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
MGSASPGLSSVSPSHLLLPPDTVSRTGLEKAAAGAVGLERRDWSPSPPATPEQGLSAFYLSYFDMLYPEDSSWAAKAPGASSREEPPEEPEQCPVIDSQAPAGSLDLVPGGLTLEEHSLEQVQSMVVGEVLKDIETACKLLNITADPMDWSPSNVQKWLLWTEHQYRLPPMGKAFQELAGKELCAMSEEQFRQRSPLGGDVLHAHLDIWKSAAWMKERTSPGAIHYCASTSEESWTDSEVDSSCSGQPIHLWQFLKELLLKPHSYGRFIRWLNKEKGIFKIEDSAQVARLWGIRKNRPAMNYDKLSRSIRQYYKKGIIRK...
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:00...
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:...
Homo sapiens (Human)
O95239
KIF4A_HUMAN
MKEEVKGIPVRVALRCRPLVPKEISEGCQMCLSFVPGEPQVVVGTDKSFTYDFVFDPSTEQEEVFNTAVAPLIKGVFKGYNATVLAYGQTGSGKTYSMGGAYTAEQENEPTVGVIPRVIQLLFKEIDKKSDFEFTLKVSYLEIYNEEILDLLCPSREKAQINIREDPKEGIKIVGLTEKTVLVALDTVSCLEQGNNSRTVASTAMNSQSSRSHAIFTISLEQRKKSDKNSSFRSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGDDKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNL...
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:2...
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:00002...
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 spind...
Homo sapiens (Human)
O95243
MBD4_HUMAN
MGTTGLESLSLGDRGAAPTVTSSERLVPDPPNDLRKEDVAMELERVGEDEEQMMIKRSSECNPLLQEPIASAQFGATAGTECRKSVPCGWERVVKQRLFGKTAGRFDVYFISPQGLKFRSKSSLANYLHKNGETSLKPEDFDFTVLSKRGIKSRYKDCSMAALTSHLQNQSNNSNWNLRTRSKCKKDVFMPPSSSSELQESRGLSNFTSTHLLLKEDEGVDDVNFRKVRKPKGKVTILKGIPIKKTKKGCRKSCSGFVQSDSKRESVCNKADAESEPVAQKSQLDRTVCISDAGACGETLSVTSEENSLVKKKERSLSSG...
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. {...
Homo sapiens (Human)
O95248
MTMR5_HUMAN
MARLADYFVLVAFGPHPRGSGEGQGQILQRFPEKDWEDNPFPQGIELFCQPSGWQLCPERNPPTFFVAVLTDINSERHYCACLTFWEPAEPSQQETTRVEDATEREEEGDEGGQTHLSPTAPAPSAQLFAPKTLVLVSRLDHTEVFRNSLGLIYAIHVEGLNVCLENVIGNLLTCTVPLAGGSQRTISLGAGDRQVIQTPLADSLPVSRCSVALLFRQLGITNVLSLFCAALTEHKVLFLSRSYQRLADACRGLLALLFPLRYSFTYVPILPAQLLEVLSTPTPFIIGVNAAFQAETQELLDVIVADLDGGTVTIPECVH...
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 thei...
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, E...
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...
Homo sapiens (Human)
O95251
KAT7_HUMAN
MPRRKRNAGSSSDGTEDSDFSTDLEHTDSSESDGTSRRSARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQVVDFSDRETKNTADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSLKDSGSDLSHRPKRRRFHESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHNLSADECKVRAQSRDKQIEERMLSHRQDDNNRHATRHQAPTERQLRYKEKVAELRKKRNSGLSKEQKEKYMEHRQTYGNTREPLLENLTSEYDLDLFRRAQARASED...
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 replicatio...
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 a...
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)....
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|Pub...
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, EC...
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 embryon...
Homo sapiens (Human)
O95255
MRP6_HUMAN
MAAPAEPCAGQGVWNQTEPEPAATSLLSLCFLRTAGVWVPPMYLWVLGPIYLLFIHHHGRGYLRMSPLFKAKMVLGFALIVLCTSSVAVALWKIQQGTPEAPEFLIHPTVWLTTMSFAVFLIHTERKKGVQSSGVLFGYWLLCFVLPATNAAQQASGAGFQSDPVRHLSTYLCLSLVVAQFVLSCLADQPPFFPEDPQQSNPCPETGAAFPSKATFWWVSGLVWRGYRRPLRPKDLWSLGRENSSEELVSRLEKEWMRNRSAARRHNKAIAFKRKGGSGMKAPETEPFLRQEGSQWRPLLKAIWQVFHSTFLLGTLSLII...
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...
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:2362595...
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|...
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 tr...
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 an...
Homo sapiens (Human)
O95256
I18RA_HUMAN
MLCLGWIFLWLVAGERIKGFNISGCSTKKLLWTYSTRSEEEFVLFCDLPEPQKSHFCHRNRLSPKQVPEHLPFMGSNDLSDVQWYQQPSNGDPLEDIRKSYPHIIQDKCTLHFLTPGVNNSGSYICRPKMIKSPYDVACCVKMILEVKPQTNASCEYSASHKQDLLLGSTGSISCPSLSCQSDAQSPAVTWYKNGKLLSVERSNRIVVDEVYDYHQGTYVCDYTQSDTVSSWTVRAVVQVRTIVGDTKLKPDILDPVEDTLEVELGKPLTISCKARFGFERVFNPVIKWYIKDSDLEWEVSVPEAKSIKSTLKDEIIERN...
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 ...
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; Ev...
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...
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:005...
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
MGIFPGIILIFLRVKFATAAVIVSGHQKSTTVSHEMSGLNWKPFVYGGLASIVAEFGTFPVDLTKTRLQVQGQSIDARFKEIKYRGMFHALFRICKEEGVLALYSGIAPALLRQASYGTIKIGIYQSLKRLFVERLEDETLLINMICGVVSGVISSTIANPTDVLKIRMQAQGSLFQGSMIGSFIDIYQQEGTRGLWRGVVPTAQRAAIVVGVELPVYDITKKHLILSGMMGDTILTHFVSSFTCGLAGALASNPVDVVRTRMMNQRAIVGHVDLYKGTVDGILKMWKHEGFFALYKGFWPNWLRLGPWNIIFFITYEQL...
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,...
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 hydro...
Homo sapiens (Human)
O95259
KCNH1_HUMAN
MTMAGGRRGLVAPQNTFLENIVRRSNDTNFVLGNAQIVDWPIVYSNDGFCKLSGYHRAEVMQKSSTCSFMYGELTDKDTIEKVRQTFENYEMNSFEILMYKKNRTPVWFFVKIAPIRNEQDKVVLFLCTFSDITAFKQPIEDDSCKGWGKFARLTRALTSSRGVLQQLAPSVQKGENVHKHSRLAEVLQLGSDILPQYKQEAPKTPPHIILHYCVFKTTWDWIILILTFYTAILVPYNVSFKTRQNNVAWLVVDSIVDVIFLVDIVLNFHTTFVGPAGEVISDPKLIRMNYLKTWFVIDLLSCLPYDVINAFENVDEVSA...
