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
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
O94236
|
EIF3D_SCHPO
|
MATGFKLPELAPVKSAWGPPETEQIGGDIPYAPFSKGDRLGKIADWSVDQPKDGREQRGRQGAFAGRFRDQYQTYGYGASSIFGYQHSEDESSFSVIDRGSVNRTRTSARNGGTLLKVRGRGQNVQRGGRGGRYGSSGGRGAGDTVVSRSSGAGGARGRRFGWKDYDKHQRLRNASVTVGDDWQLLDEVEFSHLSKLNLAAAAPVTVDSYGYIYPYDKSFDKIHVKSEKPLQALDRVHYNPTTTEDPVIQKLALNSDANIFITDSILSLLMCSTRSVYPWDIVITHQSGKLFFDKREGGPFDYLTVNENAYDSPMDADNREGVNSPGALSVEATYINQNFCVQALRETEEEKYKLPHPNPFYNSKEQSEPLAAHGYIYRDVDLSLETDEKPVKLMVRTEVDGYVKNPANDVQYISIKALNEYDPKFTNVTGSVDWRSKLESQRGAVFATEMKNNSCKLARWTVEALLAGVDSMKVGFVSRSNARDAQHHGILGVVAYKPADLASQMNLSLSNGWGIVRTIADVCLKMPDGKYVLVKDPNRPILRLYSVPPNTFEEAAGPSLEASSTA
| null | null |
cap-dependent translational initiation [GO:0002191]; formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413]
|
cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3e [GO:0071540]; eukaryotic translation initiation factor 3 complex, eIF3m [GO:0071541]
|
mRNA cap binding [GO:0098808]; translation initiation factor activity [GO:0003743]
|
PF05091;
| null |
EIF-3 subunit D family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03003, ECO:0000269|PubMed:9892665}.
| null | null | null | null | null |
FUNCTION: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs. {ECO:0000255|HAMAP-Rule:MF_03003, ECO:0000269|PubMed:11705997}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94244
|
HAT2_SCHPO
|
MSEEVVQDAPLENNELNAEIDLQKTIQEEYKLWKQNVPFLYDLVITHALEWPSLTIQWLPDKKTIPGTDYSIQRLILGTHTSGNDQNYLQIASVQLPNFDEDTTEFTPSTIRRAQATGSYTIEISQKIPHDGDVNRARYMPQKPEIIATMGEGGNAYIFDTTCHDALTTGEALPQAVLKGHTAEGFGLCWNPNLPGNLATGAEDQVICLWDVQTQSFTSSETKVISPIAKYHRHTDIVNDVQFHPQHEALLASVSDDCTLQIHDTRLNPEEEAPKVIQAHSKAINAVAINPFNDYLLATASADKTVALWDLRNPYQRLHTLEGHEDEVYGLEWSPHDEPILASSSTDRRVCIWDLEKIGEEQTPEDAEDGSPELLFMHGGHTNRISEFSWCPNERWVVGSLADDNILQIWSPSRVIWGRDHVQVSPRDLE
| null | null |
CENP-A containing chromatin assembly [GO:0034080]; chromatin remodeling [GO:0006338]; regulation of DNA-templated transcription [GO:0006355]
|
CENP-A recruiting complex [GO:0098654]; chromosome, centromeric region [GO:0000775]; cytoplasm [GO:0005737]; ESC/E(Z) complex [GO:0035098]; kinetochore [GO:0000776]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; Rpd3L complex [GO:0033698]; Rpd3L-Expanded complex [GO:0070210]
|
H3-H4 histone complex chaperone activity [GO:0000510]; histone binding [GO:0042393]; nucleosome binding [GO:0031491]
|
PF12265;PF00400;
|
2.130.10.10;
|
WD repeat RBAP46/RBAP48/MSI1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15369671}. Nucleus {ECO:0000269|PubMed:15369671}. Chromosome, centromere {ECO:0000269|PubMed:15369671}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:15369671}.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the histone acetylase B (HAT-B) complex (By similarity). The complex acetylates 'Lys-12' of histone H4 which is required for telomeric silencing (By similarity). Component of the CENP-A recruiting complex that ensures the integrity of mitotic spindles through maintenance of kinetochore factors mis6/CENP-I and cnp1/CENP-A (PubMed:15369671, PubMed:24774534, PubMed:24789708, PubMed:25375240). Maintains the deacetylated state of histones specifically in the central core of the centromeres (PubMed:15369671). {ECO:0000250|UniProtKB:P39984, ECO:0000269|PubMed:15369671, ECO:0000269|PubMed:24774534, ECO:0000269|PubMed:24789708, ECO:0000269|PubMed:25375240}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94267
|
SPT16_SCHPO
|
MAEYEIDEITFHKRLGILLTSWKNEEDGKTLFQDCDSILVTVGAHDDTNPYQKSTALHTWLLGYEFPSTLILLEKHRITILTSVNKANMLTKLAETKGAAADVNILKRTKDAEENKKLFEKIIEYIRATNKKVGVFPKDKTQGKFINEWDSIFEPVKSEFNLVDASLGLAKCLAIKDEQELANIKGASRVSVAVMSKYFVDELSTYIDQGKKITHSKFSDQMESLIDNEAFFQTKSLKLGDIDLDQLEWCYTPIIQSGGSYDLKPSAITDDRNLHGDVVLCSLGFRYKSYCSNVGRTYLFDPDSEQQKNYSFLVALQKKLFEYCRDGAVIGDIYTKILGLIRAKRPDLEPNFVRNLGAGIGIEFRESSLLVNAKNPRVLQAGMTLNLSIGFGNLINPHPKNSQSKEYALLLIDTIQITRSDPIVFTDSPKAQGDISYFFGEDDSSLEDGVKPRKPPTRGTATISSHKGKTRSETRDLDDSAEKRRVEHQKQLASRKQAEGLQRFAQGSVPSSGIEKPTVKRFESYKRDSQLPQAIGELRILVDYRAQSIILPIFGRPVPFHISTLKNASKNDEGNFVYLRLNFVSPGQIGGKKDELPFEDPNAQFIRSFTFRSSNNSRMSQVFKDIQDMKKAATKRETERKEFADVIEQDKLIEIKNKRPAHINDVYVRPAIDGKRLPGFIEIHQNGIRYQSPLRSDSHIDLLFSNMKHLFFQPCEGELIVLIHVHLKAPIMVGKRKTQDVQFYREVSDIQFDETGNKKRKYMYGDEDELEQEQEERRRRAQLDREFKSFAEKIAEASEGRIELDIPFRELAFNGVPFRSNVLLQPTTDCLVQLTDTPFTVITLNEIEIAHLERVQFGLKNFDLVFIFQDFRRPPIHINTIPMEQLDNVKEWLDSCDICFYEGPLNLNWTTIMKTVNEDPIAFFEEGGWGFLGAPSDDEGDDSVEEVSEYEASDADPSDEEEEESEEYSEDASEEDGYSESEVEDEESGEDWDELERKARQEDAKHDAFEERPSKKRHR
| null | null |
chromatin organization [GO:0006325]; constitutive heterochromatin formation [GO:0140719]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication-dependent chromatin assembly [GO:0006335]; nucleosome organization [GO:0034728]; transcription elongation by RNA polymerase II [GO:0006368]; transcription elongation-coupled chromatin remodeling [GO:0140673]
|
euchromatin [GO:0000791]; FACT complex [GO:0035101]; nucleus [GO:0005634]
|
H2A-H2B histone complex chaperone activity [GO:0000511]; histone chaperone activity [GO:0140713]; nucleosome binding [GO:0031491]
|
PF14826;PF00557;PF08512;PF08644;PF21091;
|
2.30.29.150;3.90.230.10;3.40.350.10;2.30.29.210;2.30.29.30;
|
Peptidase M24 family, SPT16 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y5B9}. Chromosome {ECO:0000250|UniProtKB:Q9Y5B9}.
| null | null | null | null | null |
FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity). {ECO:0000250|UniProtKB:Q9Y5B9}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94272
|
ATG8_SCHPO
|
MRSQFKDDFSFEKRKTESQRIREKYPDRIPVICEKVDKSDIAAIDKKKYLVPSDLTVGQFVYVIRKRIKLSPEKAIFIFIDEILPPTAALMSTIYEEHKSEDGFLYITYSGENTFGTVFPF
| null | null |
autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; cellular response to nitrogen starvation [GO:0006995]; macroautophagy [GO:0016236]; membrane fusion [GO:0061025]; protein transport [GO:0015031]; vacuole organization [GO:0007033]
|
autophagosome membrane [GO:0000421]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; fungal-type vacuole [GO:0000324]; fungal-type vacuole membrane [GO:0000329]; nucleus [GO:0005634]; phagophore assembly site [GO:0000407]
|
phosphatidylethanolamine binding [GO:0008429]; ubiquitin protein ligase binding [GO:0031625]
|
PF02991;
| null |
ATG8 family
|
PTM: The C-terminal 5 residues are removed to expose Gly-116 at the C-terminus. The C-terminal Gly is then amidated with phosphatidylethanolamine by an activating system similar to that for ubiquitin. {ECO:0000250|UniProtKB:P38182}.
|
SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane {ECO:0000269|PubMed:33138913}; Peripheral membrane protein {ECO:0000269|PubMed:33138913}.
| null | null | null | null | null |
FUNCTION: Ubiquitin-like modifier involved in autophagosomes formation. With atg4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The atg8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy (By similarity). Contributes to the maintenance of cell viability under conditions of nitrogen-depletion. Plays a role in meiosis and sporulation and contributes to oxidative stress resistance (PubMed:17295836, PubMed:19778961, PubMed:20070859). {ECO:0000250|UniProtKB:P38182, ECO:0000269|PubMed:17295836, ECO:0000269|PubMed:19778961, ECO:0000269|PubMed:20070859}.; FUNCTION: Has a lipidation-independent vacuolar function to facilitate the degradation of vacuolar integral membrane proteins during early-stationary vacuole turnover (EVT) when cells enter stationary phase. {ECO:0000269|PubMed:30451685}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94276
|
YORS_SCHPO
|
MDFKSRKYKIKKHPKDCKLHAKKYRGTLNSKGKNDNDCLIMCMRCRKVKGIDSYSKTQWSKTFTFVRGRTVSVSDPKVICRTCQPKQHDSIWCTACQQTKGINEFSKAQRHVLDPRCQICVHSQRNDGDDNLESDKFVDPFIGDDSDLDDDIYIHDKQTINSEYADDVSDNTDEERTESKGQQESNSAEEYDDDDSDEDRMEEIFQQFKKEKQIV
| null | null |
meiotic cell cycle [GO:0051321]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; silent mating-type cassette heterochromatin formation [GO:0030466]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]; subtelomeric heterochromatin formation [GO:0031509]
|
chromosome, telomeric region [GO:0000781]; nucleolus [GO:0005730]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
|
protein-macromolecule adaptor activity [GO:0030674]
|
PF12898;
|
3.30.60.210;
| null | null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Required for meiotic chromosome segregation. {ECO:0000269|PubMed:16169489}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94282
|
CTU1_SCHPO
|
MSNKLCQLCNERRPALVRPKTGQKICKECFYYVFETEIHNVIIENKLFVRGERVGIGASGGKDSTVLAYVMKLLNERYDYGLELYLISVDEGIRGYRDDSLDTVKRNQQQYGLPMKIVSYADLYDGWTMDNVVARIGTKNNCTYCGVFRRQALDRAALSLDIHHLVTGHNADDIAETILMNLLRGDVARLPRSTEITTQSDSSPTKRSKPFKYSYEKEIVLYAHYKKLDYFSTECTYSPEAFRGTARAMIKQLENIRPSSILDIIYSGESMQLASSVQEQLPQQTTCERCGFISSNRICKACMLLEGLNKGITGLGLGSDRKTKKLQSQIPACAE
|
2.7.7.-
| null |
protein urmylation [GO:0032447]; tRNA thio-modification [GO:0034227]; tRNA wobble position uridine thiolation [GO:0002143]; tRNA wobble uridine modification [GO:0002098]
|
cytosol [GO:0005829]; cytosolic tRNA wobble base thiouridylase complex [GO:0002144]; mitochondrion [GO:0005739]
|
ATP binding [GO:0005524]; nucleotidyltransferase activity [GO:0016779]; tRNA binding [GO:0000049]
|
PF01171;PF16503;
|
3.40.50.620;
|
TtcA family, CTU1/NCS6/ATPBD3 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:16823372}.
| null | null |
PATHWAY: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03053}.
| null | null |
FUNCTION: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. It is unclear whether it acts as a sulfurtransferase that transfers sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation. {ECO:0000255|HAMAP-Rule:MF_03053, ECO:0000269|PubMed:18391219}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94284
|
HMT2_SCHPO
|
MLTLNSTIKSVTGSFQSASMLARFASTHHKVLVVGGGSAGISVAHQIYNKFSKYRFANDQGKDTSLKPGEIGIVDGAKYHYYQPGWTLTGAGLSSVAKTRRELASLVPADKFKLHPEFVKSLHPRENKIVTQSGQEISYDYLVMAAGIYTDFGRIKGLTEALDDPNTPVVTIYSEKYADAVYPWIEKTKSGNAIFTQPSGVLKCAGAPQKIMWMAEDYWRRHKVRSNIDVSFYTGMPTLFSVKRYSDALLRQNEQLHRNVKINYKDELVEVKGSERKAVFKNLNDGSLFERPFDLLHAVPSMRSHEFIAKSDLADKSGFVAVDQSTTQSTKFPNVFAIGDCSGLPTSKTYAAITAQAPVMVHNLWSFVNGKNLTASYNGYTSCPLLTGYGKLILAEFLYKQEPKESFGRFSRFLDQTVPRRMFYHLKKDFFPFVYWNFAVRNGKWYGSRGLIPPHFPVN
|
1.8.5.-
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:10224084}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:10224084};
|
cellular detoxification of cadmium ion [GO:0098849]; cellular response to cadmium ion [GO:0071276]; glutathione biosynthetic process [GO:0006750]; phytochelatin biosynthetic process [GO:0046938]; sulfide oxidation, using sulfide:quinone oxidoreductase [GO:0070221]
|
mitochondrion [GO:0005739]
|
FAD binding [GO:0071949]; quinone binding [GO:0048038]; sulfide:quinone oxidoreductase activity [GO:0070224]
| null |
3.50.50.60;
|
SQRD family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10224084}.
| null | null | null | null | null |
FUNCTION: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. {ECO:0000269|PubMed:10224084}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94296
|
ATC3_SCHPO
|
MARDVDNKQNAKRISRDEDEDEFAGESMVGRTLDNPFLGEDEFEDIFGSESQYISSSGQNSTNPFLADTRIENSPLGSESKANQLNKQGTNVNHIEIPLRDFNDPTQPESFLPPPKNTFTSRIKKIKNLFKKEKKQVKPEDLGPRQIILNDYSANHFLHNAVSTCKYSAFTFLPKFLKEQFSKYANLFFLFTAVVQQIPGITPVNRYTTIGPMLIVLSVSGIKEIMEDIKRKKQDQELNESPCYVLQGTGFVEKQWKDVVVGDIVKIVSETFFPADLVLLSSSEPEGLCYIETANLDGETNLKIKQALPETAGLLKPVELGQLSGEVKSEQPNNNLYTFDATLKLLPSDRELPLSPDQLLLRGAQLRNTPWVYGIVVFTGHESKLMKNTTETPIKRTSVEKQVNSQILFLLCIFVFLCFASSLGALIHRSVYGSALSYVKYTSNRAGMFFKGLLTFWILYSNLVPISLFVTFELVRYIQAQLISSDLDMYNEETDTPAACRTSSLVEELGQVGYIFSDKTGTLTRNQMEFRQCTIAGVAYADVIPEDRQFTSEDLDSDMYIYDFDTLKENLKHSENASLIHQFLLVLSICHTVIPEYDESTNSIKYQASSPDEGALVKGAASIGYKFLARKPHLVTVSIFGKDESYELLHICEFNSTRKRMSIVFRCPDGKIRLYVKGADTVIMERLASDNPYLQTTIHHLEDYATVGLRTLCIAMREVPEDEYQRWSTVFETAASSLVDRAQKLMDAAEEIEKDLILLGATAIEDRLQDGVPDTISTLQTAGIKIWVLTGDRQETAINIGMSCKLIDEDMGLVIVNEETKEATAESVMAKLSSIYRNEATTGNVESMALVIDGVSLTYALDFSLERRFFELASLCRAVICCRVSPLQKALIVKMVKRNTGEVLLAIGDGANDVPMIQAAHVGVGISGMEGLQAVRSSDFSISQFCYLKKLLLVHGSWCYQRLSKLILYSFYKNIALYMTQFWYAFCNAFSGQVIFESWSISLYNVLFTVLPPVVIGIFDQFVSAGQLFQYPQLYQLGQRSEFFNLKRFWSWITNGFYHSLLLFLCSIAVFYYDGPNKDGLASGHWVWGTTLYAAILATVLGKAALISNHWTQYTVIATLGSFLLWIVFMPIYAVAAPAIGFSKEYYGIIPHLYGNLKFWASLLVLPTIALMRDFVWKYSSRMYYPEEYHYVQEIQKYNVTDYRPRIVGFHKAIRKIRQMQRMRKQRGYAFSQGEEDQSRILDAYDTTHTRGAYGEMR
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P39524};
|
endocytic recycling [GO:0032456]; phospholipid translocation [GO:0045332]; post-Golgi vesicle-mediated transport [GO:0006892]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]; phosphatidylethanolamine flippase activity [GO:0090555]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylserine flippase activity [GO:0140346]; phosphatidylserine floppase activity [GO:0090556]
|
PF13246;PF00702;PF16212;PF16209;
|
3.40.1110.10;2.70.150.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:P39524}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000250|UniProtKB:P39524}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:38567, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57262, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P39524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38568; Evidence={ECO:0000250|UniProtKB:P39524}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:64612, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P39524}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66133; Evidence={ECO:0000250|UniProtKB:P39524};
| null | null | null | null |
FUNCTION: Catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylserine and small amounts of ethanolamine from the lumen to the cytosolic leaflet of the trans-Golgi network and ensures the maintenance of asymmetric distribution of phospholipids. {ECO:0000250|UniProtKB:P39524}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94313
|
CARB_SCHPO
|
MALWATSMRRAIPGISKAFLGSNRVLETAGVSQLSKHLLPQWSGVPHRKISASATNFNDKVKESNTPDANAYIRSGHIKAAEHEKVKKVVVVGSGGLSIGQAGEFDYSGAQAIKALRESSVHTILINPNIATIQSSHSLADEIYFLPVTAEYLTHLIERENPDGILLTFGGQTALNVGIQLDDMGVFARNHVKVLGTPISTLKTSEDRDLFAKALNEINIPIAESVAVSTVDEALQAAEKVSYPVIIRSAYSLGGLGSGFANNKEELQSMAAKSLSLTPQILVEKSLKGWKEVEYEVVRDAANNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEEYHMLRTAAIKIIRHLGVVGECNVQYALSPNSLEYRVIEVNARLSRSSALASKATGYPLAYTAAKIALGHTLPELPNAVTKTTTANFEPSLDYVVTKIPRWDLSKFQYVNREIGSSMKSVGEVMAVGRTFEESLQKALRQVDPSFLGFMAMPFKDLDNALSVPTDRRFFAVVEAMLNQGYSIDKIHDLTKIDKWFLSKLANMAKVYKELEEIGSLYGLNKEIMLRAKKTGFSDLQISKLVGASELDVRARRKRLDVHPWVKKIDTLAAEFPAHTNYLYTSYNASSHDIDFNEHGTMVLGSGVYRIGSSVEFDWCGVSCARTLRKLGHSTIMVNYNPETVSTDFDECERLYFEELSYERVMDIYEMETASGIVVSVGGQLPQNIALKLQETGAKVLGTDPLMIDSAEDRHKFSQILDKIGVDQPAWKELTSVAEASKFANAVGYPVLVRPSYVLSGAAMSVIRDESSLKDKLENASAVSPDHPVVITKFIEGARELDVDAVASKGKLLVHAVSEHVENAGVHSGDATIALPPYSLSEDILSRCKEIAEKVCKAFQITGPYNMQIILAQNPDKPDTPDLKVIECNLRASRSFPFVSKTLGVNFIDVATRSIIDQEVPAARDLMAVHRDYVCVKVPQFSWTRLAGADPYLGVEMSSTGEVACFGKDVKEAYWAALQSTQNFKIPLPGQGILLGGDRPELAGIAADLSKLGYKLYVANKDAAKLLQPTSAEVVEFPVKDKRALRAIFEKYNIRSVFNLASARGKNVLDQDYVMRRNAVDFNVTLINDVNCAKLFVESLKEKLPSVLSEKKEMPSEVKRWSEWIGSHDL
|
6.3.4.16; 6.3.5.5
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409};
|
'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; arginine biosynthetic process [GO:0006526]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; urea cycle [GO:0000050]; UTP biosynthetic process [GO:0006228]
|
carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]
|
aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; metal ion binding [GO:0046872]
|
PF02786;PF02787;
|
3.40.50.20;3.30.1490.20;3.30.470.20;1.10.1030.10;3.40.50.1380;
|
CarB family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:200419}.
|
CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000250|UniProtKB:Q7SH52}; CATALYTIC ACTIVITY: [Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial]: Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:456216; EC=6.3.4.16; Evidence={ECO:0000250|UniProtKB:Q7SH52};
| null |
PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000305|Ref.3}.
| null | null |
FUNCTION: Large subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, hydrogencarbonate, and phosphate donated by ATP, the first step of the arginine biosynthetic pathway (Ref.3). The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate (By similarity). {ECO:0000250|UniProtKB:Q7SH52, ECO:0000269|Ref.3}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94316
|
SN114_SCHPO
|
MMEEDLYDEFGNYIGPENEEDEEELFPQAPSPTIAQVPSFEEVIPDEELEDVERAEEMALSHLEPQNAVVLHEDKQYYPSAEEVYGSNVDIMVQEQDTQPLSQPIIEPIRHKRIAIETTNVPDTVYKKEFLFGLLTGTDDVRSFIVAGHLHHGKSALLDLLVYYTHPDTKPPKRRSLRYTDTHYLERERVMSIKSTPLTLAVSDMKGKTFAFQCIDTPGHVDFVDEVAAPMAISDGVVLVVDVIEGVMINTTRIIKHAILHDMPIVLVLNKVDRLILELRLPPNDAYHKLRHVIDEVNDNICQISKDLKYRVSPELGNVCFASCDLGYCFTLSSFAKLYIDRHGGIDVDLFSKRLWGDIYFDSKTRKFAKQSLDGSGVRSFVHFILEPLYKLHTLTISDEAEKLKKHLSSFQIYLKPKDYLLDPKPLLQLICASFFGFPVGFVNAVTRHIPSPRENAARKASQSYIGPINSSIGKAILEMSREESAPLVMHVTKLYNTVDANNFYAFARVYSGQVKKGQKVKVLGENYSLEDEEDMVVAHIAEICVPCARYRLHVDGAVAGMLVLLGGVDNSISKTATIVSDNLKDDPYIFRPIAHMSESVFKVAVEPHNPSELPKLLDGLRKTNKSYPLSITKVEESGEHTIFGTGEMYMDCLLYDLRTLYSEIEIRVSDPVARFCETAVDTSSIKCFSDTPNKKNRITMVVEPLEKGISNDIENGKVNINWPQKRISEFFQKNYDWDLLASRSIWAFGPDDRGTNILRDDTLSTDVDKNVLNSVKEYIKQGFQWGTREGPLCDETIRNVNFRLMDVVLAPEQIYRGGGQIIPTARRVCYSSFLTASPRLMEPVYMVEVHAPADSLPIIYDLLTRRRGHVLQDIPRPGSPLYLVRALIPVIDSCGFETDLRVHTQGQAMCQMVFDHWQVVPGDPLDKSIKPKPLEPARGSDLARDFLIKTRRRKGLVEDVSTTRYFDQEMIDSLKEAGVVLSL
| null | null |
mRNA splicing, via spliceosome [GO:0000398]; spliceosomal tri-snRNP complex assembly [GO:0000244]
|
cytosol [GO:0005829]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; Prp19 complex [GO:0000974]; spliceosomal complex [GO:0005681]; U2-type catalytic step 2 spliceosome [GO:0071007]; U4/U6 x U5 tri-snRNP complex [GO:0046540]; U5 snRNP [GO:0005682]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; U5 snRNA binding [GO:0030623]
|
PF00679;PF03764;PF16004;PF00009;PF03144;
|
3.30.230.10;3.30.70.240;3.30.70.870;3.40.50.300;2.40.30.10;3.90.1430.10;
|
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-G/EF-2 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Component of the U5 snRNP complex required for pre-mRNA splicing. Binds GTP.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94360
|
MOB1_SCHPO
|
MFGFSNKTAKTFRVRKTEAGTKHYQLRQYAEATLGSGSLMEAVKLPKGEDLNEWIAMNTMDFYTQINMLYGTITEFCTAASCPQMNAGPSYEYYWQDDKIYTKPTRMSAPDYINNLLDWTQEKLDDKKLFPTEIGVEFPKNFRKVIQQIFRRLFRIYAHIYCSHFHVMVAMELESYLNTSFKHFVFFCREFGLMDNKEYAPMQDLVDSMV
| null | null |
cell division [GO:0051301]; division septum assembly [GO:0000917]; hippo signaling [GO:0035329]; positive regulation of mitotic actomyosin contractile ring contraction [GO:1903473]; positive regulation of protein phosphorylation [GO:0001934]; positive regulation of septation initiation signaling [GO:0031031]; protein localization [GO:0008104]; signal transduction [GO:0007165]
|
cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; medial cortex [GO:0031097]; mitotic spindle pole body [GO:0044732]; new mitotic spindle pole body [GO:0071958]; nucleus [GO:0005634]; old mitotic spindle pole body [GO:0071957]; Sid2-Mob1 complex [GO:0034973]
|
protein kinase activator activity [GO:0030295]
|
PF03637;
|
1.20.140.30;
|
MOB1/phocein family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:10769201}. Note=Spindle pole body throughout mitosis, relocates to the medial ring during interphase.
| null | null | null | null | null |
FUNCTION: Has a role in promoting the onset of septum formation during the latter stages of mitosis. {ECO:0000269|PubMed:10769201}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94363
|
RHB1_SCHPO
|
MAPIKSRRIAVLGSRSVGKSSLTVQYVENHFVESYYPTIENTFSKNIKYKGQEFATEIIDTAGQDEYSILNSKHSIGIHGYVLVYSITSKSSFEMVKIVRDKILNHTGTEWVPIVVVGNKSDLHMQRAVTAEEGKALANEWKCAWTEASARHNENVARAFELIISEIEKQANPSPPGDGKGCVIA
| null | null |
positive regulation of L-arginine import across plasma membrane [GO:1905589]; positive regulation of TORC1 signaling [GO:1904263]; small GTPase-mediated signal transduction [GO:0007264]
|
cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein serine/threonine kinase activator activity [GO:0043539]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rheb family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Regulates entry into stationary phase when extracellular nitrogen levels are adequate for growth. {ECO:0000269|PubMed:10835385}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94364
|
WAPL_SCHPO
|
MKRGKCKEKDNGLKRISSESEVWNFLDVTVSELNKQKRSPGQTVSKRLHKKQRVVSNPDLSLPSSPVKQILRNGLQNSKYGSHKTGLERSASCSSIDASANHSSTTYREQRSYLMEEGLDTQPIVPREVSSGRELDSTNHTIGTERAFLIEEDVSEDDEIQMKSIHELRFAGEQQRIVDEIEYLVDGVTFSGNSSASRYLSLIGIAEKMFDNSFRLCLKSIRDVFLRIFEEIDPKDTLHTFLQIYIFATMANEMDCMSSLLDAYSNNVKLLLQTAITLEPQVPVSILAKSLPKSVKGAVQEFVIKAELTFSFSNESLASSDSISLAAIALMKTSSGVFAESELFTELINLLIEKSYPILKENDGSNNFLLHALCSSLEKFTDFQGSEKIQKVSQILSSKLQILIDEHNETNSPKIDDTVVHACSEKLLRTLIQTVNSNSDHALAVSKSEVPLFAYKILQKFSNFSSDDETTRELIILILGLLLGLVEESHEFIQTITHVEVSFGASALDVLISFYQKNESIVEISGYVVMILSHCFLNDPKAFAQLKPLISQFYESLHKFKNFHLKLKEELMMMGSNGLAIVSIIDELHKSLQDYLRSDLVK
| null | null |
cell division [GO:0051301]; chromatin looping [GO:0140588]; homologous chromosome pairing at meiosis [GO:0007129]; mitotic sister chromatid cohesion [GO:0007064]; regulation of cohesin loading [GO:0071922]
|
nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; Wpl/Pds5 cohesin loading/unloading complex [GO:0090695]
|
ATP hydrolysis activity [GO:0016887]; ATP-dependent protein binding [GO:0043008]; cohesin unloader activity [GO:0140670]; DNA binding [GO:0003677]
|
PF07814;
|
1.25.10.10;
|
WAPL family
| null |
SUBCELLULAR LOCATION: Nucleus. Chromosome.
