: Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56188, Rhea:RHEA-COMP:11691, Rhea:RHEA-COMP:14412, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:87079, ChEBI:CHEBI:139581; EC=2.4.1.148; Evidence={ECO:0000269|PubMed:9915862}; CATALYTIC ACTIVITY: Reaction=3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-acetyl-beta-D-glucosaminyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:56192, Rhea:RHEA-COMP:11692, Rhea:RHEA-COMP:14413, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:87080, ChEBI:CHEBI:139580; EC=2.4.1.148; Evidence={ECO:0000269|PubMed:9915862};
| null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Glycosyltransferase that can synthesize all known mucin beta 6 N-acetylglucosaminides. Mediates core 2 and core 4 O-glycan branching, 2 important steps in mucin-type biosynthesis. Has also I-branching enzyme activity by converting linear into branched poly-N-acetyllactosaminoglycans, leading to introduce the blood group I antigen during embryonic development. {ECO:0000269|PubMed:9915862}.
|
Homo sapiens (Human)
|
O95396
|
MOCS3_HUMAN
|
MASREEVLALQAEVAQREEELNSLKQKLASALLAEQEPQPERLVPVSPLPPKAALSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHFRSIRLRSRRLDCAACGERPTVTDLLDYEAFCGSSATDKCRSLQLLSPEERVSVTDYKRLLDSGAFHLLLDVRPQVEVDICRLPHALHIPLKHLERRDAESLKLLKEAIWEEKQGTQEGAAVPIYVICKLGNDSQKAVKILQSLSAAQELDPLTVRDVVGGLMAWAAKIDGTFPQY
|
2.7.7.80; 2.8.1.11
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03049}; Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_03049};
|
Mo-molybdopterin cofactor biosynthetic process [GO:0006777]; molybdopterin cofactor metabolic process [GO:0043545]; protein urmylation [GO:0032447]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; molybdopterin-synthase adenylyltransferase activity [GO:0061605]; molybdopterin-synthase sulfurtransferase activity [GO:0061604]; nucleotidyltransferase activity [GO:0016779]; sulfotransferase activity [GO:0008146]; sulfurtransferase activity [GO:0016783]; thiosulfate sulfurtransferase activity [GO:0004792]; URM1 activating enzyme activity [GO:0042292]
|
PF00581;PF00899;
|
3.40.50.720;3.40.250.10;
|
HesA/MoeB/ThiF family, UBA4 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:23593335}.
|
CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate; Xref=Rhea:RHEA:43616, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12202, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:90618, ChEBI:CHEBI:90778; EC=2.7.7.80; Evidence={ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437}; CATALYTIC ACTIVITY: Reaction=[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:48612, Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12159, Rhea:RHEA-COMP:12160, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; EC=2.8.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:17459099, ECO:0000269|PubMed:18650437};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.25 mM for thiosulfate {ECO:0000269|PubMed:15073332}; KM=0.28 mM for cyanide {ECO:0000269|PubMed:15073332};
|
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.; PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03049}.
| null | null |
FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A. Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 acting as a sulfur donor for thiocarboxylation reactions. {ECO:0000255|HAMAP-Rule:MF_03049, ECO:0000269|PubMed:15073332, ECO:0000269|PubMed:19017811, ECO:0000269|PubMed:30817134}.
|
Homo sapiens (Human)
|
O95398
|
RPGF3_HUMAN
|
MKVGWPGESCWQVGLAVEDSPALGAPRVGALPDVVPEGTLLNMVLRRMHRPRSCSYQLLLEHQRPSCIQGLRWTPLTNSEESLDFSESLEQASTERVLRAGRQLHRHLLATCPNLIRDRKYHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHVKHDWAFQDRDAQFYRFPGPEPEPVRTHEMEEELAEAVALLSQRGPDALLTVALRKPPGQRTDEELDLIFEELLHIKAVAHLSNSVKRELAAVLLFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKGLVTTLHEGDDFGQLALVNDAPRAATIILREDNCHFLRVDKQDFNRIIKDVEAKTMRLEEHGKVVLVLERASQGAGPSRPPTPGRNRYTVMSGTPEKILELLLEAMGPDSSAHDPTETFLSDFLLTHRVFMPSAQLCAALLHHFHVEPAGGSEQERSTYVCNKRQQILRLVSQWVALYGSMLHTDPVATSFLQKLSDLVGRDTRLSNLLREQWPERRRCHRLENGCGNASPQMKARNLPVWLPNQDEPLPGSSCAIQVGDKVPYDICRPDHSVLTLQLPVTASVREVMAALAQEDGWTKGQVLVKVNSAGDAIGLQPDARGVATSLGLNERLFVVNPQEVHELIPHPDQLGPTVGSAEGLDLVSAKDLAGQLTDHDWSLFNSIHQVELIHYVLGPQHLRDVTTANLERFMRRFNELQYWVATELCLCPVPGPRAQLLRKFIKLAAHLKEQKNLNSFFAVMFGLSNSAISRLAHTWERLPHKVRKLYSALERLLDPSWNHRVYRLALAKLSPPVIPFMPLLLKDMTFIHEGNHTLVENLINFEKMRMMARAARMLHHCRSHNPVPLSPLRSRVSHLHEDSQVARISTCSEQSLSTRSPASTWAYVQQLKVIDNQRELSRLSRELEP
| null | null |
adaptive immune response [GO:0002250]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; angiogenesis [GO:0001525]; associative learning [GO:0008306]; cellular response to cAMP [GO:0071320]; establishment of endothelial barrier [GO:0061028]; intracellular signal transduction [GO:0035556]; negative regulation of syncytium formation by plasma membrane fusion [GO:0034242]; positive regulation of angiogenesis [GO:0045766]; positive regulation of GTPase activity [GO:0043547]; positive regulation of protein export from nucleus [GO:0046827]; positive regulation of stress fiber assembly [GO:0051496]; positive regulation of syncytium formation by plasma membrane fusion [GO:0060143]; Rap protein signal transduction [GO:0032486]; Ras protein signal transduction [GO:0007265]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of angiogenesis [GO:0045765]; regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051896]; signal transduction [GO:0007165]
|
endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; lamellipodium [GO:0030027]; membrane [GO:0016020]; microvillus [GO:0005902]; plasma membrane [GO:0005886]
|
cAMP binding [GO:0030552]; guanyl-nucleotide exchange factor activity [GO:0005085]; protein domain specific binding [GO:0019904]
|
PF00027;PF00610;PF00617;PF00618;
|
1.10.8.1240;2.60.120.10;1.10.840.10;1.20.870.10;1.10.10.10;
| null | null |
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:10777494}.
| null | null | null | null | null |
FUNCTION: Guanine nucleotide exchange factor (GEF) for RAP1A and RAP2A small GTPases that is activated by binding cAMP. Through simultaneous binding of PDE3B to RAPGEF3 and PIK3R6 is assembled in a signaling complex in which it activates the PI3K gamma complex and which is involved in angiogenesis. Plays a role in the modulation of the cAMP-induced dynamic control of endothelial barrier function through a pathway that is independent on Rho-mediated signaling. Required for the actin rearrangement at cell-cell junctions, such as stress fibers and junctional actin. {ECO:0000269|PubMed:10777494, ECO:0000269|PubMed:21840392, ECO:0000269|PubMed:9853756}.
|
Homo sapiens (Human)
|
O95399
|
UTS2_HUMAN
|
MYKLASCCLLFIGFLNPLLSLPLLDSREISFQLSAPHEDARLTPEELERASLLQILPEMLGAERGDILRKADSSTNIFNPRGNLRKFQDFSGQDPNILLSHLLARIWKPYKKRETPDCFWKYCV
| null | null |
blood vessel diameter maintenance [GO:0097746]; chemical synaptic transmission [GO:0007268]; muscle contraction [GO:0006936]; regulation of blood pressure [GO:0008217]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]; synapse [GO:0045202]
|
hormone activity [GO:0005179]; signaling receptor binding [GO:0005102]
|
PF02083;
| null |
Urotensin-2 family
| null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Highly potent vasoconstrictor.
|
Homo sapiens (Human)
|
O95400
|
CD2B2_HUMAN
|
MPKRKVTFQGVGDEEDEDEIIVPKKKLVDPVAGSGGPGSRFKGKHSLDSDEEEDDDDGGSSKYDILASEDVEGQEAATLPSEGGVRITPFNLQEEMEEGHFDADGNYFLNRDAQIRDSWLDNIDWVKIRERPPGQRQASDSEEEDSLGQTSMSAQALLEGLLELLLPRETVAGALRRLGARGGGKGRKGPGQPSSPQRLDRLSGLADQMVARGNLGVYQETRERLAMRLKGLGCQTLGPHNPTPPPSLDMFAEELAEEELETPTPTQRGEAESRGDGLVDVMWEYKWENTGDAELYGPFTSAQMQTWVSEGYFPDGVYCRKLDPPGGQFYNSKRIDFDLYT
| null | null |
spliceosomal tri-snRNP complex assembly [GO:0000244]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; fibrillar center [GO:0001650]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U5 snRNP [GO:0005682]
|
ribonucleoprotein complex binding [GO:0043021]
|
PF02213;
|
3.30.1490.40;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly nuclear.
| null | null | null | null | null |
FUNCTION: Involved in pre-mRNA splicing as component of the U5 snRNP complex that is involved in spliceosome assembly. {ECO:0000269|PubMed:15840814}.
|
Homo sapiens (Human)
|
O95402
|
MED26_HUMAN
|
MTAAPASPQQIRDRLLQAIDPQSNIRNMVAVLEVISSLEKYPITKEALEETRLGKLINDVRKKTKNEELAKRAKKLLRSWQKLIEPAHQHEAALRGLAGATGSANGGAHNCRPEVGAAGPPRSIHDLKSRNDLQRLPGQRLDRLGSRKRRGDQRDLGHPGPPPKVSKASHDPLVPNSSPLPTNGISGSPESFASSLDGSGHAGPEGSRLERDENDKHSGKIPVNAVRPHTSSPGLGKPPGPCLQPKASVLQQLDRVDETPGPPHPKGPPRCSFSPRNSRHEGSFARQQSLYAPKGSVPSPSPRPQALDATQVPSPLPLAQPSTPPVRRLELLPSAESPVCWLEQPESHQRLAGPGCKAGLSPAEPLLSRAGFSPDSSKADSDAASSGGSDSKKKKRYRPRDYTVNLDGQVAEAGVKPVRLKERKLTFDPMTRQIKPLTQKEPVRADSPVHMEQQSRTELDKQEAKASLQSPFEQTNWKELSRNEIIQSYLSRQSSLLSSSGAQTPGAHHFMSEYLKQEESTRQGARQLHVLVPQSPPTDLPGLTREVTQDDLDRIQASQWPGVNGCQDTQGNWYDWTQCISLDPHGDDGRLNILPYVCLD
| null | null |
positive regulation of gene expression [GO:0010628]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II preinitiation complex assembly [GO:0051123]; transcription initiation at RNA polymerase II promoter [GO:0006367]
|
core mediator complex [GO:0070847]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712]
|
PF08711;PF15693;PF15694;
|
1.20.930.10;
|
Mediator complex subunit 26 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional pre-initiation complex with RNA polymerase II and the general transcription factors.
|
Homo sapiens (Human)
|
O95405
|
ZFYV9_HUMAN
|
MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMKKEPAEESTTEESLRSGLPLLLKPDMPNGSGRNNDCERCSDCLVPNEVRADENEGYEHEETLGTTEFLNMTEHFSESQDMTNWKLTKLNEMNDSQVNEEKEKFLQISQPEDTNGDSGGQCVGLADAGLDLKGTCISESEECDFSTVIDTPAANYLSNGCDSYGMQDPGVSFVPKTLPSKEDSVTEEKEIEESKSECYSNIYEQRGNEATEGSGLLLNSTGDLMKKNYLHNFCSQVPSVLGQSSPKVVASLPSISVPFGGARPKQPSNLKLQIPKPLSDHLQNDFPANSGNNTKNKNDILGKAKLGENSATNVCSPSLGNISNVDTNGEHLESYEAEISTRPCLALAPDSPDNDLRAGQFGISARKPFTTLGEVAPVWVPDSQAPNCMKCEARFTFTKRRHHCRACGKVFCASCCSLKCKLLYMDRKEARVCVICHSVLMNAQAWENMMSASSQSPNPNNPAEYCSTIPPLQQAQASGALSSPPPTVMVPVGVLKHPGAEVAQPREQRRVWFADGILPNGEVADAAKLTMNGTSSAGTLAVSHDPVKPVTTSPLPAETDICLFSGSITQVGSPVGSAMNLIPEDGLPPILISTGVKGDYAVEEKPSQISVMQQLEDGGPDPLVFVLNANLLSMVKIVNYVNRKCWCFTTKGMHAVGQSEIVILLQCLPDEKCLPKDIFNHFVQLYRDALAGNVVSNLGHSFFSQSFLGSKEHGGFLYVTSTYQSLQDLVLPTPPYLFGILIQKWETPWAKVFPIRLMLRLGAEYRLYPCPLFSVRFRKPLFGETGHTIMNLLADFRNYQYTLPVVQGLVVDMEVRKTSIKIPSNRYNEMMKAMNKSNEHVLAGGACFNEKADSHLVCVQNDDGNYQTQAISIHNQPRKVTGASFFVFSGALKSSSGYLAKSSIVEDGVMVQITAENMDSLRQALREMKDFTITCGKADAEEPQEHIHIQWVDDDKNVSKGVVSPIDGKSMETITNVKIFHGSEYKANGKVIRWTEVFFLENDDQHNCLSDPADHSRLTEHVAKAFCLALCPHLKLLKEDGMTKLGLRVTLDSDQVGYQAGSNGQPLPSQYMNDLDSALVPVIHGGACQLSEGPVVMELIFYILENIV
| null | null |
endocytosis [GO:0006897]; endosomal transport [GO:0016197]; liver development [GO:0001889]; transforming growth factor beta receptor signaling pathway [GO:0007179]
|
cytosol [GO:0005829]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; intracellular membrane-bounded organelle [GO:0043231]; protein-containing complex [GO:0032991]
|
1-phosphatidylinositol binding [GO:0005545]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]
|
PF01363;PF11409;PF11979;
|
3.30.500.40;3.30.1360.220;4.10.720.10;3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm. Early endosome membrane.
| null | null | null | null | null |
FUNCTION: Early endosomal protein that functions to recruit SMAD2/SMAD3 to intracellular membranes and to the TGF-beta receptor. Plays a significant role in TGF-mediated signaling by regulating the subcellular location of SMAD2 and SMAD3 and modulating the transcriptional activity of the SMAD3/SMAD4 complex. Possibly associated with TGF-beta receptor internalization. {ECO:0000269|PubMed:15356634, ECO:0000269|PubMed:9865696}.
|
Homo sapiens (Human)
|
O95406
|
CNIH1_HUMAN
|
MAFTFAAFCYMLALLLTAALIFFAIWHIIAFDELKTDYKNPIDQCNTLNPLVLPEYLIHAFFCVMFLCAAEWLTLGLNMPLLAYHIWRYMSRPVMSGPGLYDPTTIMNADILAYCQKEGWCKLAFYLLAFFYYLYGMIYVLVSS
| null | null |
endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; immune response [GO:0006955]; signal transduction [GO:0007165]
|
endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]
| null |
PF03311;
| null |
Cornichon family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17607000}; Multi-pass membrane protein {ECO:0000269|PubMed:17607000}. Golgi apparatus membrane {ECO:0000269|PubMed:17607000}. Note=Located primarily in the ER; may cycle between the ER and the Golgi apparatus.
| null | null | null | null | null |
FUNCTION: Involved in the selective transport and maturation of TGF-alpha family proteins. {ECO:0000269|PubMed:17607000}.
|
Homo sapiens (Human)
|
O95407
|
TNF6B_HUMAN
|
MRALEGPGLSLLCLVLALPALLPVPAVRGVAETPTYPWRDAETGERLVCAQCPPGTFVQRPCRRDSPTTCGPCPPRHYTQFWNYLERCRYCNVLCGEREEEARACHATHNRACRCRTGFFAHAGFCLEHASCPPGAGVIAPGTPSQNTQCQPCPPGTFSASSSSSEQCQPHRNCTALGLALNVPGSSSHDTLCTSCTGFPLSTRVPGAEECERAVIDFVAFQDISIKRLQRLLQALEAPEGWGPTPRAGRAALQLKLRRRLTELLGAQDGALLVRLLQALRVARMPGLERSVRERFLPVH
| null | null |
apoptotic process [GO:0006915]; negative regulation of apoptotic process [GO:0043066]
|
extracellular region [GO:0005576]; extracellular space [GO:0005615]
|
signaling receptor activity [GO:0038023]
|
PF00020;
|
2.10.50.10;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Decoy receptor that can neutralize the cytotoxic ligands TNFS14/LIGHT, TNFSF15 and TNFSF6/FASL. Protects against apoptosis. {ECO:0000269|PubMed:21300286}.