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 ...
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:973...
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) c...
Homo sapiens (Human)
O95263
PDE8B_HUMAN
MGCAPSIHVSQSGVIYCRDSDESSSPRQTTSVSQGPAAPLPGLFVQTDAADAIPPSRASGPPSVARVRRARTELGSGSSAGSAAPAATTSRGRRRHCCSSAEAETQTCYTSVKQVSSAEVRIGPMRLTQDPIQVLLIFAKEDSQSDGFWWACDRAGYRCNIARTPESALECFLDKHHEIIVIDHRQTQNFDAEAVCRSIRATNPSEHTVILAVVSRVSDDHEEASVLPLLHAGFNRRFMENSSIIACYNELIQIEHGEVRSQFKLRACNSVFTALDHCHEAIEITSDDHVIQYVNPAFERMMGYHKGELLGKELADLPKS...
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 contr...
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
MLSSVMAPLWACILVAAGILATDTHHPQDSALYHLSKQLLQKYHKEVRPVYNWTKATTVYLDLFVHAILDVDAENQILKTSVWYQEVWNDEFLSWNSSMFDEIREISLPLSAIWAPDIIINEFVDIERYPDLPYVYVNSSGTIENYKPIQVVSACSLETYAFPFDVQNCSLTFKSILHTVEDVDLAFLRSPEDIQHDKKAFLNDSEWELLSVSSTYSILQSSAGGFAQIQFNVVMRRHPLVYVVSLLIPSIFLMLVDLGSFYLPPNCRARIVFKTSVLVGYTVFRVNMSNQVPRSVGSTPLIGHFFTICMAFLVLSLAKS...
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 mem...
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 wit...
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); X...
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
MGTLGKAREAPRKPSHGCRAASKARLEAKPANSPFPSHPSLAHITQFRMMVSLGHLAKGASLDDLIDSCIQSFDADGNLCRSNQLLQVMLTMHRIVISSAELLQKVITLYKDALAKNSPGLCLKICYFVRYWITEFWVMFKMDASLTDTMEEFQELVKAKGEELHCRLIDTTQINARDWSRKLTQRIKSNTSKKRKVSLLFDHLEPEELSEHLTYLEFKSFRRISFSDYQNYLVNSCVKENPTMERSIALCNGISQWVQLMVLSRPTPQLRAEVFIKFIQVAQKLHQLQNFNTLMAVIGGLCHSSISRLKETSSHVPHEI...
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 E...
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...
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 deve...
Homo sapiens (Human)
O95271
TNKS1_HUMAN
MAASRRSQHHHHHHQQQLQPAPGASAPPPPPPPPLSPGLAPGTTPASPTASGLAPFASPRHGLALPEGDGSRDPPDRPRSPDPVDGTSCCSTTSTICTVAAAPVVPAVSTSSAAGVAPNPAGSGSNNSPSSSSSPTSSSSSSPSSPGSSLAESPEAAGVSSTAPLGPGAAGPGTGVPAVSGALRELLEACRNGDVSRVKRLVDAANVNAKDMAGRKSSPLHFAAGFGRKDVVEHLLQMGANVHARDDGGLIPLHNACSFGHAEVVSLLLCQGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGADPNIRNTDGKSALD...
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 bin...
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]; peri...
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|PubM...
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|PubM...
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...
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 th...
Homo sapiens (Human)
O95273
CCDB1_HUMAN
MASATAPAAAVPTLASPLEQLRHLAEELRLLLPRVRVGEAQETTEEFNREMFWRRLNEAAVTVSREATTLTIVFSQLPLPSPQETQKFCEQVHAAIKAFIAVYYLLPKDQGITLRKLVRGATLDIVDGMAQLMEVLSVTPTQSPENNDLISYNSVWVACQQMPQIPRDNKAAALLMLTKNVDFVKDAHEEMEQAVEECDPYSGLLNDTEENNSDNHNHEDDVLGFPSNQDLYWSEDDQELIIPCLALVRASKACLKKIRMLVAENGKKDQVAQLDDIVDISDEISPSVDDLALSIYPPMCHLTVRINSAKLVSVLKKALE...
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
MDPARKAGAQAMIWTAGWLLLLLLRGGAQALECYSCVQKADDGCSPNKMKTVKCAPGVDVCTEAVGAVETIHGQFSLAVRGCGSGLPGKNDRGLDLHGLLAFIQLQQCAQDRCNAKLNLTSRALDPAGNESAYPPNGVECYSCVGLSREACQGTSPPVVSCYNASDHVYKGCFDGNVTLTAANVTVSLPVRGCVQDEFCTRDGVTGPGFTLSGSCCQGSRCNSDLRNKTYFSPRIPPLVRLPPPEPTTVASTTSVTTSTSAPVRPTSTTKPMPAPTSQTPRQGVEHEASRDEEPRLTGGAAGHQDRSNSGQYPAKGGPQQ...
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
MRFRFGVVVPPAVAGARPELLVVGSRPELGRWEPRGAVRLRPAGTAAGDGALALQEPGLWLGEVELAAEEAAQDGAEPGRVDTFWYKFLKREPGGELSWEGNGPHHDRCCTYNENNLVDGVYCLPIGHWIEATGHTNEMKHTTDFYFNIAGHQAMHYSRILPNIWLGSCPRQVEHVTIKLKHELGITAVMNFQTEWDIVQNSSGCNRYPEPMTPDTMIKLYREEGLAYIWMPTPDMSTEGRVQMLPQAVCLLHALLEKGHIVYVHCNAGVGRSTAAVCGWLQYVMGWNLRKVQYFLMAKRPAVYIDEEALARAQEDFFQK...
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 transmembr...
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 [...
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 {...
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|PubMe...
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 p...
Homo sapiens (Human)
O95279
KCNK5_HUMAN
MVDRGPLLTSAIIFYLAIGAAIFEVLEEPHWKEAKKNYYTQKLHLLKEFPCLGQEGLDKILEVVSDAAGQGVAITGNQTFNNWNWPNAMIFAATVITTIGYGNVAPKTPAGRLFCVFYGLFGVPLCLTWISALGKFFGGRAKRLGQFLTKRGVSLRKAQITCTVIFIVWGVLVHLVIPPFVFMVTEGWNYIEGLYYSFITISTIGFGDFVAGVNPSANYHALYRYFVELWIYLGLAWLSLFVNWKVSMFVEVHKAIKKRRRRRKESFESSPHSRKALQVKGSTASKDVNIFSFLSKKEETYNDLIKQIGKKAMKTSGGGE...