| null | null | null | null | null |
FUNCTION: Regulator of sister chromatid cohesion in mitosis which negatively regulates cohesin association with chromatin. {ECO:0000269|PubMed:18079700, ECO:0000269|PubMed:21300781}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94374
|
IMA2_SCHPO
|
MESRYLSDRRSRFKSKGVFKADELRRQREEQQIEIRKQKREESLNKRRNLNAVLQNDIDVEEEADQSQVQMEQQMKDEFPKLTADVMSDDIELQLGAVTKFRKYLSKETHPPIDQVIACGVVDRFVQFLESEHHLLQFEAAWALTNIASGTTDQTRIVVDSGAVPRFIQLLSSPEKDVREQVVWALGNIAGDSSACRDYVLGNGVLQPLLNILQSSASDVSMLRNATWTLSNLCRGKNPPPNWSTISVAVPILAKLLYSEDVEIIVDACWAISYLSDGPNEKIGAILDVGCAPRLVELLSSPSVNIQTPALRSVGNIVTGTDAQTQIIIDCGALNAFPSLLSHQKENIRKEACWTISNITAGNTQQIQAIIESNLIPPLVHLLSYADYKTKKEACWAISNATSGGLGQPDQIRYLVSQGVIKPLCDMLNGSDNKIIQVALDAIENILKVGEMDRTMDLENINQYAVYVEEAGGMDMIHDLQSSGNNDIYLKAYSIIEKYFSDEDAVEDLAPETENGAFTFGNGPQAQGEFKFDSQDMAM
| null | null |
cell division [GO:0051301]; mitotic nuclear pore complex disassembly [GO:0140516]; NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606]; regulation of mitotic nuclear envelope disassembly [GO:1905557]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle midzone [GO:1990023]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
GTP binding [GO:0005525]; nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]
|
PF00514;PF16186;PF01749;
|
1.20.5.690;1.25.10.10;
|
Importin alpha family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus, nucleolus. Note=Nucleus; nucleolus; nuclear rim.
| null | null | null | null | null |
FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. Involved in nuclear protein import. Required for efficient nuclera import of both an SV40 nuclear localization signal-containing reporter protein and the pap1 component of the stress response MAP kinase pathway. Required for proper mitotic progression. {ECO:0000269|PubMed:12237855, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:15937127}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94383
|
SMC1_SCHPO
|
MGRLLRLEVENFKSYRGHQIIGPFEDFTSIIGPNGAGKSNLMDAISFVLGVKSSHLRSTNVKELIYRGKILQRDNTDFTDSSNPTTAYVKLMYELDNGEQREYKRAITPSGATEYKIDEEIVTFSEYCGSLQKENILVRARNFLVFQGDVETIASQSPLELSKLVEQISGSLEYKSEYDKSKDEQDKAVNLSAHSFNKKRGINAELRQYQEQKTEAERYQSQKEKRDSAQLVYLLWKLFHLEKSISSNMAEVTRLKADSIQLIERRDENTKEIEKLKEKEGSIRRNLLAFDRKVRKQEKLIASKRPELISIAEKALESKSNLRKIQRKAAEIEKDYSDQASTLQVLENQLTSLSAAEKEFLKDMQEKEQLKGLRLLPEDKEEYEGLRSEADKLNSNLLFKLQTLNRNIKVTSQSKDSLTSIVGDLESKIKSLHESVSSLDTERADLLAKINEKIESLELEKHDQQKKRLTYSELFHKTQELNEELQSCLQKILEASADRNESKQDAKKREALYALKRIYPEVKGRIIDLCTPTQKKYESAIAAALGKNFDAIVVETQAVAKECIDYIKEQRIGIMTFFPMDTIAASPVNQKFRGTHKGARLAIDVLNFESEYERVMISAVGNTLICDSMTVARDLSYNKRLNAKTVTLEGTVIHKTGLITGGSSNNRSAKHWDDHDFDLLTQTKDRLMHQIGEIEYQKSSCVITESDTVKLHSLESEISLLKDKYTVVSRSVEDKKKEIGHYESLIKEKQPHLSELEMELRNFVKSRDELQIQVEKVEEKIFSGFCKRIGISDIHTYDEIHRTFTQSFTQKQLEFTKQKSLLENRISFEKQRVSDTRLRLERMHKFIEKDQESIDNYEQNREALESEVATAEAELELLKEDFASENSKTEKILLAASEKKLVGKRLVSELTKLSGNITLLESEIDRYVSEWHAILRKCKLEDIDVPLREGSLTSIPIDDVSNSGDITMGEEPSEPVINFEKFGVEVDYDELDEELRNDGSESMASVLQEKLREYSEELDQMSPNLRAIERLETVETRLAKLDEEFAAARKAAKNAKERFNAVKQKRLQKFQAAFSHISEQIDPIYKELTKSPAFPLGGTAYLTLDDLDEPYLGGIKFHAMPPMKRFRDMDQLSGGEKTMAALALLFAIHSYQPSPFFVLDEIDAALDQTNVTKIANYIRQHASSGFQFVVISLKNQLFSKSEALVGIYRDQQENSSRTLSINLEGYVE
| null | null |
cell division [GO:0051301]; chromatin looping [GO:0140588]; mitotic sister chromatid cohesion [GO:0007064]; sister chromatid cohesion [GO:0007062]
|
chromosome [GO:0005694]; cohesin complex [GO:0008278]; condensed chromosome, centromeric region [GO:0000779]; meiotic cohesin complex [GO:0030893]; mitotic cohesin complex [GO:0030892]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]
|
PF06470;PF02463;
|
1.20.1060.20;3.30.70.1620;3.40.50.300;
|
SMC family, SMC1 subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11069892}. Chromosome {ECO:0000269|PubMed:11069892}. Note=Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the rad21 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome separation.
| null | null | null | null | null |
FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94395
|
KU70_SCHPO
|
MENDEQIDETENFAIGKYAILFVIEVSPSMLDPVDEFTPSSLQMALICAYQLAAQRVITNPSDIMGVLLYGTESSTGRFANQMMLLDIDPPDAERIKSLQSFEKDFQFSKEKFKPCSCQVSLSSVLYHCSVIFTTKAENFEKRLFLITDNDHPAWDATERDIILQRAKDLRDLDIQVHPVFLDPPTHSFRINIFYSDFLYIVYGRQDVSNLVNRGQAQLQHMLNMITALQKPKRAHFHLKMDLGNDVRIGVEAFILLKRLESAKTNWVYAKGERFAVAVPQSKQVSFATKKELKKDEIRRSYSYGGSSVVFGSDELNKVRSFEPPTLRIIGFRDFSTLKPWHCLKPAVFLRPKDDEIIGSGAVFSAIHKKLLASNKIGIAWFVSRPNANPCFVAMLATPGSIHIRDDFELPLGIFLVQLPTADDIRSLPPINPNPISMPSNLIETMQRILRGMELRSYQPGKYNNPSLQWHYKVLQALALDEEIPTDFVDNTLPKYKAIQKRVGEYMGDVNNIVAEYRNDISDKNGIKEEEEDQGPIVKKARIEKSGKPIFAEDDRLKQLYIEGVLDKEIKALKVSQLKDILRDRGLRVSGKKADLLDNLTNYVKKL
|
3.6.4.12
| null |
DNA recombination [GO:0006310]; double-strand break repair via nonhomologous end joining [GO:0006303]; replication fork processing [GO:0031297]; stalled replication fork localization to nuclear periphery [GO:0120290]; telomere maintenance [GO:0000723]
|
chromosome, subtelomeric region [GO:0099115]; chromosome, telomeric repeat region [GO:0140445]; heterochromatin [GO:0000792]; Ku70:Ku80 complex [GO:0043564]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; site of double-strand break [GO:0035861]
|
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; damaged DNA binding [GO:0003684]; double-stranded DNA binding [GO:0003690]; telomeric DNA binding [GO:0042162]
|
PF02735;PF03730;PF03731;PF02037;
|
1.10.1600.10;2.40.290.10;4.10.970.10;1.10.720.30;3.40.50.410;
|
Ku70 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000269|PubMed:12424244}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
| null | null | null | null |
FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase. Required for mating-type switching (By similarity). Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. {ECO:0000250, ECO:0000269|PubMed:11029034, ECO:0000269|PubMed:12424244}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94396
|
PUS1_SCHPO
|
MGRGGKRTWYNGDRREAKRNRPNSIYNGEGRPENLVVGEKKPKRKVACLVGYCGSGYHGMQLNPPSKTIEGDLFDAFVKAGAVSSYNADDPKKVALARAARTDKGVHAAGNVISLKLIMEDEKLIEKVNEHLPPSIRLWDVIRTINSFNPRTYCESRIYEYMVPTYAFVPPKPSSILGNCIMKNSPMPAEPINKENINQLSRSLFYEEGKEFWDDYDIAAKEILSLYEQDPEGFVNPYSKRGAAALANSENNKGSEAGVSAKTNPDMDSDSSAIVNEFLKPDSVEDESAGSKIDPSYRLERALKHIEVLKLKNYRISADRLSVIRETLNQYVGVHNFHNFTVGQAFHQKNSNRVIRSFTASDPFMIGDTEWISCKVHGQSFMLHQIRKMIALAILVVRTGCPVERIQDAFKKTKINIPKGPGFGLLLESPFFKGYNEHKAPENNRDPIDFTKYEQKITAFKHAHIYDKIFLEEARKQVFHCFLSFIDSYNEEDFSYLSDIGITEKTQEVSSKLPDVLSSDEEEDSAENKDDLEG
|
5.4.99.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q12211}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q12211};
|
mRNA processing [GO:0006397]; mRNA pseudouridine synthesis [GO:1990481]; snRNA pseudouridine synthesis [GO:0031120]; tRNA pseudouridine synthesis [GO:0031119]
|
nucleus [GO:0005634]
|
metal ion binding [GO:0046872]; pseudouridine synthase activity [GO:0009982]; RNA binding [GO:0003723]; snRNA pseudouridine synthase activity [GO:0106032]; tRNA pseudouridine synthase activity [GO:0106029]
|
PF01416;
|
3.30.70.660;3.30.70.580;
|
TRNA pseudouridine synthase TruA family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11095668}.
|
CATALYTIC ACTIVITY: Reaction=a uridine in tRNA = a pseudouridine in tRNA; Xref=Rhea:RHEA:54572, Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13934, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000269|PubMed:11095668}; CATALYTIC ACTIVITY: Reaction=uridine in snRNA = pseudouridine in snRNA; Xref=Rhea:RHEA:51124, Rhea:RHEA-COMP:12891, Rhea:RHEA-COMP:12892, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:Q12211}; CATALYTIC ACTIVITY: Reaction=a uridine in mRNA = a pseudouridine in mRNA; Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659, ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; Evidence={ECO:0000250|UniProtKB:Q12211};
| null | null | null | null |
FUNCTION: Formation of pseudouridine at positions 27 and 28 in the anticodon stem and loop of transfer RNAs; at positions 34 and 36 of intron-containing precursor tRNA(Ile) and at position 35 in the intron-containing tRNA(Tyr) (PubMed:11095668). Catalyzes pseudouridylation at position 44 in U2 snRNA (By similarity). Also catalyzes pseudouridylation of mRNAs (By similarity). {ECO:0000250|UniProtKB:Q12211, ECO:0000269|PubMed:11095668}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94399
|
TWF1_SCHPO
|
MSASVELKPTEKFSKFLEEYSSVPVRAAIISISNENSFDVKTMVEKSESIESDFKKVRECLLGSEEPAFVLVYDDSKKNLLQLISYVPENANVRRKMLYASSRAAFVRCVTLAKLDESYFASTPEELDYQQIMKSLSKQEDQSPLRQDELERKEYNESMQSSVTHKRPLVTRGVAMSIDDKALKALSDLKSSTENNLVILSIDKEVISLSQEKQNIPPSDVKSFFSSTEPNFAFYSLPKDGSSKILFIYICPMQATVKHRMVYSSSKLGLLDSIKAELGIVIDGKIESNDAADITEKEILHAAGISSPQAETSTTKTGFSRPRPPRRR
| null | null |
actin filament depolymerization [GO:0030042]; barbed-end actin filament capping [GO:0051016]; conjugation with cellular fusion [GO:0000747]; mating projection actin fusion focus assembly [GO:1904600]; positive regulation of neuron projection development [GO:0010976]; regulation of lamellipodium assembly [GO:0010591]; sequestering of actin monomers [GO:0042989]
|
actin cortical patch [GO:0030479]; actin filament [GO:0005884]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; mating projection tip [GO:0043332]; myofibril [GO:0030016]
|
actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]
|
PF00241;
|
3.40.20.10;
|
Actin-binding proteins ADF family, Twinfilin subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. Prevents actin filament assembly by forming a 1:1 complex with actin monomers, and inhibits the nucleotide exchange reaction of actin monomers (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94421
|
SNF22_SCHPO
|
MFAVQGNQKFPKGLTKDNIQSLYQQWQVMRNQGATEENNPEFAQISSILRMVQRAHYARMQQMRNQSSEFPDAENTNLRKQQDTLPTTGFNNLPEGKAGMQTLPGRPASNGPTPPNPGNGNVGLNNPSYMNSQASPNIMNAPLQRDTSVPPAPSMVHPHTNTNANSNNLKVYANQLSQQNTSNPTYHNAYDMASMMKNGSRMNNSFPPTTPYPPANDTTVNSSLPHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIPANVSMQQQMGRRGSIPVNPSTFSASSPPSGSMLASPYNGYQNDAASFAHSKLPSSANPNTPFNSTATVDVGAAGSHFPYPQPSNLDAINAKTYFQSSSNSPAPYVYRNNLPPSATSFQPSSSRSPSVDPNTVKSAQHIPRMSPSPSASALKTQSHVPSAKVPPTSKLNHAQLAMLKSQIVAYNCLNSPNGQVPPAVQQAIFGRVYGASNEVSPSMPFQQNVPQMSSVKKDTPTRDANMRTSKAPYIQNIPNQFQRRAYSATIPVKNESLAKPSVSPMPLQQSTGKTEVAKRAQFPTNVNYSSCVDPRTYVKTPIPFSKFSSSENLSLIPSLLPPSISWDDVFLSSEIAIACSIANRIDFLEKENRPKSVNKKILQQDKSKSMIELRCLRLLEKQRSLRETINSVIPHSDSLAAGNLRLMFRNVKRQTMQEANLVLALAEKQKTEHAMRQKEKLLTHLRSIMLHRKSIVTKVDKQNKAKTQRCKDIINFHAHLEKEEKKRIERSARQRLQALRADDEAAYLQLLDKAKDTRITHLLKQTDQYLENLTRAVRIQQSNIHSGNTSGKGSNSAELEAPISEEDKNLDYFKVAHRIHEEVEQPKIFVGGTLKDYQLKGLEWMLSLYNNNLNGILADEMGLGKTIQTIAFITYLIEKKNQQGPFLIIVPLSTLTNWIMEFEKWAPSVKKIAYKGPPQLRKTLQSQIRSSNFNVLLTTFEYIIKDRPLLSRIKWVHMIIDEGHRIKNTQSKLTSTLSTYYHSQYRLILTGTPLQNNLPELWALLNFVLPKIFNSIKSFDEWFNTPFANTGGQDKIGLNEEEALLIIKRLHKVLRPFLFRRLKKDVEKELPDKVEKVIKCPLSGLQLKLYQQMKKHGMLFVDGEKGKTGIKGLQNTVMQLKKICNHPFIFEDVERAIDPSGTNVDLLWRAAGKFELLDRILPKLFLTGHKTLMFFQMTQIMTIMEDYLRSKNWKYLRLDGSTKSDDRCSLLAQFNDPKSDVYIFMLSTRAGGLGLNLQTADTVIIFDTDWNPHQDLQAQDRAHRIGQTKEVRILRLITEKSIEENILSRAQYKLDLDGKVIQAGKFDNKSTPEEREAFLRSLLEHDGDDDHDLTYGELQDDELNELISRTDEELVLFKKLDKERAATDIYGKGKPLERLLTVNELPDFYKVEVDSFAVQSSSELEDQYLERKRRRRNSISYTELTLDELNTVDDPSSTLMPRKRGRPRKKTNSGSSLSTPLSQESSLARSGRKNTPSYKQKALRRYCMEIFERLYNLQSEDGRFVNGLFLYPPNRKLYPDYYIIIKRPIALGKIKRNIKNDRYGDVGELIADFMLMFNNAYTYNEEHSIVYEDAKLMEKTLKEVIEDLEKNNSLHAYEEEALNEEQASLVFLENSEAELPLDSGIVSAEDDKVITYEDSSSSYSE
|
3.6.4.-
| null |
chromatin remodeling [GO:0006338]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
chromatin [GO:0000785]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; histone octamer slider activity [GO:0140751]
|
PF00439;PF00271;PF08880;PF14619;PF00176;
|
1.20.5.170;1.20.920.10;3.40.50.300;3.40.50.10810;
|
SNF2/RAD54 helicase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Helicase. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. {ECO:0000269|PubMed:14988732, ECO:0000269|PubMed:18622392}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94436
|
TAF14_SCHPO
|
MTTVKRTVRLITDQNVLPGGEAAVLNDQSFPVREWSIKLVCLNPQGEETDASFVDRVTYKLHPTFQNPTRTIRKPPFQIKEQGWGEFEMEIIIYYADKGGEHRFLHYLHFQQEHYHEDIELNINATRPGLLKALTATGEVPGYSDEGEEARKDKRKNESEVGAGKKKAKAKPVDMDKLAEGLQKLQEDDLLQVVQMVNENKTPDMYVRNDIEGGEFHIDLYTLPDNLLLLLYSFCAKRVTM
| null | null |
chromatin remodeling [GO:0006338]; DNA damage response [GO:0006974]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815]
|
chromatin [GO:0000785]; Ino80 complex [GO:0031011]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514]; transcription factor TFIID complex [GO:0005669]; transcription factor TFIIF complex [GO:0005674]
|
histone binding [GO:0042393]; RNA polymerase II general transcription initiation factor activity [GO:0016251]
|
PF17035;PF03366;
|
1.20.1270.220;2.60.40.1970;
|
TAF14 family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:15616156, ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Functions as a component of the DNA-binding general transcription factor complex TFIID, and the RNA polymerase II associated general transcription factor complex TFIIF. Binding of TFIID to a promoter (with or without TATA element) is the initial step in preinitiation complex (PIC) formation. TFIID plays a key role in the regulation of gene expression by RNA polymerase II through different activities such as transcription activator interaction, core promoter recognition and selectivity, TFIIA and TFIIB interaction, facilitation of DNA opening and initiation of transcription. TFIIF is essential for the initiation of transcription by RNA polymerase II. TFIIF functions include the recruitment of RNA polymerase II to the promoter bound DNA-TBP-TFIIB complex, decreasing the affinity of RNA polymerase II for non-specific DNA, allowing for the subsequent recruitment of TFIIE and TFIIH, and facilitating RNA polymerase II elongation. The TAF14 subunit has stimulatory activity. Component of the SWI/SNF complex, an ATP-dependent chromatin remodeling complex, required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors. Component of the mst2 complex which is a highly specific H3 lysine 14 (H3K14) acetyltransferase that functions together with gcn5 to regulate global levels of H3K14 acetylation (H3K14ac), critical for DNA damage checkpoint activation. {ECO:0000269|PubMed:15616156, ECO:0000269|PubMed:18622392, ECO:0000269|PubMed:22184112}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94446
|
ESA1_SCHPO
|
MSNDVDDESKIETKSYEAKDIVYKSKVFAFKDGEYRKAEILMIQKRTRGVVYYVHYNDYNKRLDEWITIDNIDLSKGIEYPPPEKPKKAHGKGKSSKRPKAVDRRRSITAPSKTEPSTPSTEKPEPSTPSGESDHGSNAGNESLPLLEEDHKPESLSKEQEVERLRFSGSMVQNPHEIARIRNINKICIGDHEIEPWYFSPYPKEFSEVDIVYICSFCFCYYGSERQFQRHREKCTLQHPPGNEIYRDDYISFFEIDGRKQRTWCRNICLLSKLFLDHKMLYYDVDPFLFYCMCRRDEYGCHLVGYFSKEKESSENYNLACILTLPQYQRHGYGKLLIQFSYELTKREHKHGSPEKPLSDLGLISYRAYWAEQIINLVLGMRTETTIDELANKTSMTTNDVLHTLQALNMLKYYKGQFIICISDGIEQQYERLKNKKRRRINGDLLADWQPPVFHPSQLRFGW
|
2.3.1.-; 2.3.1.48
| null |
DNA repair [GO:0006281]; DNA repair-dependent chromatin remodeling [GO:0140861]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of heterochromatin formation [GO:0031453]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]
|
NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; site of double-strand break [GO:0035861]; Swr1 complex [GO:0000812]
|
chromatin binding [GO:0003682]; histone H3K4 acetyltransferase activity [GO:0044016]; histone H4K16 acetyltransferase activity [GO:0046972]; metal ion binding [GO:0046872]; peptide 2-hydroxyisobutyryltransferase activity [GO:0106226]; peptide butyryltransferase activity [GO:0140065]; peptide crotonyltransferase activity [GO:0140064]; transcription coregulator activity [GO:0003712]
|
PF01853;PF11717;PF17772;
|
2.30.30.140;3.40.630.30;3.30.60.60;1.10.10.10;
|
MYST (SAS/MOZ) family
|
PTM: Autoacetylation at Lys-279 is required for proper function. {ECO:0000250|UniProtKB:Q08649}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16199868}. Chromosome {ECO:0000269|PubMed:20299449, ECO:0000269|PubMed:33723569}. Note=Localizes to pericentric heterochromatin (PubMed:20299449). Following DNA damage, localizes to sites of DNA damage, such as double stand breaks (DSBs) (PubMed:33723569). {ECO:0000269|PubMed:20299449, ECO:0000269|PubMed:33723569}.
|
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:20299449}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993; Evidence={ECO:0000269|PubMed:20299449}; CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q08649}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949; Evidence={ECO:0000250|UniProtKB:Q08649}; CATALYTIC ACTIVITY: Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780, ChEBI:CHEBI:144968; Evidence={ECO:0000269|PubMed:29192674}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181; Evidence={ECO:0000269|PubMed:29192674}; CATALYTIC ACTIVITY: Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-(2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332, ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q08649}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909; Evidence={ECO:0000250|UniProtKB:Q08649};
| null | null | null | null |
FUNCTION: Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z (PubMed:16199868). Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac (By similarity). The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation (PubMed:18505873, PubMed:33723569). The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination (PubMed:33723569). Recruitment to promoters depends on H3K4me (By similarity). Also acetylates non-histone proteins (By similarity). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively (PubMed:29192674). {ECO:0000250|UniProtKB:Q08649, ECO:0000269|PubMed:16199868, ECO:0000269|PubMed:18505873, ECO:0000269|PubMed:29192674, ECO:0000269|PubMed:33723569}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94449
|
RFC4_SCHPO
|
MSNAVSSSVFGEKNNSVAYELPWVEKYRPIVLDDIVGNEETIDRLKVIAKEGNMPHLVISGMPGIGKTTSILCLAHALLGPAYKEGVLELNASDERGIDVVRNRIKAFAQKKVILPPGRHKIIILDEADSMTAGAQQALRRTMEIYSNTTRFALACNQSNKIIEPIQSRCAILRYSRLTDQQVLQRLLNICKAEKVNYTDDGLAALIMTAEGDMRQAVNNLQSTVAGFGLVNGENVFRVADQPSPVAIHAMLTACQSGNIDVALEKLQGIWDLGFSAVDIVTNMFRVVKTMDSIPEFSRLEMLKEIGQTHMIILEGVQTLLQLSGLVCRLAKSQMKPESFII
| null | null |
DNA repair [GO:0006281]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA-templated DNA replication [GO:0006261]; mitotic DNA replication leading strand elongation [GO:1903460]; UV-damage excision repair [GO:0070914]
|
chromatin [GO:0000785]; Ctf18 RFC-like complex [GO:0031390]; cytosol [GO:0005829]; DNA replication factor C complex [GO:0005663]; Elg1 RFC-like complex [GO:0031391]; nucleus [GO:0005634]; Rad17 RFC-like complex [GO:0031389]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA clamp loader activity [GO:0003689]; DNA clamp unloader activity [GO:0061860]
|
PF00004;PF08542;
|
1.10.8.60;1.20.272.10;3.40.50.300;
|
Activator 1 small subunits family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: The elongation of primed DNA templates by DNA polymerase delta and epsilon requires the action of the accessory proteins PCNA and activator 1. {ECO:0000269|PubMed:16040599}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94451
|
PLI1_SCHPO
|
MNQANFLQELPNVLKRLETGLIIPQLKDILRVFGLRLSGTKAELITRIKQLIERIAIENNTTSWEALKKAIDGDVTSAVCILKYNTYQIYSAAAPIAPPSSASGNRSYSRPFAPVVHSRIRFRKSPFYDILEQFNAPFVVPACVGTRNTISFSFHVTPPALSKLLNDPKQYRVYLFSTPSETIGFGNCLMEFPTPQMELRINNQVAHANYRRLKGKPGTTNPADITDLVSKYAGPPGNNVVIYYMNSTKSYSVVVCFVKVYTIENLVDQIKSRKAESKEKIIERIKNDNQDADIIATSTDISLKCPLSFSRISLPVRSVFCKHIQCFDASAFLEMNKQTPSWMCPVCASHIQFSDLIIDGFMQHILESTPSNSETITVDPEGNWKLNTFDEPVESSEDEFVPKEKVIELSDGEGISTMANKSNDQPTRRASTHNSGPPAKRKRESLVIDLTISDDDENVATSTTESPSNATKENSLSRNVQSPNIDTAISNRSTNVRHGHPGFKDYTVENSPASRERSTSESAQSSVHMGYAGEGGLLSGALRAPSQQNNNNSNTQHSINLHTIVPSPYEPPLSVTPSTAITNLSIPESNRTNSSASSKSFTMNDLILPPLHLKNTTQTNNAHEDAQSSNLSQNHSLFYERIPQRPSYRIEKQNKGIYEDENEQSISAMPIPRAHPQLPKNLLSQTAGPLWDEQQDAQVDWNSELQSNNSYHNSGFEGTGNTFQSID
|
2.3.2.-
| null |
linear element assembly [GO:0030999]; non-recombinational interstrand cross-link repair [GO:0036299]; protein sumoylation [GO:0016925]; reciprocal meiotic recombination [GO:0007131]; regulation of transcription by RNA polymerase II [GO:0006357]; replication fork processing [GO:0031297]; stalled replication fork localization to nuclear periphery [GO:0120290]; telomere maintenance [GO:0000723]
|
nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
SUMO ligase activity [GO:0061665]; transcription coregulator activity [GO:0003712]; zinc ion binding [GO:0008270]
|
PF14324;PF02037;PF02891;
|
2.60.120.780;1.10.720.30;3.30.40.10;
|
PIAS family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15359282}.
| null | null |
PATHWAY: Protein modification; protein sumoylation.
| null | null |
FUNCTION: Acts as an E3 ligase mediating SUMO/Smt3 attachment to other proteins. Involved in the maintenance of the centromere and in telomere length. Regulates recombination, via extension sumoylation, particularly within the heterochromatin repeats. {ECO:0000269|PubMed:15359282}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94457
|
ERG3A_SCHPO
|
MDYLLNYADQYALDSIYNAVYPLARDNIVRQSISLFFLTWFGGMFLYLTFASLSYQFVFDKSLMDHPKFLKNQVFMEVLTALQNLPGMALLTVPWFLAELHGYSYLYDNISDYGLKYFLCSLPLFVMFSDFGIYWAHRFLHHRYVYPRLHKLHHKWIICTPYASHAFKSADGFLQSLPYHLFPFFFPLHKLTYLALFTFVNFWSIMIHDGKYISNNPIINGAAHHNGHHIYFNYNYGQFTTLFDRLGNSFRAPDEAWFDKDLRQNEDVLRVELMEYEAIRNEVEGDDDREYIANSAKKNH
|
1.14.19.20
|
COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P53045};
|
ergosterol biosynthetic process [GO:0006696]; sterol biosynthetic process [GO:0016126]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]
|
C-5 sterol desaturase activity [GO:0000248]; delta7-sterol 5(6)-desaturase activity [GO:0050046]; iron ion binding [GO:0005506]
|
PF04116;
| null |
Sterol desaturase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=episterol + 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 = 5-dehydroepisterol + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:46560, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:23929, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:52972; EC=1.14.19.20; Evidence={ECO:0000305|PubMed:18310029}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46561; Evidence={ECO:0000305|PubMed:18310029};
| null |
PATHWAY: Steroid metabolism; ergosterol biosynthesis. {ECO:0000269|PubMed:18310029}.