|
Homo sapiens (Human)
|
O95409
|
ZIC2_HUMAN
|
MLLDAGPQFPAIGVGSFARHHHHSAAAAAAAAAEMQDRELSLAAAQNGFVDSAAAHMGAFKLNPGAHELSPGQSSAFTSQGPGAYPGSAAAAAAAAALGPHAAHVGSYSGPPFNSTRDFLFRSRGFGDSAPGGGQHGLFGPGAGGLHHAHSDAQGHLLFPGLPEQHGPHGSQNVLNGQMRLGLPGEVFGRSEQYRQVASPRTDPYSAAQLHNQYGPMNMNMGMNMAAAAAHHHHHHHHHPGAFFRYMRQQCIKQELICKWIDPEQLSNPKKSCNKTFSTMHELVTHVSVEHVGGPEQSNHVCFWEECPREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFQCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHESSPQGSESSPAASSGYESSTPPGLVSPSAEPQSSSNLSPAAAAAAAAAAAAAAAVSAVHRGGGSGSGGAGGGSGGGSGSGGGGGGAGGGGGGSSGGGSGTAGGHSGLSSNFNEWYV
| null | null |
brain development [GO:0007420]; cell differentiation [GO:0030154]; central nervous system development [GO:0007417]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; visual perception [GO:0007601]
|
cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00096;PF18366;
|
3.30.160.60;
|
GLI C2H2-type zinc-finger protein family
|
PTM: Phosphorylated.; PTM: Ubiquitinated by RNF180, leading to its degradation.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm {ECO:0000250}. Note=Localizes in the cytoplasm in presence of MDFIC overexpression. Both phosphorylated and unphosphorylated forms are localized in the nucleus (By similarity). {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Acts as a transcriptional activator or repressor. Plays important roles in the early stage of organogenesis of the CNS. Activates the transcription of the serotonin transporter SERT in uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine eye-specific projections in primary visual targets. Its transcriptional activity is repressed by MDFIC. Involved in the formation of the ipsilateral retinal projection at the optic chiasm midline. Drives the expression of EPHB1 on ipsilaterally projecting growth cones. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. Associates to the basal SERT promoter region from ventrotemporal retinal segments of retinal embryos.
|
Homo sapiens (Human)
|
O95415
|
BRI3_HUMAN
|
MDHKPLLQERPPAYNLEAGQGDYACGPHGYGAIPAAPPPPPYPYLVTGIPTHHPRVYNIHSRTVTRYPANSIVVVGGCPVCRVGVLEDCFTFLGIFLAIILFPFGFICCFALRKRRCPNCGATFA
| null | null | null |
azurophil granule membrane [GO:0035577]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]
|
PF10164;
| null |
BRI3 family
| null |
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000305|PubMed:14592447}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:30983867}. Note=Co-localizes with MGAT1 and IFITM3 at the perinuclear region. {ECO:0000269|PubMed:30983867}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:30983867}. Nucleus {ECO:0000269|PubMed:30983867}. Note=Diffuse localization in the cytoplasm and nucleus. {ECO:0000269|PubMed:30983867}.
| null | null | null | null | null |
FUNCTION: Participates in tumor necrosis factor-alpha (TNF)-induced cell death (PubMed:14592447). May be a target of Wnt/beta-catenin signaling in the liver (PubMed:20538055). {ECO:0000269|PubMed:14592447, ECO:0000269|PubMed:20538055}.
|
Homo sapiens (Human)
|
O95416
|
SOX14_HUMAN
|
MSKPSDHIKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSEAEKRPYIDEAKRLRAQHMKEHPDYKYRPRRKPKNLLKKDRYVFPLPYLGDTDPLKAAGLPVGASDGLLSAPEKARAFLPPASAPYSLLDPAQFSSSAIQKMGEVPHTLATGALPYASTLGYQNGAFGSLSCPSQHTHTHPSPTNPGYVVPCNCTAWSASTLQPPVAYILFPGMTKTGIDPYSSAHATAM
| null | null |
anatomical structure morphogenesis [GO:0009653]; brain development [GO:0007420]; entrainment of circadian clock [GO:0009649]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; neuron differentiation [GO:0030182]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of neuron migration [GO:2001222]; visual perception [GO:0007601]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00505;PF12336;
|
1.10.30.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
| null | null | null | null | null |
FUNCTION: Acts as a negative regulator of transcription. {ECO:0000250}.
|
Homo sapiens (Human)
|
O95425
|
SVIL_HUMAN
|
MKRKERIARRLEGIENDTQPILLQSCTGLVTHRLLEEDTPRYMRASDPASPHIGRSNEEEETSDSSLEKQTRSKYCTETSGVHGDSPYGSGTMDTHSLESKAERIARYKAERRRQLAEKYGLTLDPEADSEYLSRYTKSRKEPDAVEKRGGKSDKQEESSRDASSLYPGTETMGLRTCAGESKDYALHVGDGSSDPEVLLNIENQRRGQELSATRQAHDLSPAAESSSTFSFSGRDSSFTEVPRSPKHAHSSSLQQAASRSPSFGDPQLSPEARPSTGKPKHEWFLQKDSEGDTPSLINWPSRVKVREKLVKEESARNSPELASESVTQRRHQPAPVHYVSFQSEHSAFDRVPSKAAGSTRQPIRGYVQPADTGHTAKLVTPETPENASECSWVASATQNVPKPPSLTVLEGDGRDSPVLHVCESKAEEEEGEGEGEEKEEDVCFTEALEQSKKTLLALEGDGLVRSPEDPSRNEDFGKPAVSTVTLEHQKELENVAQPPQAPHQPTERTGRSEMVLYIQSEPVSQDAKPTGHNREASKKRKVRTRSLSDFTGPPQLQALKYKDPASRRELELPSSKTEGPYGEISMLDTKVSVAQLRSAFLASANACRRPELKSRVERSAEGPGLPTGVERERGSRKPRRYFSPGESRKTSERFRTQPITSAERKESDRCTSHSETPTVDDEEKVDERAKLSVAAKRLLFREMEKSFDEQNVPKRRSRNTAVEQRLRRLQDRSLTQPITTEEVVIAATEPIPASCSGGTHPVMARLPSPTVARSAVQPARLQASAHQKALAKDQTNEGKELAEQGEPDSSTLSLAEKLALFNKLSQPVSKAISTRNRIDTRQRRMNARYQTQPVTLGEVEQVQSGKLIPFSPAVNTSVSTVASTVAPMYAGDLRTKPPLDHNASATDYKFSSSIENSDSPVRSILKSQAWQPLVEGSENKGMLREYGETESKRALTGRDSGMEKYGSFEEAEASYPILNRAREGDSHKESKYAVPRRGSLERANPPITHLGDEPKEFSMAKMNAQGNLDLRDRLPFEEKVEVENVMKRKFSLRAAEFGEPTSEQTGTAAGKTIAQTTAPVSWKPQDSSEQPQEKLCKNPCAMFAAGEIKTPTGEGLLDSPSKTMSIKERLALLKKSGEEDWRNRLSRRQEGGKAPASSLHTQEAGRSLIKKRVTESRESQMTIEERKQLITVREEAWKTRGRGAANDSTQFTVAGRMVKKGLASPTAITPVASPICGKTRGTTPVSKPLEDIEARPDMQLESDLKLDRLETFLRRLNNKVGGMHETVLTVTGKSVKEVMKPDDDETFAKFYRSVDYNMPRSPVEMDEDFDVIFDPYAPKLTSSVAEHKRAVRPKRRVQASKNPLKMLAAREDLLQEYTEQRLNVAFMESKRMKVEKMSSNSNFSEVTLAGLASKENFSNVSLRSVNLTEQNSNNSAVPYKRLMLLQIKGRRHVQTRLVEPRASALNSGDCFLLLSPHCCFLWVGEFANVIEKAKASELATLIQTKRELGCRATYIQTIEEGINTHTHAAKDFWKLLGGQTSYQSAGDPKEDELYEAAIIETNCIYRLMDDKLVPDDDYWGKIPKCSLLQPKEVLVFDFGSEVYVWHGKEVTLAQRKIAFQLAKHLWNGTFDYENCDINPLDPGECNPLIPRKGQGRPDWAIFGRLTEHNETILFKEKFLDWTELKRSNEKNPGELAQHKEDPRTDVKAYDVTRMVSMPQTTAGTILDGVNVGRGYGLVEGHDRRQFEITSVSVDVWHILEFDYSRLPKQSIGQFHEGDAYVVKWKFMVSTAVGSRQKGEHSVRAAGKEKCVYFFWQGRHSTVSEKGTSALMTVELDEERGAQVQVLQGKEPPCFLQCFQGGMVVHSGRREEEEENVQSEWRLYCVRGEVPVEGNLLEVACHCSSLRSRTSMVVLNVNKALIYLWHGCKAQAHTKEVGRTAANKIKEQCPLEAGLHSSSKVTIHECDEGSEPLGFWDALGRRDRKAYDCMLQDPGSFNFAPRLFILSSSSGDFAATEFVYPARAPSVVSSMPFLQEDLYSAPQPALFLVDNHHEVYLWQGWWPIENKITGSARIRWASDRKSAMETVLQYCKGKNLKKPAPKSYLIHAGLEPLTFTNMFPSWEHREDIAEITEMDTEVSNQITLVEDVLAKLCKTIYPLADLLARPLPEGVDPLKLEIYLTDEDFEFALDMTRDEYNALPAWKQVNLKKAKGLF
| null | null |
actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; barbed-end actin filament capping [GO:0051016]; positive regulation of cytokinesis [GO:0032467]; skeletal muscle tissue development [GO:0007519]
|
actin cytoskeleton [GO:0015629]; cell projection [GO:0042995]; cleavage furrow [GO:0032154]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; focal adhesion [GO:0005925]; microtubule minus-end [GO:0036449]; midbody [GO:0030496]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; podosome [GO:0002102]
|
actin filament binding [GO:0051015]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]
|
PF00626;PF02209;
|
3.40.20.10;1.10.950.10;
|
Villin/gelsolin family
| null |
SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell projection, invadopodium. Cell projection, podosome. Midbody {ECO:0000250|UniProtKB:O46385}. Cleavage furrow {ECO:0000250|UniProtKB:O46385}. Note=Tightly associated with both actin filaments and plasma membranes.
| null | null | null | null | null |
FUNCTION: [Isoform 1]: Forms a high-affinity link between the actin cytoskeleton and the membrane. Is among the first costameric proteins to assemble during myogenesis and it contributes to myogenic membrane structure and differentiation (PubMed:12711699). Appears to be involved in myosin II assembly. May modulate myosin II regulation through MLCK during cell spreading, an initial step in cell migration. May play a role in invadopodial function (PubMed:19109420). {ECO:0000269|PubMed:12711699, ECO:0000269|PubMed:19109420}.; FUNCTION: [Isoform 2]: May be involved in modulation of focal adhesions. Supervillin-mediated down-regulation of focal adhesions involves binding to TRIP6. Plays a role in cytokinesis through KIF14 interaction (By similarity). {ECO:0000250|UniProtKB:O46385}.
|
Homo sapiens (Human)
|
O95427
|
PIGN_HUMAN
|
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESMFTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSLCKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKPSHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYPLSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSLLLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLSTVLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMSTYLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLYLDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFVLVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMSMTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
|
2.-.-.-
| null |
GPI anchor biosynthetic process [GO:0006506]; preassembly of GPI anchor in ER membrane [GO:0016254]
|
cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; plasma membrane [GO:0005886]
|
mannose-ethanolamine phosphotransferase activity [GO:0051377]
|
PF01663;PF04987;
|
3.40.720.10;
|
PIGG/PIGN/PIGO family, PIGN subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
| null | null |
PATHWAY: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
| null | null |
FUNCTION: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity). May act as suppressor of replication stress and chromosome missegregation. {ECO:0000250, ECO:0000269|PubMed:23446422}.
|
Homo sapiens (Human)
|
O95428
|
PPN_HUMAN
|
MRLLLLVPLLLAPAPGSSAPKVRRQSDTWGPWSQWSPCSRTCGGGVSFRERPCYSQRRDGGSSCVGPARSHRSCRTESCPDGARDFRAEQCAEFDGAEFQGRRYRWLPYYSAPNKCELNCIPKGENFYYKHREAVVDGTPCEPGKRDVCVDGSCRVVGCDHELDSSKQEDKCLRCGGDGTTCYPVAGTFDANDLSRGYNQILIVPMGATSILIDEAAASRNFLAVKNVRGEYYLNGHWTIEAARALPAASTILHYERGAEGDLAPERLHARGPTSEPLVIELISQEPNPGVHYEYHLPLRRPSPGFSWSHGSWSDCSAECGGGHQSRLVFCTIDHEAYPDHMCQRQPRPADRRSCNLHPCPETKRWKAGPWAPCSASCGGGSQSRSVYCISSDGAGIQEAVEEAECAGLPGKPPAIQACNLQRCAAWSPEPWGECSVSCGVGVRKRSVTCRGERGSLLHTAACSLEDRPPLTEPCVHEDCPLLSDQAWHVGTWGLCSKSCSSGTRRRQVICAIGPPSHCGSLQHSKPVDVEPCNTQPCHLPQEVPSMQDVHTPASNPWMPLGPQESPASDSRGQWWAAQEHPSARGDHRGERGDPRGDQGTHLSALGPAPSLQQPPYQQPLRSGSGPHDCRHSPHGCCPDGHTASLGPQWQGCPGAPCQQSRYGCCPDRVSVAEGPHHAGCTKSYGGDSTGGMPRSRAVASTVHNTHQPQAQQNEPSECRGSQFGCCYDNVATAAGPLGEGCVGQPSHAYPVRCLLPSAHGSCADWAARWYFVASVGQCNRFWYGGCHGNANNFASEQECMSSCQGSLHGPRRPQPGASGRSTHTDGGGSSPAGEQEPSQHRTGAAVQRKPWPSGGLWRQDQQPGPGEAPHTQAFGEWPWGQELGSRAPGLGGDAGSPAPPFHSSSYRISLAGVEPSLVQAALGQLVRLSCSDDTAPESQAAWQKDGQPISSDRHRLQFDGSLIIHPLQAEDAGTYSCGSTRPGRDSQKIQLRIIGGDMAVLSEAELSRFPQPRDPAQDFGQAGAAGPLGAIPSSHPQPANRLRLDQNQPRVVDASPGQRIRMTCRAEGFPPPAIEWQRDGQPVSSPRHQLQPDGSLVISRVAVEDGGFYTCVAFNGQDRDQRWVQLRVLGELTISGLPPTVTVPEGDTARLLCVVAGESVNIRWSRNGLPVQADGHRVHQSPDGTLLIYNLRARDEGSYTCSAYQGSQAVSRSTEVKVVSPAPTAQPRDPGRDCVDQPELANCDLILQAQLCGNEYYSSFCCASCSRFQPHAQPIWQ
| null | null |
extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508]
|
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]
|
metalloendopeptidase activity [GO:0004222]; serine-type endopeptidase inhibitor activity [GO:0004867]
|
PF19236;PF05986;PF07679;PF00014;PF16626;PF08686;PF19030;PF00090;
|
2.60.120.830;2.60.40.10;4.10.410.10;2.20.100.10;
|
Papilin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O95429
|
BAG4_HUMAN
|
MSALRRSGYGPSDGPSYGRYYGPGGGDVPVHPPPPLYPLRPEPPQPPISWRVRGGGPAETTWLGEGGGGDGYYPSGGAWPEPGRAGGSHQEQPPYPSYNSNYWNSTARSRAPYPSTYPVRPELQGQSLNSYTNGAYGPTYPPGPGANTASYSGAYYAPGYTQTSYSTEVPSTYRSSGNSPTPVSRWIYPQQDCQTEAPPLRGQVPGYPPSQNPGMTLPHYPYGDGNRSVPQSGPTVRPQEDAWASPGAYGMGGRYPWPSSAPSAPPGNLYMTESTSPWPSSGSPQSPPSPPVQQPKDSSYPYSQSDQSMNRHNFPCSVHQYESSGTVNNDDSDLLDSQVQYSAEPQLYGNATSDHPNNQDQSSSLPEECVPSDESTPPSIKKIIHVLEKVQYLEQEVEEFVGKKTDKAYWLLEEMLTKELLELDSVETGGQDSVRQARKEAVCKIQAILEKLEKKGL
| null | null |
cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to tumor necrosis factor [GO:0071356]; negative regulation of apoptotic process [GO:0043066]; negative regulation of mRNA modification [GO:0090367]; negative regulation of protein targeting to mitochondrion [GO:1903215]; positive regulation of actin filament polymerization [GO:0030838]; positive regulation of cell adhesion [GO:0045785]; positive regulation of fibroblast migration [GO:0010763]; positive regulation of peptidyl-serine phosphorylation [GO:0033138]; positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051897]; positive regulation of stress fiber assembly [GO:0051496]; protein folding [GO:0006457]; protein localization to plasma membrane [GO:0072659]; protein stabilization [GO:0050821]; ruffle assembly [GO:0097178]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
adenyl-nucleotide exchange factor activity [GO:0000774]; protein-containing complex binding [GO:0044877]; protein-folding chaperone binding [GO:0051087]; RNA binding [GO:0003723]; ubiquitin protein ligase binding [GO:0031625]
|
PF02179;
|
1.20.58.120;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm.
| null | null | null | null | null |
FUNCTION: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity). Prevents constitutive TNFRSF1A signaling. Negative regulator of PRKN translocation to damaged mitochondria. {ECO:0000250, ECO:0000269|PubMed:24270810}.
|
Homo sapiens (Human)
|
O95433
|
AHSA1_HUMAN
|
MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQRYYFEGIKQTFGYGARLF
| null | null |
positive regulation of ATP-dependent activity [GO:0032781]; protein folding [GO:0006457]
|
cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]
|
ATPase activator activity [GO:0001671]; cadherin binding [GO:0045296]; Hsp90 protein binding [GO:0051879]; protein-folding chaperone binding [GO:0051087]
|
PF09229;PF08327;
|
3.30.530.20;3.15.10.20;
|
AHA1 family
|
PTM: Phosphorylation at Tyr-223 enhances binding to chaperone HSP90AA1. {ECO:0000269|PubMed:29127155}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11554768}. Endoplasmic reticulum {ECO:0000269|PubMed:11554768}. Note=May transiently interact with the endoplasmic reticulum.