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]; ...
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 mitochondri...
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:3...
Homo sapiens (Human)
O95294
RASL1_HUMAN
MAKSSSLNVRVVEGRALPAKDVSGSSDPYCLVKVDDEVVARTATVWRSLGPFWGEEYTVHLPLDFHQLAFYVLDEDTVGHDDIIGKISLSREAITADPRGIDSWINLSRVDPDAEVQGEICLSVQMLEDGQGRCLRCHVLQARDLAPRDISGTSDPFARVFWGSQSLETSTIKKTRFPHWDEVLELREMPGAPSPLRVELWDWDMVGKNDFLGMVEFSPKTLQQKPPKGWFRLLPFPRAEEDSGGNLGALRVKVRLIEDRVLPSQCYQPLMELLMESVQGPAEEDTASPLALLEELTLGDCRQDLATKLVKLFLGRGLAG...
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]; ...
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]; se...
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:0000...
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...
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}....
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-pr...
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...
Homo sapiens (Human)
O95299
NDUAA_HUMAN
MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQDKFEVLNYTSIPIFLPEVTIG...
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]
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. ...
Homo sapiens (Human)
O95302
FKBP9_HUMAN
MAFRGWRPPPPPLLLLLLWVTGQAAPVAGLGSDAELQIERRFVPDECPRTVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDIWNSEDQVQIHTYFKPPSCPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLVFDVALLDLHNPKDSISIENKVVPENCERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDE...
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
MRCPKSAVTMRNEELLLSNGTANKMNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVA...
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 compartment...
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. Speci...
Homo sapiens (Human)
O95340
PAPS2_HUMAN
MSGIKKQKTENQQKSTNVVYQAHHVSRNKRGQVVGTRGGFRGCTVWLTGLSGAGKTTISFALEEYLVSHAIPCYSLDGDNVRHGLNRNLGFSPGDREENIRRIAEVAKLFADAGLVCITSFISPFAKDRENARKIHESAGLPFFEIFVDAPLNICESRDVKGLYKRARAGEIKGFTGIDSDYEKPETPERVLKTNLSTVSDCVHQVVELLQEQNIVPYTIIKDIHELFVPENKLDHVRAEAETLPSLSITKLDLQWVQVLSEGWATPLKGFMREKEYLQVMHFDTLLDDGVINMSIPIVLPVSAEDKTRLEGCSKFVLAH...
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,...
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 yield...
Homo sapiens (Human)
O95342
ABCBB_HUMAN
MSDSVILRSIKKFGEENDGFESDKSYNNDKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIWLMFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQIPGKACVNNTIVWTNSSLNQNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGI...
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 homeostasi...
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 membra...
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 transmemb...
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...
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:R...
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 glycocheno...
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...
Homo sapiens (Human)
O95343
SIX3_HUMAN
MVFRSPLDLYSSHFLLPNFADSHHRSILLASSGGGNGAGGGGGAGGGSGGGNGAGGGGAGGAGGGGGGGSRAPPEELSMFQLPTLNFSPEQVASVCETLEETGDIERLGRFLWSLPVAPGACEAINKHESILRARAVVAFHTGNFRDLYHILENHKFTKESHGKLQAMWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHQAIGPSGMRSLAEPGCPTHGSAESPSTAASPTTSVSSLTERADTGTSI...
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 fib...
chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]
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]; signa...
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-po...
Homo sapiens (Human)
O95347
SMC2_HUMAN
MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLK...
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:00519...
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]
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 ...
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 fo...
Homo sapiens (Human)
O95352
ATG7_HUMAN
MAAATGDPGLSKLQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDMSAPTPARCCPAIGTLYNTNTLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFADLKKYHFYYWFCYPALCLPESLPLIQGPVGLDQRFSLKQIEALECAYDNLCQTEGVTALPYFLIKYDENMVLVSLLKHYSDFFQGQRTKITIGVYDPCNLAQYPGWPLRNFLVLAAHRWSSSFQSVEVVCFRDRTMQGARDVAHSIIFEVKLPEMAFSPDCPKAVGWEKNQKGGMGPRMVNLS...
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 microautop...
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 associ...
Homo sapiens (Human)
O95359
TACC2_HUMAN
MGNENSTSDNQRTLSAQTPRSAQPPGNSQNIKRKQQDTPGSPDHRDASSIGSVGLGGFCTASESSASLDPCLVSPEVTEPRKDPQGARGPEGSLLPSPPPSQEREHPSSSMPFAECPPEGCLASPAAAPEDGPQTQSPRREPAPNAPGDIAAAFPAERDSSTPYQEIAAVPSAGRERQPKEEGQKSSFSFSSGIDQSPGMSPVPLREPMKAPLCGEGDQPGGFESQEKEAAGGFPPAESRQGVASVQVTPEAPAAAQQGTESSAVLEKSPLKPMAPIPQDPAPRASDRERGQGEAPPQYLTDDLEFLRACHLPRSNSGAA...
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 pr...
Homo sapiens (Human)
O95361
TRI16_HUMAN
MAELDLMAPGPLPRATAQPPAPLSPDSGSPSPDSGSASPVEEEDVGSSEKLGRETEEQDSDSAEQGDPAGEGKEVLCDFCLDDTRRVKAVKSCLTCMVNYCEEHLQPHQVNIKLQSHLLTEPVKDHNWRYCPAHHSPLSAFCCPDQQCICQDCCQEHSGHTIVSLDAARRDKEAELQCTQLDLERKLKLNENAISRLQANQKSVLVSVSEVKAVAEMQFGELLAAVRKAQANVMLFLEEKEQAALSQANGIKAHLEYRSAEMEKSKQELERMAAISNTVQFLEEYCKFKNTEDITFPSVYVGLKDKLSGIRKVITESTVH...
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]; res...
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 th...
Homo sapiens (Human)
O95363
SYFM_HUMAN
MVGSALRRGAHAYVYLVSKASHISRGHQHQAWGSRPPAAECATQRAPGSVVELLGKSYPQDDHSNLTRKVLTRVGRNLHNQQHHPLWLIKERVKEHFYKQYVGRFGTPLFSVYDNLSPVVTTWQNFDSLLIPADHPSRKKGDNYYLNRTHMLRAHTSAHQWDLLHAGLDAFLVVGDVYRRDQIDSQHYPIFHQLEAVRLFSKHELFAGIKDGESLQLFEQSSRSAHKQETHTMEAVKLVEFDLKQTLTRLMAHLFGDELEIRWVDCYFPFTHPSFEMEINFHGEWLEVLGCGVMEQQLVNSAGAQDRIGWAFGLGLERLA...
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...
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=...
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 a...