| null | null |
FUNCTION: C-5 sterol desaturase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway (PubMed:18310029). Erg31 and erg32 catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. The lanosterol 14-alpha-demethylase erg11/cyp1 catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol. In the next steps, a complex process involving various demethylation, reduction and desaturation reactions catalyzed by the C-14 reductase erg24 and the C-4 demethylation complex erg25-erg26-erg27 leads to the production of zymosterol. Erg28 likely functions in the C-4 demethylation complex reaction by tethering erg26 and Erg27 to the endoplasmic reticulum or to facilitate interaction between these proteins. Then, the sterol 24-C-methyltransferase erg6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase erg2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturases erg31 and erg32 then catalyze the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase erg4 to produce ergosterol (Probable) (PubMed:18310029). In the genus Schizosaccharomyces, a second route exists between lanosterol and fecosterol, via the methylation of lanosterol to eburicol by erg6, followed by C14-demethylation by erg11/cyp1 and C4-demethylation by the demethylation complex erg25-erg26-erg27 (Probable) (PubMed:8586261). {ECO:0000250|UniProtKB:P32353, ECO:0000269|PubMed:18310029, ECO:0000305|PubMed:18310029, ECO:0000305|PubMed:8586261}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94459
|
SCC4_SCHPO
|
MTGLNETDARILVTSRHLFLWPLAETYFKNAEKVLQDCGVCDSFGRLLSTGLQCLYSVLMDTKMEPRVELLTRKRICEVLLSHTVEYADVEAILNRALIIAEQHNLTEYKFSLQLLLSRVFCRTSPKAAKVLLTRCVREAEEYAKVAEIYHSNNQSNPHRWVYEFLLATLEFQNVSQVANSIHNYANHHKHQHLQLLAMILNQSLPMDEISTDSDQISILCLVTQIAQCLRKGEILLAREILPKIHSKLESETFVWPSSYIDFFIDDTSKISIKWMSINQLYLLIYLISGFCYISDSTSGRASRFLQEGLRITGDFKHQERCVLEYLESQKWINNITKDMKYYLIATYLSRSRLSKAERILQSTEDDQTGFLGILKGMYLQKRGDLKKAEVHYRETAKNFSFRTDTFIISTLNLINILEDSAAASRCLESIEPLCNKHEKKIFKLWLLVLKVIREGPQVHQSNVLPRVIQQSSEYANTQLQYISLTELSERFGKLEHAEKMAISALELAKKSKDELWCLISGRILEDFYRSVQKYDKMRQQALENSAYSKLIEDIYSFV
| null | null |
cell division [GO:0051301]; chromatin looping [GO:0140588]; chromosome segregation [GO:0007059]; maintenance of mitotic sister chromatid cohesion [GO:0034088]; mitotic sister chromatid cohesion [GO:0007064]
|
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]; Scc2-Scc4 cohesin loading complex [GO:0090694]; SMC loading complex [GO:0032116]
|
ATP hydrolysis activity [GO:0016887]; cohesin loader activity [GO:0061775]; double-stranded DNA binding [GO:0003690]
|
PF10345;
| null |
SCC4/mau-2 family
| null |
SUBCELLULAR LOCATION: Nucleus. Note=Associates with chromatin. {ECO:0000305}.
| null | null | null | null | null |
FUNCTION: Involved in sister chromatid cohesion. Forms a complex with mis4, which is required for the association of the cohesin complex with chromosomes. {ECO:0000269|PubMed:16682348}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94466
|
RGA7_SCHPO
|
MLSAPSSSTTPASPPTSPPNTTSSDDFAVLKEPKVEAILNSELGLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANHSLTLQKTLSAFSDQVIEFHKNAERKRKSIKEYAKKQENAYLEAVMQMDKSKSRFKGAETEYNRALDNKNTGDSQKKVGFFKPKSNAQLTKLEDEARLKAENAESDMHSKIENAQNVQKQLLCIHRPNYIKQFFSLQREIESSLIANYLRYTKLCESNTLLNGLTIRPQKPTPTNCGLQHALDNINANTDFVQYVLHASIKHEDNKNPTDASKTKIIQPPSSYGTGSSAGKTNPPVNPTIKVTAAIPSPLQNTNPAPSTFPNPSVASPAFPNSSTSNPSTAPASASPLASTLKPSTANDTNGSSSSSSSNPRTSSPLASNAENKPPVAQQSPPVLLPTLPPIQTTTIQTSREVAPPPSSINSNRAASPFRPTSVSPQPSSPTKSLLFGARLDAIILREHSNIPNIVMQCTSQVENFGLNLQGIYRVPSSSARVNMLRSQFENNPLLQLHTPEDYENDVHAVADLLKIFFRELREPLIPDNHQRDFIDAGNVEDESRRRDAVHRAINDLPDANYSTIRHLTIHLAKIKENSDVNKMSTNNLAIIWGPTIIKQATIPEISSFSRTIEILIDYCFTIFDYD
| null | null |
actin cytoskeleton organization [GO:0030036]; Golgi to plasma membrane protein transport [GO:0043001]; mitotic division septum assembly [GO:0140278]; negative regulation of cell wall integrity MAPK cascade [GO:1903138]; positive regulation of mitotic division septum assembly [GO:0140281]; signal transduction [GO:0007165]
|
actin cortical patch [GO:0030479]; cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cell tip [GO:0051286]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; mitotic actomyosin contractile ring [GO:0110085]; mitotic actomyosin contractile ring, proximal layer [GO:0120104]
|
GTPase activator activity [GO:0005096]
|
PF00611;PF00620;
|
1.20.1270.60;1.10.555.10;
| null | null | null | null | null | null | null | null | null |
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94477
|
MYO52_SCHPO
|
MTSGIYYKGLQCWIPDEQSQWIPGSIKDCRVEGEKAFLTVQDENENETVITVKPDDLNYEGRNGLPFLRSINSDADDLTDLSYLNEPSVLDALSTRYNQLQIYTYSGIVLIAVNPFQRLPNLYTHEIVRAYSEKSRDELDPHLYAIAEDSYKCMNQEHKNQTIIISGESGAGKTVSARYIMRYFASVQALIQSTDSNFHEAPQLTAVENEILATNPIMEAFGNSKTSRNDNSSRFGKYIQILFDGNATIIGAKIQTYLLERSRLVFQPNQERNYHIFYQILAGSSSEQLEKWKLVENSQEFNYLKQGNCSTIEGVNDKEEFKATVDALKTVGIDNDTCECIFSLLAALLHIGNIEVKHSRNDAYIDSKNENLINATSLLGVDPSSLVKWLTKRKIKMASEGILKPLNEFQAVVARDSVAKFLYASLFDWLVATINKALMYSADKSNQTAKSFIGVLDIYGFEHFKKNSFEQFCINYANEKLQQEFYRHVFKLEQEEYAAEGLNWSYIDYQDNQQCISMIESRLGILSLLDEECRMPTNSDENWVSKLNDAFSKPEFKNSYQKSRFGNKEFTIKHYALDVVYCAEGFIDKNRDTISDELLELFTNSDVPFVKDLVLFRLEQTAPPADTKKIKTKPKSNTLGSMFKSSLVSLMSTINETNAHYIRCIKPNEEKEAWKFDNQMVVSQLRACGVLETIKISCAGFPSRWTFDEFVSRYYMLVPSAVRTTESLTFSKAILEKHADPTKYQIGKTKIFFRSGVTPLLESARDKALKHAAHLLYEAFAVNYYRTRFLLSRKRVRSFQAVAHGFLSRRHTEYELLSSNIIKLQSLWRTALKRKEFIQTKNSILKVQSIIRGFLLRQTLEEKTKHDATLIIQSLWLTFKAHKHYKELQYYAVRIQSLWRMKLAKRQLTELKIESTKASHLKQVSYRLESRLFEISKQLDNSEQENNKFRERIAELESHLSNYAEAKLAQERELEQTRVLISDQSQDGELKELLEEKENALIMMEEEMRQVNDANTELLRVNATLKSQLKNYDMIIVEQTSQLKEKNRIIASLTKATKILNSASSIEQSRNSEEKSRRDSSLMEMRTQKEMLVLLMNDGLKHDLDKLTEYAGRTFTTLKTLLLKDNDVEAQKLDHLFLAKLLFIIISQMWKSNLCQESVALVERYCVHTLEYVFQKTSSANERPDIGFWVANTHALLAFVYTKQQAFKHSSAFTLLSTESHESVQTIFEMIESHLSKIFFEWVRQVNNFLKPLIVQAMIITGTNTDAGDENRKLRIKFFEKPKYKITDVIHVLNKVHDSCQAYKVNYEIYNALIRSIYRFINVEAFNSLFIDERGSWKRGTNISYNYHVLKDWCLESGVPEAYLQLEELLQTSKILQFVKDDPNYVARVRDFYALNFLQIKTLLHRYDYADYEAHVPKKTMSELSKNIVAEGINQREQLTYEVLDYRLQDSFEESPSLEKIKIPDDCNVTYLRRIIDLASAEESVEQALITVGNVADNDVQNSSDEENQVPNGIKV
| null | null |
actin filament bundle organization [GO:0061572]; actin filament bundle retrograde transport [GO:0061573]; actin filament organization [GO:0007015]; establishment or maintenance of cell polarity [GO:0007163]; formin-nucleated actin cable assembly [GO:0070649]; mitotic cytokinesis [GO:0000281]; protein localization to cell cortex of cell tip [GO:1990896]; protein transport to mating projection actin fusion focus [GO:1904601]; vesicle transport along actin filament [GO:0030050]
|
actin cortical patch [GO:0030479]; actin cytoskeleton [GO:0015629]; cell cortex of cell tip [GO:0051285]; cell cortex of growing cell tip [GO:1902716]; cell division site [GO:0032153]; cell tip [GO:0051286]; cortical dynamic polarity patch [GO:0090726]; cytoplasm [GO:0005737]; lateral cell cortex [GO:0097575]; mating projection actin fusion focus [GO:1990819]; medial cortex [GO:0031097]; membrane [GO:0016020]; myosin complex [GO:0016459]; vesicle [GO:0031982]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]
|
PF01843;PF00612;PF00063;
|
1.10.10.820;1.20.5.190;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:11112691}. Note=Localized at the cell poles and septum.
| null | null | null | null | null |
FUNCTION: Involved in cell wall deposition where it has a role in the localization of mok1. {ECO:0000269|PubMed:11112691}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94487
|
PPK35_SCHPO
|
MDLLGLKELDNNKLVSKAKENGVEFSDLFLLSSGYLRDRENASASVSSKNERMVLNEERQNCWTKRNDPKGLTYYQLLKPSEVEILSRPETRRKRMACQVFFLNYYISTIEYHKLRKERLEEFTACTSSLKQSKQKRLWKEHCGRERAFLRKKRTKIQCSHFDLLVKLGQGGYGSVWLAKKRNTHELLAMKMMKKSTLQQLNEVKHILNERDILTNTNSEWLVKLYYAFQDKEKVYLAMEYVPGGDFRTFLTTKGLLHENQTRFYLAEMVAAISAVHKLGYMHRDLKPENFLIDQKGHIKLSDFGLSTAIVTSNQVNRLQHALVSAVNPQRPYLTQKQRRNIYKALLEKNENKVNSVVGSPEYMAPEVVYGKKYDRTVDYWSLGCICYECLVGYPPFSGSTLQETWTNLYYWREMLQRPSKNENGIYDKKARSVSDEAWSFITKCLTEPTSRFQSTIEIQKHPFFKRLHWNGLRKRAVPPFVPRLENQLDTSYFDDFNDEQVLDAYKDVYEKQRKAEQKAKSNGVMNGNQRQFLGFTFKYRPNARKPLVGRHREKRQLRKEKPEKKNNSTKQKDLITVSHNKGTTAIEDLDEDKRSKTKGHKTKSSRVHRLLERKGKDLYEFLL
|
2.7.11.1
| null |
ascospore-type prospore membrane formation [GO:0032120]; intracellular signal transduction [GO:0035556]; lipid droplet localization to prospore membrane leading edge [GO:0140043]; phosphorylation [GO:0016310]
|
cytosol [GO:0005829]; meiotic spindle pole body [GO:0035974]; nucleolus [GO:0005730]; nucleus [GO:0005634]; prospore membrane [GO:0005628]; spindle pole body [GO:0005816]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF00433;
|
1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
|
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=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Has a role in meiosis. {ECO:0000269|PubMed:16303567}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94488
|
MBO1_SCHPO
|
MEENSSELDSNNFNVLVDNLAGLSLTDEEVRRILSPRKEGSRQLPSSTSKDEDSEEASHKYDFEIDRDSLKSDSGSPRLHQNATAPTSSTPLQSPDESVNKLNSEDEEGNSSVAPFFLDTTNFDRLNDNITTDDEQLSPVLTANQGFQSQEQYEEDSYNNYDYTSDPSSPNYISSSLDQLPHLDDEDDLQLTPIKEERNYLHSQDAPTTNALSKKISDILIPASAMKDLKDRKNALAKEFEESQPGSSLTLKEQANVIDNLRKEVFGLKLKCYFLYDQLNKFHDQEVQDIMKQNIDLKTLTMELQRAVAGYEKKISGLESRIKPDQSFNLSTPSPAPSNLITLQSRYSQALSELETTKRAFAALRKEKSKKTNYSVGAYNEDRNVLSNMLDNERREKEALLQELESLRVQLSKKVPMPAKNTDERVIETLQRSNELLRMDISMQNEALLLRKQENDRLVKQVEELTVALNSGKMNAIVEAESSKNELWDSMMVSRMKTQEQSIELTRLYKQLQDIEEDYENKLMRMEQQWREDVDQLQEYVEEITQELQDTKEVLSKSSKESDDYEEVVGKLRTEAEREIEKFEKTIRENEESISLFKEEVEKLTDEITQLSERYNDKCHEFDELQKRLQTLEEENNKAKEDSTSKTSNLLEQLKMTEAEVDSLRKENEENKQVIALKESELVKSNDNKLLLNEQIESLNDQLSQLKTEMESVTTSKESLADYLSNLKERHNDELDSLNKKLREFEGILSSNSSLKSEIEERNNQYVTLRENFDSLQNAIMETFDKQVTHCSVNHLVQQIRKLKDENKKDQSGTDKLMKKIYHCEQSLKEKTNSLETLVSEKKELKNLLDAERRSKKAIQLELENLSSQAFRRNLSGSSSPSERSQSRELKLLQASEKRLKEQVEERNSLIKNIVTRFTQLNTGSKPVNTNVEALTTISSMNQAVNMNFRELDKSIQEFKRKCQSMEREFKTELRKLDGVLEARSKRLSQLEERVKLLGAGSTSSIPNSPRASKRVSLDSEDKKLVPASPDKSAVQRGITALKRDAEGMSHIWQLRLREMEFQLKAEQEGRKRDKLGARERLQDLIRQNRSLSRQIKTDKESNSRSPSISSQEHK
| null | null |
astral microtubule nucleation [GO:0030954]; centromere clustering at the mitotic interphase nuclear envelope [GO:0072766]; dynein-driven meiotic oscillatory nuclear movement [GO:0030989]; establishment of mitotic spindle orientation [GO:0000132]; karyogamy involved in conjugation with cellular fusion [GO:0000742]; microtubule nucleation by interphase microtubule organizing center [GO:0051415]; nuclear migration by microtubule mediated pushing forces [GO:0098863]; spindle pole body-led chromosome movement during mitotic interphase [GO:0140405]
|
equatorial microtubule organizing center [GO:0000923]; half bridge of mitotic spindle pole body [GO:0061496]; interphase microtubule organizing center [GO:0031021]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; microtubule organizing center [GO:0005815]; mitotic actomyosin contractile ring, proximal layer [GO:0120104]; mitotic spindle pole body [GO:0044732]; outer plaque of mitotic spindle pole body [GO:0061499]; static microtubule bundle [GO:0099070]
|
calmodulin binding [GO:0005516]
|
PF07989;PF12808;
|
1.10.287.1490;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:15004232, ECO:0000269|PubMed:15120067, ECO:0000269|PubMed:15659644, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:19001497}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:15004232, ECO:0000269|PubMed:15659644, ECO:0000269|PubMed:19001497}. Note=Localizes at the interphase MTOC (iMTOC) and at the equatorial MTOC (eMTOC) at the end of mitosis. {ECO:0000269|PubMed:15004232, ECO:0000269|PubMed:19001497}.
| null | null | null | null | null |
FUNCTION: Spindle pole body (SPB) component that acts as the gamma-tubulin complex-binding protein of the SPB outer plaque (PubMed:15120067, PubMed:15659644, PubMed:19001497). Promotes nucleation of all cytoplasmic microtubules by recruiting the gamma-tubulin complex to the spindle pole body (SPB), to the interphase microtubule organizing center (iMTOC), and to the equatorial MTOC (eMTOC) during anaphase (PubMed:15004232, PubMed:15120067, PubMed:15659644, PubMed:19001497). {ECO:0000269|PubMed:15004232, ECO:0000269|PubMed:15120067, ECO:0000269|PubMed:15659644, ECO:0000269|PubMed:19001497}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94489
|
EF3_SCHPO
|
MSAKSENKQSVKALEELLKHLTVCDAAEEADAAKALASFVNGPIEEQDAPSQVFSAISKQLNDKNATARERVLKGLEAVANHGSVAADVEPYLVELLPAVIAKVADKQNAVRDAAIAASKAIVRCTTPYAVKAIVPSVLESIHTTGKWNEKMNSLQLLDVLVEVAPSQLSYSLPQIIPVVSESMWDTKAEVKKQSKETMTKVCTLIANADIDRFIPELINCIAHPEEVPETIHSLGATTFVTEVQAPTLSIMVPLLARGLNERSTPIKRKTAVIIDNMSKLVEDPQVVAPFLPKLLPGLYHIKDTIGDPECRSVVQRAITTLERVGNVVDGKIPEVSTAANPEVCLETLKAVLGEIKVPTNEEVIAKYVANIAAQLVEEKDNENESWVLNITPYLTAFIDEAHIHKIVEQLRTRSIAKIPGGASHAEEEEEGEDLCNCEFSLAYGAKILLNRTRLRLKRGRRYGLCGPNGSGKSTLMRAIVNGQVEGFPTHLRTVYVEHDIDESEADTPSVDFILQDPAVPIKDRDEIVKALKENSFTDELINMPIGSLSGGWKMKLALTRAMFKNPDILLLDEPTNHLDVVNVAWLENFLVNQKDVSSIIVSHDSGFLDHVVQAIIHYERFKLRKYLGNMSEFVKKVPSAKSYYELGASEMEFKFPEPGFLEGVKTKQRAIIKVQHMSFQYPGTSKPQLNDISFQVSLSSRIAVIGPNGAGKSTLIKVLTGELLPTVGEIYQHENCRIAYVAQAAFTHLGHHPDKTPSEYIQWRFQSGEDLEAMDKASRVISEADEEAMKNKIFKIEGTQRKILGIHSRRKLKNSYEYECSFLVGENIGMKSERWVPMMSSDNAWLPRGELMETHAKMVAEVDRAEALKSGQFRPLVRKEIEEHCSLLGLDAELVSHSRIKGLSGGQKVKLVLAACTWLRPHVIVLDEPTNYLDRDSLGALSKGLKNFGGGVVLVTHSREFTEGLTEEVWAVNNGHMTPSGHNWVSGQGSGPRIQEKEEGDTFDAFGNKIEKAKKAKKLTGAELRKKKKERMARRKAGLEVSDDEL
|
3.6.4.-
| null |
cytoplasmic translation [GO:0002181]; cytoplasmic translational elongation [GO:0002182]
|
cytosol [GO:0005829]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; translation elongation factor activity [GO:0003746]
|
PF17947;PF00005;PF21040;
|
1.20.1390.20;2.40.50.990;1.25.10.10;3.40.50.300;
|
ABC transporter superfamily, ABCF family, EF3 subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000250|UniProtKB:P16521};
| null |
PATHWAY: Protein biosynthesis; polypeptide chain elongation. {ECO:0000305}.
| null | null |
FUNCTION: Ribosome-dependent ATPase that functions in cytoplasmic translation elongation (PubMed:29300771). Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (By similarity). Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied (By similarity). {ECO:0000250|UniProtKB:P16521, ECO:0000269|PubMed:29300771}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94504
|
TRX2_SCHPO
|
MRGFIANSLKPHMRSFALRRSFTSSRILRKVNAVESFGDYNTRISADKVTVVDFYADWCGPCKYLKPFLEKLSEQNQKASFIAVNADKFSDIAQKNGVYALPTMVLFRKGQELDRIVGADVKTLSSLLAKYQE
| null | null |
cell redox homeostasis [GO:0045454]; cellular detoxification [GO:1990748]
|
mitochondrion [GO:0005739]
|
protein-disulfide reductase activity [GO:0015035]
|
PF00085;
|
3.40.30.10;
|
Thioredoxin family
| null |
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Disulfide reductase which serves multiple functions in mitochondria, protecting mitochondrial components against thiol-oxidative damage as a thiol-disulfide oxidoreductase, and supporting urea cycle and respiration in mitochondria in a manner independent of active site thiols. {ECO:0000269|PubMed:12020831, ECO:0000269|PubMed:18849471}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94505
|
DPNP_SCHPO
|
MSFDAEKQLAIAAVRRASYLTEKVFNQLIKEKSAAGALTKDDKSPVTIGDFGAQAIVISMLKDAFPNDPIVGEEDSDFLRENTQTCSRVWELVQETIQHATEYKELGQIKSAEEMMSIIDQGSYHGGRNGRMWTLDPIDGTKGFLRGAQYAICLALIENGKPVVSAIGCPNLPYDFNQPETSPKGIIMSAVRNHGCFQYSLHNEKLEPVQVHMQDVQNTKDSKFCEGVEAGHSMQGTQEEIAKYLGITRGPTKMDSQAKYASLARGDGDIYLRLPTKMTFEEKIWDHAGGSLLVEEAGGVVSDMFGKPLDFGVGRTLKNNNGVIAAYKGIFEKVIEATAAVTSKDPHFQKVAQ
|
3.1.3.57; 3.1.3.7
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10850973}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P32179};
|
methionine biosynthetic process [GO:0009086]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; sulfate assimilation [GO:0000103]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
3'(2'),5'-bisphosphate nucleotidase activity [GO:0008441]; inositol-1,3,4-trisphosphate 1-phosphatase activity [GO:0052829]; inositol-1,4-bisphosphate 1-phosphatase activity [GO:0004441]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]
|
PF00459;
|
3.40.190.80;3.30.540.10;
|
Inositol monophosphatase superfamily
| null | null |
CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + H2O = adenosine 5'-phosphosulfate + phosphate; Xref=Rhea:RHEA:77639, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58243, ChEBI:CHEBI:58339; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77640; Evidence={ECO:0000305|PubMed:10850973}; CATALYTIC ACTIVITY: Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10041; Evidence={ECO:0000305|PubMed:10850973}; CATALYTIC ACTIVITY: Reaction=adenosine 2',5'-bisphosphate + H2O = AMP + phosphate; Xref=Rhea:RHEA:77643, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:194156, ChEBI:CHEBI:456215; EC=3.1.3.7; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77644; Evidence={ECO:0000305|PubMed:10850973}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate; Xref=Rhea:RHEA:15553, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58282, ChEBI:CHEBI:58469; EC=3.1.3.57; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15554; Evidence={ECO:0000305|PubMed:10850973}; CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,3,4-trisphosphate + H2O = 1D-myo-inositol 3,4-bisphosphate + phosphate; Xref=Rhea:RHEA:70319, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58414, ChEBI:CHEBI:83241; Evidence={ECO:0000269|PubMed:10850973}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70320; Evidence={ECO:0000305|PubMed:10850973};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=77 uM for 1D-myo-inositol 1,4-bisphosphate {ECO:0000269|PubMed:10850973}; Note=KM for adenosine 3',5'-bisphosphate is below 10 uM. {ECO:0000269|PubMed:10850973};
| null | null | null |
FUNCTION: Phosphatase that converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Is also able to hydrolyze inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4-trisphosphate (Ins(1,3,4)P3), but is not active on inositol 1,4,5-trisphosphate, inositol 1-phosphate, fructose 1,6-bisphosphate, AMP and ATP. {ECO:0000269|PubMed:10850973}.; FUNCTION: Confers resistance to lithium. {ECO:0000269|PubMed:10850973}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94510
|
AGN2_SCHPO
|
MASLTTALPNKAVVAHFMMGLTYNYAQSDFQNDIQNAISLGLDGFVLNFGNDSWMMSKLTLMYNAADALNLQFLLYLNLDMSEMSTVPASTLVTYVQTFANRGHQARINNNVVVGTFLGQDINFGQSSVNQGWQVAFKNALASAGINIFFMPTWPLDASTIYQTYPVADGFCKWNCWPYYTSSPTSDAEDLVYIQNSKATNKKYMATVSPIFYTHFTSKNYSFFSEGLWFTRWMQLIKDQPNYVQVLTWNDYGESTYIGPTNYAADFPVIGSNSHEWVDSFTHAPLSYSLPLFIQMYKQNTTGLPSNFSGISQLYVTYRVHSKNATASSDSIPRPDNYQNSSDVISVISFAKSSYTLRVSVNGTVLGTTNVNAGVQSANVSFIVNNTAAAGLPLFQILNGTTVIAQGYGPLNILGNNSVVLYNFNFCTTRISW
|
3.2.1.59
| null |
alpha-glucan catabolic process involved in ascospore release from ascus [GO:0072316]; ascospore release from ascus [GO:0071998]; cell division [GO:0051301]; extracellular polysaccharide catabolic process involved in ascospore release from ascus [GO:0072000]; fungal-type cell wall disassembly involved in conjugation with cellular fusion [GO:1904541]
|
ascus epiplasm [GO:0072324]; cytosol [GO:0005829]; mating projection actin fusion focus [GO:1990819]; nucleus [GO:0005634]
|
glucan endo-1,3-alpha-glucosidase activity [GO:0051118]
|
PF03659;
|
3.20.20.80;
|
Glycosyl hydrolase 71 family
| null |
SUBCELLULAR LOCATION: Ascus epiplasm {ECO:0000269|PubMed:15194814, ECO:0000269|PubMed:19542306}.
|
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->3)-alpha-D-glucosidic linkages in isolichenin, pseudonigeran and nigeran.; EC=3.2.1.59;
| null | null | null | null |
FUNCTION: Promotes the release of ascospores from asci by hydrolyzing 1,3-alpha-glucan in the ascus wall. {ECO:0000269|PubMed:15194814, ECO:0000269|PubMed:19542306}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94513
|
EIF3E_SCHPO
|
MGSELKSTSPLAVKYDLSQKIMQHLDRHLIFPLLEFLSLRQTHDPKELLQAKYDLLKDTNMTDYVANLWTNLHGGHTDEDMANAFAEKRRSVLQELSELEEEVQGILGVLENPDLIAALRQDKGQNLQHLQEHYNITPERIAVLYKFAQFQYNCGNYGGASDLLYHFRAFSKDPELNASATWGKFASEILTVDWDGAMEELGKLREMVDSKSFKDSAVQLRNRTWLLHWSLFPLFNHANGCDTLCDLFFYTPYLNTIQTSCPWLLRYLTVAVVTNQNNANQKPRNPRQSYQRRMRDLVRIISQENYEYSDPVTSFISALYTEVDFEKAQHCLRECEEVLKTDFFLVSLCDHFLEGARKLLAEAYCRIHSVISVDVLANKLEMDSAQLIQLVENRNNPSVAAASNVAADQSTEDESIESTSTNVVADDLITEAETATEAEEPEPEVQFGFKAKLDGESIIIEHPTYSAFQQIIDRTKSLSFESQNLEQSLAKSISELKHATV
| null | null |
eukaryotic translation initiation factor 3 complex assembly [GO:0070196]; formation of cytoplasmic translation initiation complex [GO:0001732]; translational initiation [GO:0006413]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; eukaryotic 43S preinitiation complex [GO:0016282]; eukaryotic 48S preinitiation complex [GO:0033290]; eukaryotic translation initiation factor 3 complex [GO:0005852]; eukaryotic translation initiation factor 3 complex, eIF3e [GO:0071540]; nucleus [GO:0005634]
|
translation initiation factor activity [GO:0003743]
|
PF09440;
| null |
EIF-3 subunit E family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:11071922, ECO:0000269|PubMed:11071923, ECO:0000269|PubMed:11134033, ECO:0000269|PubMed:15904532}.