| null | null | null | null | null |
FUNCTION: Acts as a co-chaperone of HSP90AA1 (PubMed:29127155). Activates the ATPase activity of HSP90AA1 leading to increase in its chaperone activity (PubMed:29127155). Competes with the inhibitory co-chaperone FNIP1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:27353360). Competes with the inhibitory co-chaperone TSC1 for binding to HSP90AA1, thereby providing a reciprocal regulatory mechanism for chaperoning of client proteins (PubMed:29127155). {ECO:0000269|PubMed:27353360, ECO:0000269|PubMed:29127155}.
|
Homo sapiens (Human)
|
O95436
|
NPT2B_HUMAN
|
MAPWPELGDAQPNPDKYLEGAAGQQPTAPDKSKETNKTDNTEAPVTKIELLPSYSTATLIDEPTEVDDPWNLPTLQDSGIKWSERDTKGKILCFFQGIGRLILLLGFLYFFVCSLDILSSAFQLVGGKMAGQFFSNSSIMSNPLLGLVIGVLVTVLVQSSSTSTSIVVSMVSSSLLTVRAAIPIIMGANIGTSITNTIVALMQVGDRSEFRRAFAGATVHDFFNWLSVLVLLPVEVATHYLEIITQLIVESFHFKNGEDAPDLLKVITKPFTKLIVQLDKKVISQIAMNDEKAKNKSLVKIWCKTFTNKTQINVTVPSTANCTSPSLCWTDGIQNWTMKNVTYKENIAKCQHIFVNFHLPDLAVGTILLILSLLVLCGCLIMIVKILGSVLKGQVATVIKKTINTDFPFPFAWLTGYLAILVGAGMTFIVQSSSVFTSALTPLIGIGVITIERAYPLTLGSNIGTTTTAILAALASPGNALRSSLQIALCHFFFNISGILLWYPIPFTRLPIRMAKGLGNISAKYRWFAVFYLIIFFFLIPLTVFGLSLAGWRVLVGVGVPVVFIIILVLCLRLLQSRCPRVLPKKLQNWNFLPLWMRSLKPWDAVVSKFTGCFQMRCCCCCRVCCRACCLLCDCPKCCRCSKCCEDLEEAQEGQDVPVKAPETFDNITISREAQGEVPASDSKTECTAL
| null | null |
in utero embryonic development [GO:0001701]; intracellular phosphate ion homeostasis [GO:0030643]; phosphate ion transport [GO:0006817]; protein metabolic process [GO:0019538]; response to estrogen [GO:0043627]; sodium-dependent phosphate transport [GO:0044341]
|
apical plasma membrane [GO:0016324]; brush border [GO:0005903]; brush border membrane [GO:0031526]; membrane [GO:0016020]; plasma membrane [GO:0005886]; vesicle [GO:0031982]
|
phosphate ion binding [GO:0042301]; sodium ion binding [GO:0031402]; sodium:phosphate symporter activity [GO:0005436]
|
PF02690;
| null |
SLC34A transporter family
| null |
SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q9DBP0}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at the brush border membranes of enterocytes. {ECO:0000250|UniProtKB:Q9DBP0}.
|
CATALYTIC ACTIVITY: [Isoform 1]: Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:10329428}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256; Evidence={ECO:0000305|PubMed:10329428}; CATALYTIC ACTIVITY: [Isoform 2]: Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; Evidence={ECO:0000269|PubMed:10610722}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71256; Evidence={ECO:0000305|PubMed:10610722};
| null | null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.6. {ECO:0000269|PubMed:10329428};
| null |
FUNCTION: Involved in actively transporting phosphate into cells via Na(+) cotransport. {ECO:0000269|PubMed:10329428}.
|
Homo sapiens (Human)
|
O95445
|
APOM_HUMAN
|
MFHQIWAALLYFYGIILNSIYQCPEHSQLTTLGVDGKEFPEVHLGQWYFIAGAAPTKEELATFDPVDNIVFNMAAGSAPMQLHLRATIRMKDGLCVPRKWIYHLTEGSTDLRTEGRPDMKTELFSSSCPGGIMLNETGQGYQRFLLYNRSPHPPEKCVEEFKSLTSCLDSKAFLLTPRNQEACELSNN
| null | null |
cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; high-density lipoprotein particle assembly [GO:0034380]; high-density lipoprotein particle clearance [GO:0034384]; high-density lipoprotein particle remodeling [GO:0034375]; lipoprotein metabolic process [GO:0042157]; negative regulation of plasma lipoprotein oxidation [GO:0034445]; reverse cholesterol transport [GO:0043691]
|
discoidal high-density lipoprotein particle [GO:0034365]; extracellular region [GO:0005576]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; spherical high-density lipoprotein particle [GO:0034366]; very-low-density lipoprotein particle [GO:0034361]
|
antioxidant activity [GO:0016209]; lipid transporter activity [GO:0005319]; phospholipid binding [GO:0005543]
|
PF11032;
|
2.40.128.20;
|
Calycin superfamily, Lipocalin family
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17525477, ECO:0000269|PubMed:18279674, ECO:0000269|PubMed:18460466}. Note=Present in high density lipoprotein (HDL) and to a lesser extent in triglyceride-rich lipoproteins (TGRLP) and low density lipoproteins (LDL).
| null | null | null | null | null |
FUNCTION: Probably involved in lipid transport. Can bind sphingosine-1-phosphate, myristic acid, palmitic acid and stearic acid, retinol, all-trans-retinoic acid and 9-cis-retinoic acid. {ECO:0000269|PubMed:17525477, ECO:0000269|PubMed:19733574}.
|
Homo sapiens (Human)
|
O95447
|
LCA5L_HUMAN
|
MSLADLTKTNIDEHFFGVALENNRRSAACKRSPGTGDFSRNSNASNKSVDYSRSQCSCGSLSSQYDYSEDFLCDCSEKAINRNYLKQPVVKEKEKKKYNVSKISQSKGQKEISVEKKHTWNASLFNSQIHMIAQRRDAMAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAIETRKTLAAQTATKTLQVEVKHLQQKLKEKDRELEIKNIYSHRILKNLHDTEDYPKVSSTKSVQADRKILPFTSMRHQGTQKSDVPPLTTKGKKATGNIDHKEKSTEINHEIPHCVNKLPKQEDSKRKYEDLSGEEKHLEVQILLENTGRQKDKKEDQEKKNIFVKEEQELPPKIIEVIHPERESNQEDVLVREKFKRSMQRNGVDDTLGKGTAPYTKGPLRQRRHYSFTEATENLHHGLPASGGPANAGNMRYSHSTGKHLSNREEMELEHSDSGYEPSFGKSSRIKVKDTTFRDKKSSLMEELFGSGYVLKTDQSSPGVAKGSEEPLQSKESHPLPPSQASTSHAFGDSKVTVVNSIKPSSPTEGKRKIII
| null | null |
intraciliary transport [GO:0042073]
|
axoneme [GO:0005930]
| null |
PF15619;
| null |
LCA5 family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O95450
|
ATS2_HUMAN
|
MDPPAGAARRLLCPALLLLLLLLPPPLLPPPPPPANARLAAAADPPGGPLGHGAERILAVPVRTDAQGRLVSHVVSAATSRAGVRARRAAPVRTPSFPGGNEEEPGSHLFYNVTVFGRDLHLRLRPNARLVAPGATMEWQGEKGTTRVEPLLGSCLYVGDVAGLAEASSVALSNCDGLAGLIRMEEEEFFIEPLEKGLAAQEAEQGRVHVVYRRPPTSPPLGGPQALDTGASLDSLDSLSRALGVLEEHANSSRRRARRHAADDDYNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIILLSYGKSMSLIEIGNPSQSLENVCRWAYLQQKPDTGHDEYHDHAIFLTRQDFGPSGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDEVRLGSIMAPLVQAAFHRFHWSRCSQQELSRYLHSYDCLLDDPFAHDWPALPQLPGLHYSMNEQCRFDFGLGYMMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTMCAPGKHCFKGHCIWLTPDILKRDGSWGAWSPFGSCSRTCGTGVKFRTRQCDNPHPANGGRTCSGLAYDFQLCSRQDCPDSLADFREEQCRQWDLYFEHGDAQHHWLPHEHRDAKERCHLYCESRETGEVVSMKRMVHDGTRCSYKDAFSLCVRGDCRKVGCDGVIGSSKQEDKCGVCGGDNSHCKVVKGTFTRSPKKHGYIKMFEIPAGARHLLIQEVDATSHHLAVKNLETGKFILNEENDVDASSKTFIAMGVEWEYRDEDGRETLQTMGPLHGTITVLVIPVGDTRVSLTYKYMIHEDSLNVDDNNVLEEDSVVYEWALKKWSPCSKPCGGGSQFTKYGCRRRLDHKMVHRGFCAALSKPKAIRRACNPQECSQPVWVTGEWEPCSQTCGRTGMQVRSVRCIQPLHDNTTRSVHAKHCNDARPESRRACSRELCPGRWRAGPWSQCSVTCGNGTQERPVLCRTADDSFGICQEERPETARTCRLGPCPRNISDPSKKSYVVQWLSRPDPDSPIRKISSKGHCQGDKSIFCRMEVLSRYCSIPGYNKLCCKSCNLYNNLTNVEGRIEPPPGKHNDIDVFMPTLPVPTVAMEVRPSPSTPLEVPLNASSTNATEDHPETNAVDEPYKIHGLEDEVQPPNLIPRRPSPYEKTRNQRIQELIDEMRKKEMLGKF
|
3.4.24.14
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
collagen catabolic process [GO:0030574]; collagen fibril organization [GO:0030199]; extracellular matrix organization [GO:0030198]; lung development [GO:0030324]; protein processing [GO:0016485]; skin development [GO:0043588]; spermatogenesis [GO:0007283]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]
|
metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; zinc ion binding [GO:0008270]
|
PF17771;PF19236;PF05986;PF01562;PF01421;PF19030;PF00090;
|
2.60.120.830;3.40.1620.60;3.40.390.10;2.20.100.10;
| null |
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.; PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Can also be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}.
|
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=Cleaves the N-propeptide of collagen chain alpha1(I) at Pro-|-Gln and of alpha1(II) and alpha2(I) at Ala-|-Gln.; EC=3.4.24.14;
| null | null | null | null |
FUNCTION: Cleaves the propeptides of type I and II collagen prior to fibril assembly (By similarity). Does not act on type III collagen (By similarity). Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form with reduced collagen-binding activity (PubMed:31152061). {ECO:0000250|UniProtKB:P79331, ECO:0000269|PubMed:31152061}.
|
Homo sapiens (Human)
|
O95452
|
CXB6_HUMAN
|
MDWGTLHTFIGGVNKHSTSIGKVWITVIFIFRVMILVVAAQEVWGDEQEDFVCNTLQPGCKNVCYDHFFPVSHIRLWALQLIFVSTPALLVAMHVAYYRHETTRKFRRGEKRNDFKDIEDIKKQKVRIEGSLWWTYTSSIFFRIIFEAAFMYVFYFLYNGYHLPWVLKCGIDPCPNLVDCFISRPTEKTVFTIFMISASVICMLLNVAELCYLLLKVCFRRSKRAQTQKNHPNHALKESKQNEMNELISDSGQNAITGFPS
| null | null |
cell-cell signaling [GO:0007267]; cellular response to glucose stimulus [GO:0071333]; ear morphogenesis [GO:0042471]; gap junction assembly [GO:0016264]; gap junction-mediated intercellular transport [GO:1990349]; inner ear development [GO:0048839]; maintenance of blood-brain barrier [GO:0035633]; negative regulation of cell population proliferation [GO:0008285]; response to electrical stimulus [GO:0051602]; response to lipopolysaccharide [GO:0032496]; sensory perception of sound [GO:0007605]; sinoatrial node development [GO:0003163]; transmembrane transport [GO:0055085]
|
actin filament [GO:0005884]; apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; connexin complex [GO:0005922]; gap junction [GO:0005921]
|
actin filament binding [GO:0051015]; beta-tubulin binding [GO:0048487]; gap junction channel activity [GO:0005243]; gap junction channel activity involved in cell communication by electrical coupling [GO:1903763]; microtubule binding [GO:0008017]
|
PF00029;
|
1.20.1440.80;
|
Connexin family, Beta-type (group I) subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Cell junction, gap junction.
| null | null | null | null | null |
FUNCTION: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
|
Homo sapiens (Human)
|
O95453
|
PARN_HUMAN
|
MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFTAPSTVGKRNLSPSQEEAGLEDGVSGEISDTELEQTDSCAEPLSEGRKKAKKLKRMKKELSPAGSISKNSPATLFEVPDTW
|
3.1.13.4
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11359775, ECO:0000269|PubMed:15358788}; Note=Divalent metal cations. Mg(2+) is the most probable. {ECO:0000269|PubMed:11359775, ECO:0000269|PubMed:15358788};
|
box H/ACA RNA 3'-end processing [GO:0000495]; female gamete generation [GO:0007292]; miRNA catabolic process [GO:0010587]; ncRNA deadenylation [GO:0110008]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; polyadenylation-dependent snoRNA 3'-end processing [GO:0071051]; positive regulation of telomerase activity [GO:0051973]; positive regulation of telomere maintenance via telomerase [GO:0032212]; regulation of telomerase RNA localization to Cajal body [GO:1904872]; RNA modification [GO:0009451]; telomerase RNA stabilization [GO:0090669]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleus [GO:0005634]; postsynapse [GO:0098794]
|
cation binding [GO:0043169]; metal ion binding [GO:0046872]; mRNA 3'-UTR binding [GO:0003730]; nuclease activity [GO:0004518]; poly(A)-specific ribonuclease activity [GO:0004535]; protein kinase binding [GO:0019901]; RNA binding [GO:0003723]; telomerase RNA binding [GO:0070034]
|
PF04857;PF08675;
|
3.30.70.330;3.30.420.10;
|
CAF1 family
|
PTM: Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress. {ECO:0000269|PubMed:20932473}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9736620}. Cytoplasm {ECO:0000269|PubMed:9736620}. Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:22442037}. Note=Some nuclear fraction is nucleolar.
|
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4; Evidence={ECO:0000269|PubMed:10801819, ECO:0000269|PubMed:9736620};
| null | null | null | null |
FUNCTION: 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization (PubMed:10882133, PubMed:11359775, PubMed:12748283, PubMed:15175153, PubMed:9736620). Also able to recognize and trim poly(A) tails of microRNAs such as MIR21 and H/ACA box snoRNAs (small nucleolar RNAs) leading to microRNAs degradation or snoRNA increased stability (PubMed:22442037, PubMed:25049417). {ECO:0000269|PubMed:10882133, ECO:0000269|PubMed:11359775, ECO:0000269|PubMed:12748283, ECO:0000269|PubMed:15175153, ECO:0000269|PubMed:22442037, ECO:0000269|PubMed:25049417, ECO:0000269|PubMed:9736620}.
|
Homo sapiens (Human)
|
O95456
|
PSMG1_HUMAN
|
MAATFFGEVVKAPCRAGTEDEEEEEEGRRETPEDREVRLQLARKREVRLLRRQTKTSLEVSLLEKYPCSKFIIAIGNNAVAFLSSFVMNSGVWEEVGCAKLWNEWCRTTDTTHLSSTEAFCVFYHLKSNPSVFLCQCSCYVAEDQQYQWLEKVFGSCPRKNMQITILTCRHVTDYKTSESTGSLPSPFLRALKTQNFKDSACCPLLEQPNIVHDLPAAVLSYCQVWKIPAILYLCYTDVMKLDLITVEAFKPILSTRSLKGLVKNIPQSTEILKKLMTTNEIQSNIYT
| null | null |
cerebellar granule cell precursor proliferation [GO:0021930]; chaperone-mediated protein complex assembly [GO:0051131]; proteasome core complex assembly [GO:0080129]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]
|
molecular adaptor activity [GO:0060090]; proteasome binding [GO:0070628]
|
PF16094;
| null |
PSMG1 family
|
PTM: Degraded by the proteasome upon completion of 20S proteasome maturation.
|
SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum.
| null | null | null | null | null |
FUNCTION: Chaperone protein which promotes assembly of the 20S proteasome as part of a heterodimer with PSMG2. The PSMG1-PSMG2 heterodimer binds to the PSMA5 and PSMA7 proteasome subunits, promotes assembly of the proteasome alpha subunits into the heteroheptameric alpha ring and prevents alpha ring dimerization. {ECO:0000269|PubMed:16251969, ECO:0000269|PubMed:17707236}.
|
Homo sapiens (Human)
|
O95460
|
MATN4_HUMAN
|
MRGLLCWPVLLLLLQPWETQLQLTGPRCHTGPLDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQGTMTGLAIQYAMNVAFSVAEGARPPEERVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLDEHVFLVESFDLIQEFGLQFQSRLCGKDQCAEGGHGCQHQCVNAWAMFHCTCNPGYKLAADNKSCLAIDLCAEGTHGCEHHCVNSPGSYFCHCQVGFVLQQDQRSCRAIDYCSFGNHSCQHECVSTPGGPRCHCREGHDLQPDGRSCQVRDLCNGVDHGCEFQCVSEGLSYRCLCPEGRQLQADGKSCNRCREGHVDLVLLVDGSKSVRPQNFELVKRFVNQIVDFLDVSPEGTRVGLVQFSSRVRTEFPLGRYGTAAEVKQAVLAVEYMERGTMTGLALRHMVEHSFSEAQGARPRALNVPRVGLVFTDGRSQDDISVWAARAKEEGIVMYAVGVGKAVEAELREIASEPAELHVSYAPDFGTMTHLLENLRGSICPEEGISAGTELRSPCECESLVEFQGRTLGALESLTLNLAQLTARLEDLENQLANQK
| null | null |
extracellular matrix organization [GO:0030198]
|
collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; matrilin complex [GO:0120216]
|
calcium ion binding [GO:0005509]
|
PF12662;PF14670;PF10393;PF00092;
|
1.20.5.30;2.10.25.10;3.40.50.410;
| null | null |
SUBCELLULAR LOCATION: Secreted.