Homo sapiens (Human)
O95365
ZBT7A_HUMAN
MAGGVDGPIGIPFPDHSSDILSGLNEQRTQGLLCDVVILVEGREFPTHRSVLAACSQYFKKLFTSGAVVDQQNVYEIDFVSAEALTALMDFAYTATLTVSTANVGDILSAARLLEIPAVSHVCADLLDRQILAADAGADAGQLDLVDQIDQRNLLRAKEYLEFFQSNPMNSLPPAAAAAAASFPWSAFGASDDDLDATKEAVAAAVAAVAAGDCNGLDFYGPGPPAERPPTGDGDEGDSNPGLWPERDEDAPTGGLFPPPVAPPAATQNGHYGRGGEEEAASLSEAAPEPGDSPGFLSGAAEGEDGDGPDVDGLAASTLL...
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 reg...
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 acet...
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]GACCCCC...
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|PubMe...
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...
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 lysophospholipa...
Homo sapiens (Human)
O95373
IPO7_HUMAN
MDPNTIIEALRGTMDPALREAAERQLNEAHKSLNFVSTLLQITMSEQLDLPVRQAGVIYLKNMITQYWPDRETAPGDISPYTIPEEDRHCIRENIVEAIIHSPELIRVQLTTCIHHIIKHDYPSRWTAIVDKIGFYLQSDNSACWLGILLCLYQLVKNYEYKKPEERSPLVAAMQHFLPVLKDRFIQLLSDQSDQSVLIQKQIFKIFYALVQYTLPLELINQQNLTEWIEILKTVVNRDVPNETLQVEEDDRPELPWWKCKKWALHILARLFERYGSPGNVSKEYNEFAEVFLKAFAVGVQQVLLKVLYQYKEKQYMAPR...
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:...
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 i...
Homo sapiens (Human)
O95376
ARI2_HUMAN
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALNEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYKSNSAQLLVEARVQPNPSKHVPTSHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGVSCMAQDCPLRTPEDFVFPLLPNEELREKYRRYLFRDYVESHYQLQLCPGADCPMVIRVQEPRARRVQCNRCNEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKH...
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-l...
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:193400...
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 comp...
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:000...
Homo sapiens (Human)
O95382
M3K6_HUMAN
MAGPCPRSGAERAGSCWQDPLAVALSRGRQLAAPPGRGCARSRPLSVVYVLTREPQPGLEPREGTEAEPLPLRCLREACAQVPRPRPPPQLRSLPFGTLELGDTAALDAFYNADVVVLEVSSSLVQPSLFYHLGVRESFSMTNNVLLCSQADLPDLQALREDVFQKNSDCVGSYTLIPYVVTATGRVLCGDAGLLRGLADGLVQAGVGTEALLTPLVGRLARLLEATPTDSCGYFRETIRRDIRQARERFSGPQLRQELARLQRRLDSVELLSPDIIMNLLLSYRDVQDYSAIIELVETLQALPTCDVAEQHNVCFHYTF...
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-[p...
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
MRWFLPWTLAAVTAAAASTVLATALSPAPTTMDFTPAPLEDTSSRPQFCKWPCECPPSPPRCPLGVSLITDGCECCKMCAQQLGDNCTEAAICDPHRGLYCDYSGDRPRYAIGVCAQVVGVGCVLDGVRYNNGQSFQPNCKYNCTCIDGAVGCTPLCLRVRPPRLWCPHPRRVSIPGHCCEQWVCEDDAKRPRKTAPRDTGAFDAVGEVEAWHRNCIAYTSPWSPCSTSCGLGVSTRISNVNAQCWPEQESRLCNLRPCDVDIHTLIKAGKKCLAVYQPEASMNFTLAGCISTRSYQPKYCGVCMDNRCCIPYKSKTIDV...
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 differentiatio...
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 fibrobla...
Homo sapiens (Human)
O95389
CCN6_HUMAN
MQGLLFSTLLLAGLAQFCCRVQGTGPLDTTPEGRPGEVSDAPQRKQFCHWPCKCPQQKPRCPPGVSLVRDGCGCCKICAKQPGEICNEADLCDPHKGLYCDYSVDRPRYETGVCAYLVAVGCEFNQVHYHNGQVFQPNPLFSCLCVSGAIGCTPLFIPKLAGSHCSGAKGGKKSDQSNCSLEPLLQQLSTSYKTMPAYRNLPLIWKKKCLVQATKWTPCSRTCGMGISNRVTNENSNCEMRKEKRLCYIQPCDSNILKTIKIPKGKTCQPTFQLSKAEKFVFSGCSSTQSYKPTFCGICLDKRCCIPNKSKMITIQFDCP...
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...
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|Pub...
Homo sapiens (Human)
O95390
GDF11_HUMAN
MVLAAPLLLGFLLLALELRPRGEAAEGPAAAAAAAAAAAAAGVGGERSSRPAPSVAPEPDGCPVCVWRQHSRELRLESIKSQILSKLRLKEAPNISREVVKQLLPKAPPLQQILDLHDFQGDALQPEDFLEEDEYHATTETVISMAQETDPAVQTDGSPLCCHFHFSPKVMFTKVLKAQLWVYLRPVPRPATVYLQILRLKPLTGEGTAGGGGGGRRHIRIRSLKIELHSRSGHWQSIDFKQVLHSWFRQPQSNWGIEINAFDPSGTDLAVTSLGPGAEGLHPFMELRVLENTKRSRRNLGLDCDEHSSESRCCRYPLTV...
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];...
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 ...
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 r...
Homo sapiens (Human)
O95391
SLU7_HUMAN
MSATVVDAVNAAPLSGSKEMSLEEPKKMTREDWRKKKELEEQRKLGNAPAEVDEEGKDINPHIPQYISSVPWYIDPSKRPTLKHQRPQPEKQKQFSSSGEWYKRGVKENSIITKYRKGACENCGAMTHKKKDCFERPRRVGAKFTGTNIAPDEHVQPQLMFDYDGKRDRWNGYNPEEHMKIVEEYAKVDLAKRTLKAQKLQEELASGKLVEQANSPKHQWGEEEPNSQMEKDHNSEDEDEDKYADDIDMPGQNFDSKRRITVRNLRIREDIAKYLRNLDPNSAYYDPKTRAMRENPYANAGKNPDEVSYAGDNFVRYTGD...
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 [G...
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 regul...
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...
Homo sapiens (Human)
O95393
BMP10_HUMAN
MGSLVLTLCALFCLAAYLVSGSPIMNLEQSPLEEDMSLFGDVFSEQDGVDFNTLLQSMKDEFLKTLNLSDIPTQDSAKVDPPEYMLELYNKFATDRTSMPSANIIRSFKNEDLFSQPVSFNGLRKYPLLFNVSIPHHEEVIMAELRLYTLVQRDRMIYDGVDRKITIFEVLESKGDNEGERNMLVLVSGEIYGTNSEWETFDVTDAIRRWQKSGSSTHQLEVHIESKHDEAEDASSGRLEIDTSAQNKHNPLLIVFSDDQSSDKERKEELNEMISHEQLPELDNLGLDSFSSGPGEEALLQMRSNIIYDSTARIRRNAKG...