| null | null | null | null | null |
FUNCTION: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation (Potential). Required for maintaining the basal level of atf1 and for transcriptional activation of core environmental stress response genes (CESR genes) in response to histidine starvation (PubMed:18502752). May positively regulate proteasome activity (PubMed:12553909). Required for nuclear localization of the proteasome subunit rpn501/rpn502 (PubMed:12553909). {ECO:0000255|HAMAP-Rule:MF_03004, ECO:0000269|PubMed:12553909, ECO:0000269|PubMed:18502752}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94529
|
POB3_SCHPO
|
MAAKTVQYDNIYLNLSEKPGKLRIAPSGLGWKSPSLAEPFTLPISEIRRFCWSRFARGYELKIILKSKDPVSLDGFSQEDLDDLINVIKQNFDMGIEQKEFSIKGWNWGEANFLGSELVFDVNSRPAFEIPISAVTNTNLSGKNEVALEFSTTDDKQIPSAQVDELVEMRLYVPGTTAKEDAADGEEVEQNAANLFYESLKERADIGQAAGDAIVSFSEILLLTPRGRYDIDMYETCMRLRGKTYDYKVEYSSINSLFLLPKPDEQHVVFVIGLEPPLRQGQTRYPFLVTQFVRDEDMEVDLNIEETVLKEKYADKVKASYDQPAFEVVSQIFRGLTGRKVTTPAEFLSHEGHAAVKCSYKANEGQLYCLDKSFLFIPKPTLLMNTSDITRVTLSRVGMSVSAARTFDLTFTLRSGTSYQFSNINRVEQSALVAFLESKQIKIHNDLADETQQTLLTSALDDEDEEGDEEMEEALSEDEDFQAESESDVAEEYDENAESSDEEGASGAEGSE
| null | null |
constitutive heterochromatin formation [GO:0140719]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA replication-dependent chromatin assembly [GO:0006335]; nucleosome organization [GO:0034728]; regulation of chromatin organization [GO:1902275]; transcription elongation-coupled chromatin remodeling [GO:0140673]
|
cytosol [GO:0005829]; euchromatin [GO:0000791]; FACT complex [GO:0035101]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]
|
DNA binding [GO:0003677]; H2A-H2B histone complex chaperone activity [GO:0000511]; histone binding [GO:0042393]; nucleosome binding [GO:0031491]
|
PF21103;PF17292;PF08512;PF03531;
|
2.30.29.150;2.30.29.30;2.30.29.220;
|
SSRP1 family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04636}. Chromosome {ECO:0000250|UniProtKB:Q04636}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. {ECO:0000250|UniProtKB:Q04636}.
| null | null | null | null | null |
FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (By similarity). {ECO:0000250|UniProtKB:Q04636}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94532
|
FOR3_SCHPO
|
MASKMPEGSPPTSRSIQSRNSSYSTSSNERIGTPSTISLSENSDLSKLQSTNDFESREDLSLTSDDNNDPEYVMCYNTVYHQKTKINDKLLSETEQLRKIYPLESRVFPKPTIVKEITNERTKRYTFYDDDAPLTNQHTVLDEATYNRILKRIDFFIEKVVEVPPTYHFLSLLNVQLRIQPIWWMDEFAERNGIESLLSALRNLGHYPERASKTPLESQIIQSLFHCLNSENCRRRYQSSAKCSVPGFNALGTIAETVLSKSLNSARMATFLLKFLCNKKGLSYFKAVIRAFEWLVEQKLSKTRFSAWMHSFNDVITGVRVCADSSPQAIVHMDEFEDTDCLIDYLVATLALIRDLCAAPPDLQLRCALRHELLSAGLQKAIDSLLKWRNRHVRDALQLLIKEHNADARRFRSGSDVNNVDRKCVKKQMNYREESHTPHGNTTRKTSTPVSNNRPTTPEQQAVWDVFQRIYTRFTGSEGSKESFIKLLEYFVTEPDNGKIQKSMQLLTHTLEALEGFKTAKADTNVGLTILSQRLLDKLGTAEEIAEYKTKYNGAMLENKHLKEQVESMLSQLNVGPRDPMQFLKKQLDELKAELNLRDNLLASMQREFETRYRAQIQAYNKLQSQMEHVQNSNEQHLQPGLLNKVSKSFDSVHRRNLSQDSLDAMTEQFSYHVEPNILSGSGIPVRVHTPSKTEDLDESFSGSEISSSPSPLLPDVSDTVEEQQKLLLKSPPPPPPAVIVPTPAPAPIPVPPPAPIMGGPPPPPPPPGVAGAGPPPPPPPPPAVSAGGSRYYAPAPQAEPEPKIDETSLTEEQKIQLEEARKQRKAADDAARAAIEKYTSIPSLRDLHKPTRPLKRVHWQRVDPLPGPNVFTKFCLNFDITAKVFIDNGLLDFLDEKFDNTPREDFVAVEISDQRSSLLPDTVEQNMAIILRSVSNMPVEDLVQKFLVEPDFLPASILYFDRASLASTNAYTDPFIPYSTDYTKKNPKEPTADVNSLSYFEKFFVLFVVNLRHYFQERMKALKFRSTLFGDLEILEVRMKEVIDTSDSIMEDKNFAEFFQVLLIIGNYFNEPYDRASAFSLYMIYRLETLRDSSSALTLMHYFDEIIRTRFPELLQAESTFKKIQSVSGYNIDAMVAGVDGAYDEFCDFQTSLKDGALSKCDQHHPDDKAYDILSEWLPEAKERIRNIKKLKTDMLTKLENTVKYLCEYDSIDKVRNSFFKNLNSFYEMYSIAKAENEERFEKEKRRIMSEDRDKLIRGRQKTSIVAKYRNKRELPEDSDDKQDTASKDKNSLETIDEKMEDASKIEGDAKTGDDNEMEDLDKMEDLEKPDYAEEKDPYITVMSELRSRIQNVPKRTVTVYSDEGVATLEPGAQGDDVVDKAKMILEKMEGHSQLLTSSANPDEEVLRAKLKAAERLQKPAIPRTRRKGHTEPKSAKSLLAELTNGSNASNLVENDRQKQ
| null | null |
actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; actin filament bundle organization [GO:0061572]; barbed-end actin filament capping [GO:0051016]; establishment or maintenance of bipolar cell polarity [GO:0061245]; mitotic actomyosin contractile ring assembly [GO:1903475]; protein localization to mitotic actomyosin contractile ring [GO:1904498]; regulation of cell shape [GO:0008360]
|
cell cortex of cell tip [GO:0051285]; cell cortex of growing cell tip [GO:1902716]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; mating projection tip [GO:0043332]; medial cortex [GO:0031097]; medial cortex septin ring [GO:0036391]; mitotic actomyosin contractile ring [GO:0110085]
|
actin binding [GO:0003779]; small GTPase binding [GO:0031267]
|
PF06367;PF02181;
|
1.20.58.2220;1.25.10.10;
|
Formin homology family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:11696322, ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:11696322, ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:15809031, ECO:0000269|PubMed:16823372}. Note=Found at the cell cortex and the growing tips of interphase cells. Localized to the septum region during cell division and upon cell division begins to localize to the new end, with some remaining at the older end. {ECO:0000269|PubMed:11696322, ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:15809031}.
| null | null | null | null | null |
FUNCTION: Involved in controlling polarized cell growth. Required for interphase actin cable formation and microtubule organization. {ECO:0000269|PubMed:11696322, ECO:0000269|PubMed:12415007, ECO:0000269|PubMed:15809031}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94534
|
ALP14_SCHPO
|
MSQDQEEDYSKLPLESRIVHKVWKVRLSAYEECSKSFSLSADGSDNCFELWNNQSELWKSVLTDSNVAAQEAGTAAFVAYCRFSDPSHLLKAREISVLSISEKCLTSPRAGTRENALEALMLLVEADSAAPVIESIIPSLSARSPKVIASNVAAIASLVEQFGAKVIPSKMIIPHISNLFGHADKNVRKEASRLTVNIYRWTGDPLKDLLFKDLRPVQTKELESLFAELPTEPPKQTRFLKSQQPTSEPNVETQVEEQPALENEESEPEPSDDQFDLVEEVDVLPNVDPNLETLMASSKWKDRKEALDKLLPVLSQPKIKDNDFFNLVAILTKSVSKDANIMVVINAAHCIQAMAKGLRSNFSKYASTSINALLERSKEKKANVIESLSSAMDAVLATSSLDDLAELIASFAGNKNPQIKSSCFSLFSRSFSNMTSLPSKFTVDTCAKACVPGVSDTFEPVRSAAAEALGVLMKLVGERAINQYLSPLDDIRKSKIRSFYETATVKAKAPTKKSKVKPSKQEESKVVVPSNAKAVKKSVVPSSPVVPSPRKATNKSLSMDVSKGNAFENGPLLPRPTTRPVSRGLSRGTSSSLQQKVKASTPLNSGALNETVQNLKNMELDDPAPQPAKHSRVDRYEHPKVLEDNDSTISSLESLKRENEELREQLKVEHEENISMQKQLSELKGELNTLRSARKASPIGDRKPAFMRRANTDFLELSTSPSFQRSVREFEPTRPKLYSSIDVNQRSPLASAKTNGNFTFHAELPRSPFSSRANNINPDWTKAIDLAAKLKQKITEMKQTDQRHQGLIH
| null | null |
attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; cell division [GO:0051301]; cytoplasmic microtubule organization [GO:0031122]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; meiotic centromere clustering [GO:1990571]; microtubule nucleation by spindle pole body [GO:0051417]; microtubule polymerization [GO:0046785]; mitotic spindle assembly [GO:0090307]; mitotic spindle elongation [GO:0000022]; mitotic spindle organization [GO:0007052]; protein transport along microtubule to kinetochore [GO:0140210]
|
cytoplasmic microtubule [GO:0005881]; cytoplasmic microtubule plus-end [GO:1904511]; cytosol [GO:0005829]; kinetochore [GO:0000776]; meiotic spindle [GO:0072687]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686]; mitotic spindle microtubule [GO:1990498]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; outer kinetochore [GO:0000940]; spindle pole [GO:0000922]; spindle pole body [GO:0005816]; static microtubule bundle [GO:0099070]; TACC/TOG complex [GO:0070850]
|
microtubule binding [GO:0008017]; microtubule plus end polymerase [GO:0061863]; microtubule plus-end binding [GO:0051010]
|
PF21041;
|
1.25.10.10;
|
TOG/XMAP215 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Chromosome, centromere, kinetochore. Note=Kinetochore periphery. Spindle localization is alp7-dependent.
| null | null | null | null | null |
FUNCTION: Required for bipolar spindle formation and proper chromosome segregation. Has a role in connecting the kinetochores and the plus end of pole to chromosome microtubules. Also required for the activation of the spindle checkpoint pathway. {ECO:0000269|PubMed:11432827, ECO:0000269|PubMed:14742702}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94537
|
IRE1_SCHPO
|
MKSLKGRLLFLRKFVFFSLLILLFAHGASSSSSSFNYFDKRTNGKANNELALFSPTADSPSSVDGVLELPSAENVFAESSLYNAFIVATVDGSLHSYDRITGQELWSLFTNANPGLSYTKDENSLLSSKFLSQSNFKSYNSTHGEFYSDSTLNISYLSDDDTVWFVEPIDGGILYAFNLQTGLVRLPHSIKDLVHASPIRLLNNNVFVGSKNTTLFTIDVSNGDIVSQYPSGHRYETHHSVHNLGTKRDSVPSGADSDLSFKDPSGKKLSESLDLLDDFNYQVTVSNKSFVDIARTEYFITIYSDSNVILDLVYIDWTPTKNEIMYESFHSSSFDSKLALSSYDSSLHIVDTHSKFIKQNIPLMSPAATVFDIVTLPHNKKIDKSQTPAKFPTSVLLRQPIDTYLETMFPQIARNKTEHVYINHIGNAWFAMSERHYPLVSLAPEASFLYYNGFYIPLNSIFGLHSLMATPKPFFALPGLPGYDIPSYVESEGSTKTLPSIGKKPIPLLDPNPISSTPISITFWVIMFLSVSFTIVTFFSILRIRSSEVRPLKSQKNTVSINNKIDTSKRRRKGKRRKRVSDEHSASSNFNEIESQASFEQNQTLDILSENIVEIQDKSTDPLQKSLDSSLKSHLPEATVIQNTDGSVTVNSLTVYPEVIGYGSHGTIVYRGVYEDREVAVKRVLMEFYDLASREITLLQQSDNHPNIVRYYCKQKSDQFLYIVIELCKCNLSDLIEKPIAYDDLFKSIDLVSLLYQIAFGVSHLHSLDLVHRDLKPQNILLVVNNSPNLSKTRVRALISDFGLSKKLDFNQSSLRNTTFEAAGSYGWRSPEILSGSLSQQSKEIQVKTREGRIRQASHATDIFALGCIFYYTLTGGMHPFGSHYDCEGNILKGNYCLVHLQSLGECGVLAADLIEDMIAFEPSKRPTIEVVLNHPLFWDYAKKLDFLIDVSDRFEVEERDPPSPLLQMLENNSKSVIGENWTTCLHSSLVDNLGKYRKYDGSKILDILRVLRNKRHHYQDLPESVRRVLGDLPDGFTSYFVEKFPMLLLHCYHLVKDVLYEESQFKRYLEY
|
2.7.11.1; 3.1.26.-
| null |
IRE1-mediated unfolded protein response [GO:0036498]; mRNA processing [GO:0006397]; phosphorylation [GO:0016310]; positive regulation of gene expression [GO:0010628]; positive regulation of reticulophagy [GO:0140501]
|
endoplasmic reticulum [GO:0005783]; IRE1-TRAF2-ASK1 complex [GO:1990604]
|
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; RNA endonuclease activity [GO:0004521]; unfolded protein binding [GO:0051082]
|
PF00069;PF06479;
|
1.20.1440.180;1.10.510.10;2.130.10.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type I membrane protein {ECO:0000269|PubMed:16823372}.
|
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=2.7.11.1; Evidence={ECO:0000305|PubMed:15821139}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000305|PubMed:15821139};
| null | null | null | null |
FUNCTION: Endoplasmic reticulum (ER) membrane-resident kinase/endoribonuclease involved in unfolded protein response (UPR) (PubMed:23066505). Initiates the selective decay of a subset of ER-localized-mRNAs that is required to survive ER stress (PubMed:23066505). Rather than relying on a transcriptional program to up-regulate genes that enhance ER protein folding capacity as in S.cerevisiae, S.pombe cells reduce the amount of specific proteins entering the organelle by decreasing the level of ER-targeted mRNAs using ire1-dependent mRNA degradation (PubMed:23066505). The sole mRNA cleaved upon ire1 activation that escapes decay is the ER chaperone bip1 mRNA which is more stable and hence is present at an increased steady-state after ire1 cleavage (PubMed:23066505). Promotes ER stress-induced ER-phagy and via up-regulation of the protein level of the ER-phagy receptor epr1 (Ref.5). {ECO:0000269|PubMed:23066505, ECO:0000269|Ref.5}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94544
|
LKHA4_SCHPO
|
MKLRLDPSTQSNYHDVSISKLDWHARIDFDQELLHGKVSFVIQSARVSQALSHIILDTSYLEIKNVTINDIPTPFRVDKRRGFLGSALHIVPADEIPSSKSCILTILYSTTKDCTALQFLKPEQTIGGKFPYVFSECQAIHARSFIPCQDTPSVKVPCTFKIRSKLPVIASGIPCGTANFCNGSLEYLFEQKNPIPSYLFCILSGDLASTNIGPRSSVYTEPGNLLACKYEFEHDMENFMEAAEQLTLPYCWTRYDFVILPPSFPYGGMENPNATFATPTLIAGDRSNVNVIAHELAHSWSGNLVTNESWQCFWLNEGMTVFLERKILGRLYGEPTRQFEAIIGWGELEESVKLLGEDSEYTKLIQNLEGRDPDDAFSTVPYEKGSNFLYEIERVIGGPSVFEPFLPFYFRKFAKSTVNEVKFKHALYEYFSPLGLASKLDSIDWDTWYHAPGMPPVKPHFDTTLADPCYKLAESWTNSAKNSDDPSKFSSKDIENWSAGQKSLFLDVVYEAVSFPHNYIKRMGDVYSFAESKNAELSFRFFKLALKSKYKPLYNTIAERVGSVGRMKFVRPIFRLLNEADRAFAIETFEKYKHFYHKICASQVEKDLGLSE
|
3.3.2.10; 3.4.11.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q10740}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q10740};
|
cytoplasm to vacuole targeting by the NVT pathway [GO:0120113]; peptide catabolic process [GO:0043171]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]
|
cytosol [GO:0005829]; fungal-type vacuole lumen [GO:0000328]; multivesicular body [GO:0005771]; nucleus [GO:0005634]; NVT complex [GO:0061957]
|
aminopeptidase activity [GO:0004177]; epoxide hydrolase activity [GO:0004301]; leukotriene-A4 hydrolase activity [GO:0004463]; metalloaminopeptidase activity [GO:0070006]; zinc ion binding [GO:0008270]
|
PF09127;PF01433;PF17900;
|
3.30.2010.30;1.10.390.10;1.25.40.320;2.60.40.1730;
|
Peptidase M1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=an epoxide + H2O = an ethanediol; Xref=Rhea:RHEA:19037, ChEBI:CHEBI:15377, ChEBI:CHEBI:32955, ChEBI:CHEBI:140594; EC=3.3.2.10; Evidence={ECO:0000250|UniProtKB:Q10740};
| null | null | null | null |
FUNCTION: Aminopeptidase that preferentially cleaves di- and tripeptides. Also has low epoxide hydrolase activity (in vitro). Can hydrolyze the epoxide leukotriene LTA(4) but it forms preferentially 5,6-dihydroxy-7,9,11,14-eicosatetraenoic acid rather than the cytokine leukotriene B(4) as the product compared to the homologous mammalian enzyme (in vitro). {ECO:0000250|UniProtKB:Q10740}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94547
|
SRK1_SCHPO
|
MRFKSIQQNIEDEGKVNVREVNPDSYAERDHGYTAGIFSDAEENFGITQQVADSTQNPTSKPKSRHAHFHETVHENPSEYSRSKCKQPTNEKEYDKAIEALVAKAIVEEHSGQQFPVYKGLEQYTLLQKMGDGAFSNVYKAIHNRTGEKVAIKVVQRAQPNTDPRDPRKRQGVESHNILKEVQIMRRVKHPNIIQLLEFIQTPEYYYLVLELADGGELFHQIVRLTYFSEDLSRHVITQVAHAIRYLHEDCGVVHRDIKPENLLFDSIDFVPSRVRKYRAGDDPDKVDEGEFIPGVGAGTIGRIRLADFGLSKVVWDSHTQTPCGTMGYTAPEIVRDERYSKGVDMWALGCVLYTILCGFPPFYDESISLLTKKVSRGEYSFLSPWWDDISKSAKDLISHLLTVDPESRYDIHQFLAHPWISGSREPTFPATDAPNTAQRENPFTYDFLEPEDVAAAGSAARTPGVNSLREVFNISYAAHRMEQEKIRKRGQRGNQGIMNFMGDMDDLMEENDDYDDGTKSVEHSMKRVNLSGENDPSLASRQPAQSQQQSSQRSRNKFKGFQLNLSKATLYNRRHRQKV
|
2.7.11.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15629716};
|
cellular response to osmotic stress [GO:0071470]; cellular response to oxidative stress [GO:0034599]; meiotic cell cycle [GO:0051321]; mitotic DNA damage checkpoint signaling [GO:0044773]; negative regulation of G2/M transition of mitotic cell cycle [GO:0010972]; negative regulation of induction of conjugation with cellular fusion [GO:0010515]; negative regulation of protein localization to nucleus [GO:1900181]; phosphorylation [GO:0016310]
|
ascospore-type prospore [GO:0042764]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily
|
PTM: Phosphorylated by sty1. {ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:12589433}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:12589433}. Nucleus, nucleolus {ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:15629716}. Spore core {ECO:0000269|PubMed:12589433}. Note=Translocates from the cytoplasm to the nucleus during environmental stress in a sty1-dependent manner. {ECO:0000269|PubMed:12080074}.
|
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=2.7.11.1; Evidence={ECO:0000269|PubMed:15629716}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:15629716};
| null | null | null | null |
FUNCTION: Delays the mitotic G2/M transition by promoting nuclear exclusion of cdc25 (PubMed:12080074, PubMed:15629716). During osmotic stress, inhibits the G2/M transition in a sty1 stress-activated MAPK pathway-dependent manner (PubMed:12080074, PubMed:12589433, PubMed:15629716). {ECO:0000269|PubMed:12080074, ECO:0000269|PubMed:12589433, ECO:0000269|PubMed:15629716}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94561
|
PRX_SCHPO
|
MDAPRRSSRLAAKIANVLDSKGTIIPEAAPVMLKKPAKDESVDSTIQVGDVIPDITLPDEDGTSIRLRDITANKGLVIFAYPKASTPGCTKQGCGFRDNYPKIQASDYEVLGLSFDTSKAQKAFKDKQNFPYHLLSDPKGELIKKLGAEKPGGGKLFRSHWIFEKGTGKCIVKEIDISPLVSVDKAFAVITDSEP
|
1.11.1.24
| null |
cell redox homeostasis [GO:0045454]; cellular detoxification of hydrogen peroxide [GO:0061692]; cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; removal of superoxide radicals [GO:0019430]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
thioredoxin peroxidase activity [GO:0008379]; thioredoxin-dependent peroxiredoxin activity [GO:0140824]
|
PF00578;
|
3.40.30.10;
|
Peroxiredoxin family, BCP/PrxQ subfamily
|
PTM: The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this atypical 2-Cys peroxiredoxin, C(R) is present in the same subunit to form an intramolecular disulfide. The disulfide is subsequently reduced by thioredoxin. {ECO:0000250|UniProtKB:P40553}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O; Xref=Rhea:RHEA:62620, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:30879, ChEBI:CHEBI:35924, ChEBI:CHEBI:50058; EC=1.11.1.24; Evidence={ECO:0000250|UniProtKB:P40553};
| null | null | null | null |
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (By similarity). Acts as a scavenger of H(2)O(2) (PubMed:20356456). {ECO:0000250|UniProtKB:P40553, ECO:0000269|PubMed:20356456}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94580
|
WSS2_SCHPO
|
MELKFSCRGNVIALSFNENDTVLDAKEKLGQEIDVSPSLIKLLYKGNLSDDSHLQDVVKNESKIMCLIRQDKDIVNQAISQLKVPDYSTNTYSLKPKKPHTTPKPASIYTFNELVVLDYPHKDRALRYLERLRDDTGIKKIMDSHRWTVPLLSEMDPAEHTRHDSKTLGLNHNQGAHIELRLRTDRYDGFRDYKTVKSTLIHELTHNVHGEHDSSFWELFRQLTKEADAADLLGKPGSYVSDRASYTPQQDNDDEDQKNHRRDLLLAAAERRKQSGSKVQKE
|
3.4.24.-
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305|PubMed:27871365};
|
DNA repair [GO:0006281]; protein sumoylation [GO:0016925]; proteolysis [GO:0006508]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
double-stranded DNA binding [GO:0003690]; metallopeptidase activity [GO:0008237]; proteasome binding [GO:0070628]; single-stranded DNA binding [GO:0003697]; transition metal ion binding [GO:0046914]; zinc ion binding [GO:0008270]
|
PF00240;PF08325;
| null |
Peptidase M3 family, WSS1-like metalloprotease (WLM) subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Metalloendopeptidase that acts selectively on DNA-binding proteins. DNA is needed to bring the protease and substrates together to enable proteolysis. Involved in the repair of toxic DNA-protein cross-links (DPCs) such as covalently trapped topoisomerase 1 (TOP1) adducts on DNA lesions or DPCs induced by reactive compounds such as formaldehyde. {ECO:0000250|UniProtKB:P38838}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94584
|
PSS_SCHPO
|
MVRSRVSPGLKLQSDASNQSNDKENKLLAYVNDNRHFSLIRALHLADLITLMNGFCGVMSIFSSLRYCLSGQQSAFHLWNAMYFMPFALFFDFLDGKVARWRGKSSLMGQELDSLADLISFGVSPAVFAFCCGFQTFLDTVILSLFVLCGLTRLARFNVSVNSIPKDGSGKSQFFEGTPIPTTLSLVTVCGVCILKGKTHENLPWGEWCGNTPFAFHPLVVLFVLSGIAMTSKKLKVPKI
|
2.7.8.8
| null |
CDP-diacylglycerol biosynthetic process [GO:0016024]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphatidylserine biosynthetic process [GO:0006659]; phosphatidylserine metabolic process [GO:0006658]; plasma membrane organization [GO:0007009]
|
cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]
|
CDP-diacylglycerol-serine O-phosphatidyltransferase activity [GO:0003882]
|
PF01066;
|
1.20.120.1760;
|
CDP-alcohol phosphatidyltransferase class-I family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane. Note=During log-phase growth, concentrates at the cell and nuclear peripheries as well endoplasmic reticulum membranes, while in stationary-phase cells, is redistributed to unusual cytoplasmic structures of unknown origin.
|
CATALYTIC ACTIVITY: Reaction=a CDP-1,2-diacyl-sn-glycerol + L-serine = a 1,2-diacyl-sn-glycero-3-phospho-L-serine + CMP + H(+); Xref=Rhea:RHEA:16913, ChEBI:CHEBI:15378, ChEBI:CHEBI:33384, ChEBI:CHEBI:57262, ChEBI:CHEBI:58332, ChEBI:CHEBI:60377; EC=2.7.8.8; Evidence={ECO:0000269|PubMed:17905925};
| null |
PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 1/2.
| null | null |
FUNCTION: Phosphatidylserine synthase involved in the regulation of processes such as cell morphology, cytokinesis, actin cytoskeleton, and cell wall remodeling and integrity. Also plays a role in the physiological adaptations required for stationary-phase survival. {ECO:0000269|PubMed:17905925, ECO:0000269|PubMed:19366728}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94603
|
JHD1_SCHPO
|
MDSWLEYDDIINQDIDIPSNDLSGSGTLCVGVHSSLLENSLNSIDSFISSKEEISWCGNQSTPIATKSHLSCINPQYVNPFDTSPVSVDTEFQDTYLLDAPSFAQPHFSERQSVDKTRSRCLSRNRRRKRHPNLHKNHQRLLGMSFPQDGFRRMPAESVNFSYFRDTGFNEPTIFPSSDTQNTRQLNLSKIATLIGYDCPLALVDVVTQKQIPNKMDMESWVKYMSLEPSKRGRIYDVLSLEVSTTKLAYYVRKPNIVRDLDLVNTVWPPGSFALGEYPHVDTYCLMSAENSYTEFHIEFGGSSAYYNILDGCKIFYLIPGTSKNWEAYTAWLTSSNDSDKKFLPNMVDVCYCVEVHSQQTILVPSGWIYAVVTPCDTISIAGNFLTFLHIYPQLSIYNLELQLGIEKEYQYPYFESIMWYTAIHFYLAFPDNSSRDGIDDIIAEYETGRLFDINAFTEQELDGFEELLNYLYIRAQILRDCDIIIDIYNEPVKISKNNGYNSAYTMVPPDLDEICVDFVQKFGAWITYHHRRSAKHPSCNCFSHLQTKLIDSGPKPANNSYQHQSNFIGVVISTNHNIIKKCQESQIQTGKNNCSFQLVKKRIKSTKKAPSWRSIIKAFKKRENTRCNFLSSLHATTFREDIVVRPKIKSFVLEQLIFQALFSFAINWTPSFFLNHSNFENIALSKETFNFGGEANCENTDTTLFTTWGDQGFRPSDSICYNDFNLLETANSDAEASIHELELQPLNAVNEREVDISQTDMTPSTALDTRVDTRVDSLPEFSNLILSPSSNDDSFQLDDLLSPSSSNLKQQIQKVVPQNSLEFSVGEKEKKAAEYSLLHTFSYKRLSMENEKPDTTKVPLKYNIQHEEMKAYRRKNDLEYIDQHFASSKSGISNGRNNNKEVNLTKAENVGIKKRRIMKNENNIYDFEDHSPVREKWGHRLRSRGAS
|
1.14.11.27
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250};
|
heterochromatin boundary formation [GO:0033696]; regulation of regulatory ncRNA-mediated heterochromatin formation [GO:0010964]; regulation of siRNA-independent facultative heterochromatin formation [GO:1902801]; regulation of transcription by RNA polymerase II [GO:0006357]
|
heterochromatin [GO:0000792]; heterochromatin island [GO:1990342]; nucleus [GO:0005634]
|
histone demethylase activity [GO:0032452]; histone H3K36me/H3K36me2 demethylase activity [GO:0140680]; histone H3K9 demethylase activity [GO:0032454]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712]
|
PF17811;PF02373;
|
2.60.120.650;
|
JHDM1 histone demethylase family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773576}.