| null | null | null | null | null |
FUNCTION: Major component of the extracellular matrix of cartilage.
|
Homo sapiens (Human)
|
O95461
|
LARG1_HUMAN
|
MLGICRGRRKFLAASLSLLCIPAITWIYLFSGSFEDGKPVSLSPLESQAHSPRYTASSQRERESLEVRMREVEEENRALRRQLSLAQGRAPSHRRGNHSKTYSMEEGTGDSENLRAGIVAGNSSECGQQPVVEKCETIHVAIVCAGYNASRDVVTLVKSVLFHRRNPLHFHLIADSIAEQILATLFQTWMVPAVRVDFYNADELKSEVSWIPNKHYSGIYGLMKLVLTKTLPANLERVIVLDTDITFATDIAELWAVFHKFKGQQVLGLVENQSDWYLGNLWKNHRPWPALGRGYNTGVILLLLDKLRKMKWEQMWRLTAERELMGMLSTSLADQDIFNAVIKQNPFLVYQLPCFWNVQLSDHTRSEQCYRDVSDLKVIHWNSPKKLRVKNKHVEFFRNLYLTFLEYDGNLLRRELFGCPSEADVNSENLQKQLSELDEDDLCYEFRRERFTVHRTHLYFLHYEYEPAADSTDVTLVAQLSMDRLQMLEAICKHWEGPISLALYLSDAEAQQFLRYAQGSEVLMSRHNVGYHIVYKEGQFYPVNLLRNVAMKHISTPYMFLSDIDFLPMYGLYEYLRKSVIQLDLANTKKAMIVPAFETLRYRLSFPKSKAELLSMLDMGTLFTFRYHVWTKGHAPTNFAKWRTATTPYRVEWEADFEPYVVVRRDCPEYDRRFVGFGWNKVAHIMELDVQEYEFIVLPNAYMIHMPHAPSFDITKFRSNKQYRICLKTLKEEFQQDMSRRYGFAALKYLTAENNS
|
2.4.-.-; 2.4.1.-; 2.4.2.-
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:25138275}; Note=Binds 2 Mn(2+) ions per subunit. The xylosyltransferase part binds one Mn(2+) and the beta-1,3-glucuronyltransferase part binds one Mn(2+). {ECO:0000269|PubMed:25138275};
|
acetylcholine receptor signaling pathway [GO:0095500]; astrocyte differentiation [GO:0048708]; basement membrane organization [GO:0071711]; behavioral fear response [GO:0001662]; blood vessel development [GO:0001568]; bone development [GO:0060348]; cardiac muscle cell development [GO:0055013]; connective tissue development [GO:0061448]; cytoskeleton organization [GO:0007010]; dentate gyrus development [GO:0021542]; determination of adult lifespan [GO:0008340]; gene expression [GO:0010467]; glycoprotein biosynthetic process [GO:0009101]; glycosphingolipid biosynthetic process [GO:0006688]; intracellular protein transport [GO:0006886]; localization of cell [GO:0051674]; long-term synaptic potentiation [GO:0060291]; macrophage differentiation [GO:0030225]; memory [GO:0007613]; multicellular organism growth [GO:0035264]; multicellular organism reproduction [GO:0032504]; muscle cell cellular homeostasis [GO:0046716]; myelination [GO:0042552]; N-acetylglucosamine metabolic process [GO:0006044]; nerve development [GO:0021675]; neuromuscular process controlling posture [GO:0050884]; neuromuscular synaptic transmission [GO:0007274]; neuron migration [GO:0001764]; plasma membrane organization [GO:0007009]; post-embryonic hindlimb morphogenesis [GO:0035129]; post-translational protein modification [GO:0043687]; potassium ion transmembrane transport [GO:0071805]; principal sensory nucleus of trigeminal nerve development [GO:0021740]; protein glycosylation [GO:0006486]; protein localization to plasma membrane [GO:0072659]; protein O-linked glycosylation [GO:0006493]; protein O-linked mannosylation [GO:0035269]; protein targeting to membrane [GO:0006612]; protein-containing complex assembly [GO:0065003]; reactive gliosis [GO:0150103]; response to light stimulus [GO:0009416]; response to mechanical stimulus [GO:0009612]; retina layer formation [GO:0010842]; retina vasculature development in camera-type eye [GO:0061298]; sensory perception of sound [GO:0007605]; skeletal muscle fiber development [GO:0048741]; skeletal muscle fiber differentiation [GO:0098528]; skeletal muscle organ development [GO:0060538]; skeletal muscle tissue regeneration [GO:0043403]; striated muscle cell development [GO:0055002]; striated muscle contraction [GO:0006941]; synaptic assembly at neuromuscular junction [GO:0051124]; walking behavior [GO:0090659]; water transport [GO:0006833]
|
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
acetylglucosaminyltransferase activity [GO:0008375]; glucuronosyltransferase activity [GO:0015020]; glycosyltransferase activity [GO:0016757]; hexosyltransferase activity [GO:0016758]; manganese ion binding [GO:0030145]; UDP-xylosyltransferase activity [GO:0035252]; xylosyltransferase activity [GO:0042285]
|
PF13896;PF01501;
| null |
Glycosyltransferase 49 family; Glycosyltransferase 8 family
| null |
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15958417, ECO:0000269|PubMed:25279699}; Single-pass type II membrane protein {ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15958417}.
|
CATALYTIC ACTIVITY: Reaction=3-O-[beta-D-GlcA-(1->3)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + UDP-alpha-D-xylose = 3-O-[alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + H(+) + UDP; Xref=Rhea:RHEA:57336, Rhea:RHEA-COMP:17482, Rhea:RHEA-COMP:17483, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:177336, ChEBI:CHEBI:177352; Evidence={ECO:0000269|PubMed:22223806, ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:57337; Evidence={ECO:0000305|PubMed:22223806, ECO:0000305|PubMed:25279697, ECO:0000305|PubMed:25279699}; CATALYTIC ACTIVITY: Reaction=3-O-{(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + UDP-alpha-D-glucuronate = 3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + H(+) + UDP; Xref=Rhea:RHEA:67924, Rhea:RHEA-COMP:17484, Rhea:RHEA-COMP:17486, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:177354, ChEBI:CHEBI:177355; Evidence={ECO:0000269|PubMed:22223806, ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:25138275, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:32975514}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67925; Evidence={ECO:0000305|PubMed:22223806, ECO:0000305|PubMed:25138275, ECO:0000305|PubMed:25279697, ECO:0000305|PubMed:25279699, ECO:0000305|PubMed:32975514}; CATALYTIC ACTIVITY: Reaction=3-O-{beta-D-GlcA-(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + UDP-alpha-D-xylose = 3-O-{(1->[3)-alpha-D-Xyl-(1->3)-beta-D-GlcA-(1->](n+1)-4)-beta-D-Xyl-(1->4)-Rib-ol-P-Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-O-6-P-alpha-D-Man}-L-Thr-[protein] + H(+) + UDP; Xref=Rhea:RHEA:68368, Rhea:RHEA-COMP:17485, Rhea:RHEA-COMP:17486, ChEBI:CHEBI:15378, ChEBI:CHEBI:57632, ChEBI:CHEBI:58223, ChEBI:CHEBI:177354, ChEBI:CHEBI:177355; Evidence={ECO:0000269|PubMed:22223806, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68369; Evidence={ECO:0000305|PubMed:22223806, ECO:0000305|PubMed:25279697, ECO:0000305|PubMed:25279699};
| null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699}.
|
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5 for xylosyltransferase activity. Optimum pH is from 5.5 to 8.0 for Beta-1,3-glucuronyltransferase activity. {ECO:0000269|PubMed:23125099};
| null |
FUNCTION: Bifunctional glycosyltransferase with both alpha-1,3-xylosyltransferase and beta-1,3-glucuronyltransferase activities involved in the maturation of alpha-dystroglycan (DAG1) by glycosylation leading to DAG1 binding to laminin G-like domain-containing extracellular proteins with high affinity (PubMed:15661757, PubMed:15752776, PubMed:21987822, PubMed:22223806, PubMed:23125099, PubMed:25279697, PubMed:25279699). Elongates the glucuronyl-beta-1,4-xylose-beta disaccharide primer structure initiated by B4GAT1 by adding repeating units [-3-Xylose-alpha-1,3-GlcA-beta-1-] to produce a heteropolysaccharide (PubMed:22223806, PubMed:23125099, PubMed:25138275, PubMed:25279697, PubMed:25279699, PubMed:32975514). Requires the phosphorylation of core M3 (O-mannosyl trisaccharide) by POMK to elongate the glucuronyl-beta-1,4-xylose-beta disaccharide primer (PubMed:21987822). Plays a key role in skeletal muscle function and regeneration (By similarity). {ECO:0000250|UniProtKB:Q9Z1M7, ECO:0000269|PubMed:15661757, ECO:0000269|PubMed:15752776, ECO:0000269|PubMed:21987822, ECO:0000269|PubMed:22223806, ECO:0000269|PubMed:23125099, ECO:0000269|PubMed:25138275, ECO:0000269|PubMed:25279697, ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:32975514}.
|
Homo sapiens (Human)
|
O95466
|
FMNL1_HUMAN
|
MGNAAGSAEQPAGPAAPPPKQPAPPKQPMPAAGELEERFNRALNCMNLPPDKVQLLSQYDNEKKWELICDQERFQVKNPPAAYIQKLKSYVDTGGVSRKVAADWMSNLGFKRRVQESTQVLRELETSLRTNHIGWVQEFLNEENRGLDVLLEYLAFAQCSVTYDMESTDNGASNSEKNKPLEQSVEDLSKGPPSSVPKSRHLTIKLTPAHSRKALRNSRIVSQKDDVHVCIMCLRAIMNYQSGFSLVMNHPACVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHDIILAAFDNFKEVCGEQHRFEKLMEYFRNEDSNIDFMVACMQFINIVVHSVENMNFRVFLQYEFTHLGLDLYLERLRLTESDKLQVQIQAYLDNIFDVGALLEDTETKNAVLEHMEELQEQVALLTERLRDAENESMAKIAELEKQLSQARKELETLRERFSESTAMGPSRRPPEPEKAPPAAPTRPSALELKVEELEEKGLIRILRGPGDAVSIEILPVAVATPSGGDAPTPGVPTGSPSPDLAPAAEPAPGAAPPPPPPLPGLPSPQEAPPSAPPQAPPLPGSPEPPPAPPLPGDLPPPPPPPPPPPGTDGPVPPPPPPPPPPPGGPPDALGRRDSELGPGVKAKKPIQTKFRMPLLNWVALKPSQITGTVFTELNDEKVLQELDMSDFEEQFKTKSQGPSLDLSALKSKAAQKAPSKATLIEANRAKNLAITLRKGNLGAERICQAIEAYDLQALGLDFLELLMRFLPTEYERSLITRFEREQRPMEELSEEDRFMLCFSRIPRLPERMTTLTFLGNFPDTAQLLMPQLNAIIAASMSIKSSDKLRQILEIVLAFGNYMNSSKRGAAYGFRLQSLDALLEMKSTDRKQTLLHYLVKVIAEKYPQLTGFHSDLHFLDKAGSVSLDSVLADVRSLQRGLELTQREFVRQDDCMVLKEFLRANSPTMDKLLADSKTAQEAFESVVEYFGENPKTTSPGLFFSLFSRFIKAYKKAEQEVEQWKKEAAAQEAGADTPGKGEPPAPKSPPKARRPQMDLISELKRRQQKEPLIYESDRDGAIEDIITVIKTVPFTARTGKRTSRLLCEASLGEEMPL
| null | null |
actin filament severing [GO:0051014]; cell migration [GO:0016477]; cortical actin cytoskeleton organization [GO:0030866]; regulation of cell shape [GO:0008360]
|
bleb [GO:0032059]; cell cortex [GO:0005938]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]
|
actin filament binding [GO:0051015]; GTPase activating protein binding [GO:0032794]; small GTPase binding [GO:0031267]
|
PF06367;PF06371;PF02181;
|
1.20.58.2220;1.25.10.10;
|
Formin homology family
|
PTM: Myristoylation mediates membrane localization and blebbing. {ECO:0000269|PubMed:19815554}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000269|PubMed:19815554}; Lipid-anchor {ECO:0000269|PubMed:19815554}. Cytoplasmic vesicle, phagosome {ECO:0000250}. Note=Recruited to actin-rich phagosomes during phagocytosis. Translocates to the plasma membrane upon activation by RAC1 (By similarity). {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm, cell cortex. Cell projection, bleb. Note=Colocalized with F-actin in bleb protrusions.
| null | null | null | null | null |
FUNCTION: May play a role in the control of cell motility and survival of macrophages (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the cortical actin filament dynamics and cell shape. {ECO:0000250, ECO:0000269|PubMed:21834987}.
|
Homo sapiens (Human)
|
O95467
|
GNAS3_HUMAN
|
MDRRSRAQQWRRARHNYNDLCPPIGRRAATALLWLSCSIALLRALATSNARAQQRAAAQQRRSFLNAHHRSGAQVFPESPESESDHEHEEADLELSLPECLEYEEEFDYETESETESEIESETDFETEPETAPTTEPETEPEDDRGPVVPKHSTFGQSLTQRLHALKLRSPDASPSRAPPSTQEPQSPREGEELKPEDKDPRDPEESKEPKEEKQRRRCKPKKPTRRDASPESPSKKGPIPIRRH
| null | null |
female pregnancy [GO:0007565]; negative regulation of multicellular organism growth [GO:0040015]; positive regulation of cold-induced thermogenesis [GO:0120162]; protein secretion [GO:0009306]; response to parathyroid hormone [GO:0071107]
|
cytoplasm [GO:0005737]; extracellular region [GO:0005576]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; transport vesicle [GO:0030133]
| null |
PF06390;
| null |
NESP55 family
|
PTM: Binds keratan sulfate chains. {ECO:0000250|UniProtKB:O18979}.; PTM: May be proteolytically processed to give rise to a number of active peptides. {ECO:0000269|PubMed:10729789}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000250}. Secreted {ECO:0000250}. Note=Neuroendocrine secretory granules. {ECO:0000250}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O95470
|
SGPL1_HUMAN
|
MPSTDLLMLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFVFQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQGLSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGGFLIVFMEKAGYPLEHPFDFRVKGVTSISADTHKYGYAPKGSSLVLYSDKKYRNYQFFVDTDWQGGIYASPTIAGSRPGGISAACWAALMHFGENGYVEATKQIIKTARFLKSELENIKGIFVFGNPQLSVIALGSRDFDIYRLSNLMTAKGWNLNQLQFPPSIHFCITLLHARKRVAIQFLKDIRESVTQIMKNPKAKTTGMGAIYGMAQTTVDRNMVAELSSVFLDSLYSTDTVTQGSQMNGSPKPH
|
4.1.2.27
|
COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:24809814};
|
androgen metabolic process [GO:0008209]; apoptotic signaling pathway [GO:0097190]; ceramide metabolic process [GO:0006672]; coenzyme A biosynthetic process [GO:0015937]; estrogen metabolic process [GO:0008210]; face morphogenesis [GO:0060325]; fatty acid metabolic process [GO:0006631]; fibroblast migration [GO:0010761]; hemopoiesis [GO:0030097]; kidney development [GO:0001822]; Leydig cell differentiation [GO:0033327]; luteinization [GO:0001553]; platelet-derived growth factor receptor signaling pathway [GO:0048008]; post-embryonic development [GO:0009791]; regulation of multicellular organism growth [GO:0040014]; roof of mouth development [GO:0060021]; skeletal system morphogenesis [GO:0048705]; spermatogenesis [GO:0007283]; sphingolipid catabolic process [GO:0030149]; vasculogenesis [GO:0001570]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
|
aspartate 1-decarboxylase activity [GO:0004068]; pyridoxal phosphate binding [GO:0030170]; sphinganine-1-phosphate aldolase activity [GO:0008117]
|
PF00282;
|
6.10.140.2150;3.90.1150.10;3.40.640.10;
|
Group II decarboxylase family, Sphingosine-1-phosphate lyase subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14570870}; Single-pass type III membrane protein {ECO:0000255}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8R0X7}.
|
CATALYTIC ACTIVITY: Reaction=sphinganine 1-phosphate = hexadecanal + phosphoethanolamine; Xref=Rhea:RHEA:18593, ChEBI:CHEBI:17600, ChEBI:CHEBI:57939, ChEBI:CHEBI:58190; EC=4.1.2.27; Evidence={ECO:0000269|PubMed:11018465, ECO:0000269|PubMed:22784711, ECO:0000269|PubMed:24809814, ECO:0000269|PubMed:28165339}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18594; Evidence={ECO:0000269|PubMed:11018465, ECO:0000269|PubMed:22784711}; CATALYTIC ACTIVITY: Reaction=sphing-4-enine 1-phosphate = (2E)-hexadecenal + phosphoethanolamine; Xref=Rhea:RHEA:33507, ChEBI:CHEBI:17585, ChEBI:CHEBI:58190, ChEBI:CHEBI:60119; EC=4.1.2.27; Evidence={ECO:0000269|PubMed:22784711}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33508; Evidence={ECO:0000269|PubMed:22784711};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.2 uM for sphingosine 1-phosphate {ECO:0000269|PubMed:24809814};
|
PATHWAY: Lipid metabolism; sphingolipid metabolism. {ECO:0000269|PubMed:11018465, ECO:0000269|PubMed:24809814, ECO:0000269|PubMed:28165339}.