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:0...
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 an...
Homo sapiens (Human)
O95394
AGM1_HUMAN
MDLGAITKYSALHAKPNGLILQYGTAGFRTKAEHLDHVMFRMGLLAVLRSKQTKSTIGVMVTASHNPEEDNGVKLVDPLGEMLAPSWEEHATCLANAEEQDMQRVLIDISEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGGRYGKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELLVEIGESL...
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
MVQWKRLCQLHYLWALGCYMLLATVALKLSFRLKCDSDHLGLESRESQSQYCRNILYNFLKLPAKRSINCSGVTRGDQEAVLQAILNNLEVKKKREPFTDTHYLSLTRDCEHFKAERKFIQFPLSKEEVEFPIAYSMVIHEKIENFERLLRAVYAPQNIYCVHVDEKSPETFKEAVKAIISCFPNVFIASKLVRVVYASWSRVQADLNCMEDLLQSSVPWKYFLNTCGTDFPIKSNAEMVQALKMLNGRNSMESEVPPKHKETRWKYHFEVVRDTLHLTNKKKDPPPYNLTMFTGNAYIVASRDFVQHVLKNPKSQQLIE...
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-gly...
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:13...
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 ...
Homo sapiens (Human)
O95396
MOCS3_HUMAN
MASREEVLALQAEVAQREEELNSLKQKLASALLAEQEPQPERLVPVSPLPPKAALSRDEILRYSRQLVLPELGVHGQLRLGTACVLIVGCGGLGCPLAQYLAAAGVGRLGLVDYDVVEMSNLARQVLHGEALAGQAKAFSAAASLRRLNSAVECVPYTQALTPATALDLVRRYDVVADCSDNVPTRYLVNDACVLAGRPLVSASALRFEGQITVYHYDGGPCYRCIFPQPPPAETVTNCADGGVLGVVTGVLGCLQALEVLKIAAGLGPSYSGSLLLFDALRGHFRSIRLRSRRLDCAACGERPTVTDLLDYEAFCGSSA...
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]; thios...
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, ...
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 URM...
Homo sapiens (Human)
O95398
RPGF3_HUMAN
MKVGWPGESCWQVGLAVEDSPALGAPRVGALPDVVPEGTLLNMVLRRMHRPRSCSYQLLLEHQRPSCIQGLRWTPLTNSEESLDFSESLEQASTERVLRAGRQLHRHLLATCPNLIRDRKYHLRLYRQCCSGRELVDGILALGLGVHSRSQVVGICQVLLDEGALCHVKHDWAFQDRDAQFYRFPGPEPEPVRTHEMEEELAEAVALLSQRGPDALLTVALRKPPGQRTDEELDLIFEELLHIKAVAHLSNSVKRELAAVLLFEPHSKAGTVLFSQGDKGTSWYIIWKGSVNVVTHGKGLVTTLHEGDDFGQLALVNDAP...
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:00...
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 ...
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
MPKRKVTFQGVGDEEDEDEIIVPKKKLVDPVAGSGGPGSRFKGKHSLDSDEEEDDDDGGSSKYDILASEDVEGQEAATLPSEGGVRITPFNLQEEMEEGHFDADGNYFLNRDAQIRDSWLDNIDWVKIRERPPGQRQASDSEEEDSLGQTSMSAQALLEGLLELLLPRETVAGALRRLGARGGGKGRKGPGQPSSPQRLDRLSGLADQMVARGNLGVYQETRERLAMRLKGLGCQTLGPHNPTPPPSLDMFAEELAEEELETPTPTQRGEAESRGDGLVDVMWEYKWENTGDAELYGPFTSAQMQTWVSEGYFPDGVYCR...
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
MTAAPASPQQIRDRLLQAIDPQSNIRNMVAVLEVISSLEKYPITKEALEETRLGKLINDVRKKTKNEELAKRAKKLLRSWQKLIEPAHQHEAALRGLAGATGSANGGAHNCRPEVGAAGPPRSIHDLKSRNDLQRLPGQRLDRLGSRKRRGDQRDLGHPGPPPKVSKASHDPLVPNSSPLPTNGISGSPESFASSLDGSGHAGPEGSRLERDENDKHSGKIPVNAVRPHTSSPGLGKPPGPCLQPKASVLQQLDRVDETPGPPHPKGPPRCSFSPRNSRHEGSFARQQSLYAPKGSVPSPSPRPQALDATQVPSPLPLAQ...
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 comple...
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...
Homo sapiens (Human)
O95405
ZFYV9_HUMAN
MENYFQAEAYNLDKVLDEFEQNEDETVSSTLLDTKWNKILDPPSHRLSFNPTLASVNESAVSNESQPQLKVFSLAHSAPLTTEEEDHCANGQDCNLNPEIATMWIDENAVAEDQLIKRNYSWDDQCSAVEVGEKKCGNLACLPDEKNVLVVAVMHNCDKRTLQNDLQDCNNYNSQSLMDAFSCSLDNENRQTDQFSFSINESTEKDMNSEKQMDPLNRPKTEGRSVNHLCPTSSDSLASVCSPSQLKDDGSIGRDPSMSAITSLTVDSVISSQGTDGCPAVKKQENYIPDEDLTGKISSPRTDLGSPNSFSHMSEGILMK...
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 a...
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
MLLDAGPQFPAIGVGSFARHHHHSAAAAAAAAAEMQDRELSLAAAQNGFVDSAAAHMGAFKLNPGAHELSPGQSSAFTSQGPGAYPGSAAAAAAAAALGPHAAHVGSYSGPPFNSTRDFLFRSRGFGDSAPGGGQHGLFGPGAGGLHHAHSDAQGHLLFPGLPEQHGPHGSQNVLNGQMRLGLPGEVFGRSEQYRQVASPRTDPYSAAQLHNQYGPMNMNMGMNMAAAAAHHHHHHHHHPGAFFRYMRQQCIKQELICKWIDPEQLSNPKKSCNKTFSTMHELVTHVSVEHVGGPEQSNHVCFWEECPREGKPFKAKYKL...
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:00458...
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 transc...
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}.; SUBCELLULA...
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 different...
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...