|
CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29969, ChEBI:CHEBI:30031, ChEBI:CHEBI:61976; EC=1.14.11.27; Evidence={ECO:0000250|UniProtKB:P40034};
| null | null | null | null |
FUNCTION: May be a histone demethylase that specifically demethylates 'Lys-36' of histone H3, thereby playing a central role in histone code (By similarity). Represses transcriptional silencing by negatively affecting heterochromatin stability. {ECO:0000250|UniProtKB:P40034, ECO:0000269|PubMed:12773576}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94609
|
UBA1_SCHPO
|
MSNNMNIDQTDQNTIDEGLYSRQLYVLGHEAMKQMSQSNVLIIGCKGLGVEIAKNVCLAGVKSVTLYDPQPTRIEDLSSQYFLTEDDIGVPRAKVTVSKLAELNQYVPVSVVDELSTEYLKNFKCVVVTETSLTKQLEINDFTHKNHIAYIAADSRGLFGSIFCDFGENFICTDTDGNEPLTGMIASITDDGVVTMLEETRHGLENGDFVKFTEVKGMPGLNDGTPRKVEVKGPYTFSIGSVKDLGSAGYNGVFTQVKVPTKISFKSLRESLKDPEYVYPDFGKMMRPPQYHIAFQALSAFADAHEGSLPRPRNDIDAAEFFEFCKKIASTLQFDVELDEKLIKEISYQARGDLVAMSAFLGGAVAQEVLKATTSKFYPLKQYFYFDSLESLPSSVTISEETCKPRGCRYDGQIAVFGSEFQEKIASLSTFLVGAGAIGCEMLKNWAMMGVATGESGHISVTDMDSIEKSNLNRQFLFRPRDVGKLKSECASTAVSIMNPSLTGKITSYQERVGPESEGIFGDEFFEKLSLVTNALDNVEARMYVDRRCVFFEKPLLESGTLGTKGNTQVVVPHLTESYGSSQDPPEKSFPICTLKNFPNRIEHTIAWARDLFEGLFKQPIDNVNMYLSSPNFLETSLKTSSNPREVLENIRDYLVTEKPLSFEECIMWARLQFDKFFNNNIQQLLFNFPKDSVTSTGQPFWSGPKRAPTPLSFDIHNREHFDFIVAAASLYAFNYGLKSETDPAIYERVLAGYNPPPFAPKSGIKIQVNENEEAPETAANKDKQELKSIADSLPPPSSLVGFRLTPAEFEKDDDSNHHIDFITAASNLRAMNYDITPADRFKTKFVAGKIVPAMCTSTAVVSGLVCLELVKLVDGKKKIEEYKNGFFNLAIGLFTFSDPIASPKMKVNGKEIDKIWDRYNLPDCTLQELIDYFQKEEGLEVTMLSSGVSLLYANFQPPKKLAERLPLKISELVEQITKKKLEPFRKHLVLEICCDDANGEDVEVPFICIKL
|
6.2.1.45
| null |
DNA damage response [GO:0006974]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium ion binding [GO:0000287]; ubiquitin activating enzyme activity [GO:0004839]
|
PF16191;PF16190;PF09358;PF00899;PF10585;
|
3.40.50.720;2.40.30.180;3.50.50.80;3.40.50.12550;1.10.10.2660;3.10.290.60;
|
Ubiquitin-activating E1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
|
CATALYTIC ACTIVITY: Reaction=ATP + ubiquitin + [E1 ubiquitin-activating enzyme]-L-cysteine = AMP + diphosphate + S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine.; EC=6.2.1.45; Evidence={ECO:0000269|PubMed:23416107};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23416107}.
| null | null |
FUNCTION: Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin-proteasome system. Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. {ECO:0000269|PubMed:23416107}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94614
|
CHR4_SCHPO
|
MDSASSMRNRSPLGVPEFSYSSQSVNNIRGIKSRNRSSIGHSITDPQVASRINAFYLSNVQSSIPFETDAIGPAYGIGDMIAPEMNDTQSLSASVTNMKKENFYSRPNVSSSSILLTIKRATSSQETKRDRPLPNIRNSAPSATRSHSTPCVAPGYLRTSNEAADVVFPHEEAHFSNHNPKPNNGSPLQKQVVADLPFPLPVSDEEQLDWIRANEDLVHSQDIDEALEWAEYVLRFTQSHLPYLQTYESENLHEINYLESMCENALYKIREFSELENAKAMYFDAYVYETGAFDVESDIQRAWDLYSSSANLGYTRSLYRLGVLLEDQGNLEEAVEYFEKGVSENDSACCWRLSLLILEGMLDGVGEYAHRHASGLELLERSADTADADVPSGLYSHALVNLHEHPGLVDLGSENIRVPIDEATALKSFAKAAFLGHSSAQLRMGAVYEFGKYGCPVVPRYSLFYYSAAAKRGETEADLAVAKWYLNGSDGIPVDEDLAFMHAERASMAGNANAQFLMGYLFDTRGNTEQATYWYNEAAKAGHSEAIERLALLENQIQEPEPENITSSQYPNQDVIKEIPVTASETSPPHAPAVSSTPVTSAPPVSQTKVTKVSVPKKTSKKFLIKHNKCIIS
| null | null |
fungal-type cell wall beta-glucan biosynthetic process [GO:0070880]; mitotic division septum assembly [GO:0140278]
|
1,3-beta-D-glucan synthase complex [GO:0000148]; cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytosol [GO:0005829]; division septum [GO:0000935]; nucleus [GO:0005634]
| null |
PF08238;PF13181;
|
1.25.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15449309}. Note=Localizes to the cell tips and septum during vegetative growth.
| null | null | null | null | null |
FUNCTION: Involved in septum formation. Required for the proper localization of chs2 at the septum. {ECO:0000269|PubMed:15449309}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94623
|
REV1_SCHPO
|
MAFNQRKRRRPVGIADFDEANDEAYESVGFHDYADYFSRKQRKLQNQNAALYKSIDEDSKSDLFHGLAIAINGYTKPSYTELRQMIVSNGGTFIQYVDGKTSISYLVCSFLTPSKARQWKHQKVVKPEWIVDCIKQKKILPWINYRTFQASSAQATLSFVASKPSQPEGNLEDIQTSSQEEEHDNEKDKTKESKAKGFLDDLSGLSASSLHNYQLLKNPNVRNSTTQNQDFLENFFSSSRLHHLSTWKADFKNEIQAMTTASEPVRPIMKDKSKKSRFLLHVDFDCFFASVSTRFSHELRLKPVAVAHGIKNSEIASCNYEARKFGIKNGMYVGTAKNLCPSLRVVDYDFGAYESVSREFYTILVNTLHDYIKVISIDEALLDITSSVSSFQDCFEIAESIRSQVREKTNCEVSVGIGPNVLLARLALRKAKPHNVYSLSIENVFDVLSPLSVQDLPGVGSSQAQKLFNLYGVRTIGQLQRIEKFNLQETFGVNYGLHLYNISRGIDTDIINNETPRRSISVDVNWGVRFVFQEDGIDFLKRLLHELLSRMGKCQVLLHQIQLRILKRADGAPFSPPKYLGAGEVTSFTKSSTFTSATNSFDLIWKKVTSMYKTINVDPGDVRGIGLQALKIIKDNSKIRKDYRSIQSITSRNKVSLKGASVDISSKDKEIISQKKQLSPKLIPSTPYDLPSSSQISSSALAQLPPSMQSDIQQQLRLQKRSITEYPSQLDPLFMVELPTPIRNEVNDNHEIAMNKRLSLKSHADNKIDERGKKKIRQENAFDKLLQISKKSKTINKPNVDYLTLKELPKDLQKQILKESNLQKSDLISEVKLEKPHIVTFQHVQSLEDLRGLLTKWYSKASKGPNIHDVNYFANYVCRVIREEKNLGKAQMMLKWLYQLNRKECNKPWEKAIDKIIETVQGECLQRNIPPLMIF
|
2.7.7.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions. {ECO:0000250};
|
error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; mitochondrial DNA repair [GO:0043504]
|
mitochondrial chromosome [GO:0000262]; mitotic spindle [GO:0072686]; nucleolus [GO:0005730]; nucleus [GO:0005634]; site of double-strand break [GO:0035861]
|
damaged DNA binding [GO:0003684]; deoxycytidyl transferase activity [GO:0017125]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]
|
PF16589;PF00817;PF11799;PF16727;
|
3.30.70.270;3.40.1170.60;6.10.250.1490;1.10.150.20;3.40.50.10190;3.30.1490.100;1.20.58.1280;
|
DNA polymerase type-Y family
| null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}. Mitochondrion {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents. Involved in mitochondrial DNA mutagenesis (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94632
|
EGT1_SCHPO
|
MTEIENIGALEVLFSPESIEQSLKRCQLPSTLLYDEKGLRLFDEITNLKEYYLYESELDILKKFSDSIANQLLSPDLPNTVIELGCGNMRKTKLLLDAFEKKGCDVHFYALDLNEAELQKGLQELRQTTNYQHVKVSGICGCFERLLQCLDRFRSEPNSRISMLYLGASIGNFDRKSAASFLRSFASRLNIHDNLLISFDHRNKAELVQLAYDDPYRITEKFEKNILASVNAVFGENLFDENDWEYKSVYDEDLGVHRAYLQAKNEVTVIKGPMFFQFKPSHLILIEESWKNSDQECRQIIEKGDFKLVSKYESTIADYSTYVITKQFPAMLQLPLQPCPSLAEWDALRKVWLFITNKLLNKDNMYTAWIPLRHPPIFYIGHVPVFNDIYLTKIVKNKATANKKHFWEWFQRGIDPDIEDPSKCHWHSEVPESWPSPDQLREYEKESWEYHIVKLCKAMDELSTSEKRILWLCYEHVAMHVETTLYIYVQSFQNANQTVSICGSLPEPAEKLTKAPLWVNVPETEIAVGMPLTTQYTSVGSNLQSSDLSAHENTDELFYFAWDNEKPMRKKLVSSFSIANRPISNGEYLDFINKKSKTERVYPKQWAEIDGTLYIRTMYGLLPLDDYLGWPVMTSYDDLNNYASSQGCRLPTEDELNCFYDRVLERTDEPYVSTEGKATGFQQLHPLALSDNSSNQIFTGAWEWTSTVLEKHEDFEPEELYPDYTRDFFDGKHNVVLGGSFATATRISNRRSFRNFYQAGYKYAWIGARLVKN
|
1.21.3.10; 2.1.1.44
|
COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:Q7RX33}; Note=Binds 1 Fe(2+) ion per monomer. {ECO:0000250|UniProtKB:Q7RX33};
|
ergothioneine biosynthetic process [GO:0052699]; hercynylcysteine sulfoxide biosynthetic process [GO:1903253]; hercynylselenocysteine biosynthetic process [GO:1903255]; meiotic cell cycle [GO:0051321]; methylation [GO:0032259]; N-alpha,N-alpha,N-alpha-trimethyl-L-histidine biosynthesis from histidine [GO:0052707]; selenoneine biosynthetic process [GO:1903257]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
calcium ion binding [GO:0005509]; dimethylhistidine N-methyltransferase activity [GO:0030745]; hercynylcysteine sulfoxide synthase activity [GO:0061686]; hercynylselenocysteine synthase [GO:0044876]; histidine N-methyltransferase activity [GO:0052706]; monooxygenase activity [GO:0004497]
|
PF03781;PF10017;
|
3.90.1580.10;3.40.50.150;
|
Methyltransferase superfamily, EgtD family; EgtB family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
|
CATALYTIC ACTIVITY: Reaction=L-histidine + 3 S-adenosyl-L-methionine = 3 H(+) + hercynine + 3 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:38471, ChEBI:CHEBI:15378, ChEBI:CHEBI:15781, ChEBI:CHEBI:57595, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.44; Evidence={ECO:0000250|UniProtKB:Q7RX33}; CATALYTIC ACTIVITY: Reaction=hercynine + L-cysteine + O2 = H2O + S-(hercyn-2-yl)-L-cysteine S-oxide; Xref=Rhea:RHEA:42704, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:15781, ChEBI:CHEBI:35235, ChEBI:CHEBI:82706; EC=1.21.3.10; Evidence={ECO:0000250|UniProtKB:Q7RX33};
| null |
PATHWAY: Amino-acid biosynthesis; ergothioneine biosynthesis. {ECO:0000269|PubMed:24828577}.
| null | null |
FUNCTION: Catalyzes the SAM-dependent triple methylation of the alpha-amino group of histidine to form hercynine and subsequent conjugation with cysteine and oxygen to form hercynylcysteine sulfoxide, the first two steps in the biosynthesis pathway of ergothioneine (PubMed:24828577). May play a role in meiosis (PubMed:16303567). {ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:24828577}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94640
|
SIR2_SCHPO
|
MASNPLDNNMPTTPVEEKIPVASYSPSSSGSSSGASLLVDIMCGSKETEDEEVDSDEWDKPETENISDLDERSEMVRYLRASGYAKFLEKYLIEEELPVRSILKKLGINLPSALEEFEDIDLLPLLKEVLKREVARRIKLPHFNTFEDVVNLLKKAKNVVVLVGAGISTSLGILDFRSDNGFYARLARHGLSEPSEMFDIHTFRENPEIFYTFARDLLPETNHYSPSHAFIRLLEKKNKLSTLFTQNIDNLEKKTGLSDNKIIQCHGSFATATCIKCKHKVDGSELYEDIRNQRVSYCNECGKPPLKLRRVGQNKKEKHYFSDGDSESSEDDLAQPGIMKPDITFFGEALPDSFFNKVGSGELEETDLLICIGTSLKVAPVSELISVIPPTTPQIYISRTPVRHTQFDVNFLSPYCDWVIVEICKRAGWLNELQALCDLPECHSGSKTRAFETDLDIKFEEPSTYHITSTTNGSC
|
2.3.1.286
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
|
DNA repair [GO:0006281]; epigenetic regulation of gene expression [GO:0040029]; heterochromatin formation [GO:0031507]; negative regulation of transcription by RNA polymerase II [GO:0000122]
|
chromatin [GO:0000785]; chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; nuclear inner membrane [GO:0005637]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; rDNA heterochromatin [GO:0033553]; Set3 complex [GO:0034967]; subtelomeric heterochromatin [GO:0140720]
|
histone deacetylase activity [GO:0004407]; histone H3K14 deacetylase activity [GO:0031078]; histone H3K4 deacetylase activity [GO:1990162]; histone H3K9 deacetylase activity [GO:0032129]; histone H4K16 deacetylase activity [GO:0034739]; metal ion binding [GO:0046872]; NAD+ binding [GO:0070403]; NAD-dependent histone H3K9 deacetylase activity [GO:0046969]; NAD-dependent histone H4K16 deacetylase activity [GO:0046970]; transcription corepressor activity [GO:0003714]; transferase activity [GO:0016740]
|
PF04574;PF02146;
|
3.30.1600.10;3.40.50.1220;
|
Sirtuin family, Class I subfamily
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15545655}. Chromosome, centromere {ECO:0000269|PubMed:15545655}. Chromosome, telomere {ECO:0000269|PubMed:15545655}. Note=Nuclear throughout the cell cycle. Binds to centromeres, telomeric sites and sites between the silent mating-type loci.
|
CATALYTIC ACTIVITY: Reaction=H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide; Xref=Rhea:RHEA:43636, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969, ChEBI:CHEBI:57540, ChEBI:CHEBI:61930, ChEBI:CHEBI:83767; EC=2.3.1.286; Evidence={ECO:0000255|PROSITE-ProRule:PRU00236};
| null | null | null | null |
FUNCTION: Involved in silencing within the mating-type region, at the telomeres, and according to PubMed:12867036 also within centromeric DNA regions. Required for the localization of swi6 to the telomeres, silent mating type region, and according to PubMed:12867036 to the centromeric DNA regions. According to PubMed:15545655 not required for the localization of swi6 to centromeric foci. Deacetylates histone H3 on 'Lys-9' and 'Lys-16' of histone H4. This has a direct role in heterochromatin assembly. {ECO:0000269|PubMed:12867036, ECO:0000269|PubMed:15545655}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94641
|
HS104_SCHPO
|
MADYPFTDKAAKTLSDAYSIAQSYGHSQLTPIHIAAALLSDSDSNGTTLLRTIVDKAGGDGQKFERSVTSRLVRLPAQDPPPEQVTLSPESAKLLRNAHELQKTQKDSYIAQDHFIAVFTKDDTLKSLLAEAGVTPKAFEFAVNNVRGNKRIDSKNAEEGFDALNKFTVDLTELARNGQLDPVIGREDEIRRTIRVLSRRTKNNPVLIGEPGVGKTSIAEGLARRIIDDDVPANLSNCKLLSLDVGSLVAGSKFRGEFEERIKSVLKEVEESETPIILFVDEMHLLMGAGSGGEGGMDAANLLKPMLARGKLHCIGATTLAEYKKYIEKDAAFERRFQIILVKEPSIEDTISILRGLKEKYEVHHGVTISDRALVTAAHLASRYLTSRRLPDSAIDLVDEAAAAVRVTRESQPEVLDNLERKLRQLRVEIRALEREKDEASKERLKAARKEAEQVEEETRPIREKYELEKSRGSELQDAKRRLDELKAKAEDAERRNDFTLAADLKYYGIPDLQKRIEYLEQQKRKADAEAIANAQPGSEPLLIDVVGPDQINEIVARWTGIPVTRLKTTEKERLLNMEKVLSKQVIGQNEAVTAVANAIRLSRAGLSDPNQPIASFLFCGPSGTGKTLLTKALASFMFDDENAMIRIDMSEYMEKHSVSRLIGAPPGYVGHEAGGQLTEQLRRRPYSVILFDEIEKAAPEVLTVLLQVLDDGRITSGQGQVVDAKNAVIIMTSNLGAEYLTTDNESDDGKIDSTTREMVMNSIRGFFRPEFLNRISSIVIFNRLRRVDIRNIVENRILEVQKRLQSNHRSIKIEVSDEAKDLLGSAGYSPAYGARPLNRVIQNQVLNPMAVLILNGQLRDKETAHVVVQNGKIFVKPNHEANANGSADIDMDGIDDDVNDEELE
| null | null |
cellular heat acclimation [GO:0070370]; cellular response to misfolded protein [GO:0071218]; chaperone cofactor-dependent protein refolding [GO:0051085]; protein refolding [GO:0042026]; protein unfolding [GO:0043335]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleolar peripheral inclusion body [GO:0140602]; nucleus [GO:0005634]; protein aggregate center [GO:0140453]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent protein disaggregase activity [GO:0140545]; misfolded protein binding [GO:0051787]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF00004;PF07724;PF17871;PF02861;PF10431;
|
1.10.8.60;1.10.1780.10;3.40.50.300;
|
ClpA/ClpB family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Required, in concert with Hsp40 and Hsp70 and small Hsps, for the dissociation, resolubilization and refolding of aggregates of damaged proteins after heat or other environmental stresses. Extracts proteins from aggregates by unfolding and threading them in an ATP-dependent process through the axial channel of the protein hexamer, after which they can be refolded by components of the Hsp70/Hsp40 chaperone system (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94649
|
ATG2_SCHPO
|
MRLPSWLKNSSSWLWTAALSRTVQRRLLAFALRKLIGSILLENVQPEDIDILFSKGVLMLSNLQLNCSFLNAVVSLPMINFTKGTLRRLILRLNVTDIVNLNVELEVNGLSLEIELVPPDESLSSTTYEDAPSQLDILDNVVEYMNKTASQDFEDEVINEGLESEIDGSSHNLLDSILQKCLASTSVLMQDALVYIGTANMSTRLEAKLDFMSFSSVKSNSTSRLLNINGITVSMVRPISKSNAGSSSPPRSEESFVSMDSSSSIVEGFENDLSPSQVTLNESSIISSNREEESFYSVHDSVTQKKTRTSWLIFQCSGEFRLVFSIESSNLLVIESHVPSCVLNINSQVIAFLLYLYGYFLPAPSTPGFSSNKPPLTMLQLDIHISSVQILTHCKLPESQDFSMHNDVDELLHTIPSNGAVFEMKINQIQIFNDNNDIDELTMTFSDLDIFMDSVTLVSFGKSLQSPCSLIFKKLERIVSLFIHIPGGEISLPLGKALLLQESFVEFTNDISNLQNFLSNSDPFKRSIQETFEAPKPFEVEMNQPSFEIIALFDELQLQILNELSTQSLYKLTLRVSHLQFTRKSTGSLSSVLIFVKKIGCQSELFNCENSDWTKVSSSTAFHLSNSLFETHDTTGTSNFAVSIQQEKHYYPVFQPAPTEFSYPEKHFYFAVDNFNVFISKEVVRLFKTLYETIASSLVTPVTPNKLVTSDYKNVLKIRTRTFSLSLLNDDGSSFALKCIRIKHYMCWAGAQLISLSLRLYNVSAEYLSESLEILPVVSFIRNLRNDEKYLLNADFSYALKRSSGSNDNTIFVKITDLGYEHYPTCPWISDLLKTYFPQDPEVPFLAFPDFPFNIKLDLRESIIGLNPRTLEAKLLLYLKSLDVEIDALVASNPLNIRIMAAETVVYIIDKLNQSVLEGKTSVLKREILNSSLHFPGLSIKDTIEFVVKSLGYVEISQLKNLTLSLVVNAEEGVFSTLITVDNLDAQVQSCADSTELLIKVLSDLGSTEDEEISDCYLALPIEDYAKSLTEVDYNFFENRGIDYKSNPTEQSTVLVSSDNDISSQEIKIVDDYYISSNEHSTHASDLASVSSEEFVIDDGSSSIIDISDELQDESSSRDSLKKGIELIEDYYLSQSTSKLESSVEGKNYLLKVKFKDINVNWDLHDGYDWEATRATISSAIEKLCDSSSQNDKISPEAKTLLFQSIVIKSFSKVGRLNINHVSEPIDSDEFADYLSKSISYHLRLGKSKSKKIGIEIKDLQGSFTVYADSNEPNAVLNDLDIGLKDLIIYDHLSTSTWNKFFGRDSRSPSSKNRNQHMNAQIVTVRPLPELNNRELRLEFSVLPCKMYIDQDTLDFLIRFLTFQTPSSSETLNTEPDLPFFQSICINATHVTIDFKFKSADKVGLRSGKLPDLGSLIVMQGSEVFLRQLQIYGLSGAEEFLNALLNVWLQDIRNNQLSKVLNGVVPIRTMFTVGRGIKDIFVSPVRGLQGNHSVGSFRHGIIKFTEKYVNDFLSLNAQGATGTHSLLRQAESYLERGSNASASASRARSYYAEQPETIEQGLRQGYSGLKQGLLGAKSTLMGLPRETRSHKSLGGVAQTVGRKVPLIVLQPMIGATEAVSKTLLGLSNSLQPQRRQDMREKYKRPG
| null | null |
autophagosome assembly [GO:0000045]; glycophagy [GO:0061723]; intermembrane phospholipid transfer [GO:0120010]; macroautophagy [GO:0016236]; meiotic cell cycle [GO:0051321]; piecemeal microautophagy of the nucleus [GO:0034727]; reticulophagy [GO:0061709]; sporulation resulting in formation of a cellular spore [GO:0030435]
|
endoplasmic reticulum membrane [GO:0005789]; phagophore [GO:0061908]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]
|
lipid transfer activity [GO:0120013]; phosphatidylinositol-3-phosphate binding [GO:0032266]; protein-membrane adaptor activity [GO:0043495]
|
PF09333;PF13329;PF12624;
| null |
ATG2 family
| null |
SUBCELLULAR LOCATION: Preautophagosomal structure membrane {ECO:0000269|PubMed:23950735}; Peripheral membrane protein {ECO:0000269|PubMed:23950735}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P53855}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53855}. Note=Localizes to the IM-ERES contact site. {ECO:0000250|UniProtKB:P53855}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:30911189}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out); Xref=Rhea:RHEA:38663, ChEBI:CHEBI:57262; Evidence={ECO:0000269|PubMed:30911189}; CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895, ChEBI:CHEBI:64612; Evidence={ECO:0000269|PubMed:30911189};
| null | null | null | null |
FUNCTION: Lipid transfer protein required for autophagosomes completion and peroxisome degradation (PubMed:16303567, PubMed:30911189). Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion (PubMed:30911189). Atg2 binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, using basic residues in its N-terminal region (NR) and to the expanding edge of the IM through its C-terminal region (PubMed:30911189). The latter binding is assisted by an atg18-PtdIns3P interaction (PubMed:30911189). Atg2 then extracts phospholipids from the membrane source using its NR and transfers them to atg9 to the IM through its predicted beta-sheet-rich structure for membrane expansion (PubMed:30911189). Atg2 is also involved in the recruitment of lipids to a restricted region close to the vacuole, termed the vacuole-isolation membrane contact site (VICS), which is also essential for autophagosome formation (By similarity). May have a role in sporulation (PubMed:16303567). {ECO:0000250|UniProtKB:P53855, ECO:0000269|PubMed:16303567, ECO:0000269|PubMed:30911189}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94652
|
GLE1_SCHPO
|
MDTKTTPLIHAKLDEKIISSYNDANGLDIDDLWDIYNEKTRRMIHIISQRYKPKKQSPFPVIADENVRIFPPLHKTIDWAKKRNVEEQNLIEQSITESQRIFSEKQRLEQERFNRELLEKKRIEAERQRLKDEEERRKKELMEKEKKEKERIRLIEEQKHKENEQRRLKQEQIDAKRKEEEAREKRMKETFKDDPEEDSNMAWSIIHKIKTEVVAPISEKKELKNYCFTQKRKITPRLGQITKSNSQIMKITQLLQQTFQEARNTDPLVYKWVLNFFCKSVVKQAEAEVAVNPISAYPLAKVCLLLQTQNADLKDLLFARLQKNCPWVIPFWYDHGTENGKKKMGFKKLSDGHWEQNTTYNERQCGIFAVYAAILSLDDSLAPESWRTFSRLLNLPSPSQLMKSDLELGQTLCSIVSTYLDIAGQSLLRIYGRQAKKLIVCSFSEAYLGANGGGSQYGRLRIVGEDWMKGQGGLKFSFEP
| null | null |
poly(A)+ mRNA export from nucleus [GO:0016973]; protein transport [GO:0015031]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear membrane [GO:0031965]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore cytoplasmic filaments [GO:0044614]; nucleus [GO:0005634]
|
inositol hexakisphosphate binding [GO:0000822]; phospholipid binding [GO:0005543]; translation initiation factor binding [GO:0031369]
|
PF07817;
|
1.25.40.510;
|
GLE1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus, nuclear pore complex {ECO:0000250}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Cytoplasmic side {ECO:0000269|PubMed:16823372}. Nucleus membrane {ECO:0000269|PubMed:16823372}; Peripheral membrane protein {ECO:0000269|PubMed:16823372}; Nucleoplasmic side {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. It is specifically involved in a terminal step of poly(A)+ mRNA transport through the NPC (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94655
|
YPT7_SCHPO
|
MAGKKKHLLKVIILGESGVGKTSIMNQYVNRKFSKDYKATIGADFLTKEVLVDDKVVTLQLWDTAGQERFQSLGVAFYRGADCCVLVYDVNNSKSFETLDSWRDEFLIQASPSNPETFPFILLGNKVDVEEQKRMVSKSKALAFCQARGEIPYFETSAKEAINVQEAFETVAKLALENMDSDDIAADFTDPIHLDMESQKTSCYC
| null | null |
endocytosis [GO:0006897]; endosome to lysosome transport [GO:0008333]; Golgi to vacuole transport [GO:0006896]; intracellular protein transport [GO:0006886]; positive regulation of vacuole fusion, non-autophagic [GO:0061191]; regulation of vacuole fusion, non-autophagic [GO:0032889]; signaling [GO:0023052]; vacuole fusion, non-autophagic [GO:0042144]
|
cytosol [GO:0005829]; fungal-type vacuole membrane [GO:0000329]; late endosome [GO:0005770]; phagocytic vesicle [GO:0045335]; vacuolar membrane [GO:0005774]; vacuole [GO:0005773]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]
|
PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rab family
| null |
SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250|UniProtKB:P32939}.