| null | null |
FUNCTION: Cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine. Elevates stress-induced ceramide production and apoptosis (PubMed:11018465, PubMed:14570870, PubMed:24809814, PubMed:28165339). Required for global lipid homeostasis in liver and cholesterol homeostasis in fibroblasts. Involved in the regulation of pro-inflammatory response and neutrophil trafficking. Modulates neuronal autophagy via phosphoethanolamine production which regulates accumulation of aggregate-prone proteins such as APP (By similarity). Seems to play a role in establishing neuronal contact sites and axonal maintenance (By similarity). {ECO:0000250|UniProtKB:Q8R0X7, ECO:0000250|UniProtKB:Q9V7Y2, ECO:0000269|PubMed:11018465, ECO:0000269|PubMed:14570870, ECO:0000269|PubMed:24809814, ECO:0000269|PubMed:28165339}.
|
Homo sapiens (Human)
|
O95471
|
CLD7_HUMAN
|
MANSGLQLLGFSMALLGWVGLVACTAIPQWQMSSYAGDNIITAQAMYKGLWMDCVTQSTGMMSCKMYDSVLALSAALQATRALMVVSLVLGFLAMFVATMGMKCTRCGGDDKVKKARIAMGGGIIFIVAGLAALVACSWYGHQIVTDFYNPLIPTNIKYEFGPAIFIGWAGSALVILGGALLSCSCPGNESKAGYRVPRSYPKSNSSKEYV
| null | null |
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell adhesion [GO:0007162]; negative regulation of protein-containing complex assembly [GO:0031333]; positive regulation of cell motility [GO:2000147]; positive regulation of cell population proliferation [GO:0008284]; response to ethanol [GO:0045471]
|
apicolateral plasma membrane [GO:0016327]; basolateral plasma membrane [GO:0016323]; bicellular tight junction [GO:0005923]; lateral plasma membrane [GO:0016328]; plasma membrane [GO:0005886]
|
cell adhesion molecule binding [GO:0050839]; identical protein binding [GO:0042802]; protein domain specific binding [GO:0019904]; structural molecule activity [GO:0005198]
|
PF00822;
|
1.20.140.150;
|
Claudin family
|
PTM: Phosphorylated. {ECO:0000269|PubMed:16054130}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12673207, ECO:0000269|PubMed:14502431, ECO:0000269|PubMed:20375010}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000269|PubMed:16054130}. Cell junction, tight junction {ECO:0000269|PubMed:16054130}. Note=Co-localizes with EPCAM at the basolateral cell membrane and tight junction. {ECO:0000269|PubMed:16054130}.
| null | null | null | null | null |
FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. {ECO:0000250}.
|
Homo sapiens (Human)
|
O95475
|
SIX6_HUMAN
|
MFQLPILNFSPQQVAGVCETLEESGDVERLGRFLWSLPVAPAACEALNKNESVLRARAIVAFHGGNYRELYHILENHKFTKESHAKLQALWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRHLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQQQVLSQGSGRALRAEGDGTPEVLGVATSPAASLSSKAATSAISITSSDSECDI
| null | null |
animal organ morphogenesis [GO:0009887]; eye development [GO:0001654]; regulation of transcription by RNA polymerase II [GO:0006357]; visual perception [GO:0007601]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837]
|
PF00046;PF16878;
|
1.10.10.60;
|
SIX/Sine oculis homeobox family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
| null | null | null | null | null |
FUNCTION: May be involved in eye development.
|
Homo sapiens (Human)
|
O95476
|
CNEP1_HUMAN
|
MMRTQCLLGLRTFVAFAAKLWSFFIYLLRRQIRTVIQYQTVRYDILPLSPVSRNRLAQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQHCTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRLW
|
3.1.3.16
| null |
canonical Wnt signaling pathway [GO:0060070]; gamete generation [GO:0007276]; mesoderm development [GO:0007498]; mitotic nuclear membrane disassembly [GO:0007077]; nuclear envelope organization [GO:0006998]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of triglyceride biosynthetic process [GO:0010867]; protein dephosphorylation [GO:0006470]; protein localization to nucleus [GO:0034504]
|
cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; lipid droplet [GO:0005811]; Nem1-Spo7 phosphatase complex [GO:0071595]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]
|
myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722]
|
PF03031;
|
3.40.50.1000;
|
Dullard family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
|
CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] + phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474, ChEBI:CHEBI:61977; EC=3.1.3.16;
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 mM for p-nitrophenylphosphate {ECO:0000269|PubMed:17420445};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. {ECO:0000269|PubMed:17420445};
| null |
FUNCTION: Serine/threonine protein phosphatase forming with CNEP1R1 an active phosphatase complex that dephosphorylates and may activate LPIN1 and LPIN2. LPIN1 and LPIN2 are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol. May antagonize BMP signaling. {ECO:0000269|PubMed:17420445, ECO:0000269|PubMed:22134922}.
|
Homo sapiens (Human)
|
O95477
|
ABCA1_HUMAN
|
MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLESSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSRDNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKSMELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLCVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIEAVFPGQYGIPRPWYFPCTKSYWFGEESDEKSHPGSNQKRISEICMEEEPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVESSLSSCRNSSSTVSYLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDRLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGTLPARRNRRAFGDKQSCLRPFTEDDAADPNDSDIDPESRETDLLSGMDGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWMYNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCQAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPACQCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGVSNTQALPPSQEVNDAIKQMKKHLKLAKDSSADRFLNSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGINGSVATFVLELFTDNKLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKPVQDFFGLAFPGSVLKEKHRNMLQYQLPSSLSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDDHLKDLSLHKNQTVVDVAVLTSFLQDEKVKESYV
|
7.6.2.1
| null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cellular response to cholesterol [GO:0071397]; cellular response to cytokine stimulus [GO:0071345]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cellular response to retinoic acid [GO:0071300]; cellular response to xenobiotic stimulus [GO:0071466]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; endosomal transport [GO:0016197]; export across plasma membrane [GO:0140115]; G protein-coupled receptor signaling pathway [GO:0007186]; high-density lipoprotein particle assembly [GO:0034380]; intracellular cholesterol transport [GO:0032367]; lipoprotein biosynthetic process [GO:0042158]; lysosome organization [GO:0007040]; negative regulation of cholesterol storage [GO:0010887]; negative regulation of macrophage derived foam cell differentiation [GO:0010745]; peptide secretion [GO:0002790]; phagocytosis, engulfment [GO:0006911]; phospholipid efflux [GO:0033700]; phospholipid homeostasis [GO:0055091]; phospholipid translocation [GO:0045332]; platelet dense granule organization [GO:0060155]; positive regulation of cholesterol efflux [GO:0010875]; positive regulation of high-density lipoprotein particle assembly [GO:0090108]; protein secretion [GO:0009306]; protein transmembrane transport [GO:0071806]; regulation of Cdc42 protein signal transduction [GO:0032489]; regulation of high-density lipoprotein particle assembly [GO:0090107]; response to laminar fluid shear stress [GO:0034616]; response to vitamin B3 [GO:0033552]; reverse cholesterol transport [GO:0043691]; signal release [GO:0023061]
|
basolateral plasma membrane [GO:0016323]; endocytic vesicle [GO:0030139]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; intracellular vesicle [GO:0097708]; membrane raft [GO:0045121]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]
|
ABC-type transporter activity [GO:0140359]; apolipoprotein A-I binding [GO:0034186]; apolipoprotein A-I receptor activity [GO:0034188]; apolipoprotein binding [GO:0034185]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase binding [GO:0051117]; ATPase-coupled transmembrane transporter activity [GO:0042626]; cholesterol binding [GO:0015485]; cholesterol transfer activity [GO:0120020]; floppase activity [GO:0140328]; high-density lipoprotein particle binding [GO:0008035]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine floppase activity [GO:0090554]; phosphatidylserine floppase activity [GO:0090556]; phospholipid transporter activity [GO:0005548]; protein transmembrane transporter activity [GO:0008320]; signaling receptor binding [GO:0005102]; small GTPase binding [GO:0031267]; sphingolipid floppase activity [GO:0046623]; syntaxin binding [GO:0019905]
|
PF12698;PF00005;
|
3.40.50.300;
|
ABC transporter superfamily, ABCA family
|
PTM: Phosphorylation on Ser-2054 regulates phospholipid efflux. {ECO:0000269|PubMed:12196520}.; PTM: Palmitoylated by ZDHHC8 (PubMed:19556522). Palmitoylation is essential for localization to the plasma membrane (PubMed:19556522). {ECO:0000269|PubMed:19556522}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19258317, ECO:0000269|PubMed:19556522, ECO:0000269|PubMed:24097981, ECO:0000269|PubMed:35974019}; Multi-pass membrane protein {ECO:0000255}. Endosome {ECO:0000269|PubMed:24097981}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:24097981}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57643, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24097981, ECO:0000269|PubMed:35974019}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38585; Evidence={ECO:0000305|PubMed:24097981}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24097981}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38569; Evidence={ECO:0000305|PubMed:24097981}; CATALYTIC ACTIVITY: Reaction=a sphingomyelin(in) + ATP + H2O = a sphingomyelin(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38903, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17636, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24097981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38904; Evidence={ECO:0000269|PubMed:24097981}; CATALYTIC ACTIVITY: Reaction=ATP + cholesterol(in) + H2O = ADP + cholesterol(out) + H(+) + phosphate; Xref=Rhea:RHEA:39051, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16113, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:35974019, ECO:0000305|PubMed:10533863, ECO:0000305|PubMed:14754908, ECO:0000305|PubMed:24097981}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39052; Evidence={ECO:0000305|PubMed:10533863, ECO:0000305|PubMed:14754908, ECO:0000305|PubMed:24097981};
| null | null | null | null |
FUNCTION: Catalyzes the translocation of specific phospholipids from the cytoplasmic to the extracellular/lumenal leaflet of membrane coupled to the hydrolysis of ATP (PubMed:24097981, PubMed:35974019). Thereby, participates in phospholipid transfer to apolipoproteins to form nascent high density lipoproteins/HDLs (PubMed:14754908). Transports preferentially phosphatidylcholine over phosphatidylserine (PubMed:24097981). May play a similar role in the efflux of intracellular cholesterol to apolipoproteins and the formation of nascent high density lipoproteins/HDLs (PubMed:10533863, PubMed:14754908, PubMed:24097981, PubMed:35974019). Translocates phospholipids from the outer face of the plasma membrane and forces it through its gateway and annulus into an elongated hydrophobic tunnel in its extracellular domain (PubMed:35974019). {ECO:0000269|PubMed:10533863, ECO:0000269|PubMed:14754908, ECO:0000269|PubMed:24097981, ECO:0000269|PubMed:35974019}.
|
Homo sapiens (Human)
|
O95479
|
G6PE_HUMAN
|
MWNMLIVAMCLALLGCLQAQELQGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGRGHSFSFHGAALTAPKQGQELMAKALESLSCPKDMAPSHCAEHKDQFLQLSQYRQLKTAEDYQALNKDIEAQLQHAGLREAGRIFYFSVPPFAYEDIARNINSSCRPGPGAWLRVVLEKPFGHDHFSAQQLATELGTFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEIIMKETVDAEGRTSFYEEYGVIRDVLQNHLTEVLTLVAMELPHNVSSAEAVLRHKLQVFQALRGLQRGSAVVGQYQSYSEQVRRELQKPDSFHSLTPTFAAVLVHIDNLRWEGVPFILMSGKALDERVGYARILFKNQACCVQSEKHWAAAQSQCLPRQLVFHIGHGDLGSPAVLVSRNLFRPSLPSSWKEMEGPPGLRLFGSPLSDYYAYSPVRERDAHSVLLSHIFHGRKNFFITTENLLASWNFWTPLLESLAHKAPRLYPGGAENGRLLDFEFSSGRLFFSQQQPEQLVPGPGPAPMPSDFQVLRAKYRESPLVSAWSEELISKLANDIEATAVRAVRRFGQFHLALSGGSSPVALFQQLATAHYGFPWAHTHLWLVDERCVPLSDPESNFQGLQAHLLQHVRIPYYNIHPMPVHLQQRLCAEEDQGAQIYAREISALVANSSFDLVLLGMGADGHTASLFPQSPTGLDGEQLVVLTTSPSQPHRRMSLSLPLINRAKKVAVLVMGRMKREITTLVSRVGHEPKKWPISGVLPHSGQLVWYMDYDAFLG
|
1.1.1.363; 1.1.1.47; 3.1.1.31
| null |
glucose metabolic process [GO:0006006]; pentose-phosphate shunt, oxidative branch [GO:0009051]; regulation of cortisol biosynthetic process [GO:2000064]; response to alcohol [GO:0097305]; response to nutrient levels [GO:0031667]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]
|
6-phosphogluconolactonase activity [GO:0017057]; carbohydrate binding [GO:0030246]; glucose 1-dehydrogenase (NAD+) activity [GO:0047934]; glucose 1-dehydrogenase (NADP+) activity [GO:0047935]; glucose 1-dehydrogenase [NAD(P)] activity [GO:0047936]; glucose-6-phosphate dehydrogenase activity [GO:0004345]; NADP binding [GO:0050661]
|
PF02781;PF00479;PF01182;
|
3.40.50.1360;3.40.50.720;
|
Glucose-6-phosphate dehydrogenase family; Glucosamine/galactosamine-6-phosphate isomerase family, 6-phosphogluconolactonase subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000305|PubMed:18628520}.
|
CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.363; Evidence={ECO:0000269|PubMed:18628520, ECO:0000269|PubMed:23132696}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15842; Evidence={ECO:0000305|PubMed:18628520}; CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NAD(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:38215, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:57955, ChEBI:CHEBI:61548; EC=1.1.1.363; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38216; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; CATALYTIC ACTIVITY: Reaction=6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate + H(+); Xref=Rhea:RHEA:12556, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57955, ChEBI:CHEBI:58759; EC=3.1.1.31; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12557; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; CATALYTIC ACTIVITY: Reaction=2-deoxy-D-glucose 6-phosphate + NAD(+) = 2-deoxy-6-phospho-D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:62064, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:84760, ChEBI:CHEBI:145420; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62065; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; CATALYTIC ACTIVITY: Reaction=2-deoxy-D-glucose 6-phosphate + NADP(+) = 2-deoxy-6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:62068, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:84760, ChEBI:CHEBI:145420; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62069; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; CATALYTIC ACTIVITY: Reaction=D-galactose 6-phosphate + NADP(+) = 6-phospho-D-galactono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:62072, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:91004, ChEBI:CHEBI:145419; Evidence={ECO:0000269|PubMed:12858176}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62073; Evidence={ECO:0000305|PubMed:12858176}; CATALYTIC ACTIVITY: Reaction=D-galactose 6-phosphate + NAD(+) = 6-phospho-D-galactono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:62076, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:91004, ChEBI:CHEBI:145419; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62077; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; CATALYTIC ACTIVITY: Reaction=D-glucosamine 6-phosphate + NADP(+) = 2-amino-2-deoxy-6-phospho-D-glucono-1,5-lactone + 2 H(+) + NADPH; Xref=Rhea:RHEA:62088, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58725, ChEBI:CHEBI:145423; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62089; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; CATALYTIC ACTIVITY: Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14294; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; CATALYTIC ACTIVITY: Reaction=D-glucose + NADP(+) = D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:14405, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.47; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14406; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; CATALYTIC ACTIVITY: Reaction=D-glucose 6-sulfate + NADP(+) = 6-sulfo-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:62080, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:145424, ChEBI:CHEBI:145427; Evidence={ECO:0000250|UniProtKB:Q8CFX1}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:62081; Evidence={ECO:0000250|UniProtKB:Q8CFX1};
| null |
PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000269|PubMed:12858176, ECO:0000269|PubMed:18628520, ECO:0000269|PubMed:23132696}.; PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 2/3. {ECO:0000250|UniProtKB:Q8CFX1}.; PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage). {ECO:0000250|UniProtKB:Q8CFX1}.
| null | null |
FUNCTION: Bifunctional enzyme localized in the lumen of the endoplasmic reticulum that catalyzes the first two steps of the oxidative branch of the pentose phosphate pathway/shunt, an alternative to glycolysis and a major source of reducing power and metabolic intermediates for biosynthetic processes (By similarity). Has a hexose-6-phosphate dehydrogenase activity, with broad substrate specificity compared to glucose-6-phosphate 1-dehydrogenase/G6PD, and catalyzes the first step of the pentose phosphate pathway (PubMed:12858176, PubMed:18628520, PubMed:23132696). In addition, acts as a 6-phosphogluconolactonase and catalyzes the second step of the pentose phosphate pathway (By similarity). May have a dehydrogenase activity for alternative substrates including glucosamine 6-phosphate and glucose 6-sulfate (By similarity). The main function of this enzyme is to provide reducing equivalents such as NADPH to maintain the adequate levels of reductive cofactors in the oxidizing environment of the endoplasmic reticulum (PubMed:12858176, PubMed:18628520, PubMed:23132696). By producing NADPH that is needed by reductases of the lumen of the endoplasmic reticulum like corticosteroid 11-beta-dehydrogenase isozyme 1/HSD11B1, indirectly regulates their activity (PubMed:18628520). {ECO:0000250|UniProtKB:Q8CFX1, ECO:0000269|PubMed:12858176, ECO:0000269|PubMed:18628520, ECO:0000269|PubMed:23132696}.