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
MKRKERIARRLEGIENDTQPILLQSCTGLVTHRLLEEDTPRYMRASDPASPHIGRSNEEEETSDSSLEKQTRSKYCTETSGVHGDSPYGSGTMDTHSLESKAERIARYKAERRRQLAEKYGLTLDPEADSEYLSRYTKSRKEPDAVEKRGGKSDKQEESSRDASSLYPGTETMGLRTCAGESKDYALHVGDGSSDPEVLLNIENQRRGQELSATRQAHDLSPAAESSSTFSFSGRDSSFTEVPRSPKHAHSSSLQQAASRSPSFGDPQLSPEARPSTGKPKHEWFLQKDSEGDTPSLINWPSRVKVREKLVKEESARNSP...
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:00021...
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 memb...
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 myos...
Homo sapiens (Human)
O95427
PIGN_HUMAN
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVN...
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 misseg...
Homo sapiens (Human)
O95428
PPN_HUMAN
MRLLLLVPLLLAPAPGSSAPKVRRQSDTWGPWSQWSPCSRTCGGGVSFRERPCYSQRRDGGSSCVGPARSHRSCRTESCPDGARDFRAEQCAEFDGAEFQGRRYRWLPYYSAPNKCELNCIPKGENFYYKHREAVVDGTPCEPGKRDVCVDGSCRVVGCDHELDSSKQEDKCLRCGGDGTTCYPVAGTFDANDLSRGYNQILIVPMGATSILIDEAAASRNFLAVKNVRGEYYLNGHWTIEAARALPAASTILHYERGAEGDLAPERLHARGPTSEPLVIELISQEPNPGVHYEYHLPLRRPSPGFSWSHGSWSDCSAEC...
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
MSALRRSGYGPSDGPSYGRYYGPGGGDVPVHPPPPLYPLRPEPPQPPISWRVRGGGPAETTWLGEGGGGDGYYPSGGAWPEPGRAGGSHQEQPPYPSYNSNYWNSTARSRAPYPSTYPVRPELQGQSLNSYTNGAYGPTYPPGPGANTASYSGAYYAPGYTQTSYSTEVPSTYRSSGNSPTPVSRWIYPQQDCQTEAPPLRGQVPGYPPSQNPGMTLPHYPYGDGNRSVPQSGPTVRPQEDAWASPGAYGMGGRYPWPSSAPSAPPGNLYMTESTSPWPSSGSPQSPPSPPVQQPKDSSYPYSQSDQSMNRHNFPCSVHQ...
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 regu...
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
MAKWGEGDPRWIVEERADATNVNNWHWTERDASNWSTDKLKTLFLAVQVQNEEGKCEVTEVSKLDGEASINNRKGKLIFFYEWSVKLNWTGTSKSGVQYKGHVEIPNLSDENSVDEVEISVSLAKDEPDTNLVALMKEEGVKLLREAMGIYISTLKTEFTQGMILPTMNGESVDPVGQPALKTEERKAKPAPSKTQARPVGVKIPTCKITLKETFLTSPEELYRVFTTQELVQAFTHAPATLEADRGGKFHMVDGNVSGEFTDLVPEKHIVMKWRFKSWPEGHFATITLTFIDKNGETELCMEGRGIPAPEEERTRQGWQ...
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 clien...
Homo sapiens (Human)
O95436
NPT2B_HUMAN
MAPWPELGDAQPNPDKYLEGAAGQQPTAPDKSKETNKTDNTEAPVTKIELLPSYSTATLIDEPTEVDDPWNLPTLQDSGIKWSERDTKGKILCFFQGIGRLILLLGFLYFFVCSLDILSSAFQLVGGKMAGQFFSNSSIMSNPLLGLVIGVLVTVLVQSSSTSTSIVVSMVSSSLLTVRAAIPIIMGANIGTSITNTIVALMQVGDRSEFRRAFAGATVHDFFNWLSVLVLLPVEVATHYLEIITQLIVESFHFKNGEDAPDLLKVITKPFTKLIVQLDKKVISQIAMNDEKAKNKSLVKIWCKTFTNKTQINVTVPSTA...
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 ACTIVIT...
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 l...
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
MSLADLTKTNIDEHFFGVALENNRRSAACKRSPGTGDFSRNSNASNKSVDYSRSQCSCGSLSSQYDYSEDFLCDCSEKAINRNYLKQPVVKEKEKKKYNVSKISQSKGQKEISVEKKHTWNASLFNSQIHMIAQRRDAMAHRILSARLHKIKGLKNELADMHHKLEAILTENQFLKQLQLRHLKAIGKYENSQNNLPQIMAKHQNEVKNLRQLLRKSQEKERTLSRKLRETDSQLLKTKDILQALQKLSEDKNLAEREELTHKLSIITTKMDANDKKIQSLEKQLRLNCRAFSRQLAIETRKTLAAQTATKTLQVEVKHL...
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
MDPPAGAARRLLCPALLLLLLLLPPPLLPPPPPPANARLAAAADPPGGPLGHGAERILAVPVRTDAQGRLVSHVVSAATSRAGVRARRAAPVRTPSFPGGNEEEPGSHLFYNVTVFGRDLHLRLRPNARLVAPGATMEWQGEKGTTRVEPLLGSCLYVGDVAGLAEASSVALSNCDGLAGLIRMEEEEFFIEPLEKGLAAQEAEQGRVHVVYRRPPTSPPLGGPQALDTGASLDSLDSLSRALGVLEEHANSSRRRARRHAADDDYNIEVLLGVDDSVVQFHGKEHVQKYLLTLMNIVNEIYHDESLGAHINVVLVRIIL...
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, re...
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). {E...
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 o...
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
MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFP...
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-de...
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 ...
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:...
Homo sapiens (Human)
O95460
MATN4_HUMAN
MRGLLCWPVLLLLLQPWETQLQLTGPRCHTGPLDLVFVIDSSRSVRPFEFETMRQFLMGLLRGLNVGPNATRVGVIQYSSQVQSVFPLRAFSRREDMERAIRDLVPLAQGTMTGLAIQYAMNVAFSVAEGARPPEERVPRVAVIVTDGRPQDRVAEVAAQARARGIEIYAVGVQRADVGSLRAMASPPLDEHVFLVESFDLIQEFGLQFQSRLCGKDQCAEGGHGCQHQCVNAWAMFHCTCNPGYKLAADNKSCLAIDLCAEGTHGCEHHCVNSPGSYFCHCQVGFVLQQDQRSCRAIDYCSFGNHSCQHECVSTPGGPR...
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
MLGICRGRRKFLAASLSLLCIPAITWIYLFSGSFEDGKPVSLSPLESQAHSPRYTASSQRERESLEVRMREVEEENRALRRQLSLAQGRAPSHRRGNHSKTYSMEEGTGDSENLRAGIVAGNSSECGQQPVVEKCETIHVAIVCAGYNASRDVVTLVKSVLFHRRNPLHFHLIADSIAEQILATLFQTWMVPAVRVDFYNADELKSEVSWIPNKHYSGIYGLMKLVLTKTLPANLERVIVLDTDITFATDIAELWAVFHKFKGQQVLGLVENQSDWYLGNLWKNHRPWPALGRGYNTGVILLLLDKLRKMKWEQMWRLTA...