| null | null | null | null | null |
FUNCTION: Ypt/Rab-type GTPases are key regulators of membrane trafficking and intracellular vesicular transport. They act as molecular switches that convert between GTP-bound and GDP-bound states, and regulate virtually all steps of membrane traffic from the formation of the transport vesicle at the donor membrane to its fusion at the target membrane. In the GDP-bound state, Ypt proteins are predominantly cytosolic, solubilized through the interaction with a GDP dissociation inhibitor (GDI). In the GTP-bound state, the proteins are membrane bound and interact with specific effector proteins that select cargo, promote vesicle movement, or verify the correct site of fusion (By similarity). Ypt7 is necessary for trafficking from the endosome to the vacuole and for homotypic vacuole fusion (PubMed:19453973, PubMed:9443913). Plays an important role in sporulation (PubMed:16357443). {ECO:0000250|UniProtKB:P32939, ECO:0000269|PubMed:16357443, ECO:0000269|PubMed:19453973, ECO:0000269|PubMed:9443913}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94679
|
CND1_SCHPO
|
MSLDLLSRLKKYIHDEENSDLDSIYAECENAGLTAVVNDVIDTLLLGTSSCFDEDCLEKLFAICSHFADLSSSVRNKVYDLLTSNISSESAILEDMISANATDFTVPQTNLETTGIAFQLTVNSLSSSNQLSVIRSSTNTVKGRKKNPTTNSNWNGISHVNALLDAIITLFQKKLSRVWTTSSERDMFLSLFLKPIYTLMESEINIKNASFRSRLFNIIGLAVQFHNHTTAAETNIIQNLQYFEHLSEYAADLVHIVTVQFNSVTLAEGIIRTLCSLEFNDNDVKGPKQVALFLVRLSSLIPNLCLKQLTQLVKLLDSESYTLRCAIIEVLANVVIDQIHDEAQNEMSESVPATVQSLMDLLSERLLDISPYCRTKVLHVFIKIFDLPIKYPRKRQEIAELVIRCLQDRSSHVRRNAIKLFSKLLTTHPFSVMHNGLLTRNIWEKGLSIIEEQLNSLQPKQQEKVVDSELEVDENLLEDATMIQDDESHEGESHLENSLSEYVDSVPAEEIVKVNLTKRFYLEALQYIDIVEAGAKIISQLLFAKNKSEVIESMDFFVFCNSFGISSSKLYIKKMIHLIWVKGTSDEGNNIQNHVLSCYKTLFFEPPPNSGTNEAANYIARNLISLTYDASLAELTSLEQMLCILMKDGYFSHLVITKLWQVYSYQKKDISRTQRRGSIIVIGMLALGNTDVVMQGLDHLIQIGLGPPGLEDLVLARYTCIAIKRIGKDASGSSNINFPNSHTLCQKLCMLLLRPSFSEEWFGLEEQAIEAIYAVAKHPDELCTNIILLLTKQLFKPSNHENTTSNDDHAMDEDLDDSPEEETLKDEEEIGIRLAHLIFLVGHVAIKQLVYIEYCEAEFKRRKADAERLAVQNSNNPINGQETSEYDLITGTSEDDFSEAMTFIRERELLYGENSLLSRFAPLVVELCSNHKSHNNQSLLLAASLTLSKFMCLSNNFCMEHLPLLITILEKCDNPIIRNNLVIGLADLTVCFNHFIDEISEYLYRRLMDEESSVKKTCFMTLAFLILAGQIKVKGQLGIMARSLEDEDARISDLARMFFTDFAAKDNSVYNNFIDIFSVLSRSAEEQDEDDAKFKRIIRFLTSFIEKERHTKQLAERLAARLDRCKTQRQWDHVVYALSLLPHKADNIQKLIDDGYHE
| null | null |
cell division [GO:0051301]; meiotic chromosome condensation [GO:0010032]; mitotic chromosome condensation [GO:0007076]
|
condensed chromosome, centromeric region [GO:0000779]; condensin complex [GO:0000796]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; kinetochore [GO:0000776]; nucleolar peripheral inclusion body [GO:0140602]; nucleolus [GO:0005730]; nucleus [GO:0005634]
|
double-stranded DNA binding [GO:0003690]; histone binding [GO:0042393]
|
PF12717;PF12922;
|
1.25.10.10;
|
CND1 (condensin subunit 1) family
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromosome foci in interphase cells. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. Dissociation from chromosomes is observed in late telophase.
| null | null | null | null | null |
FUNCTION: Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94680
|
PDAT_SCHPO
|
MASSKKSKTHKKKKEVKSPIDLPNSKKPTRALSEQPSASETQSVSNKSRKSKFGKRLNFILGAILGICGAFFFAVGDDNAVFDPATLDKFGNMLGSSDLFDDIKGYLSYNVFKDAPFTTDKPSQSPSGNEVQVGLDMYNEGYRSDHPVIMVPGVISSGLESWSFNNCSIPYFRKRLWGSWSMLKAMFLDKQCWLEHLMLDKKTGLDPKGIKLRAAQGFEAADFFITGYWIWSKVIENLAAIGYEPNNMLSASYDWRLSYANLEERDKYFSKLKMFIEYSNIVHKKKVVLISHSMGSQVTYYFFKWVEAEGYGNGGPTWVNDHIEAFINISGSLIGAPKTVAALLSGEMKDTAQLNQFSVYGLEKFFSRSERAMMVRTMGGVSSMLPKGGDVVWGNASWAPDDLNQTNFSNGAIIRYREDIDKDHDEFDIDDALQFLKNVTDDDFKVMLAKNYSHGLAWTEKEVLKNNEMPSKWINPLETSLPYAPDMKIYCVHGVGKPTERGYYYTNNPEGQPVIDSSVNDGTKVENGIVMDDGDGTLPILALGLVCNKVWQTKRFNPANTSITNYEIKHEPAAFDLRGGPRSAEHVDILGHSELNEIILKVSSGHGDSVPNRYISDIQEIINEINLDKPRN
|
2.3.1.158
| null |
diacylglycerol metabolic process [GO:0046339]; lipid droplet formation [GO:0140042]; lipid storage [GO:0019915]; triglyceride biosynthetic process [GO:0019432]
|
cortical endoplasmic reticulum [GO:0032541]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular space [GO:0005615]; perinuclear endoplasmic reticulum [GO:0097038]
|
O-acyltransferase activity [GO:0008374]; phospholipid:diacylglycerol acyltransferase activity [GO:0046027]; triglyceride lipase activity [GO:0004806]
|
PF02450;
|
3.40.50.1820;
|
AB hydrolase superfamily, Lipase family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000255}.
|
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + a glycerophospholipid = a monoacylglycerophospholipid + a triacyl-sn-glycerol; Xref=Rhea:RHEA:14057, ChEBI:CHEBI:17815, ChEBI:CHEBI:64615, ChEBI:CHEBI:136912, ChEBI:CHEBI:136913; EC=2.3.1.158; Evidence={ECO:0000269|PubMed:12963726};
| null |
PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. {ECO:0000305|PubMed:12963726}.
| null | null |
FUNCTION: Catalyzes triacylglycerol (TAG) formation by an acyl-CoA independent pathway. The enzyme specifically transfers acyl groups from the sn-2 position of a phospholipid to diacylglycerol (DAG), thus forming an sn-1-lysophospholipid. Plays a major role in triacylglycerol formation at log phase (PubMed:12963726, PubMed:26990381). Involved in lipid particle synthesis from the endoplasmic reticulum, promoting localized TAG production at discrete ER subdomains (PubMed:26990381, PubMed:28011631). {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:26990381, ECO:0000269|PubMed:28011631}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94684
|
TFB3_SCHPO
|
MDDEGARKVDEKCPLCQADRYLNPNMKLLINPECYHKMCESCVDRIFTTGPAQCPTPGCNKILRKAKFREQTFEDAQIEREVDVRKRISRIFNKGQQEFDSLQAYNDYLEEVEILTFNLIYKIDVEETEEKVKQYEKQNRDSIAANSARAAAEARILAQNEILLKRQKQEAREAAIREHQKEKERREQVEQQIIFDLATSGKDPNKIIQLSDSLKKQQENIASSVSNISRSSSILLSDVQQVAEDTTPFSPLAGEKDGSKYFSYSKNTYQDLYLEKVSHEPGRKCGFRIEDCHLRCLYEAFSGIDYDLESLKKLEVAS
| null | null |
DNA repair [GO:0006281]; nucleotide-excision repair [GO:0006289]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation at RNA polymerase II promoter [GO:0006367]
|
cytosol [GO:0005829]; nucleotide-excision repair factor 3 complex [GO:0000112]; nucleus [GO:0005634]; transcription factor TFIIH holo complex [GO:0005675]; transcription factor TFIIK complex [GO:0070985]
|
cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]; RNA polymerase II general transcription initiation factor activity [GO:0016251]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
|
PF06391;PF17121;
|
3.30.40.10;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Acts as a component of the general transcription and DNA repair factor IIH (TFIIH or factor B), which is essential for both basal and activated transcription, and is involved in nucleotide excision repair (NER) of damaged DNA. TFIIH has CTD kinase activity and DNA-dependent ATPase activity, and is essential for polymerase II transcription (By similarity). {ECO:0000250}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94687
|
TAS3_SCHPO
|
MEKGIKKYLPSLPFLACISDFPENHGTSRRSATVSLERVHELFTEHWLSNLKNRREKRQELAEEAVYCRSEMLSQRKLLAAVDFPQQLKNSPAKAKATHTSSGVTKEVRASKKYTSSNVEFPLVTDGKEKPVKSKQLRKNSVTEFEKPIETKKSKHRKSRNKFLDKSSGSMEIESWDNSTSDSIIESSSRLHESISLRENDIRSSDSKSVGWDDNSTGFRESSKSLDHTDTSMFMELDSNSDPQFRPKYQAKSSWFAPDDPEASWGNLDDGWGETNGSWSSTDDTKHYKNEWAESINLDNFNRPSQQEDYDKPKNTQVSRSSNHHRRYDSYHPDSRSDSYRSKREHYDNRDTGPRSKHLEKSSYVYNQNFEDRTHLSDHGAHFHLGNANDFNMQGSSRKRKASDRQRESRENELPTKKLNASDSHNPLASLTTDKNDLYINWLKSLSFFQTNSSCAEALVKVIPHYHNKLIDFSQVLQLVFSASEKFPIQENQPLPEQLMFLSNLEKQTPFAKAVGSSIYKLVTGKNLSLDFASQILKEASILEHKNEK
| null | null |
chromosome segregation [GO:0007059]; heterochromatin formation [GO:0031507]; pericentric heterochromatin formation [GO:0031508]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; silent mating-type cassette heterochromatin formation [GO:0030466]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]
|
chromosome, subtelomeric region [GO:0099115]; cytoplasm [GO:0005737]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; RITS complex [GO:0030958]; spindle pole body [GO:0005816]
|
molecular adaptor activity [GO:0060090]
|
PF21487;
|
1.20.920.40;6.10.140.1690;
| null | null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
| null | null | null | null | null |
FUNCTION: Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin formation and accurate chromosome segregation. A member of the RNA-induced transcriptional silencing (RITS) complex which is involved in the biosynthesis of dsRNA from primer siRNAs provided by the RNA-directed RNA polymerase (RDRC) complex. {ECO:0000269|PubMed:14704433, ECO:0000269|PubMed:15607976}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94701
|
INN1_SCHPO
|
MSKNPLGTLVVRIWKAKNLPNKALVGKQSPYCVCRVGEVVKRTQTDKRSGQEPSWNAVLEFNIPSESYHIMKITVFHEGFRKHPHLIGDTVLSFEKAMKEELQSEWYELKNEFQFAGELSVQFKFIPTDPLYFDRASSKPVLQFPYSSVAALTPVPKKPSKPSKPRKKVPVSHPLPPTPPSREEHVSVPRESSLFTYEDDPLPSFPSPYMVDDYYTQDVFVSDNVNDYSYGVQNPTNPRLSVEDYDANHSSLPPVPPPHLILPTASSSQIFH
| null | null |
actin cortical patch localization [GO:0051666]; establishment or maintenance of bipolar cell polarity [GO:0061245]; mitotic actomyosin contractile ring assembly [GO:1903475]; mitotic cytokinesis [GO:0000281]
|
cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cell tip [GO:0051286]; mitotic actomyosin contractile ring [GO:0110085]; mitotic actomyosin contractile ring, intermediate layer [GO:0120105]; nucleus [GO:0005634]
|
cytoskeletal protein-membrane anchor activity [GO:0106006]; phospholipid binding [GO:0005543]
|
PF00168;
|
2.60.40.150;
|
INN1/fic1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum and the cell tip. {ECO:0000269|PubMed:19139265}.
| null | null | null | null | null |
FUNCTION: Involved in the ingression of the plasma membrane during cytokinesis, leading to the separation of the daughter cells. Unlike its S.cerevisiae ortholog INN1, it does not play an essential role, probably because the actinomyosin ring is connected to the cell cortex by many more proteins. {ECO:0000269|PubMed:19139265}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94720
|
FIL1_SCHPO
|
MNYNDTTEFCFPFGQPSFPTSAMTEGSFDGQFSEFDPTFTSPADTALSDIANLPIDLHKDALFANAPGKGDVDFDSVSMLQLLSDYPLAFNSTENNQKLQTNPSARWSLLDSMDFDNQRQCSDLESAQLGDSGLLKSTILSNSHIDIAALSSSKTSEPTPPFSYVQTPCIPTPSSALIDTPFPGALDSEFGFDESQAPLFPASDGDCQRAFASISYPTNYGCKLSNLGFMSPQSPVKRELNDSTSPSKLSESSSSLTGSSSALLSQSEFLGSVPSLSDSIATVDPFFSFESFETDEKARSLLMDASLKLPQFSTPNLSSNSSSLSLKSTLAEGMKGSTPLAAVKTEKASKAARVMKQKKHREHVCFNCGVTETPLWRRTSDKLNFLCNACGLYNKQYGVMRPLSPRNKGSSKALENLVCANCSSTKTSLWRKDRHGQTVCNACGLYARLHGHNRPIGLKKNKITRRRRGKGPGGEDGMSDEVKSEFPVLSKSVTMAEILSSKGLESPQLTNSVSVSKMPNTDADVSLEHAKISFDSLDNSVIVKKEEEIENKFSVSC
| null | null |
negative regulation of TORC1 signaling [GO:1904262]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of autophagy [GO:0010508]; positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cytosol [GO:0005829]; nucleus [GO:0005634]
|
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]; zinc ion binding [GO:0008270]
|
PF00320;
|
3.30.50.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000305|PubMed:29432178}. Cytoplasm {ECO:0000269|PubMed:16823372}.
| null | null | null | null | null |
FUNCTION: Activates genes required for amino acid biosynthesis and acts as a master transcriptional regulator during amino acid starvation (PubMed:29432178). Binds variations of the DNA sequence 5'-GAT[AC]GC-3' (PubMed:29432178). {ECO:0000269|PubMed:29432178}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94737
|
MAPK1_PNECA
|
MDSKHSVFNVMGQEFVLQKGYEVIKGLGKGSYGVVCSAKNIEVEDNNKVAIKKITNIFSKKMLAKRALREIMLLQHFRNHKNITTLYDMDIVDPSKFNELYLYEELMQANLNSIIRSDQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPSNLLINADCKLKICDFGLSRGISVNQGQGTEYMTEYVTTRWYRAPEVMLSFQSYSKAIDLWSVGCILAELLGRKPFFKGSNYVDQLNQIFCILGTPNENIISKIKSASAQSYIRSLPTLPKMPYSKIFPYANPDALDLLNCLLTFDPYDRISCEEALEHPYLIIWHDPNKEPVCSEQFDFGFEAIDSIEEIRQMIINEVSRFKGLTGNQKLYHSISNT
|
2.7.11.24
| null |
cellular component organization [GO:0016043]; MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; positive regulation of growth rate [GO:0040010]; response to oxidative stress [GO:0006979]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP-dependent protein binding [GO:0043008]; MAP kinase activity [GO:0004707]; protein serine kinase activity [GO:0106310]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, MAP kinase subfamily
|
PTM: Dually phosphorylated on Thr-186 and Tyr-188, which activates the enzyme.
| 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=2.7.11.24; Evidence={ECO:0000269|PubMed:10564487}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.24; Evidence={ECO:0000269|PubMed:10564487};
| null | null | null | null |
FUNCTION: Serine-threonine protein kinase which may be involved in maintenance of cell integrity. Functionally complements SLT2 null mutant in S.cerevisiae. {ECO:0000269|PubMed:10564487}.
|
Pneumocystis carinii
|
O94740
|
CDC37_SCHPO
|
MAIDYSKWDKLELSDDSDIEVHPNVDKKSFIRWRQRDIHEKRAVRKQKMEDIKGAMAMNRRLLSRISEMETVLEKESPSDPYVLLGSFLEAKKSEDMDSAIPGGMSYHHMLMSLLKVIKDAEDTTEEKSMDDSDKCLRRLKSHKERLLKLLEDAQKEYDTLEAESKNYITSEDLHLGFDSTYVQKKEPEKPKKTKTKKETIQVIESLNNPTPPTDFPGAKEQASTGNAPKNPVNENESEDEEGLSLSEDGKKFANIDFGDYSSSEEFLKEHLNILADEEESDAILLEAFNAELEGKPSLAKQYVHQALLISYCRQLGPNGLSIFFQKIKDPNHQSQRLFLEDVHNTYVRIHERSAAISKEQAESGEGVEQIQLCAVDPNTKLSITIPEAGSTDPETQKARAAFESFPPNLQKALMTNDLDKINVVLGKMAVENAEEVVEKLSSTGMLSIEEGIIDTTKGETIPQLS
| null | null |
cell cycle [GO:0007049]; cell division [GO:0051301]; protein folding [GO:0006457]; protein stabilization [GO:0050821]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
|
heat shock protein binding [GO:0031072]; protein kinase binding [GO:0019901]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
|
PF08564;PF08565;PF03234;
|
1.20.58.610;
|
CDC37 family
| null |
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Note=When in the nucleus associated with chromatin.
| null | null | null | null | null |
FUNCTION: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. {ECO:0000269|PubMed:12861001, ECO:0000269|PubMed:14652737}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94742
|
SEM1_YEAST
|
MSTDVAAAQAQSKIDLTKKKNEEINKKSLEEDDEFEDFPIDTWANGETIKSNAVTQTNIWEENWDDVEVDDDFTNELKAELDRYKRENQ
| null | null |
double-strand break repair via homologous recombination [GO:0000724]; filamentous growth [GO:0030447]; maintenance of DNA trinucleotide repeats [GO:0035753]; mRNA export from nucleus [GO:0006406]; positive regulation of transcription by RNA polymerase II [GO:0045944]; proteasome assembly [GO:0043248]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; regulation of cell cycle [GO:0051726]; SAGA complex localization to transcription regulatory region [GO:0072742]; ubiquitin-dependent protein catabolic process [GO:0006511]
|
cytosol [GO:0005829]; proteasome complex [GO:0000502]; proteasome regulatory particle, lid subcomplex [GO:0008541]; proteasome storage granule [GO:0034515]; transcription export complex 2 [GO:0070390]
|
molecular adaptor activity [GO:0060090]; protein folding chaperone [GO:0044183]
|
PF05160;
|
6.10.250.1210;
|
DSS1/SEM1 family
| null | null | null | null | null | null | null |
FUNCTION: Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation. {ECO:0000269|PubMed:15117943, ECO:0000269|PubMed:19289793}.
|
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
|
O94751
|
BUB1_SCHPO
|
MSDWRLTENVLDQNIPETKPRESKTRLEEIQRLALFQEELDIIEELDDPVDVWYRCIEWLLETRFLGMETVNKMLDDAIQYLERCRFALNDVRHLLIQLAKIKQSYETPDELQQAAKQFYQLASKGIGLELALFYEEYGSLLIRMQRWKEASEVFHAAVSREARPLVRLLRNAAEFSRAYDLHNAHPSIHDAPYSSPFPPPRIVLGSKPVSSSTLPSKPKSFQVFSDASSSRDSQNASDLPQAKSLESEANTPNLPLLYDKSSGKRVEYSAFNFLALYENGEERSMEECRAQRYLSSIQPNTAASFPKVVPKNEISVHHDSSSSNVSPIYKNPVAEQSDTPTRSLPKNYAYVAKSTSPELKVFDTVMPVALSPKPAQKPPSPTIHTKAALADILDIFNQPLRSESLEKSSKSPISAQSSYLGTPLKNDENSSNSGATSLTGRSQEEHLDFIPSLTPSKNYPSKIYSPNKNLDFSHTASKAETYKNSNELENVKREQPFSELLPSTLQEETATGTTSTTFANAKRRPEDSNISPTNPKKLHTLPRSPQYSTVDSNSVLSPAMPKGYMFVNENQSMKHESSVSNPVATIPHENGKHDFGQLSPIEHKPFFPKNDDELPGPSGYLTMPYEEAMASLSNLPTLINPLDQSLRDLLFQVLRPSLLRDKDYHEHETSFALVEHIESFVSKIKPKAGGPGRRRSSNRHSLDGPEFHLFYPPNTNLSVISKLGQGAFAPVYLVKSKIETENGDVSQGGAENNESKLFALKIETPPSCFEFYLTRQAMTRLKGLRETNSILPVHQLHMFHDTSHLLMDYRPQGSILDLVNSMHNSTFSSSGMDEILVVFFSIEFLRIIEALHTHKIIHGDLKADNALLRLETVADSEWSPIYSPEGLYGWSFKGIYLIDFGRGIDLSLFEEKVKFIADWDTDLQDCIEMREGRPWTYQIDYHGLAAIIYTMLFGQYIETRIEVINGQRRQVLTQRMKRYWNQDLWHRLFDLLLNPTLHVSEENLPMTEELSKIRIEMEEWLVNHSTGGSGLKGLLKSIEKRKI
|
2.7.11.1
| null |
attachment of mitotic spindle microtubules to kinetochore [GO:0051315]; cell division [GO:0051301]; homologous chromosome segregation [GO:0045143]; meiosis I spindle assembly checkpoint signaling [GO:1905318]; meiotic centromeric cohesion protection in anaphase I [GO:1990813]; meiotic sister chromatid cohesion, centromeric [GO:0051754]; meiotic spindle assembly checkpoint signaling [GO:0033316]; mitotic sister chromatid biorientation [GO:1990758]; mitotic spindle assembly checkpoint signaling [GO:0007094]; phosphorylation [GO:0016310]; regulation of homologous chromosome segregation [GO:0060629]
|
bub1-bub3 complex [GO:1990298]; chromosome, centromeric core domain [GO:0034506]; chromosome, centromeric region [GO:0000775]; inner kinetochore [GO:0000939]; kinetochore [GO:0000776]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; old mitotic spindle pole body [GO:0071957]; outer kinetochore [GO:0000940]
|
ATP binding [GO:0005524]; histone H2AS121 kinase activity [GO:0072371]; identical protein binding [GO:0042802]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]
|
PF08311;PF00069;
|
1.25.40.430;1.10.510.10;
|
Protein kinase superfamily, Ser/Thr protein kinase family, BUB1 subfamily
|
PTM: Autophosphorylated. {ECO:0000250}.
|
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Chromosome, centromere. Note=Associates with kinetochores and centromeres during the early stages of mitosis.
|
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=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Involved in cell cycle checkpoint enforcement. Acts to stabilize the spindle during mitosis. Required for the correct localization of bub3 and mad3 to the kinetochore. Appears to have a role in chromosome segregation. Catalyzes the phosphorylation of bub3. {ECO:0000269|PubMed:15509783, ECO:0000269|PubMed:15525673, ECO:0000269|PubMed:9864354}.
|
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
|
O94753
|
VPL2_PLEER
|
MSFKTLSALALALGAAVQFASAAVPLVQKRATCDDGRTTANAACCILFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMGDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVGAAHLPAGFSLSDVEQACAATPFPALTADPGPVTSVPPVPGS
|
1.11.1.16
|
COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:12884090}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:12884090}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:12884090}; Note=Binds 2 calcium ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:12884090};
|
cellular response to oxidative stress [GO:0034599]; hydrogen peroxide catabolic process [GO:0042744]; lignin catabolic process [GO:0046274]; response to reactive oxygen species [GO:0000302]
|
extracellular region [GO:0005576]
|
heme binding [GO:0020037]; manganese peroxidase activity [GO:0016689]; metal ion binding [GO:0046872]; reactive-black-5:hydrogen-peroxide oxidoreductase activity [GO:0052750]
|
PF00141;PF11895;
|
1.10.520.10;1.10.420.10;
|
Peroxidase family, Ligninase subfamily
| null |
SUBCELLULAR LOCATION: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297, ECO:0000269|PubMed:9987124}.
|
CATALYTIC ACTIVITY: Reaction=1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol + H2O2 = glycolaldehyde + guaiacol + H2O + vanillin; Xref=Rhea:RHEA:22396, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17071, ChEBI:CHEBI:18346, ChEBI:CHEBI:28591, ChEBI:CHEBI:53650; EC=1.11.1.16; Evidence={ECO:0000269|PubMed:12884090, ECO:0000269|PubMed:16246366, ECO:0000269|PubMed:9987124}; CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 Mn(2+) = 2 H2O + 2 Mn(3+); Xref=Rhea:RHEA:22776, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:29035, ChEBI:CHEBI:29041; EC=1.11.1.16; Evidence={ECO:0000269|PubMed:12884090, ECO:0000269|PubMed:16246366, ECO:0000269|PubMed:9987124};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=19 uM for manganese {ECO:0000269|PubMed:12884090}; KM=3000 uM for veratryl alcohol {ECO:0000269|PubMed:12884090}; KM=4 uM for reactive black 5 {ECO:0000269|PubMed:12884090}; KM=3 uM for 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonate) (ABTS) {ECO:0000269|PubMed:12884090};
| null | null | null |
FUNCTION: A versatile ligninolytic peroxidase that combines the substrate specificity characteristics of the two other ligninolytic peroxidases, manganese peroxidase and lignin peroxidase. {ECO:0000269|PubMed:9987124}.
|
Pleurotus eryngii (Boletus of the steppes)
|
O94759
|
TRPM2_HUMAN
|
MEPSALRKAGSEQEEGFEGLPRRVTDLGMVSNLRRSNSSLFKSWRLQCPFGNNDKQESLSSWIPENIKKKECVYFVESSKLSDAGKVVCQCGYTHEQHLEEATKPHTFQGTQWDPKKHVQEMPTDAFGDIVFTGLSQKVKKYVRVSQDTPSSVIYHLMTQHWGLDVPNLLISVTGGAKNFNMKPRLKSIFRRGLVKVAQTTGAWIITGGSHTGVMKQVGEAVRDFSLSSSYKEGELITIGVATWGTVHRREGLIHPTGSFPAEYILDEDGQGNLTCLDSNHSHFILVDDGTHGQYGVEIPLRTRLEKFISEQTKERGGVAIKIPIVCVVLEGGPGTLHTIDNATTNGTPCVVVEGSGRVADVIAQVANLPVSDITISLIQQKLSVFFQEMFETFTESRIVEWTKKIQDIVRRRQLLTVFREGKDGQQDVDVAILQALLKASRSQDHFGHENWDHQLKLAVAWNRVDIARSEIFMDEWQWKPSDLHPTMTAALISNKPEFVKLFLENGVQLKEFVTWDTLLYLYENLDPSCLFHSKLQKVLVEDPERPACAPAAPRLQMHHVAQVLRELLGDFTQPLYPRPRHNDRLRLLLPVPHVKLNVQGVSLRSLYKRSSGHVTFTMDPIRDLLIWAIVQNRRELAGIIWAQSQDCIAAALACSKILKELSKEEEDTDSSEEMLALAEEYEHRAIGVFTECYRKDEERAQKLLTRVSEAWGKTTCLQLALEAKDMKFVSHGGIQAFLTKVWWGQLSVDNGLWRVTLCMLAFPLLLTGLISFREKRLQDVGTPAARARAFFTAPVVVFHLNILSYFAFLCLFAYVLMVDFQPVPSWCECAIYLWLFSLVCEEMRQLFYDPDECGLMKKAALYFSDFWNKLDVGAILLFVAGLTCRLIPATLYPGRVILSLDFILFCLRLMHIFTISKTLGPKIIIVKRMMKDVFFFLFLLAVWVVSFGVAKQAILIHNERRVDWLFRGAVYHSYLTIFGQIPGYIDGVNFNPEHCSPNGTDPYKPKCPESDATQQRPAFPEWLTVLLLCLYLLFTNILLLNLLIAMFNYTFQQVQEHTDQIWKFQRHDLIEEYHGRPAAPPPFILLSHLQLFIKRVVLKTPAKRHKQLKNKLEKNEEAALLSWEIYLKENYLQNRQFQQKQRPEQKIEDISNKVDAMVDLLDLDPLKRSGSMEQRLASLEEQVAQTAQALHWIVRTLRASGFSSEADVPTLASQKAAEEPDAEPGGRKKTEEPGDSYHVNARHLLYPNCPVTRFPVPNEKVPWETEFLIYDPPFYTAERKDAAAMDPMGDTLEPLSTIQYNVVDGLRDRRSFHGPYTVQAGLPLNPMGRTGLRGRGSLSCFGPNHTLYPMVTRWRRNEDGAICRKSIKKMLEVLVVKLPLSEHWALPGGSREPGEMLPRKLKRILRQEHWPSFENLLKCGMEVYKGYMDDPRNTDNAWIETVAVSVHFQDQNDVELNRLNSNLHACDSGASIRWQVVDRRIPLYANHKTLLQKAAAEFGAHY
| null | null |
calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane import into cytosol [GO:0097553]; calcium ion transmembrane transport [GO:0070588]; calcium ion transport [GO:0006816]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cellular response to calcium ion [GO:0071277]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to purine-containing compound [GO:0071415]; cellular response to temperature stimulus [GO:0071502]; dendritic cell chemotaxis [GO:0002407]; dendritic cell differentiation [GO:0097028]; protein homotetramerization [GO:0051289]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of filopodium assembly [GO:0051489]; release of sequestered calcium ion into cytosol [GO:0051209]; response to heat [GO:0009408]; response to hydroperoxide [GO:0033194]; response to purine-containing compound [GO:0014074]; temperature homeostasis [GO:0001659]; zinc ion transmembrane transport [GO:0071577]
|
cell projection [GO:0042995]; cytoplasmic vesicle membrane [GO:0030659]; ficolin-1-rich granule membrane [GO:0101003]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]; tertiary granule membrane [GO:0070821]
|
calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; intracellularly gated calcium channel activity [GO:0015278]; ligand-gated calcium channel activity [GO:0099604]; manganese ion transmembrane transporter activity [GO:0005384]; mono-ADP-D-ribose binding [GO:0072571]; monoatomic cation channel activity [GO:0005261]; sodium channel activity [GO:0005272]
|
PF00520;PF18139;
|
3.40.50.450;3.90.79.10;
|
Transient receptor (TC 1.A.4) family, LTrpC subfamily, TRPM2 sub-subfamily
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11385575, ECO:0000269|PubMed:11509734, ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:12594222, ECO:0000269|PubMed:15561722, ECO:0000269|PubMed:16601673, ECO:0000269|PubMed:19171771, ECO:0000269|PubMed:20650899, ECO:0000269|PubMed:20660597, ECO:0000269|PubMed:22493272, ECO:0000269|PubMed:25918360, ECO:0000269|PubMed:27068538, ECO:0000269|PubMed:27383051, ECO:0000269|PubMed:30467180}; Multi-pass membrane protein {ECO:0000269|PubMed:30467180}. Perikaryon {ECO:0000250|UniProtKB:E9PTA2}. Cell projection {ECO:0000250|UniProtKB:E9PTA2}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:E9PTA2}. Lysosome {ECO:0000269|PubMed:27068538}. Note=Detected at the cell membrane and in intracellular vesicles in cortical neurons. Detected on neuronal cell bodies and neurites (By similarity). Detected on the cell membrane in polymorphonuclear neutrophils. Detected on cytoplasmic vesicles and lysosomes in immature bone marrow dendritic cells (By similarity). {ECO:0000250|UniProtKB:E9PTA2, ECO:0000250|UniProtKB:Q91YD4}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:11960981, ECO:0000269|PubMed:12594222}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:11960981}; Multi-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:12594222}; Multi-pass membrane protein {ECO:0000255}.