|
Homo sapiens (Human)
|
O95484
|
CLD9_HUMAN
|
MASTGLELLGMTLAVLGWLGTLVSCALPLWKVTAFIGNSIVVAQVVWEGLWMSCVVQSTGQMQCKVYDSLLALPQDLQAARALCVIALLLALLGLLVAITGAQCTTCVEDEGAKARIVLTAGVILLLAGILVLIPVCWTAHAIIQDFYNPLVAEALKRELGASLYLGWAAAALLMLGGGLLCCTCPPPQVERPRGPRLGYSIPSRSGASGLDKRDYV
| null | null |
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]
|
bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]; virus receptor activity [GO:0001618]
|
PF00822;
|
1.20.140.150;
|
Claudin family
| null |
SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane {ECO:0000269|PubMed:20375010, ECO:0000269|PubMed:31175426}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250|UniProtKB:O95832}.; FUNCTION: (Microbial infection) Acts as a receptor for hepatitis C virus (HCV) entry into hepatic cells. {ECO:0000269|PubMed:17804490, ECO:0000269|PubMed:20375010}.
|
Homo sapiens (Human)
|
O95486
|
SC24A_HUMAN
|
MSQPGIPASGGAPASLQAQNGAALASGSPYTNGPVQNALLSSQESVSQGYNFQLPGSYPHPIPAKTLNPVSGQSNYGGSQGSGQTLNRPPVASNPVTPSLHSGPAPRMPLPASQNPATTPMPSSSFLPEANLPPPLNWQYNYPSTASQTNHCPRASSQPTVSGNTSLTTNHQYVSSGYPSLQNSFIKSGPSVPPLVNPPLPTTFQPGAPHGPPPAGGPPPVRALTPLTSSYRDVPQPLFNSAVNQEGITSNTNNGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSVGYSYPSLPPGYQNTTPPGATGVPPSSLNYPSGPQAFTQTPLGANHLTTSMSGLSLQPEGLRVVNLLQERNMLPSTPLKPPVPNLHEDIQKLNCNPELFRCTLTSIPQTQALLNKAKLPLGLLLHPFKDLVQLPVVTSSTIVRCRSCRTYINPFVSFLDQRRWKCNLCYRVNDVPEEFLYNPLTRVYGEPHRRPEVQNATIEFMAPSEYMLRPPQPPVYLFVFDVSHNAVETGYLNSVCQSLLDNLDLLPGNTRTKIGFITFDSTIHFYGLQESLSQPQMLIVSDIEDVFIPMPENLLVNLNESKELVQDLLKTLPQMFTKTLETQSALGPALQAAFKLMSPTGGRMSVFQTQLPTLGVGALKPREEPNHRSSAKDIHMTPSTDFYKKLALDCSGQQVAVDLFLLSGQYSDLASLGCISRYSAGSVYYYPSYHHQHNPVQVQKLQKELQRYLTRKIGFEAVMRIRCTKGLSIHTFHGNFFVRSTDLLSLPNVNPDAGYAVQMSVEESLTDTQLVSFQSALLYTSSKGERRIRVHTLCLPVVSTLNDVFLGADVQAISGLLANMAVDRSMTASLSDARDALVNAVIDSLSAYRSSVLSNQQPGLMVPFSLRLFPLFVLALLKQKSFQTGTNARLDERIFAMCQVKNQPLVYLMLTTHPSLYRVDNLSDEGALNISDRTIPQPPILQLSVEKLSRDGAFLMDAGSVLMLWVGKNCTQNFLSQVLGVQNYASIPQPMTDLPELDTPESARIIAFISWLREQRPFFPILYVIRDESPMKANFLQNMIEDRTESALSYYEFLLHIQQQVNK
| null | null |
cholesterol homeostasis [GO:0042632]; COPII-coated vesicle cargo loading [GO:0090110]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; positive regulation of protein secretion [GO:0050714]; regulation of cholesterol transport [GO:0032374]
|
COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]
|
SNARE binding [GO:0000149]; zinc ion binding [GO:0008270]
|
PF00626;PF08033;PF04815;PF04811;PF04810;
|
2.60.40.1670;1.20.120.730;3.40.20.10;3.40.50.410;2.30.30.380;
|
SEC23/SEC24 family, SEC24 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000305|PubMed:17499046}; Peripheral membrane protein {ECO:0000305|PubMed:17499046}; Cytoplasmic side {ECO:0000305|PubMed:17499046}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:17499046}; Peripheral membrane protein {ECO:0000305|PubMed:17499046}; Cytoplasmic side {ECO:0000305|PubMed:17499046}. Cytoplasm, cytosol {ECO:0000305|PubMed:17499046}.
| null | null | null | null | null |
FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex (PubMed:17499046, PubMed:18843296, PubMed:20427317). Plays a central role in cargo selection within the COPII complex and together with SEC24B may have a different specificity compared to SEC24C and SEC24D. May package preferentially cargos with cytoplasmic DxE or LxxLE motifs and may also recognize conformational epitopes (PubMed:17499046, PubMed:18843296). {ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
|
Homo sapiens (Human)
|
O95487
|
SC24B_HUMAN
|
MSAPAGSSHPAASARIPPKFGGAAVSGAAAPAGPGAGPAPHQQNGPAQNQMQVPSGYGLHHQNYIAPSGHYSQGPGKMTSLPLDTQCGDYYSALYTVPTQNVTPNTVNQQPGAQQLYSRGPPAPHIVGSTLGSFQGAASSASHLHTSASQPYSSFVNHYNSPAMYSASSSVASQGFPSTCGHYAMSTVSNAAYPSVSYPSLPAGDTYGQMFTSQNAPTVRPVKDNSFSGQNTAISHPSPLPPLPSQQHHQQQSLSGYSTLTWSSPGLPSTQDNLIRNHTGSLAVANNNPTITVADSLSCPVMQNVQPPKSSPVVSTVLSGSSGSSSTRTPPTANHPVEPVTSVTQPSELLQQKGVQYGEYVNNQASSAPTPLSSTSDDEEEEEEDEEAGVDSSSTTSSASPMPNSYDALEGGSYPDMLSSSASSPAPDPAPEPDPASAPAPASAPAPVVPQPSKMAKPFGYGYPTLQPGYQNATAPLISGVQPSNPVYSGFQQYPQQYPGVNQLSSSIGGLSLQSSPQPESLRPVNLTQERNILPMTPVWAPVPNLNADLKKLNCSPDSFRCTLTNIPQTQALLNKAKLPLGLLLHPFRDLTQLPVITSNTIVRCRSCRTYINPFVSFIDQRRWKCNLCYRVNDVPEEFMYNPLTRSYGEPHKRPEVQNSTVEFIASSDYMLRPPQPAVYLFVLDVSHNAVEAGYLTILCQSLLENLDKLPGDSRTRIGFMTFDSTIHFYNLQEGLSQPQMLIVSDIDDVFLPTPDSLLVNLYESKELIKDLLNALPNMFTNTRETHSALGPALQAAFKLMSPTGGRVSVFQTQLPSLGAGLLQSREDPNQRSSTKVVQHLGPATDFYKKLALDCSGQQTAVDLFLLSSQYSDLASLACMSKYSAGCIYYYPSFHYTHNPSQAEKLQKDLKRYLTRKIGFEAVMRIRCTKGLSMHTFHGNFFVRSTDLLSLANINPDAGFAVQLSIEESLTDTSLVCFQTALLYTSSKGERRIRVHTLCLPVVSSLADVYAGVDVQAAICLLANMAVDRSVSSSLSDARDALVNAVVDSLSAYGSTVSNLQHSALMAPSSLKLFPLYVLALLKQKAFRTGTSTRLDDRVYAMCQIKSQPLVHLMKMIHPNLYRIDRLTDEGAVHVNDRIVPQPPLQKLSAEKLTREGAFLMDCGSVFYIWVGKGCDNNFIEDVLGYTNFASIPQKMTHLPELDTLSSERARSFITWLRDSRPLSPILHIVKDESPAKAEFFQHLIEDRTEAAFSYYEFLLHVQQQICK
| null | null |
aorta morphogenesis [GO:0035909]; auditory receptor cell stereocilium organization [GO:0060088]; cochlear nucleus development [GO:0021747]; COPII-coated vesicle cargo loading [GO:0090110]; coronary artery morphogenesis [GO:0060982]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; intracellular protein transport [GO:0006886]; lung lobe morphogenesis [GO:0060463]; neural tube closure [GO:0001843]; outflow tract morphogenesis [GO:0003151]; pulmonary artery morphogenesis [GO:0061156]; regulation of cargo loading into COPII-coated vesicle [GO:1901301]; regulation of establishment of planar polarity involved in neural tube closure [GO:0090178]
|
COPII vesicle coat [GO:0030127]; cytosol [GO:0005829]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; ER to Golgi transport vesicle membrane [GO:0012507]
|
SNARE binding [GO:0000149]; zinc ion binding [GO:0008270]
|
PF00626;PF08033;PF04815;PF04811;PF04810;
|
2.60.40.1670;1.20.120.730;3.40.20.10;3.40.50.410;2.30.30.380;
|
SEC23/SEC24 family, SEC24 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10075675}; Peripheral membrane protein {ECO:0000305|PubMed:10075675}; Cytoplasmic side {ECO:0000305|PubMed:10075675}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:10075675}; Peripheral membrane protein {ECO:0000269|PubMed:10075675}; Cytoplasmic side {ECO:0000269|PubMed:10075675}. Cytoplasm, cytosol {ECO:0000269|PubMed:10075675}.
| null | null | null | null | null |
FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules for their transport to the Golgi complex (PubMed:17499046, PubMed:18843296, PubMed:20427317). Plays a central role in cargo selection within the COPII complex and together with SEC24A may have a different specificity compared to SEC24C and SEC24D. May package preferentially cargos with cytoplasmic DxE or LxxLE motifs and may also recognize conformational epitopes (PubMed:17499046, PubMed:18843296). {ECO:0000269|PubMed:17499046, ECO:0000269|PubMed:18843296, ECO:0000269|PubMed:20427317}.
|
Homo sapiens (Human)
|
O95490
|
AGRL2_HUMAN
|
MVSSGCRMRSLWFIIVISFLPNTEGFSRAALPFGLVRRELSCEGYSIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAFKIMTQRCNNRTQCIVVTGSDVFPDPCPGTYKYLEVQYECVPYIFVCPGTLKAIVDSPCIYEAEQKAGAWCKDPLQAADKIYFMPWTPYRTDTLIEYASLEDFQNSRQTTTYKLPNRVDGTGFVVYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINYANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEQNNGMIVISQLNPYTLRFEATWETVYDKRAASNAFMICGVLYVVRSVYQDNESETGKNSIDYIYNTRLNRGEYVDVPFPNQYQYIAAVDYNPRDNQLYVWNNNFILRYSLEFGPPDPAQVPTTAVTITSSAELFKTIISTTSTTSQKGPMSTTVAGSQEGSKGTKPPPAVSTTKIPPITNIFPLPERFCEALDSKGIKWPQTQRGMMVERPCPKGTRGTASYLCMISTGTWNPKGPDLSNCTSHWVNQLAQKIRSGENAASLANELAKHTKGPVFAGDVSSSVRLMEQLVDILDAQLQELKPSEKDSAGRSYNKLQKREKTCRAYLKAIVDTVDNLLRPEALESWKHMNSSEQAHTATMLLDTLEEGAFVLADNLLEPTRVSMPTENIVLEVAVLSTEGQIQDFKFPLGIKGAGSSIQLSANTVKQNSRNGLAKLVFIIYRSLGQFLSTENATIKLGADFIGRNSTIAVNSHVISVSINKESSRVYLTDPVLFTLPHIDPDNYFNANCSFWNYSERTMMGYWSTQGCKLVDTNKTRTTCACSHLTNFAILMAHREIAYKDGVHELLLTVITWVGIVISLVCLAICIFTFCFFRGLQSDRNTIHKNLCINLFIAEFIFLIGIDKTKYAIACPIFAGLLHFFFLAAFAWMCLEGVQLYLMLVEVFESEYSRKKYYYVAGYLFPATVVGVSAAIDYKSYGTEKACWLHVDNYFIWSFIGPVTFIILLNIIFLVITLCKMVKHSNTLKPDSSRLENIKSWVLGAFALLCLLGLTWSFGLLFINEETIVMAYLFTIFNAFQGVFIFIFHCALQKKVRKEYGKCFRHSYCCGGLPTESPHSSVKASTTRTSARYSSGTQSRIRRMWNDTVRKQSESSFISGDINSTSTLNQGMTGNYLLTNPLLRPHGTNNPYNTLLAETVVCNAPSAPVFNSPGHSLNNARDTSAMDTLPLNGNFNNSYSLHKGDYNDSVQVVDCGLSLNDTAFEKMIISELVHNNLRGSSKTHNLELTLPVKPVIGGSSSEDDAIVADASSLMHSDNPGLELHHKELEAPLIPQRTHSLLYQPQKKVKSEGTDSYVSQLTAEAEDHLQSPNRDSLYTSMPNLRDSPYPESSPDMEEDLSPSRRSENEDIYYKSMPNLGAGHQLQMCYQISRGNSDGYIIPINKEGCIPEGDVREGQMQLVTSL
| null | null |
adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; cell surface receptor signaling pathway [GO:0007166]; G protein-coupled receptor signaling pathway [GO:0007186]
|
membrane [GO:0016020]
|
carbohydrate binding [GO:0030246]; G protein-coupled receptor activity [GO:0004930]; latrotoxin receptor activity [GO:0016524]
|
PF00002;PF16489;PF02140;PF01825;PF02793;PF02354;PF02191;
|
1.25.40.610;2.60.120.740;2.60.220.50;4.10.1240.10;1.20.1070.10;
|
G-protein coupled receptor 2 family, Adhesion G-protein coupled receptor (ADGR) subfamily
|
PTM: Proteolytically cleaved into 2 subunits, an extracellular subunit and a seven-transmembrane subunit. {ECO:0000250|UniProtKB:O88917}.
|
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: Calcium-independent receptor of low affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis. {ECO:0000250|UniProtKB:O88923}.
|
Homo sapiens (Human)
|
O95497
|
VNN1_HUMAN
|
MTTQLPAYVAILLFYVSRASCQDTFTAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNLFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYASSIEALSSGNKEFKGTVFFDEFTFVKLTGVAGNYTVCQKDLCCHLSYKMSENIPNEVYALGAFDGLHTVEGRYYLQICTLLKCKTTNLNTCGDSAETASTRFEMFSLSGTFGTQYVFPEVLLSENQLAPGEFQVSTDGRLFSLKPTSGPVLTVTLFGRLYEKDWASNASSGLTAQARIIMLIVIAPIVCSLSW
|
3.5.1.92
| null |
acute inflammatory response [GO:0002526]; cell-cell adhesion [GO:0098609]; chronic inflammatory response [GO:0002544]; coenzyme A catabolic process [GO:0015938]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; pantothenate metabolic process [GO:0015939]; positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway [GO:1902177]; positive regulation of T cell differentiation in thymus [GO:0033089]; response to oxidative stress [GO:0006979]
|
azurophil granule membrane [GO:0035577]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
pantetheine hydrolase activity [GO:0017159]
|
PF00795;PF19018;
|
3.60.110.10;
|
Carbon-nitrogen hydrolase superfamily, BTD/VNN family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:11491533}; Lipid-anchor, GPI-anchor {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(R)-pantetheine + H2O = (R)-pantothenate + cysteamine; Xref=Rhea:RHEA:13445, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753, ChEBI:CHEBI:29032, ChEBI:CHEBI:58029; EC=3.5.1.92; Evidence={ECO:0000269|PubMed:11491533, ECO:0000269|PubMed:25478849};
| null | null | null | null |
FUNCTION: Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine. {ECO:0000269|PubMed:10567687, ECO:0000269|PubMed:11491533, ECO:0000269|PubMed:25478849}.
|
Homo sapiens (Human)
|
O95498
|
VNN2_HUMAN
|
MVTSSFPISVAVFALITLQVGTQDSFIAAVYEHAVILPNKTETPVSQEDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVNWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSEPQFNVPEKPELVTFNTAFGRFGIFTCFDIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLVANTHHVSLNMTGSGIYAPNGPKVYHYDMKTELGKLLLSEVDSHPLSSLAYPTAVNWNAYATTIKPFPVQKNTFRGFISRDGFNFTELFENAGNLTVCQKELCCHLSYRMLQKEENEVYVLGAFTGLHGRRRREYWQVCTLLKCKTTNLTTCGRPVETASTRFEMFSLSGTFGTEYVFPEVLLTEIHLSPGKFEVLKDGRLVNKNGSSGPILTVSLFGRWYTKDSLYSSCGTSNSAITYLLIFILLMIIALQNIVML
|
3.5.1.92
| null |
pantothenate metabolic process [GO:0015939]
|
extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]
|
pantetheine hydrolase activity [GO:0017159]
|
PF00795;PF19018;
|
3.60.110.10;
|
Carbon-nitrogen hydrolase superfamily, BTD/VNN family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
|
CATALYTIC ACTIVITY: Reaction=(R)-pantetheine + H2O = (R)-pantothenate + cysteamine; Xref=Rhea:RHEA:13445, ChEBI:CHEBI:15377, ChEBI:CHEBI:16753, ChEBI:CHEBI:29032, ChEBI:CHEBI:58029; EC=3.5.1.92; Evidence={ECO:0000269|PubMed:11491533}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13446; Evidence={ECO:0000305|PubMed:11491533};
| null | null | null | null |
FUNCTION: Amidohydrolase that hydrolyzes specifically one of the carboamide linkages in D-pantetheine thus recycling pantothenic acid (vitamin B5) and releasing cysteamine (PubMed:11491533). Involved in the thymus homing of bone marrow cells. May regulate beta-2 integrin-mediated cell adhesion, migration and motility of neutrophil. {ECO:0000269|PubMed:11491533}.