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 develop...
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...
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,...
Homo sapiens (Human)
O95466
FMNL1_HUMAN
MGNAAGSAEQPAGPAAPPPKQPAPPKQPMPAAGELEERFNRALNCMNLPPDKVQLLSQYDNEKKWELICDQERFQVKNPPAAYIQKLKSYVDTGGVSRKVAADWMSNLGFKRRVQESTQVLRELETSLRTNHIGWVQEFLNEENRGLDVLLEYLAFAQCSVTYDMESTDNGASNSEKNKPLEQSVEDLSKGPPSSVPKSRHLTIKLTPAHSRKALRNSRIVSQKDDVHVCIMCLRAIMNYQSGFSLVMNHPACVNEIALSLNNKNPRTKALVLELLAAVCLVRGGHDIILAAFDNFKEVCGEQHRFEKLMEYFRNEDSNI...
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). ...
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
MPSTDLLMLKAFEPYLEILEVYSTKAKNYVNGHCTKYEPWQLIAWSVVWTLLIVWGYEFVFQPESLWSRFKKKCFKLTRKMPIIGRKIQDKLNKTKDDISKNMSFLKVDKEYVKALPSQGLSSSAVLEKLKEYSSMDAFWQEGRASGTVYSGEEKLTELLVKAYGDFAWSNPLHPDIFPGLRKIEAEIVRIACSLFNGGPDSCGCVTSGGTESILMACKAYRDLAFEKGIKTPEIVAPQSAHAAFNKAASYFGMKIVRVPLTKMMEVDVRAMRRAISRNTAMLVCSTPQFPHGVIDPVPEVAKLAVKYKIPLHVDACLGG...
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]...
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}; Physiologic...
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 chole...
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-containin...
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 th...
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 biosynt...
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-...
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 differ...
Homo sapiens (Human)
O95477
ABCA1_HUMAN
MACWPQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQIKKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKVFLQGYQLHLTSLCNGSKSEEMIQLGDQEVSELCGLPREKLAAAERVLRSNMDILKPILRTLNSTSPFPSKELAEATKTLLHSLGTLAQELFSMRSWSDMRQEVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIK...
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]; c...
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 r...
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:...
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=Rh...
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 (Pub...
Homo sapiens (Human)
O95479
G6PE_HUMAN
MWNMLIVAMCLALLGCLQAQELQGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGRGHSFSFHGAALTAPKQGQELMAKALESLSCPKDMAPSHCAEHKDQFLQLSQYRQLKTAEDYQALNKDIEAQLQHAGLREAGRIFYFSVPPFAYEDIARNINSSCRPGPGAWLRVVLEKPFGHDHFSAQQLATELGTFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEIIMKETVDAEGRTSFYEEYGVIRDVLQNHLTEVLTLVAMELPHNVSSAEAVLRHKLQVFQALRGLQRGSAVVGQYQSYSEQV...
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 [...
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}; Physiolog...
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...
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). H...
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...
Homo sapiens (Human)
O95486
SC24A_HUMAN
MSQPGIPASGGAPASLQAQNGAALASGSPYTNGPVQNALLSSQESVSQGYNFQLPGSYPHPIPAKTLNPVSGQSNYGGSQGSGQTLNRPPVASNPVTPSLHSGPAPRMPLPASQNPATTPMPSSSFLPEANLPPPLNWQYNYPSTASQTNHCPRASSQPTVSGNTSLTTNHQYVSSGYPSLQNSFIKSGPSVPPLVNPPLPTTFQPGAPHGPPPAGGPPPVRALTPLTSSYRDVPQPLFNSAVNQEGITSNTNNGSMVVHSSYDEIEGGGLLATPQLTNKNPKMSRSVGYSYPSLPPGYQNTTPPGATGVPPSSLNYPSG...
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...
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...
Homo sapiens (Human)
O95487
SC24B_HUMAN
MSAPAGSSHPAASARIPPKFGGAAVSGAAAPAGPGAGPAPHQQNGPAQNQMQVPSGYGLHHQNYIAPSGHYSQGPGKMTSLPLDTQCGDYYSALYTVPTQNVTPNTVNQQPGAQQLYSRGPPAPHIVGSTLGSFQGAASSASHLHTSASQPYSSFVNHYNSPAMYSASSSVASQGFPSTCGHYAMSTVSNAAYPSVSYPSLPAGDTYGQMFTSQNAPTVRPVKDNSFSGQNTAISHPSPLPPLPSQQHHQQQSLSGYSTLTWSSPGLPSTQDNLIRNHTGSLAVANNNPTITVADSLSCPVMQNVQPPKSSPVVSTVLSG...
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 p...
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...
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...
Homo sapiens (Human)
O95490
AGRL2_HUMAN
MVSSGCRMRSLWFIIVISFLPNTEGFSRAALPFGLVRRELSCEGYSIDLRCPGSDVIMIESANYGRTDDKICDADPFQMENTDCYLPDAFKIMTQRCNNRTQCIVVTGSDVFPDPCPGTYKYLEVQYECVPYIFVCPGTLKAIVDSPCIYEAEQKAGAWCKDPLQAADKIYFMPWTPYRTDTLIEYASLEDFQNSRQTTTYKLPNRVDGTGFVVYDGAVFFNKERTRNIVKFDLRTRIKSGEAIINYANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEQNNGMIVISQLNPYTLRFEATWETVYDKRAASNAFMICGV...
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
MTTQLPAYVAILLFYVSRASCQDTFTAAVYEHAAILPNATLTPVSREEALALMNRNLDILEGAITSAADQGAHIIVTPEDAIYGWNFNRDSLYPYLEDIPDPEVNWIPCNNRNRFGQTPVQERLSCLAKNNSIYVVANIGDKKPCDTSDPQCPPDGRYQYNTDVVFDSQGKLVARYHKQNLFMGENQFNVPKEPEIVTFNTTFGSFGIFTCFDILFHDPAVTLVKDFHVDTIVFPTAWMNVLPHLSAVEFHSAWAMGMRVNFLASNIHYPSKKMTGSGIYAPNSSRAFHYDMKTEEGKLLLSQLDSHPSHSAVVNWTSYA...
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-...
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
MVTSSFPISVAVFALITLQVGTQDSFIAAVYEHAVILPNKTETPVSQEDALNLMNENIDILETAIKQAAEQGARIIVTPEDALYGWKFTRETVFPYLEDIPDPQVNWIPCQDPHRFGHTPVQARLSCLAKDNSIYVLANLGDKKPCNSRDSTCPPNGYFQYNTNVVYNTEGKLVARYHKYHLYSEPQFNVPEKPELVTFNTAFGRFGIFTCFDIFFYDPGVTLVKDFHVDTILFPTAWMNVLPLLTAIEFHSAWAMGMGVNLLVANTHHVSLNMTGSGIYAPNGPKVYHYDMKTELGKLLLSEVDSHPLSSLAYPTAVNW...