| null | null | null | null | null |
FUNCTION: [Isoform 1]: Nonselective, voltage-independent cation channel that mediates Na(+) and Ca(2+) influx, leading to increased cytoplasmic Ca(2+) levels (PubMed:11385575, PubMed:11509734, PubMed:11804595, PubMed:11960981, PubMed:12594222, PubMed:15561722, PubMed:16601673, PubMed:19171771, PubMed:20660597, PubMed:25620041, PubMed:27068538, PubMed:27383051, PubMed:28775320, PubMed:29745897, PubMed:30467180). Functions as a ligand-gated ion channel (PubMed:19171771, PubMed:25620041, PubMed:28775320, PubMed:30467180). Binding of ADP-ribose to the cytoplasmic Nudix domain causes a conformation change; the channel is primed but still requires Ca(2+) binding to trigger channel opening (PubMed:19171771, PubMed:25620041, PubMed:28775320, PubMed:29745897, PubMed:30467180). Extracellular calcium passes through the channel and increases channel activity (PubMed:19171771). Contributes to Ca(2+) release from intracellular stores in response to ADP-ribose (PubMed:19454650). Plays a role in numerous processes that involve signaling via intracellular Ca(2+) levels (Probable). Besides, mediates the release of lysosomal Zn(2+) stores in response to reactive oxygen species, leading to increased cytosolic Zn(2+) levels (PubMed:25562606, PubMed:27068538). Activated by moderate heat (35 to 40 degrees Celsius) (PubMed:16601673). Activated by intracellular ADP-ribose, beta-NAD (NAD(+)) and similar compounds, and by oxidative stress caused by reactive oxygen or nitrogen species (PubMed:11385575, PubMed:11509734, PubMed:11804595, PubMed:11960981, PubMed:15561722, PubMed:16601673, PubMed:19171771, PubMed:25620041, PubMed:27068538, PubMed:27383051, PubMed:30467180). The precise physiological activators are under debate; the true, physiological activators may be ADP-ribose and ADP-ribose-2'-phosphate (PubMed:20650899, PubMed:25918360). Activation by ADP-ribose and beta-NAD is strongly increased by moderate heat (35 to 40 degrees Celsius) (PubMed:16601673). Likewise, reactive oxygen species lower the threshold for activation by moderate heat (37 degrees Celsius) (PubMed:22493272). Plays a role in mediating behavorial and physiological responses to moderate heat and thereby contributes to body temperature homeostasis. Plays a role in insulin secretion, a process that requires increased cytoplasmic Ca(2+) levels (By similarity). Required for normal IFNG and cytokine secretion and normal innate immune immunity in response to bacterial infection. Required for normal phagocytosis and cytokine release by macrophages exposed to zymosan (in vitro). Plays a role in dendritic cell differentiation and maturation, and in dendritic cell chemotaxis via its role in regulating cytoplasmic Ca(2+) levels (By similarity). Plays a role in the regulation of the reorganization of the actin cytoskeleton and filopodia formation in response to reactive oxygen species via its role in increasing cytoplasmic Ca(2+) and Zn(2+) levels (PubMed:27068538). Confers susceptibility to cell death following oxidative stress (PubMed:12594222, PubMed:25562606). {ECO:0000250|UniProtKB:Q91YD4, ECO:0000269|PubMed:11385575, ECO:0000269|PubMed:11509734, ECO:0000269|PubMed:11804595, ECO:0000269|PubMed:11960981, ECO:0000269|PubMed:12594222, ECO:0000269|PubMed:15561722, ECO:0000269|PubMed:16601673, ECO:0000269|PubMed:19171771, ECO:0000269|PubMed:19454650, ECO:0000269|PubMed:20650899, ECO:0000269|PubMed:20660597, ECO:0000269|PubMed:22493272, ECO:0000269|PubMed:25562606, ECO:0000269|PubMed:25620041, ECO:0000269|PubMed:25918360, ECO:0000269|PubMed:27068538, ECO:0000269|PubMed:27383051, ECO:0000269|PubMed:28775320, ECO:0000269|PubMed:29745897, ECO:0000269|PubMed:30467180, ECO:0000305}.; FUNCTION: [Isoform 2]: Lacks cation channel activity. Does not mediate cation transport in response to oxidative stress or ADP-ribose. {ECO:0000269|PubMed:11960981}.; FUNCTION: [Isoform 3]: Lacks cation channel activity and negatively regulates the channel activity of isoform 1. Negatively regulates susceptibility to cell death in reposponse to oxidative stress. {ECO:0000269|PubMed:12594222}.
|
Homo sapiens (Human)
|
O94760
|
DDAH1_HUMAN
|
MAGLGHPAAFGRATHAVVRALPESLGQHALRSAKGEEVDVARAERQHQLYVGVLGSKLGLQVVELPADESLPDCVFVEDVAVVCEETALITRPGAPSRRKEVDMMKEALEKLQLNIVEMKDENATLDGGDVLFTGREFFVGLSKRTNQRGAEILADTFKDYAVSTVPVADGLHLKSFCSMAGPNLIAIGSSESAQKALKIMQQMSDHRYDKLTVPDDIAANCIYLNIPNKGHVLLHRTPEEYPESAKVYEKLKDHMLIPVSMSELEKVDGLLTCCSVLINKKVDS
|
3.5.3.18
| null |
arginine catabolic process [GO:0006527]; arginine metabolic process [GO:0006525]; citrulline metabolic process [GO:0000052]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cellular response to hypoxia [GO:1900038]; negative regulation of vascular permeability [GO:0043116]; nitric oxide mediated signal transduction [GO:0007263]; nitric oxide metabolic process [GO:0046209]; positive regulation of angiogenesis [GO:0045766]; positive regulation of nitric oxide biosynthetic process [GO:0045429]; regulation of systemic arterial blood pressure [GO:0003073]
|
cytosol [GO:0005829]; extracellular exosome [GO:0070062]
|
amino acid binding [GO:0016597]; catalytic activity [GO:0003824]; dimethylargininase activity [GO:0016403]; metal ion binding [GO:0046872]
|
PF19420;
| null |
DDAH family
| null | null |
CATALYTIC ACTIVITY: Reaction=H2O + N(omega),N(omega)-dimethyl-L-arginine = dimethylamine + L-citrulline; Xref=Rhea:RHEA:17305, ChEBI:CHEBI:15377, ChEBI:CHEBI:57743, ChEBI:CHEBI:58040, ChEBI:CHEBI:58326; EC=3.5.3.18; Evidence={ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506, ECO:0000269|PubMed:21493890, ECO:0000269|PubMed:37296100}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17306; Evidence={ECO:0000305|PubMed:19663506}; CATALYTIC ACTIVITY: Reaction=H2O + N(omega)-methyl-L-arginine = L-citrulline + methylamine; Xref=Rhea:RHEA:25173, ChEBI:CHEBI:15377, ChEBI:CHEBI:57743, ChEBI:CHEBI:59338, ChEBI:CHEBI:114953; EC=3.5.3.18; Evidence={ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25174; Evidence={ECO:0000305|PubMed:19663506};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=69 uM for asymmetric dimethylarginine (ADMA) {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; KM=54 uM for monomethyl-L-arginine (MMA) {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; KM=3.1 uM for S-methyl-L-thiocitrulline {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; Vmax=356 nmol/min/mg enzyme with ADMA {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506}; Vmax=154 nmol/min/mg enzyme with NMA {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506};
| null |
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506};
| null |
FUNCTION: Hydrolyzes N(G),N(G)-dimethyl-L-arginine (ADMA) and N(G)-monomethyl-L-arginine (MMA) which act as inhibitors of NOS. Has therefore a role in the regulation of nitric oxide generation. {ECO:0000269|PubMed:18171027, ECO:0000269|PubMed:19663506, ECO:0000269|PubMed:21493890, ECO:0000269|PubMed:37296100}.
|
Homo sapiens (Human)
|
O94761
|
RECQ4_HUMAN
|
MERLRDVRERLQAWERAFRRQRGRRPSQDDVEAAPEETRALYREYRTLKRTTGQAGGGLRSSESLPAAAEEAPEPRCWGPHLNRAATKSPQSTPGRSRQGSVPDYGQRLKANLKGTLQAGPALGRRPWPLGRASSKASTPKPPGTGPVPSFAEKVSDEPPQLPEPQPRPGRLQHLQASLSQRLGSLDPGWLQRCHSEVPDFLGAPKACRPDLGSEESQLLIPGESAVLGPGAGSQGPEASAFQEVSIRVGSPQPSSSGGEKRRWNEEPWESPAQVQQESSQAGPPSEGAGAVAVEEDPPGEPVQAQPPQPCSSPSNPRYHGLSPSSQARAGKAEGTAPLHIFPRLARHDRGNYVRLNMKQKHYVRGRALRSRLLRKQAWKQKWRKKGECFGGGGATVTTKESCFLNEQFDHWAAQCPRPASEEDTDAVGPEPLVPSPQPVPEVPSLDPTVLPLYSLGPSGQLAETPAEVFQALEQLGHQAFRPGQERAVMRILSGISTLLVLPTGAGKSLCYQLPALLYSRRSPCLTLVVSPLLSLMDDQVSGLPPCLKAACIHSGMTRKQRESVLQKIRAAQVHVLMLTPEALVGAGGLPPAAQLPPVAFACIDEAHCLSQWSHNFRPCYLRVCKVLRERMGVHCFLGLTATATRRTASDVAQHLAVAEEPDLHGPAPVPTNLHLSVSMDRDTDQALLTLLQGKRFQNLDSIIIYCNRREDTERIAALLRTCLHAAWVPGSGGRAPKTTAEAYHAGMCSRERRRVQRAFMQGQLRVVVATVAFGMGLDRPDVRAVLHLGLPPSFESYVQAVGRAGRDGQPAHCHLFLQPQGEDLRELRRHVHADSTDFLAVKRLVQRVFPACTCTCTRPPSEQEGAVGGERPVPKYPPQEAEQLSHQAAPGPRRVCMGHERALPIQLTVQALDMPEEAIETLLCYLELHPHHWLELLATTYTHCRLNCPGGPAQLQALAHRCPPLAVCLAQQLPEDPGQGSSSVEFDMVKLVDSMGWELASVRRALCQLQWDHEPRTGVRRGTGVLVEFSELAFHLRSPGDLTAEEKDQICDFLYGRVQARERQALARLRRTFQAFHSVAFPSCGPCLEQQDEERSTRLKDLLGRYFEEEEGQEPGGMEDAQGPEPGQARLQDWEDQVRCDIRQFLSLRPEEKFSSRAVARIFHGIGSPCYPAQVYGQDRRFWRKYLHLSFHALVGLATEELLQVAR
|
5.6.2.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:28653661, ECO:0000312|PDB:5LST}; Note=Binds a Zn(2+) ion per subunit. {ECO:0000269|PubMed:28653661, ECO:0000312|PDB:5LST};
|
DNA duplex unwinding [GO:0032508]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; telomere maintenance [GO:0000723]; telomeric D-loop disassembly [GO:0061820]
|
chromosome [GO:0005694]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; bubble DNA binding [GO:0000405]; DNA/DNA annealing activity [GO:1990814]; four-way junction helicase activity [GO:0009378]; helicase activity [GO:0004386]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; oxidized purine DNA binding [GO:0032357]; telomeric D-loop binding [GO:0061821]
|
PF00270;PF11719;PF00271;
|
1.10.10.1460;3.40.50.300;
|
Helicase family, RecQ subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15317757}. Nucleus {ECO:0000269|PubMed:10552928}.
|
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000269|PubMed:28653661}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
| null | null | null | null |
FUNCTION: An ATP-dependent DNA helicase which unwinds dsDNA with a 3'-overhang in a 3'-5' direction (PubMed:28653661). Does not unwind more than 18 bp of dsDNA (PubMed:28653661). May modulate chromosome segregation. The N-terminal domain (residues 1-54) binds DNA Y-shaped DNA better than ss- or dsDNA (PubMed:22730300). The core helicase domain binds ssDNA (PubMed:22730300, PubMed:28653661). {ECO:0000269|PubMed:15317757, ECO:0000269|PubMed:22730300, ECO:0000269|PubMed:28653661}.
|
Homo sapiens (Human)
|
O94762
|
RECQ5_HUMAN
|
MSSHHTTFPFDPERRVRSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCFRANLFYDVQFKELISDPYGNLKDFCLKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFGMGVDKANVRFVAHWNIAKSMAGYYQESGRAGRDGKPSWCRLYYSRNDRDQVSFLIRKEVAKLQEKRGNKASDKATIMAFDALVTFCEELGCRHAAIAKYFGDALPACAKGCDHCQNPTAVRRRLEALERSSSWSKTCIGPSQGNGFDPELYEGGRKGYGDFSRYDEGSGGSGDEGRDEAHKREWNLFYQKQMQLRKGKDPKIEEFVPPDENCPLKEASSRRIPRLTVKAREHCLRLLEEALSSNRQSTRTADEADLRAKAVELEHETFRNAKVANLYKASVLKKVADIHRASKDGQPYDMGGSAKSCSAQAEPPEPNEYDIPPASHVYSLKPKRVGAGFPKGSCPFQTATELMETTRIREQAPQPERGGEHEPPSRPCGLLDEDGSEPLPGPRGEVPGGSAHYGGPSPEKKAKSSSGGSSLAKGRASKKQQLLATAAHKDSQSIARFFCRRVESPALLASAPEAEGACPSCEGVQGPPMAPEKYTGEEDGAGGHSPAPPQTEECLRERPSTCPPRDQGTPEVQPTPAKDTWKGKRPRSQQENPESQPQKRPRPSAKPSVVAEVKGSVSASEQGTLNPTAQDPFQLSAPGVSLKEAANVVVKCLTPFYKEGKFASKELFKGFARHLSHLLTQKTSPGRSVKEEAQNLIRHFFHGRARCESEADWHGLCGPQR
|
5.6.2.4
|
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LB8}; Note=Binds a Zn(2+) ion per subunit. {ECO:0000269|PubMed:28100692, ECO:0007744|PDB:5LB3, ECO:0007744|PDB:5LB5, ECO:0007744|PDB:5LB8};
|
cell division [GO:0051301]; cellular response to camptothecin [GO:0072757]; cellular response to xenobiotic stimulus [GO:0071466]; chromosome separation [GO:0051304]; DNA metabolic process [GO:0006259]; DNA repair [GO:0006281]; DNA replication [GO:0006260]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via homologous recombination [GO:0000724]; mitotic cell cycle [GO:0000278]; mitotic DNA-templated DNA replication [GO:1990506]; negative regulation of double-strand break repair via homologous recombination [GO:2000042]; negative regulation of transcription elongation by RNA polymerase II [GO:0034244]; replication-born double-strand break repair via sister chromatid exchange [GO:1990414]
|
chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; replication fork [GO:0005657]; transcription preinitiation complex [GO:0097550]
|
3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; four-way junction helicase activity [GO:0009378]; helicase activity [GO:0004386]; identical protein binding [GO:0042802]; isomerase activity [GO:0016853]; metal ion binding [GO:0046872]; RNA polymerase II complex binding [GO:0000993]
|
PF00270;PF00271;PF06959;PF16124;
|
6.10.250.2460;6.10.250.3140;3.40.50.300;
|
Helicase family, RecQ subfamily
|
PTM: Phosphorylated by CDK1 at Ser-727; this phosphorylation is required for RECQL5-mediated disruption of RAD51 filaments on stalled replication forks. {ECO:0000269|PubMed:28575661}.
|
SUBCELLULAR LOCATION: [Isoform Beta]: Nucleus, nucleoplasm {ECO:0000269|PubMed:10710432, ECO:0000269|PubMed:23180761, ECO:0000269|PubMed:23715498}. Nucleus {ECO:0000269|PubMed:23180761}. Note=Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks. Re-localizes from the nucleolus into the nucleus after replicative stress and significantly associates with WRN during S-phase (PubMed:23180761). {ECO:0000269|PubMed:20643585, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22973052, ECO:0000269|PubMed:23180761, ECO:0000269|PubMed:23715498}.; SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm {ECO:0000269|PubMed:10710432}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm {ECO:0000269|PubMed:10710432}.
|
CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000305|PubMed:28100692}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:28100692};
| null | null | null | null |
FUNCTION: DNA helicase that plays an important role in DNA replication, transcription and repair (PubMed:20643585, PubMed:22973052, PubMed:28100692). Probably unwinds DNA in a 3'-5' direction (Probable) (PubMed:28100692). Binds to the RNA polymerase II subunit POLR2A during transcription elongation and suppresses transcription-associated genomic instability (PubMed:20231364). Associates also with POLR1A and enforces the stability of ribosomal DNA arrays (PubMed:27502483). Plays an important role in mitotic chromosome separation after cross-over events and cell cycle progress (PubMed:22013166). Mechanistically, removes RAD51 filaments protecting stalled replication forks at common fragile sites and stimulates MUS81-EME1 endonuclease leading to mitotic DNA synthesis (PubMed:28575661). Required for efficient DNA repair, including repair of inter-strand cross-links (PubMed:23715498). Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination. A core helicase fragment (residues 11-609) binds preferentially to splayed duplex, looped and ssDNA (PubMed:28100692). {ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:20348101, ECO:0000269|PubMed:20643585, ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22973052, ECO:0000269|PubMed:23715498, ECO:0000269|PubMed:23748380, ECO:0000269|PubMed:27502483, ECO:0000269|PubMed:28100692, ECO:0000269|PubMed:28575661, ECO:0000305|PubMed:28100692}.
|
Homo sapiens (Human)
|
O94763
|
RMP_HUMAN
|
MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEKVVTNCQERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHVRKTIDDLKKVMKNFESRVEFTEDLQKMSDAAGDIVDIREEIKCDFEFKAKHRIAHKPHSKPKTSDIFEADIANDVKSKDLLADKELWARLEELERQEELLGELDSKPDTVIANGEDTTSSEEEKEDRNTNVNAMHQVTDSHTPCHKDVASSEPFSGQVNSQLNCSVNGSSSYHSDDDDDDDDDDDDDNIDDDDGDNDHEALGVGDNSIPTIYFSHTVEPKRVRINTGKNTTLKFSEKKEEAKRKRKNSTGSGHSAQELPTIRTPADIYRAFVDVVNGEYVPRKSILKSRSRENSVCSDTSESSAAEFDDRRGVLRSISCEEATCSDTSESILEEEPQENQKKLLPLSVTPEAFSGTVIEKEFVSPSLTPPPAIAHPALPTIPERKEVLLEASEETGKRVSKFKAARLQQKD
| null | null |
cellular response to growth factor stimulus [GO:0071363]; cellular response to steroid hormone stimulus [GO:0071383]; negative regulation of intrinsic apoptotic signaling pathway [GO:2001243]; negative regulation of phosphatase activity [GO:0010923]; negative regulation of transcription by RNA polymerase II [GO:0000122]; protein stabilization [GO:0050821]; regulation of cell growth [GO:0001558]; regulation of transcription by RNA polymerase II [GO:0006357]; response to virus [GO:0009615]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]; RPAP3/R2TP/prefoldin-like complex [GO:1990062]
|
chromatin binding [GO:0003682]; phosphatase inhibitor activity [GO:0019212]; phosphoprotein binding [GO:0051219]; protein phosphatase inhibitor activity [GO:0004864]; RNA polymerase II complex binding [GO:0000993]; transcription corepressor activity [GO:0003714]
|
PF02996;
|
1.10.287.370;
|
RNA polymerase II subunit 5-mediating protein family
|
PTM: Phosphorylated. Phosphorylation occurs essentially on serine residues. Phosphorylation occurs in response to androgen treatment in prostate cancer cells in a mTOR-dependent manner. Phosphorylated; hyperhosphorylated in mitochondria in a mTORC-dependent signaling pathway. Phosphorylated at Ser-372 by RPS6KB1 in a growth factor- and rapamycin-dependent manner. S6K1-mediated mitochondrial phosphorylation at Ser-372 disrupts the URI1-PPP1CC complex in the mitochondrion, relieves PPP1CC phosphatase inhibition activity and hence engages a negative feedback diminishing RPS6KB1 kinase activity, preventing sustained S6K1-dependent signaling. {ECO:0000269|PubMed:17936702, ECO:0000269|PubMed:21397856, ECO:0000269|PubMed:21730289, ECO:0000269|PubMed:9878255}.
|
SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion. Cell projection, dendrite {ECO:0000250}. Note=Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 at mitochondrion.
| null | null | null | null | null |
FUNCTION: Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.; FUNCTION: Plays a central role in maintaining S6K1 signaling and BAD phosphorylation under normal growth conditions thereby protecting cells from potential deleterious effects of sustained S6K1 signaling. The URI1-PPP1CC complex acts as a central component of a negative feedback mechanism that counteracts excessive S6K1 survival signaling to BAD in response to growth factors. Mediates inhibition of PPP1CC phosphatase activity in mitochondria. Coordinates the regulation of nutrient-sensitive gene expression availability in a mTOR-dependent manner. Seems to be a scaffolding protein able to assemble a prefoldin-like complex that contains PFDs and proteins with roles in transcription and ubiquitination.
|
Homo sapiens (Human)
|
O94766
|
B3GA3_HUMAN
|
MKLKLKNVFLAYFLVSIAGLLYALVQLGQPCDCLPPLRAAAEQLRQKDLRISQLQAELRRPPPAPAQPPEPEALPTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKAQRLREGEPGWVHPRGVEQRNKALDWLRGRGGAVGGEKDPPPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLVDPKDLEPRAANCTRVLVWHTRTEKPKMKQEEQLQRQGRGSDPAIEV
|
2.4.1.135
|
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
|
carbohydrate metabolic process [GO:0005975]; chondroitin sulfate proteoglycan biosynthetic process [GO:0050650]; dermatan sulfate proteoglycan biosynthetic process [GO:0050651]; glycosaminoglycan biosynthetic process [GO:0006024]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; positive regulation of catalytic activity [GO:0043085]; positive regulation of intracellular protein transport [GO:0090316]; protein glycosylation [GO:0006486]
|
cis-Golgi network [GO:0005801]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; membrane [GO:0016020]
|
galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity [GO:0015018]; glucuronosyltransferase activity [GO:0015020]; metal ion binding [GO:0046872]; protein phosphatase activator activity [GO:0072542]
|
PF03360;
| null |
Glycosyltransferase 43 family
|
PTM: N-glycosylated.
|
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:21763480}; Single-pass type II membrane protein {ECO:0000269|PubMed:21763480}. Golgi apparatus, cis-Golgi network {ECO:0000269|PubMed:21763480, ECO:0000269|PubMed:25893793}.
|
CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:24168, Rhea:RHEA-COMP:12571, Rhea:RHEA-COMP:12573, ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223, ChEBI:CHEBI:132090, ChEBI:CHEBI:132093; EC=2.4.1.135; Evidence={ECO:0000269|PubMed:25893793};
| null |
PATHWAY: Protein modification; protein glycosylation.
| null | null |
FUNCTION: Glycosaminoglycans biosynthesis (PubMed:25893793). Involved in forming the linkage tetrasaccharide present in heparan sulfate and chondroitin sulfate. Transfers a glucuronic acid moiety from the uridine diphosphate-glucuronic acid (UDP-GlcUA) to the common linkage region trisaccharide Gal-beta-1,3-Gal-beta-1,4-Xyl covalently bound to a Ser residue at the glycosaminylglycan attachment site of proteoglycans. Can also play a role in the biosynthesis of l2/HNK-1 carbohydrate epitope on glycoproteins. Shows strict specificity for Gal-beta-1,3-Gal-beta-1,4-Xyl, exhibiting negligible incorporation into other galactoside substrates including Galbeta1-3Gal beta1-O-benzyl, Galbeta1-4GlcNAc and Galbeta1-4Glc. Stimulates 2-phosphoxylose phosphatase activity of PXYLP1 in presence of uridine diphosphate-glucuronic acid (UDP-GlcUA) during completion of linkage region formation (PubMed:24425863). {ECO:0000269|PubMed:24425863, ECO:0000269|PubMed:25893793}.
|
Homo sapiens (Human)
|
O94768
|
ST17B_HUMAN
|
MSRRRFDCRSISGLLTTTPQIPIKMENFNNFYILTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSCPRVINLHEVYENTSEIILILEYAAGGEIFSLCLPELAEMVSENDVIRLIKQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGIIAYMLLTHTSPFVGEDNQETYLNISQVNVDYSEETFSSVSQLATDFIQSLLVKNPEKRPTAEICLSHSWLQQWDFENLFHPEETSSSSQTQDHSVRSSEDKTSKSSCNGTCGDREDKENIPEDSSMVSKRFRFDDSLPNPHELVSDLLC
|
2.7.11.1
| null |
apoptotic process [GO:0006915]; intracellular signal transduction [GO:0035556]; positive regulation of apoptotic process [GO:0043065]; positive regulation of fibroblast apoptotic process [GO:2000271]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]
|
actin cytoskeleton [GO:0015629]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Flemming body [GO:0090543]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;
|
1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, DAP kinase subfamily
|
PTM: Autophosphorylated.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9786912}. Cell membrane {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250}. Note=Colocalizes with STK17B at the plasma membrane. {ECO:0000250}.
|
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=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1;
| null | null | null | null |
FUNCTION: Phosphorylates myosin light chains (By similarity). Acts as a positive regulator of apoptosis. {ECO:0000250, ECO:0000269|PubMed:9786912}.
|
Homo sapiens (Human)
|
O94769
|
ECM2_HUMAN
|
MKIAVLFCFFLLIIFQTDFGKNEEIPRKQRRKIYHRRLRKSSTSHKHRSNRQLGIQQTTVFTPVARLPIVNFDYSMEEKFESFSSFPGVESSYNVLPGKKGHCLVKGITMYNKAVWSPEPCTTCLCSDGRVLCDETMCHPQRCPQTVIPEGECCPVCSATVSYSLLSGIALNDRNEFSGDSSEQREPTNLLHKQLPPPQVGMDRIVRKEALQSEEDEEVKEEDTEQKRETPESRNQGQLYSEGDSRGGDRKQRPGEERRLAHQQQRQGREEEEDEEEEGEEGEEDEEDEEDPVRGDMFRMPSRSPLPAPPRGTLRLPSGCSLSYRTISCINAMLTQIPPLTAPQITSLELTGNSIASIPDEAFNGLPNLERLDLSKNNITSSGIGPKAFKLLKKLMRLNMDGNNLIQIPSQLPSTLEELKVNENNLQAIDEESLSDLNQLVTLELEGNNLSEANVNPLAFKPLKSLAYLRLGKNKFRIIPQGLPGSIEELYLENNQIEEITEICFNHTRKINVIVLRYNKIEENRIAPLAWINQENLESIDLSYNKLYHVPSYLPKSLLHLVLLGNQIERIPGYVFGHMEPGLEYLYLSFNKLADDGMDRVSFYGAYHSLRELFLDHNDLKSIPPGIQEMKALHFLRLNNNKIRNILPEEICNAEEDDDSNLEHLHLENNYIKIREIPSYTFSCIRSYSSIVLKPQNIK
| null | null |
cell-matrix adhesion [GO:0007160]; extracellular matrix organization [GO:0030198]; positive regulation of cell-substrate adhesion [GO:0010811]
|
extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; interstitial matrix [GO:0005614]
|
collagen V binding [GO:0070052]; heparin binding [GO:0008201]; integrin binding [GO:0005178]
|
PF12799;PF13855;PF00093;
|
6.20.200.20;3.80.10.10;
|
Small leucine-rich proteoglycan (SLRP) family, SLRP class I subfamily
| null |
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q5FW85}.