|
Homo sapiens (Human)
|
O95500
|
CLD14_HUMAN
|
MASTAVQLLGFLLSFLGMVGTLITTILPHWRRTAHVGTNILTAVSYLKGLWMECVWHSTGIYQCQIYRSLLALPQDLQAARALMVISCLLSGIACACAVIGMKCTRCAKGTPAKTTFAILGGTLFILAGLLCMVAVSWTTNDVVQNFYNPLLPSGMKFEIGQALYLGFISSSLSLIGGTLLCLSCQDEAPYRPYQAPPRATTTTANTAPAYQPPAAYKDNRAPSVTSATHSGYRLNDYV
| null | null |
bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; protein-containing complex assembly [GO:0065003]
|
bicellular tight junction [GO:0005923]; endoplasmic reticulum [GO:0005783]; plasma membrane [GO:0005886]
|
identical protein binding [GO:0042802]; structural molecule activity [GO:0005198]
|
PF00822;
|
1.20.140.150;
|
Claudin family
| null |
SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein.
| null | null | null | null | null |
FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space, through calcium-independent cell-adhesion activity. {ECO:0000250}.
|
Homo sapiens (Human)
|
O95503
|
CBX6_HUMAN
|
MELSAVGERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSRLIAAFEQKERERELYGPKKRGPKPKTFLLKARAQAEALRISDVHFSVKPSASASSPKLHSSAAVHRLKKDIRRCHRMSRRPLPRPDPQGGSPGLRPPISPFSETVRIINRKVKPREPKRNRIILNLKVIDKGAGGGGAGQGAGALARPKVPSRNRVIGKSKKFSESVLRTQIRHMKFGAFALYKPPPAPLVAPSPGKAEASAPGPGLLLAAPAAPYDARSSGSSGCPSPTPQSSDPDDTPPKLLPETVSPSAPSWREPEVLDLSLPPESAATSKRAPPEVTAAAGPAPPTAPEPAGASSEPEAGDWRPEMSPCSNVVVTDVTSNLLTVTIKEFCNPEDFEKVAAGVAGAAGGGGSIGASK
| null | null |
chromatin organization [GO:0006325]; negative regulation of transcription by RNA polymerase II [GO:0000122]
|
chromatin [GO:0000785]; heterochromatin [GO:0000792]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PcG protein complex [GO:0031519]; PRC1 complex [GO:0035102]
|
chromatin binding [GO:0003682]; methylated histone binding [GO:0035064]; single-stranded RNA binding [GO:0003727]
|
PF17218;PF00385;
|
2.40.50.40;
| null |
PTM: Ubiquitinated. Ubiquitination regulates the function of the Polycomb group (PcG) multiprotein PRC1-like complex. Deubiquitinated by USP26. {ECO:0000269|PubMed:28839133}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18927235}. Chromosome {ECO:0000269|PubMed:18927235}. Note=Uniformely distributed in the nucleoplasm (PubMed:18927235). Localizes to the inactivated X chromosome in females (By similarity). {ECO:0000250|UniProtKB:Q9DBY5, ECO:0000269|PubMed:18927235}.
| null | null | null | null | null |
FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (PubMed:21282530). PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility. Possibly contributes to the target selectivity of the PRC1 complex by binding specific regions of chromatin (PubMed:18927235). Recruitment to chromatin might occur in an H3K27me3-independent fashion (By similarity). May have a PRC1-independent function in embryonic stem cells (By similarity). {ECO:0000250|UniProtKB:Q9DBY5, ECO:0000269|PubMed:18927235, ECO:0000269|PubMed:21282530}.
|
Homo sapiens (Human)
|
O95528
|
GTR10_HUMAN
|
MGHSPPVLPLCASVSLLGGLTFGYELAVISGALLPLQLDFGLSCLEQEFLVGSLLLGALLASLVGGFLIDCYGRKQAILGSNLVLLAGSLTLGLAGSLAWLVLGRAVVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEAGITVGILLSYALNYALAGTPWGWRHMFGWATAPAVLQSLSLLFLPAGTDETATHKDLIPLQGGEAPKLGPGRPRYSFLDLFRARDNMRGRTTVGLGLVLFQQLTGQPNVLCYASTIFSSVGFHGGSSAVLASVGLGAVKVAATLTAMGLVDRAGRRALLLAGCALMALSVSGIGLVSFAVPMDSGPSCLAVPNATGQTGLPGDSGLLQDSSLPPIPRTNEDQREPILSTAKKTKPHPRSGDPSAPPRLALSSALPGPPLPARGHALLRWTALLCLMVFVSAFSFGFGPVTWLVLSEIYPVEIRGRAFAFCNSFNWAANLFISLSFLDLIGTIGLSWTFLLYGLTAVLGLGFIYLFVPETKGQSLAEIDQQFQKRRFTLSFGHRQNSTGIPYSRIEISAAS
| null | null |
artery development [GO:0060840]; cell redox homeostasis [GO:0045454]; circulatory system development [GO:0072359]; dehydroascorbic acid transport [GO:0070837]; embryonic skeletal joint development [GO:0072498]; galactose transmembrane transport [GO:0015757]; glucose import across plasma membrane [GO:0098708]; glucose transmembrane transport [GO:1904659]; hexose transmembrane transport [GO:0008645]; negative regulation of connective tissue growth factor production [GO:0032683]; negative regulation of gene expression [GO:0010629]; negative regulation of integrin-mediated signaling pathway [GO:2001045]; negative regulation of proteoglycan biosynthetic process [GO:1902729]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of gene expression [GO:0010628]; positive regulation of proteoglycan biosynthetic process [GO:1902730]; positive regulation of transforming growth factor beta receptor signaling pathway [GO:0030511]; regulation of extracellular matrix organization [GO:1903053]; skin development [GO:0043588]; transport across blood-brain barrier [GO:0150104]
|
cytosol [GO:0005829]; endomembrane system [GO:0012505]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
carbohydrate:proton symporter activity [GO:0005351]; D-glucose transmembrane transporter activity [GO:0055056]; dehydroascorbic acid transmembrane transporter activity [GO:0033300]; symporter activity [GO:0015293]
|
PF00083;
|
1.20.1250.20;
|
Major facilitator superfamily, Sugar transporter (TC 2.A.1.1) family, Glucose transporter subfamily
| null |
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:16550171}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:16550171}.
|
CATALYTIC ACTIVITY: Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376, ChEBI:CHEBI:4167; Evidence={ECO:0000269|PubMed:11592815};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.28 mM for 2-deoxy-D-glucose {ECO:0000269|PubMed:11592815};
| null | null | null |
FUNCTION: Facilitative glucose transporter required for the development of the cardiovascular system. {ECO:0000269|PubMed:11592815, ECO:0000269|PubMed:16550171}.
|
Homo sapiens (Human)
|
O95544
|
NADK_HUMAN
|
MEMEQEKMTMNKELSPDAAAYCCSACHGDETWSYNHPIRGRAKSRSLSASPALGSTKEFRRTRSLHGPCPVTTFGPKACVLQNPQTIMHIQDPASQRLTWNKSPKSVLVIKKMRDASLLQPFKELCTHLMEENMIVYVEKKVLEDPAIASDESFGAVKKKFCTFREDYDDISNQIDFIICLGGDGTLLYASSLFQGSVPPVMAFHLGSLGFLTPFSFENFQSQVTQVIEGNAAVVLRSRLKVRVVKELRGKKTAVHNGLGENGSQAAGLDMDVGKQAMQYQVLNEVVIDRGPSSYLSNVDVYLDGHLITTVQGDGVIVSTPTGSTAYAAAAGASMIHPNVPAIMITPICPHSLSFRPIVVPAGVELKIMLSPEARNTAWVSFDGRKRQEIRHGDSISITTSCYPLPSICVRDPVSDWFESLAQCLHWNVRKKQAHFEEEEEEEEEG
|
2.7.1.23
|
COFACTOR: Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Evidence={ECO:0000269|PubMed:11594753};
|
ATP metabolic process [GO:0046034]; NAD metabolic process [GO:0019674]; NADP biosynthetic process [GO:0006741]; phosphorylation [GO:0016310]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; NAD+ kinase activity [GO:0003951]
|
PF01513;PF20143;
| null |
NAD kinase family
| null | null |
CATALYTIC ACTIVITY: Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); Xref=Rhea:RHEA:18629, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540, ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23; Evidence={ECO:0000269|PubMed:11594753};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.3 mM for ATP {ECO:0000269|PubMed:11594753}; KM=0.54 mM for NAD {ECO:0000269|PubMed:11594753}; Vmax=6.7 umol/min/mg enzyme {ECO:0000269|PubMed:11594753};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000269|PubMed:11594753};
|
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:11594753};
| null |
Homo sapiens (Human)
|
O95551
|
TYDP2_HUMAN
|
MELGSCLEGGREAAEEEGEPEVKKRRLLCVEFASVASCDAAVAQCFLAENDWEMERALNSYFEPPVEESALERRPETISEPKTYVDLTNEETTDSTTSKISPSEDTQQENGSMFSLITWNIDGLDLNNLSERARGVCSYLALYSPDVIFLQEVIPPYYSYLKKRSSNYEIITGHEEGYFTAIMLKKSRVKLKSQEIIPFPSTKMMRNLLCVHVNVSGNELCLMTSHLESTRGHAAERMNQLKMVLKKMQEAPESATVIFAGDTNLRDREVTRCGGLPNNIVDVWEFLGKPKHCQYTWDTQMNSNLGITAACKLRFDRIFFRAAAEEGHIIPRSLDLLGLEKLDCGRFPSDHWGLLCNLDIIL
|
3.1.4.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19794497, ECO:0000269|PubMed:22405347, ECO:0000269|PubMed:22822062, ECO:0000269|PubMed:27060144, ECO:0000269|PubMed:27099339}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19794497, ECO:0000269|PubMed:22405347, ECO:0000269|PubMed:22822062}; Note=Binds 1 magnesium or manganese ion per subunit. {ECO:0000269|PubMed:19794497, ECO:0000269|PubMed:22405347, ECO:0000269|PubMed:22822062, ECO:0000269|PubMed:27060144, ECO:0000269|PubMed:27099339};
|
cell surface receptor signaling pathway [GO:0007166]; double-strand break repair [GO:0006302]; neuron development [GO:0048666]
|
aggresome [GO:0016235]; cytoplasm [GO:0005737]; nuclear body [GO:0016604]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]
|
5'-tyrosyl-DNA phosphodiesterase activity [GO:0070260]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; nuclease activity [GO:0004518]; single-stranded DNA binding [GO:0003697]; transcription corepressor activity [GO:0003714]; tyrosyl-RNA phosphodiesterase activity [GO:0036317]
|
PF03372;PF14555;
|
1.10.8.10;3.60.10.10;
|
CCR4/nocturin family
|
PTM: Ubiquitinated by TRAF6. {ECO:0000269|PubMed:21980489}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12743594}. Nucleus, PML body {ECO:0000269|PubMed:19794497, ECO:0000269|PubMed:21921940}. Nucleus, nucleolus {ECO:0000269|PubMed:21921940}. Cytoplasm. Note=Localizes to nucleolar cavities following stress; localization to nucleolus is dependent on PML protein. {ECO:0000269|PubMed:21921940}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22908287}. Note=(Microbial infection) In case of infection by picornavirus, relocalizes to cytoplasmic sites distinct from those containing viral proteins associated with RNA replication or encapsidation. {ECO:0000269|PubMed:22908287}.
| null |
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 uM for single-stranded 5'-tyrosyl DNA {ECO:0000269|PubMed:22822062}; Note=kcat is 3 sec(-1) with single-stranded 5'-tyrosyl DNA as substrate.;
| null | null | null |
FUNCTION: DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DNA double-strand breaks/DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation (PubMed:27060144, PubMed:27099339). Thereby, protects the transcription of many genes involved in neurological development and maintenance from the abortive activity of TOP2. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DSBs due to DNA damage by radiation and free radicals. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Acts as a regulator of ribosome biogenesis following stress. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non-canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. {ECO:0000269|PubMed:19794497, ECO:0000269|PubMed:21030584, ECO:0000269|PubMed:21921940, ECO:0000269|PubMed:21980489, ECO:0000269|PubMed:22405347, ECO:0000269|PubMed:22822062, ECO:0000269|PubMed:24658003, ECO:0000269|PubMed:27060144, ECO:0000269|PubMed:27099339}.; FUNCTION: (Microbial infection) Also acts as a 5'-tyrosyl-RNA phosphodiesterase following picornavirus infection: its activity is hijacked by picornavirus and acts by specifically cleaving the protein-RNA covalent linkage generated during the viral genomic RNA replication steps of a picornavirus infection, without impairing the integrity of viral RNA. {ECO:0000269|PubMed:22908287}.
|
Homo sapiens (Human)
|
O95562
|
SFT2B_HUMAN
|
MDKLKKVLSGQDTEDRSGLSEVVEASSLSWSTRIKGFIACFAIGILCSLLGTVLLWVPRKGLHLFAVFYTFGNIASIGSTIFLMGPVKQLKRMFEPTRLIATIMVLLCFALTLCSAFWWHNKGLALIFCILQSLALTWYSLSFIPFARDAVKKCFAVCLA
| null | null |
protein transport [GO:0015031]; vesicle-mediated transport [GO:0016192]
|
cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; extracellular exosome [GO:0070062]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]
| null |
PF04178;
| null |
SFT2 family
| null |
SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex. {ECO:0000250|UniProtKB:P38166}.
|
Homo sapiens (Human)
|
O95563
|
MPC2_HUMAN
|
MSAAGARGLRATYHRLLDKVELMLPEKLRPLYNHPAGPRTVFFWAPIMKWGLVCAGLADMARPAEKLSTAQSAVLMATGFIWSRYSLVIIPKNWSLFAVNFFVGAAGASQLFRIWRYNQELKAKAHK
| null | null |
acetyl-CoA biosynthetic process from pyruvate [GO:0006086]; mitochondrial pyruvate transmembrane transport [GO:0006850]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]
|
inner mitochondrial membrane protein complex [GO:0098800]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
|
identical protein binding [GO:0042802]; pyruvate transmembrane transporter activity [GO:0050833]
|
PF03650;
| null |
Mitochondrial pyruvate carrier (MPC) (TC 2.A.105) family
| null |
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:22628558, ECO:0000269|PubMed:26253029, ECO:0000269|PubMed:29472561}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=H(+)(out) + pyruvate(out) = H(+)(in) + pyruvate(in); Xref=Rhea:RHEA:64720, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378; Evidence={ECO:0000269|PubMed:22628558, ECO:0000269|PubMed:26253029, ECO:0000269|PubMed:27317664, ECO:0000269|PubMed:29472561};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.1 mM for pyruvate {ECO:0000269|PubMed:29472561};
| null | null | null |
FUNCTION: Mediates the uptake of pyruvate into mitochondria. {ECO:0000269|PubMed:22628558, ECO:0000269|PubMed:26253029, ECO:0000269|PubMed:27317664, ECO:0000269|PubMed:29472561}.
|
Homo sapiens (Human)
|
O95568
|
MET18_HUMAN
|
MTFQFNFTIEDHLENELTPIRDGALTLDSSKELSVSESQKGEERDRKCSAEQFDLPQDHLWEHKSMENAAPSQDTDSPLSAASSSRNLEPHGKQPSLRAAKEHAMPKDLKKMLENKVIETLPGFQHVKLSVVKTILLKENFPGENIVSKSFSSHSDLITGVYEGGLKIWECTFDLLAYFTKAKVKFAGKKVLDLGCGSGLLGITAFKGGSKEIHFQDYNSMVIDEVTLPNVVANSTLEDEENDVNEPDVKRCRKPKVTQLYKCRFFSGEWSEFCKLVLSSEKLFVKYDLILTSETIYNPDYYSNLHQTFLRLLSKNGRVLLASKAHYFGVGGGVHLFQKFVEERDVFKTRILKIIDEGLKRFIIEITFKFPG
|
2.1.1.85
| null |
peptidyl-lysine monomethylation [GO:0018026]; regulation of ribosome biogenesis [GO:0090069]; regulation of rRNA processing [GO:2000232]; regulation of translation [GO:0006417]; regulation of translational elongation [GO:0006448]
|
cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
|
heat shock protein binding [GO:0031072]; protein-L-histidine N-tele-methyltransferase activity [GO:0018064]; protein-lysine N-methyltransferase activity [GO:0016279]
|
PF13489;
|
3.40.50.150;
|
Methyltransferase superfamily, METTL18 family
|
PTM: Monomethylated at His-154 through automethylation (PubMed:33693809). Automethylation at His-154 positively regulates the methyltransferase activity toward RPL3 (PubMed:33693809). Probably methylated on other residues (PubMed:33693809). {ECO:0000269|PubMed:33693809}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:33693809}. Nucleus {ECO:0000269|PubMed:33693809}. Nucleus, nucleolus {ECO:0000269|PubMed:33693809}.
|
CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) + N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600, ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85; Evidence={ECO:0000269|PubMed:33693809, ECO:0000269|PubMed:35674491}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370; Evidence={ECO:0000269|PubMed:33693809, ECO:0000269|PubMed:35674491};
| null | null | null | null |
FUNCTION: Protein-L-histidine N-tele-methyltransferase that specifically monomethylates RPL3, thereby regulating translation elongation (PubMed:23349634, PubMed:33693809, PubMed:35674491). Histidine methylation of RPL3 regulates translation elongation by slowing ribosome traversal on tyrosine codons: slower elongation provides enough time for proper folding of synthesized proteins and prevents cellular aggregation of tyrosine-rich proteins (PubMed:35674491). {ECO:0000269|PubMed:23349634, ECO:0000269|PubMed:33693809, ECO:0000269|PubMed:35674491}.