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|Pub...
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 o...
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
MELSAVGERVFAAESIIKRRIRKGRIEYLVKWKGWAIKYSTWEPEENILDSRLIAAFEQKERERELYGPKKRGPKPKTFLLKARAQAEALRISDVHFSVKPSASASSPKLHSSAAVHRLKKDIRRCHRMSRRPLPRPDPQGGSPGLRPPISPFSETVRIINRKVKPREPKRNRIILNLKVIDKGAGGGGAGQGAGALARPKVPSRNRVIGKSKKFSESVLRTQIRHMKFGAFALYKPPPAPLVAPSPGKAEASAPGPGLLLAAPAAPYDARSSGSSGCPSPTPQSSDPDDTPPKLLPETVSPSAPSWREPEVLDLSLPPE...
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...
Homo sapiens (Human)
O95528
GTR10_HUMAN
MGHSPPVLPLCASVSLLGGLTFGYELAVISGALLPLQLDFGLSCLEQEFLVGSLLLGALLASLVGGFLIDCYGRKQAILGSNLVLLAGSLTLGLAGSLAWLVLGRAVVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEAGITVGILLSYALNYALAGTPWGWRHMFGWATAPAVLQSLSLLFLPAGTDETATHKDLIPLQGGEAPKLGPGRPRYSFLDLFRARDNMRGRTTVGLGLVLFQQLTGQPNVLCYASTIFSSVGFHGGSSAVLASVGLGAVKVAATLTAMGLVDRAGRRALLLAGCALMALSVSGIGLVSFA...
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 t...
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
MEMEQEKMTMNKELSPDAAAYCCSACHGDETWSYNHPIRGRAKSRSLSASPALGSTKEFRRTRSLHGPCPVTTFGPKACVLQNPQTIMHIQDPASQRLTWNKSPKSVLVIKKMRDASLLQPFKELCTHLMEENMIVYVEKKVLEDPAIASDESFGAVKKKFCTFREDYDDISNQIDFIICLGGDGTLLYASSLFQGSVPPVMAFHLGSLGFLTPFSFENFQSQVTQVIEGNAAVVLRSRLKVRVVKELRGKKTAVHNGLGENGSQAAGLDMDVGKQAMQYQVLNEVVIDRGPSSYLSNVDVYLDGHLITTVQGDGVIVST...
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
MELGSCLEGGREAAEEEGEPEVKKRRLLCVEFASVASCDAAVAQCFLAENDWEMERALNSYFEPPVEESALERRPETISEPKTYVDLTNEETTDSTTSKISPSEDTQQENGSMFSLITWNIDGLDLNNLSERARGVCSYLALYSPDVIFLQEVIPPYYSYLKKRSSNYEIITGHEEGYFTAIMLKKSRVKLKSQEIIPFPSTKMMRNLLCVHVNVSGNELCLMTSHLESTRGHAAERMNQLKMVLKKMQEAPESATVIFAGDTNLRDREVTRCGGLPNNIVDVWEFLGKPKHCQYTWDTQMNSNLGITAACKLRFDRIFF...
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|...
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:00002...
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 phosp...
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
MTFQFNFTIEDHLENELTPIRDGALTLDSSKELSVSESQKGEERDRKCSAEQFDLPQDHLWEHKSMENAAPSQDTDSPLSAASSSRNLEPHGKQPSLRAAKEHAMPKDLKKMLENKVIETLPGFQHVKLSVVKTILLKENFPGENIVSKSFSSHSDLITGVYEGGLKIWECTFDLLAYFTKAKVKFAGKKVLDLGCGSGLLGITAFKGGSKEIHFQDYNSMVIDEVTLPNVVANSTLEDEENDVNEPDVKRCRKPKVTQLYKCRFFSGEWSEFCKLVLSSEKLFVKYDLILTSETIYNPDYYSNLHQTFLRLLSKNGRVL...
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=2.1.1.8...
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 ...
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:0...
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 transferre...
Homo sapiens (Human)
O95573
ACSL3_HUMAN
MNNHVSSKPSTMKLKHTINPILLYFIHFLISLYTILTYIPFYFFSESRQEKSNRIKAKPVNSKPDSAYRSVNSLDGLASVLYPGCDTLDKVFTYAKNKFKNKRLLGTREVLNEEDEVQPNGKIFKKVILGQYNWLSYEDVFVRAFNFGNGLQMLGQKPKTNIAIFCETRAEWMIAAQACFMYNFQLVTLYATLGGPAIVHALNETEVTNIITSKELLQTKLKDIVSLVPRLRHIITVDGKPPTWSEFPKGIIVHTMAAVEALGAKASMENQPHSKPLPSDIAVIMYTSGSTGLPKGVMISHSNIIAGITGMAERIPELGE...
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 regul...
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 memb...
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}; PhysiologicalDi...
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...
Homo sapiens (Human)
O95600
KLF8_HUMAN
MVDMDKLINNLEVQLNSEGGSMQVFKQVTASVRNRDPPEIEYRSNMTSPTLLDANPMENPALFNDIKIEPPEELLASDFSLPQVEPVDLSFHKPKAPLQPASMLQAPIRPPKPQSSPQTLVVSTSTSDMSTSANIPTVLTPGSVLTSSQSTGSQQILHVIHTIPSVSLPNKMGGLKTIPVVVQSLPMVYTTLPADGGPAAITVPLIGGDGKNAGSVKVDPTSMSPLEIPSDSEESTIESGSSALQSLQGLQQEPAAMAQMQGEESLDLKRRRIHQCDFAGCSKVYTKSSHLKAHRRIHTGEKPYKCTWDGCSWKFARSDE...
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:16...
Homo sapiens (Human)
O95602
RPA1_HUMAN
MLISKNMPWRRLQGISFGMYSAEELKKLSVKSITNPRYLDSLGNPSANGLYDLALGPADSKEVCSTCVQDFSNCSGHLGHIELPLTVYNPLLFDKLYLLLRGSCLNCHMLTCPRAVIHLLLCQLRVLEVGALQAVYELERILNRFLEENPDPSASEIREELEQYTTEIVQNNLLGSQGAHVKNVCESKSKLIALFWKAHMNAKRCPHCKTGRSVVRKEHNSKLTITFPAMVHRTAGQKDSEPLGIEEAQIGKRGYLTPTSAREHLSALWKNEGFFLNYLFSGMDDDGMESRFNPSVFFLDFLVVPPSRYRPVSRLGDQMF...
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:...
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:112509...
Homo sapiens (Human)