|
Homo sapiens (Human)
|
O95571
|
ETHE1_HUMAN
|
MAEAVLRVARRQLSQRGGSGAPILLRQMFEPVSCTFTYLLGDRESREAVLIDPVLETAPRDAQLIKELGLRLLYAVNTHCHADHITGSGLLRSLLPGCQSVISRLSGAQADLHIEDGDSIRFGRFALETRASPGHTPGCVTFVLNDHSMAFTGDALLIRGCGRTDFQQGCAKTLYHSVHEKIFTLPGDCLIYPAHDYHGFTVSTVEEERTLNPRLTLSCEEFVKIMGNLNLPKPQQIDFAVPANMRCGVQTPTA
|
1.13.11.18
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459, ECO:0000269|PubMed:25596185}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459, ECO:0000269|PubMed:25596185};
|
glutathione metabolic process [GO:0006749]; hydrogen sulfide metabolic process [GO:0070813]
|
cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]
|
identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; sulfur dioxygenase activity [GO:0050313]
|
PF00753;
|
3.60.15.10;
|
Metallo-beta-lactamase superfamily, Glyoxalase II family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12398897}. Nucleus {ECO:0000269|PubMed:12398897}. Mitochondrion matrix {ECO:0000269|PubMed:14732903}.
|
CATALYTIC ACTIVITY: Reaction=H2O + O2 + S-sulfanylglutathione = glutathione + 2 H(+) + sulfite; Xref=Rhea:RHEA:12981, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17359, ChEBI:CHEBI:57925, ChEBI:CHEBI:58905; EC=1.13.11.18; Evidence={ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459, ECO:0000269|PubMed:25596185};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.34 mM for glutathione persulfide (GSSH) {ECO:0000269|PubMed:23144459}; Vmax=113 umol/min/mg enzyme (in the presence of equimolar amounts of GSSH and GSH and at 22 degrees Celsius) {ECO:0000269|PubMed:23144459};
| null | null | null |
FUNCTION: Sulfur dioxygenase that plays an essential role in hydrogen sulfide catabolism in the mitochondrial matrix. Hydrogen sulfide (H(2)S) is first oxidized by SQRDL, giving rise to cysteine persulfide residues. ETHE1 consumes molecular oxygen to catalyze the oxidation of the persulfide, once it has been transferred to a thiophilic acceptor, such as glutathione (R-SSH). Plays an important role in metabolic homeostasis in mitochondria by metabolizing hydrogen sulfide and preventing the accumulation of supraphysiological H(2)S levels that have toxic effects, due to the inhibition of cytochrome c oxidase. First described as a protein that can shuttle between the nucleus and the cytoplasm and suppress p53-induced apoptosis by sequestering the transcription factor RELA/NFKB3 in the cytoplasm and preventing its accumulation in the nucleus (PubMed:12398897). {ECO:0000269|PubMed:12398897, ECO:0000269|PubMed:14732903, ECO:0000269|PubMed:19136963, ECO:0000269|PubMed:23144459}.
|
Homo sapiens (Human)
|
O95573
|
ACSL3_HUMAN
|
MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPVNSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPNGKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGKPPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGEEDVYIGYLPLAHVLELSAELVCLSHGCRIGYSSPQTLADQSSKIKKGSKGDTSMLKPTLMAAVPEIMDRIYKNVMNKVSEMSSFQRNLFILAYNYKMEQISKGRNTPLCDSFVFRKVRSLLGGNIRLLLCGGAPLSATTQRFMNICFCCPVGQGYGLTESAGAGTISEVWDYNTGRVGAPLVCCEIKLKNWEEGGYFNTDKPHPRGEILIGGQSVTMGYYKNEAKTKADFFEDENGQRWLCTGDIGEFEPDGCLKIIDRKKDLVKLQAGEYVSLGKVEAALKNLPLVDNICAYANSYHSYVIGFVVPNQKELTELARKKGLKGTWEELCNSCEMENEVLKVLSEAAISASLEKFEIPVKIRLSPEPWTPETGLVTDAFKLKRKELKTHYQADIERMYGRK
|
6.2.1.15; 6.2.1.2; 6.2.1.3
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
fatty acid metabolic process [GO:0006631]; long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic process [GO:0035338]; long-chain fatty-acyl-CoA metabolic process [GO:0035336]; neuron differentiation [GO:0030182]; positive regulation of Golgi to plasma membrane protein transport [GO:0042998]; positive regulation of phosphatidylcholine biosynthetic process [GO:2001247]; positive regulation of secretion [GO:0051047]; very-low-density lipoprotein particle assembly [GO:0034379]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; lipid droplet [GO:0005811]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; perinuclear region of cytoplasm [GO:0048471]; peroxisomal membrane [GO:0005778]; plasma membrane [GO:0005886]
|
arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; medium-chain fatty acid-CoA ligase activity [GO:0031956]; palmitoyl-CoA ligase activity [GO:0090433]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]
|
PF00501;
|
3.40.50.12780;
|
ATP-dependent AMP-binding enzyme family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}.
|
CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:22633490}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15422; Evidence={ECO:0000305|PubMed:22633490}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = (5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:19713, ChEBI:CHEBI:30616, ChEBI:CHEBI:32395, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368, ChEBI:CHEBI:456215; EC=6.2.1.15; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19714; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=(E)-hexadec-2-enoate + ATP + CoA = (2E)-hexadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:36139, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61526, ChEBI:CHEBI:72745, ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:22633490}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:36140; Evidence={ECO:0000305|PubMed:22633490}; CATALYTIC ACTIVITY: Reaction=15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoate + ATP + CoA = 15-hydroxy-(5Z,8Z,11Z,13E)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52116, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:78832, ChEBI:CHEBI:136409, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52117; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate + ATP + CoA = 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52112, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:90718, ChEBI:CHEBI:136408, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52113; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoate + ATP + CoA = 5-hydroxy-(6E,8Z,11Z,14Z)-eicosatetraenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52108, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:65341, ChEBI:CHEBI:136407, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52109; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + ATP + CoA = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52016, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:84024, ChEBI:CHEBI:136117, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52017; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + ATP + CoA = 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:52012, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:76625, ChEBI:CHEBI:136115, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52013; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=a medium chain fatty acid + ATP + CoA = a medium-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:48340, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:59558, ChEBI:CHEBI:90546, ChEBI:CHEBI:456215; EC=6.2.1.2; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:48341; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + hexadecanoate = AMP + diphosphate + hexadecanoyl-CoA; Xref=Rhea:RHEA:30751, ChEBI:CHEBI:7896, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30752; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + tetradecanoate = AMP + diphosphate + tetradecanoyl-CoA; Xref=Rhea:RHEA:33619, ChEBI:CHEBI:30616, ChEBI:CHEBI:30807, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33620; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + dodecanoate = AMP + diphosphate + dodecanoyl-CoA; Xref=Rhea:RHEA:33623, ChEBI:CHEBI:18262, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33624; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + octadecanoate = AMP + diphosphate + octadecanoyl-CoA; Xref=Rhea:RHEA:33615, ChEBI:CHEBI:25629, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33616; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=ATP + CoA + eicosanoate = AMP + diphosphate + eicosanoyl-CoA; Xref=Rhea:RHEA:46208, ChEBI:CHEBI:30616, ChEBI:CHEBI:32360, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57380, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46209; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoate + ATP + CoA = (9Z)-octadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33607, ChEBI:CHEBI:30616, ChEBI:CHEBI:30823, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33608; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoate + ATP + CoA = (9Z)-hexadecenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33647, ChEBI:CHEBI:30616, ChEBI:CHEBI:32372, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33648; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z)-octadecadienoate + ATP + CoA = (9Z,12Z)-octadecadienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:33651, ChEBI:CHEBI:30245, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57383, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=(9Z,12Z,15Z)-octadecatrienoate + ATP + CoA = (9Z,12Z,15Z)-octadecatrienoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44936, ChEBI:CHEBI:30616, ChEBI:CHEBI:32387, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74034, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44937; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + ATP + CoA = (4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:44932, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:74298, ChEBI:CHEBI:77016, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44933; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + ATP + CoA = (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:67848, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:58562, ChEBI:CHEBI:73862, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67849; Evidence={ECO:0000250|UniProtKB:Q63151}; CATALYTIC ACTIVITY: Reaction=a fatty acid + ATP + CoA = a fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:38883, ChEBI:CHEBI:28868, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636, ChEBI:CHEBI:456215; Evidence={ECO:0000250|UniProtKB:Q63151}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38884; Evidence={ECO:0000250|UniProtKB:Q63151};
| null | null | null | null |
FUNCTION: Acyl-CoA synthetases (ACSL) activates long-chain fatty acids for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:22633490). Required for the incorporation of fatty acids into phosphatidylcholine, the major phospholipid located on the surface of VLDL (very low density lipoproteins) (PubMed:18003621). Has mainly an anabolic role in energy metabolism. Mediates hepatic lipogenesis. Preferentially uses myristate, laurate, arachidonate and eicosapentaenoate as substrates. Both isoforms exhibit the same level of activity (By similarity). {ECO:0000250|UniProtKB:Q63151, ECO:0000269|PubMed:18003621, ECO:0000269|PubMed:22633490}.
|
Homo sapiens (Human)
|
O95600
|
KLF8_HUMAN
|
MVDMDKLINNLEVQLNSEGGSMQVFKQVTASVRNRDPPEIEYRSNMTSPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLIGGDGKNAGSVKVDPTSMSPLEIPSDSEESTIESGSSALQSLQGLQQEPAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDELTRHFRKHTGIKPFRCTDCNRSFSRSDHLSLHRRRHDTM
| null | null |
negative regulation of transcription by RNA polymerase II [GO:0000122]; regulation of transcription by RNA polymerase II [GO:0006357]
|
aggresome [GO:0016235]; chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF00096;
|
3.30.160.60;
|
Sp1 C2H2-type zinc-finger protein family
|
PTM: Sumoylation at Lys-67 represses transcriptional activity and reduces cell cycle progression into the G(1) phase. Has no effect on subcellular location. {ECO:0000269|PubMed:16617055}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16617055}.
| null | null | null | null | null |
FUNCTION: Transcriptional repressor and activator. Binds to CACCC-boxes promoter elements. Also binds the GT-box of cyclin D1 promoter and mediates cell cycle progression at G(1) phase as a downstream target of focal adhesion kinase (FAK). {ECO:0000269|PubMed:10756197, ECO:0000269|PubMed:12820964, ECO:0000269|PubMed:16617055}.
|
Homo sapiens (Human)
|
O95602
|
RPA1_HUMAN
|
MLISKNMPWRRLQGISFGMYSAEELKKLSVKSITNPRYLDSLGNPSANGLYDLALGPADSKEVCSTCVQDFSNCSGHLGHIELPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAVIHLLLCQLRVLEVGALQAVYELERILNRFLEENPDPSASEIREELEQYTTEIVQNNLLGSQGAHVKNVCESKSKLIALFWKAHMNAKRCPHCKTGRSVVRKEHNSKLTITFPAMVHRTAGQKDSEPLGIEEAQIGKRGYLTPTSAREHLSALWKNEGFFLNYLFSGMDDDGMESRFNPSVFFLDFLVVPPSRYRPVSRLGDQMFTNGQTVNLQAVMKDVVLIRKLLALMAQEQKLPEEVATPTTDEEKDSLIAIDRSFLSTLPGQSLIDKLYNIWIRLQSHVNIVFDSEMDKLMMDKYPGIRQILEKKEGLFRKHMMGKRVDYAARSVICPDMYINTNEIGIPMVFATKLTYPQPVTPWNVQELRQAVINGPNVHPGASMVINEDGSRTALSAVDMTQREAVAKQLLTPATGAPKPQGTKIVCRHVKNGDILLLNRQPTLHRPSIQAHRARILPEEKVLRLHYANCKAYNADFDGDEMNAHFPQSELGRAEAYVLACTDQQYLVPKDGQPLAGLIQDHMVSGASMTTRGCFFTREHYMELVYRGLTDKVGRVKLLSPSILKPFPLWTGKQVVSTLLINIIPEDHIPLNLSGKAKITGKAWVKETPRSVPGFNPDSMCESQVIIREGELLCGVLDKAHYGSSAYGLVHCCYEIYGGETSGKVLTCLARLFTAYLQLYRGFTLGVEDILVKPKADVKRQRIIEESTHCGPQAVRAALNLPEAASYDEVRGKWQDAHLGKDQRDFNMIDLKFKEEVNHYSNEINKACMPFGLHRQFPENSLQMMVQSGAKGSTVNTMQISCLLGQIELEGRRPPLMASGKSLPCFEPYEFTPRAGGFVTGRFLTGIKPPEFFFHCMAGREGLVDTAVKTSRSGYLQRCIIKHLEGLVVQYDLTVRDSDGSVVQFLYGEDGLDIPKTQFLQPKQFPFLASNYEVIMKSQHLHEVLSRADPKKALHHFRAIKKWQSKHPNTLLRRGAFLSYSQKIQEAVKALKLESENRNGRSPGTQEMLRMWYELDEESRRKYQKKAAACPDPSLSVWRPDIYFASVSETFETKVDDYSQEWAAQTEKSYEKSELSLDRLRTLLQLKWQRSLCEPGEAVGLLAAQSIGEPSTQMTLNTFHFAGRGEMNVTLGIPRLREILMVASANIKTPMMSVPVLNTKKALKRVKSLKKQLTRVCLGEVLQKIDVQESFCMEEKQNKFQVYQLRFQFLPHAYYQQEKCLRPEDILRFMETRFFKLLMESIKKKNNKASAFRNVNTRRATQRDLDNAGELGRSRGEQEGDEEEEGHIVDAEAEEGDADASDAKRKEKQEEEVDYESEEEEEREGEENDDEDMQEERNPHREGARKTQEQDEEVGLGTEEDPSLPALLTQPRKPTHSQEPQGPEAMERRVQAVREIHPFIDDYQYDTEESLWCQVTVKLPLMKINFDMSSLVVSLAHGAVIYATKGITRCLLNETTNNKNEKELVLNTEGINLPELFKYAEVLDLRRLYSNDIHAIANTYGIEAALRVIEKEIKDVFAVYGIAVDPRHLSLVADYMCFEGVYKPLNRFGIRSNSSPLQQMTFETSFQFLKQATMLGSHDELRSPSACLVVGKVVRGGTGLFELKQPLR
|
2.7.7.6
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:34887565}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P24928, ECO:0000269|PubMed:34887565};
|
negative regulation of protein localization to nucleolus [GO:1904750]
|
chromosome [GO:0005694]; nucleoplasm [GO:0005654]; RNA polymerase I complex [GO:0005736]
|
chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; DNA/RNA hybrid binding [GO:0071667]; magnesium ion binding [GO:0000287]; RNA polymerase I activity [GO:0001054]; zinc ion binding [GO:0008270]
|
PF04997;PF00623;PF04983;PF05000;PF04998;
|
1.10.132.30;1.10.357.120;2.40.40.20;3.30.70.2850;6.10.250.2940;3.30.1490.180;4.10.860.120;1.10.274.100;
|
RNA polymerase beta' chain family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:36271492, ECO:0000305|PubMed:34887565}. Chromosome {ECO:0000250|UniProtKB:O35134}.
|
CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21249; Evidence={ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492};
| null | null | null | null |
FUNCTION: Catalytic core component of RNA polymerase I (Pol I), a DNA-dependent RNA polymerase which synthesizes ribosomal RNA precursors using the four ribonucleoside triphosphates as substrates. Transcribes 47S pre-rRNAs from multicopy rRNA gene clusters, giving rise to 5.8S, 18S and 28S ribosomal RNAs (PubMed:11250903, PubMed:11283244, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492). Pol I-mediated transcription cycle proceeds through transcription initiation, transcription elongation and transcription termination stages. During transcription initiation, Pol I pre-initiation complex (PIC) is recruited by the selectivity factor 1 (SL1/TIF-IB) complex bound to the core promoter that precedes an rDNA repeat unit. The PIC assembly bends the promoter favoring the formation of the transcription bubble and promoter escape. Once the polymerase has escaped from the promoter it enters the elongation phase during which RNA is actively polymerized, based on complementarity with the template DNA strand. Highly processive, assembles in structures referred to as 'Miller trees' where many elongating Pol I complexes queue and transcribe the same rDNA coding regions. At terminator sequences downstream of the rDNA gene, PTRF interacts with Pol I and halts Pol I transcription leading to the release of the RNA transcript and polymerase from the DNA (PubMed:11250903, PubMed:11283244, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492). Forms Pol I active center together with the second largest subunit POLR1B/RPA2. Appends one nucleotide at a time to the 3' end of the nascent RNA, with POLR1A/RPA1 contributing a Mg(2+)-coordinating DxDGD motif, and POLR1B/RPA2 participating in the coordination of a second Mg(2+) ion and providing lysine residues believed to facilitate Watson-Crick base pairing between the incoming nucleotide and the template base. Typically, Mg(2+) ions direct a 5' nucleoside triphosphate to form a phosphodiester bond with the 3' hydroxyl of the preceding nucleotide of the nascent RNA, with the elimination of pyrophosphate. Has proofreading activity: Pauses and backtracks to allow the cleavage of a missincorporated nucleotide via POLR1H/RPA12. High Pol I processivity is associated with decreased transcription fidelity (By similarity) (PubMed:11250903, PubMed:11283244, PubMed:16858408, PubMed:34671025, PubMed:34887565, PubMed:36271492). {ECO:0000250|UniProtKB:P10964, ECO:0000269|PubMed:11250903, ECO:0000269|PubMed:11283244, ECO:0000269|PubMed:16858408, ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492}.
|
Homo sapiens (Human)
|
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