| null | null | null | null | null |
FUNCTION: Promotes matrix assembly and cell adhesiveness. {ECO:0000250|UniProtKB:Q5FW85}.
|
Homo sapiens (Human)
|
O94776
|
MTA2_HUMAN
|
MAANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEESKQPGVSEQQRHQLKHRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEKEDCFFYSLVFDPVQKTLLADQGEIRVGCKYQAEIPDRLVEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQRNGYDLAKAMSTLVPQGGPVLCRDEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKTTDRYIQQKRLKAAEADSKLKQVYIPTYTKPNPNQIISVGSKPGMNGAGFQKGLTCESCHTTQSAQWYAWGPPNMQCRLCASCWIYWKKYGGLKTPTQLEGATRGTTEPHSRGHLSRPEAQSLSPYTTSANRAKLLAKNRQTFLLQTTKLTRLARRMCRDLLQPRRAARRPYAPINANAIKAECSIRLPKAAKTPLKIHPLVRLPLATIVKDLVAQAPLKPKTPRGTKTPINRNQLSQNRGLGGIMVKRAYETMAGAGVPFSANGRPLASGIRSSSQPAAKRQKLNPADAPNPVVFVATKDTRALRKALTHLEMRRAARRPNLPLKVKPTLIAVRPPVPLPAPSHPASTNEPIVLED
| null | null |
chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of cell fate specification [GO:0042659]; regulation of fibroblast migration [GO:0010762]; regulation of stem cell differentiation [GO:2000736]
|
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; histone deacetylase complex [GO:0000118]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; NuRD complex [GO:0016581]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667]
|
chromatin binding [GO:0003682]; histone deacetylase activity [GO:0004407]; histone deacetylase binding [GO:0042826]; metal ion binding [GO:0046872]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; sequence-specific DNA binding [GO:0043565]; transcription coactivator activity [GO:0003713]; transcription corepressor activity [GO:0003714]
|
PF01426;PF01448;PF00320;PF17226;PF00249;
|
2.30.30.490;4.10.1240.50;1.10.10.60;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512, ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}.
| null | null | null | null | null |
FUNCTION: May function as a transcriptional coregulator (PubMed:16428440, PubMed:28977666). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). {ECO:0000269|PubMed:16428440, ECO:0000269|PubMed:28977666}.
|
Homo sapiens (Human)
|
O94777
|
DPM2_HUMAN
|
MATGTDQVVGLGLVAVSLIIFTYYTAWVILLPFIDSQHVIHKYFLPRAYAVAIPLAAGLLLLLFVGLFISYVMLKTKRVTKKAQ
| null | null |
dolichol metabolic process [GO:0019348]; GPI anchor biosynthetic process [GO:0006506]; protein O-linked mannosylation [GO:0035269]; regulation of protein stability [GO:0031647]
|
dolichol-phosphate-mannose synthase complex [GO:0033185]; endoplasmic reticulum membrane [GO:0005789]; glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex [GO:0000506]
|
enzyme activator activity [GO:0008047]; enzyme regulator activity [GO:0030234]
|
PF07297;
| null |
DPM2 family
| null |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein.
| null | null |
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:10835346}.
| null | null |
FUNCTION: Regulates the biosynthesis of dolichol phosphate-mannose (PubMed:10835346). Regulatory subunit of the dolichol-phosphate mannose (DPM) synthase complex; essential for the ER localization and stable expression of DPM1 (PubMed:10835346). Part of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis (PubMed:16162815). May act by regulating the GPI-GNT complex (PubMed:10944123). {ECO:0000269|PubMed:10835346, ECO:0000269|PubMed:10944123, ECO:0000269|PubMed:16162815}.
|
Homo sapiens (Human)
|
O94778
|
AQP8_HUMAN
|
MSGEIAMCEPEFGNDKAREPSVGGRWRVSWYERFVQPCLVELLGSALFIFIGCLSVIENGTDTGLLQPALAHGLALGLVIATLGNISGGHFNPAVSLAAMLIGGLNLVMLLPYWVSQLLGGMLGAALAKAVSPEERFWNASGAAFVTVQEQGQVAGALVAEIILTTLLALAVCMGAINEKTKGPLAPFSIGFAVTVDILAGGPVSGGCMNPARAFGPAVVANHWNFHWIYWLGPLLAGLLVGLLIRCFIGDGKTRLILKAR
| null | null |
ammonium import across plasma membrane [GO:0140157]; ammonium transmembrane transport [GO:0072488]; B cell differentiation [GO:0030183]; cellular detoxification [GO:1990748]; cellular response to cAMP [GO:0071320]; hydrogen peroxide transmembrane transport [GO:0080170]; methylammonium transport [GO:0015843]; regulation of cholesterol biosynthetic process [GO:0045540]; transepithelial water transport [GO:0035377]; urea transport [GO:0015840]; water transport [GO:0006833]
|
apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; intracellular canaliculus [GO:0046691]; intracellular vesicle [GO:0097708]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum [GO:0005790]; smooth endoplasmic reticulum membrane [GO:0030868]
|
ammonium transmembrane transporter activity [GO:0008519]; methylammonium channel activity [GO:0015264]; urea channel activity [GO:0015265]; water channel activity [GO:0015250]
|
PF00230;
|
1.20.1080.10;
|
MIP/aquaporin (TC 1.A.8) family
|
PTM: Sulfenylation at Cys-53(C53-SOH) when hydrogen peroxide flows through the AQP8 channel, making it susceptible to hydrogen sulfide produced by CBS. {ECO:0000269|PubMed:29732408}.; PTM: Persulfidation at Cys-53 is required to gate AQP8 channel; under stress condition, hydrogen peroxide accumulates in the cell leading to CBS activation that produces hydrogen sulfide inducing persulfidation of oxidized Cys-53 (C53-SOH). {ECO:0000269|PubMed:29732408}.; PTM: N-glycosylated. {ECO:0000250|UniProtKB:P56405}.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18948439}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000269|PubMed:22622463, ECO:0000269|PubMed:34292591, ECO:0000305|PubMed:28042826}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:P56404, ECO:0000250|UniProtKB:P56405}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P56405}; Multi-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P56404}; Multi-pass membrane protein {ECO:0000255}. Note=Localized at the hepatocyte canalicular plasma membrane (PubMed:18948439). Localized at the apical membrane of the gall-bladder epithelial cells lining both the neck and corpus regions, the pancreatic acinar cells and mucosal epithelium of the colon and jejunum (By similarity). Trafficking from intracellular vesicles to the hepatocyte canalicular plasma membrane is induced by glucagon or the second messenger 3',5'-cyclic AMP and the translocation is protein kinase A and microtubule-dependent. Localized at the brush border membranes of epithelial cells from jejunum (By similarity). Localized at the luminal membranes of crypts in ascending colon (By similarity). {ECO:0000250|UniProtKB:P56404, ECO:0000250|UniProtKB:P56405, ECO:0000269|PubMed:18948439}.
|
CATALYTIC ACTIVITY: Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377; Evidence={ECO:0000269|PubMed:15948717, ECO:0000269|PubMed:18948439, ECO:0000269|PubMed:26972385}; CATALYTIC ACTIVITY: Reaction=H2O2(out) = H2O2(in); Xref=Rhea:RHEA:74375, ChEBI:CHEBI:16240; Evidence={ECO:0000269|PubMed:23541115, ECO:0000269|PubMed:26972385, ECO:0000269|PubMed:29732408, ECO:0000269|PubMed:30579780}; CATALYTIC ACTIVITY: Reaction=formamide(out) = formamide(in); Xref=Rhea:RHEA:74387, ChEBI:CHEBI:16397; Evidence={ECO:0000269|PubMed:15948717}; CATALYTIC ACTIVITY: Reaction=methylamine(out) = methylamine(in); Xref=Rhea:RHEA:74391, ChEBI:CHEBI:59338; Evidence={ECO:0000269|PubMed:15948717};
| null | null | null | null |
FUNCTION: Channel that allows the facilitated permeation of water and uncharged molecules, such as hydrogen peroxide and the neutral form of ammonia (NH3), through cellular membranes such as plasma membrane, inner mitochondrial membrane and endoplasmic reticulum membrane of several tissues (PubMed:15948717, PubMed:18948439, PubMed:23541115, PubMed:26972385, PubMed:29732408, PubMed:30579780). The transport of the ammonia neutral form induces a parallel transport of proton, at alkaline pH when the concentration of ammonia is high (By similarity). However, it is unclear whether the transport of proton takes place via the aquaporin or via an endogenous pathway (By similarity). Also, may transport ammonia analogs such as formamide and methylamine, a transport favourited at basic pH due to the increase of unprotonated (neutral) form, which is expected to favor diffusion (PubMed:15948717). Does not transport urea or glycerol (PubMed:15948717). The water transport mechanism is mercury- and copper-sensitive and passive in response to osmotic driving forces (PubMed:15948717). At the canicular plasma membrane, mediates the osmotic transport of water toward the bile canaliculus and facilitates the cAMP-induced bile canalicular water secretion, a process involved in bile formation (PubMed:18948439). In addition, mediates the hydrogen peroxide release from hepatocyte mitochondria that modulates the SREBF2-mediated cholesterol synthesis and facilitates the mitochondrial ammonia uptake which is metabolized into urea, mainly under glucagon stimulation (PubMed:30579780, PubMed:34292591). In B cells, transports the CYBB-generated hydrogen peroxide from the external leaflet of the plasma membrane to the cytosol to promote B cell activation and differentiation for signal amplification (By similarity). In the small intestine and colon system, mediates water transport through mitochondria and apical membrane of epithelial cells (By similarity). May play an important role in the adaptive response of proximal tubule cells to acidosis possibly by facilitating the mitochondrial ammonia transport (PubMed:22622463). {ECO:0000250|UniProtKB:P56404, ECO:0000250|UniProtKB:P56405, ECO:0000269|PubMed:15948717, ECO:0000269|PubMed:18948439, ECO:0000269|PubMed:22622463, ECO:0000269|PubMed:23541115, ECO:0000269|PubMed:26972385, ECO:0000269|PubMed:29732408, ECO:0000269|PubMed:30579780, ECO:0000269|PubMed:34292591}.
|
Homo sapiens (Human)
|
O94779
|
CNTN5_HUMAN
|
MASSWKLMLFLSVTMCLSEYSKSLPGLSTSYAALLRIKKSSSSSLFGSKTRPRYSSPSLGTLSASSPSWLGAAQNYYSPINLYHSSDAFKQDESVDYGPVFVQEPDDIIFPTDSDEKKVALNCEVRGNPVPSYRWLRNGTEIDLESDYRYSLIDGTFIISNPSEAKDSGHYQCLATNTVGSILSREATLQFAYLGNFSGRTRSAVSVREGQGVVLMCSPPPHSPEIIYSWVFNEFPSFVAEDSRRFISQETGNLYISKVQTSDVGSYICLVKNTVTNARVLSPPTPLTLRNDGVMGEYEPKIEVHFPFTVTAAKGTTVKMECFALGNPVPTITWMKVNGYIPSKARLRKSQAVLEIPNVQLDDAGIYECRAENSRGKNSFRGQLQVYTYPHWVEKLNDTQLDSGSPLRWECKATGKPRPTYRWLKNGVPLSPQSRVEMVNGVLMIHNVNQSDAGMYQCLAENKYGAIYASAELKILASAPTFALNQLKKTIIVTKDQEVVIECKPQGSPKPTISWKKGDRAVRENKRIAILPDGSLRILNASKSDEGKYVCRGENVFGSAEIIASLSVKEPTRIELTPKRTELTVGESIVLNCKAIHDASLDVTFYWTLKGQPIDFEEEGGHFESIRAQASSADLMIRNILLMHAGRYGCRVQTTADSVSDEAELLVRGPPGPPGIVIVEEITESTATLSWSPAADNHSPISSYNLQARSPFSLGWQTVKTVPEIITGDMESAMAVDLNPWVEYEFRVVATNPIGTGDPSTPSRMIRTNEAVPKTAPTNVSGRSGRRHELVIAWEPVSEEFQNGEGFGYIVAFRPNGTRGWKEKMVTSSEASKFIYRDESVPPLTPFEVKVGVYNNKGDGPFSQIVVICSAEGEPSAAPTDVKATSVSVSEILVAWKHIKESLGRPQGFEVGYWKDMEQEDTAETVKTRGNESFVILTGLEGNTLYHFTVRAYNGAGYGPPSSEVSATTKKSPPSQAPSNLRWEQQGSQVSLGWEPVIPLANESEVVGYKVFYRQEGHSNSQVIETQKLQAVVPLPDAGVYIIEVRAYSEGGDGTASSQIRVPSYSGGKITSAQSTLHSLSTSSSSVTLLLALMIPSTSW
| null | null |
axon guidance [GO:0007411]; brain development [GO:0007420]; cell-cell adhesion [GO:0098609]; presynapse assembly [GO:0099054]; sensory perception of sound [GO:0007605]
|
axon [GO:0030424]; extracellular region [GO:0005576]; GABA-ergic synapse [GO:0098982]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]; side of membrane [GO:0098552]
|
cell-cell adhesion mediator activity [GO:0098632]
|
PF00041;PF07679;PF13927;
|
2.60.40.10;
|
Immunoglobulin superfamily, Contactin family
| null |
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Contactins mediate cell surface interactions during nervous system development. Has some neurite outgrowth-promoting activity in the cerebral cortical neurons but not in hippocampal neurons. Probably involved in neuronal activity in the auditory system (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O94782
|
UBP1_HUMAN
|
MPGVIPSESNGLSRGSPSKKNRLSLKFFQKKETKRALDFTDSQENEEKASEYRASEIDQVVPAAQSSPINCEKRENLLPFVGLNNLGNTCYLNSILQVLYFCPGFKSGVKHLFNIISRKKEALKDEANQKDKGNCKEDSLASYELICSLQSLIISVEQLQASFLLNPEKYTDELATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETCQLLKKEEVKNVAELPTKVEEIPHPKEEMNGINSIEMDSMRHSEDFKEKLPKGNGKRKSDTEFGNMKKKVKLSKEHQSLEENQRQTRSKRKATSDTLESPPKIIPKYISENESPRPSQKKSRVKINWLKSATKQPSILSKFCSLGKITTNQGVKGQSKENECDPEEDLGKCESDNTTNGCGLESPGNTVTPVNVNEVKPINKGEEQIGFELVEKLFQGQLVLRTRCLECESLTERREDFQDISVPVQEDELSKVEESSEISPEPKTEMKTLRWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYGGGLSKINTPLLTPLKLSLEEWSTKPTNDSYGLFAVVMHSGITISSGHYTASVKVTDLNSLELDKGNFVVDQMCEIGKPEPLNEEEARGVVENYNDEEVSIRVGGNTQPSKVLNKKNVEAIGLLGGQKSKADYELYNKASNPDKVASTAFAENRNSETSDTTGTHESDRNKESSDQTGINISGFENKISYVVQSLKEYEGKWLLFDDSEVKVTEEKDFLNSLSPSTSPTSTPYLLFYKKL
|
3.4.19.12
| null |
DNA repair [GO:0006281]; monoubiquitinated protein deubiquitination [GO:0035520]; positive regulation of error-prone translesion synthesis [GO:1904333]; positive regulation of receptor signaling pathway via JAK-STAT [GO:0046427]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; regulation of DNA repair [GO:0006282]; response to UV [GO:0009411]; skeletal system development [GO:0001501]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
|
cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type endopeptidase activity [GO:0004197]; peptidase activity [GO:0008233]
|
PF00443;
|
3.90.70.10;
|
Peptidase C19 family
|
PTM: Autocatalytic cleavage of USP1 following UV irradiation inactivates it, leading to an increase in ubiquitinated PCNA, recruitment of POLH and translesion synthesis. {ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995}.; PTM: [Ubiquitin carboxyl-terminal hydrolase 1, N-terminal fragment]: Ubiquitinated by the CRL2(KLHDC2) complex following autocatalytic cleavage, leading to its degradation: the CRL2(KLHDC2) complex recognizes the diglycine (Gly-Gly) at the C-terminus. {ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:30526872}.
|
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15694335}.
|
CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:26388029, ECO:0000269|PubMed:9806842};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.7 uM for ubiquitin vinyl sulfone (in presence of WDR48) {ECO:0000269|PubMed:18082604}; KM=1.4 uM for ubiquitin vinyl sulfone (in absence of WDR48) {ECO:0000269|PubMed:18082604};
| null | null | null |
FUNCTION: Negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2 (PubMed:15694335). Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA (PubMed:16531995, PubMed:20147293). Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity (PubMed:18082604, PubMed:26388029). {ECO:0000269|PubMed:15694335, ECO:0000269|PubMed:16531995, ECO:0000269|PubMed:18082604, ECO:0000269|PubMed:20147293, ECO:0000269|PubMed:26388029}.
|
Homo sapiens (Human)
|
O94788
|
AL1A2_HUMAN
|
MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQGPQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFGPVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQSPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
|
1.2.1.36
| null |
9-cis-retinoic acid biosynthetic process [GO:0042904]; blood vessel development [GO:0001568]; cardiac muscle tissue development [GO:0048738]; cell population proliferation [GO:0008283]; cellular response to retinoic acid [GO:0071300]; determination of bilateral symmetry [GO:0009855]; embryonic camera-type eye development [GO:0031076]; embryonic digestive tract development [GO:0048566]; embryonic forelimb morphogenesis [GO:0035115]; face development [GO:0060324]; heart morphogenesis [GO:0003007]; hindbrain development [GO:0030902]; kidney development [GO:0001822]; liver development [GO:0001889]; lung development [GO:0030324]; midgut development [GO:0007494]; morphogenesis of embryonic epithelium [GO:0016331]; negative regulation of cell population proliferation [GO:0008285]; neural crest cell development [GO:0014032]; neural tube development [GO:0021915]; neuron differentiation [GO:0030182]; pancreas development [GO:0031016]; pituitary gland development [GO:0021983]; positive regulation of apoptotic process [GO:0043065]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of gene expression [GO:0010628]; protein homotetramerization [GO:0051289]; proximal/distal pattern formation [GO:0009954]; regulation of vascular endothelial cell proliferation [GO:1905562]; response to cytokine [GO:0034097]; response to estradiol [GO:0032355]; response to retinoic acid [GO:0032526]; response to vitamin A [GO:0033189]; retinal metabolic process [GO:0042574]; retinoic acid biosynthetic process [GO:0002138]; retinoic acid metabolic process [GO:0042573]; retinoic acid receptor signaling pathway involved in somitogenesis [GO:0090242]; retinol metabolic process [GO:0042572]; ureter maturation [GO:0035799]; vitamin A metabolic process [GO:0006776]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; perinuclear region of cytoplasm [GO:0048471]
|
3-chloroallyl aldehyde dehydrogenase activity [GO:0004028]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; retinal binding [GO:0016918]; retinal dehydrogenase activity [GO:0001758]
|
PF00171;
| null |
Aldehyde dehydrogenase family
| null |
SUBCELLULAR LOCATION: Cytoplasm.
|
CATALYTIC ACTIVITY: Reaction=H2O + NAD(+) + retinal = 2 H(+) + NADH + retinoate; Xref=Rhea:RHEA:16177, ChEBI:CHEBI:15035, ChEBI:CHEBI:15036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36; Evidence={ECO:0000269|PubMed:29240402, ECO:0000269|PubMed:33565183}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16178; Evidence={ECO:0000269|PubMed:29240402, ECO:0000269|PubMed:33565183}; CATALYTIC ACTIVITY: Reaction=all-trans-retinal + H2O + NAD(+) = all-trans-retinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:42080, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17898, ChEBI:CHEBI:35291, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.36; Evidence={ECO:0000250|UniProtKB:Q62148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:42081; Evidence={ECO:0000250|UniProtKB:Q62148}; CATALYTIC ACTIVITY: Reaction=all-trans-13,14-dihydroretinal + H2O + NAD(+) = all-trans-13,14-dihydroretinoate + 2 H(+) + NADH; Xref=Rhea:RHEA:75119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:194182, ChEBI:CHEBI:194183; Evidence={ECO:0000250|UniProtKB:Q62148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:75120; Evidence={ECO:0000250|UniProtKB:Q62148};
| null |
PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000269|PubMed:29240402}.
| null | null |
FUNCTION: Catalyzes the NAD-dependent oxidation of aldehyde substrates, such as all-trans-retinal and all-trans-13,14-dihydroretinal, to their corresponding carboxylic acids, all-trans-retinoate and all-trans-13,14-dihydroretinoate, respectively (PubMed:29240402, PubMed:33565183). Retinoate signaling is critical for the transcriptional control of many genes, for instance it is crucial for initiation of meiosis in both male and female (Probable) (PubMed:33565183). Recognizes retinal as substrate, both in its free form and when bound to cellular retinol-binding protein (By similarity). Can metabolize octanal and decanal, but has only very low activity with benzaldehyde, acetaldehyde and propanal (By similarity). Displays complete lack of activity with citral (By similarity). {ECO:0000250|UniProtKB:Q63639, ECO:0000269|PubMed:29240402, ECO:0000269|PubMed:33565183, ECO:0000305|PubMed:22075477}.
|
Homo sapiens (Human)
|
O94804
|
STK10_HUMAN
|
MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNEVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYHDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHSKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLEHPFVSSITSNKALRELVAEAKAEVMEEIEDGRDEGEEEDAVDAASTLENHTQNSSEVSPPSLNADKPLEESPSTPLAPSQSQDSVNEPCSQPSGDRSLQTTSPPVVAPGNENGLAVPVPLRKSRPVSMDARIQVAQEKQVAEQGGDLSPAANRSQKASQSRPNSSALETLGGEKLANGSLEPPAQAAPGPSKRDSDCSSLCTSESMDYGTNLSTDLSLNKEMGSLSIKDPKLYKKTLKRTRKFVVDGVEVSITTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQTQLSNKHELQLEQMHKRFEQEINAKKKFFDTELENLERQQKQQVEKMEQDHAVRRREEARRIRLEQDRDYTRFQEQLKLMKKEVKNEVEKLPRQQRKESMKQKMEEHTQKKQLLDRDFVAKQKEDLELAMKRLTTDNRREICDKERECLMKKQELLRDREAALWEMEEHQLQERHQLVKQQLKDQYFLQRHELLRKHEKEREQMQRYNQRMIEQLKVRQQQEKARLPKIQRSEGKTRMAMYKKSLHINGGGSAAEQREKIKQFSQQEEKRQKSERLQQQQKHENQMRDMLAQCESNMSELQQLQNEKCHLLVEHETQKLKALDESHNQNLKEWRDKLRPRKKALEEDLNQKKREQEMFFKLSEEAECPNPSTPSKAAKFFPYSSADAS
|
2.7.11.1
| null |
cell cycle [GO:0007049]; lymphocyte aggregation [GO:0071593]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468]; regulation of lymphocyte migration [GO:2000401]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886]; specific granule membrane [GO:0035579]
|
ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00069;PF12474;
|
1.10.510.10;
|
Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily
|
PTM: Autophosphorylates following homodimerization, leading to activation of the protein.
|
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19255442}; Peripheral membrane protein {ECO:0000269|PubMed:19255442}.
|
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=2.7.11.1; Evidence={ECO:0000269|PubMed:18239682}; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:18239682};
| null | null | null | null |
FUNCTION: Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo. {ECO:0000269|PubMed:11903060, ECO:0000269|PubMed:12639966, ECO:0000269|PubMed:19255442}.
|
Homo sapiens (Human)
|
O94805
|
ACL6B_HUMAN
|
MSGGVYGGDEVGALVFDIGSFSVRAGYAGEDCPKADFPTTVGLLAAEEGGGLELEGDKEKKGKIFHIDTNALHVPRDGAEVMSPLKNGMIEDWECFRAILDHTYSKHVKSEPNLHPVLMSEAPWNTRAKREKLTELMFEQYNIPAFFLCKTAVLTAFANGRSTGLVLDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFISMQCRELFQEMAIDIIPPYMIAAKEPVREGAPPNWKKKEKLPQVSKSWHNYMCNEVIQDFQASVLQVSDSPYDEQVAAQMPTVHYEMPNGYNTDYGAERLRIPEGLFDPSNVKGLSGNTMLGVGHVVTTSIGMCDIDIRPGLYGSVIVTGGNTLLQGFTDRLNRELSQKTPPSMRLKLIASNSTMERKFSPWIGGSILASLGTFQQMWISKQEYEEGGKQCVERKCP
| null | null |
chromatin organization [GO:0006325]; chromatin remodeling [GO:0006338]; dendrite development [GO:0016358]; negative regulation of cell differentiation [GO:0045596]; nervous system development [GO:0007399]; neuron maturation [GO:0042551]; positive regulation of cell differentiation [GO:0045597]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of double-strand break repair [GO:2000781]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of stem cell population maintenance [GO:1902459]; positive regulation of T cell differentiation [GO:0045582]; regulation of G0 to G1 transition [GO:0070316]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA polymerase II [GO:0006357]
|
bBAF complex [GO:0140092]; brahma complex [GO:0035060]; chromatin [GO:0000785]; GBAF complex [GO:0140288]; kinetochore [GO:0000776]; nBAF complex [GO:0071565]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; RSC-type complex [GO:0016586]; SWI/SNF complex [GO:0016514]
|
chromatin binding [GO:0003682]; structural constituent of cytoskeleton [GO:0005200]; transcription coactivator activity [GO:0003713]
|
PF00022;
|
3.30.420.40;
|
Actin family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000303|PubMed:26601204}.
| null | null | null | null | null |
FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner. Belongs to the neuron-specific chromatin remodeling complex (nBAF complex), as such plays a role in remodeling mononucleosomes in an ATP-dependent fashion, and is required for postmitotic neural development and dendritic outgrowth. During neural development a switch from a stem/progenitor to a postmitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to postmitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. ACTL6B/BAF53B is not essential for assembly of the nBAF complex but is required for targeting the complex and CREST to the promoter of genes essential for dendritic growth (By similarity). Essential for neuronal maturation and dendrite development (PubMed:31031012). {ECO:0000250|UniProtKB:Q99MR0, ECO:0000269|PubMed:31031012, ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
|
Homo sapiens (Human)
|
O94806
|
KPCD3_HUMAN
|
MSANNSPPSAQKSVLPTAIPAVLPAASPCSSPKTGLSARLSNGSFSAPSLTNSRGSVHTVSFLLQIGLTRESVTIEAQELSLSAVKDLVCSIVYQKFPECGFFGMYDKILLFRHDMNSENILQLITSADEIHEGDLVEVVLSALATVEDFQIRPHTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLPGPGLSVPRPLQPEYVALPSEESHVHQEPSKRIPSWSGRPIWMEKMVMCRVKVPHTFAVHSYTRPTICQYCKRLLKGLFRQGMQCKDCKFNCHKRCASKVPRDCLGEVTFNGEPSSLGTDTDIPMDIDNNDINSDSSRGLDDTEEPSPPEDKMFFLDPSDLDVERDEEAVKTISPSTSNNIPLMRVVQSIKHTKRKSSTMVKEGWMVHYTSRDNLRKRHYWRLDSKCLTLFQNESGSKYYKEIPLSEILRISSPRDFTNISQGSNPHCFEIITDTMVYFVGENNGDSSHNPVLAATGVGLDVAQSWEKAIRQALMPVTPQASVCTSPGQGKDHKDLSTSISVSNCQIQENVDISTVYQIFADEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKMRFPTKQESQLRNEVAILQNLHHPGIVNLECMFETPERVFVVMEKLHGDMLEMILSSEKSRLPERITKFMVTQILVALRNLHFKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRSKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAFMYPPNPWREISGEAIDLINNLLQVKMRKRYSVDKSLSHPWLQDYQTWLDLREFETRIGERYITHESDDARWEIHAYTHNLVYPKHFIMAPNPDDMEEDP
|
2.7.11.13
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
|
intracellular signal transduction [GO:0035556]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; protein kinase C-activating G protein-coupled receptor signaling pathway [GO:0007205]; protein phosphorylation [GO:0006468]; sphingolipid biosynthetic process [GO:0030148]
|
cytosol [GO:0005829]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
|
PF00130;PF00169;PF00069;
|
3.30.60.20;2.30.29.30;1.10.510.10;
|
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, PKD subfamily
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18076381}. Membrane {ECO:0000269|PubMed:18076381}. Note=Translocation to the cell membrane is required for kinase activation.
|
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=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.11.13;
| null | null | null | null |
FUNCTION: Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O94808
|
GFPT2_HUMAN
|
MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKRGKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMKRLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSASDDPSRAIQTLQMELQQIMKGNFSAFMQKEIFEQPESVFNTMRGRVNFETNTVLLGGLKDHLKEIRRCRRLIVIGCGTSYHAAVATRQVLEELTELPVMVELASDFLDRNTPVFRDDVCFFISQSGETADTLLALRYCKDRGALTVGVTNTVGSSISRETDCGVHINAGPEIGVASTKAYTSQFISLVMFGLMMSEDRISLQNRRQEIIRGLRSLPELIKEVLSLEEKIHDLALELYTQRSLLVMGRGYNYATCLEGALKIKEITYMHSEGILAGELKHGPLALIDKQMPVIMVIMKDPCFAKCQNALQQVTARQGRPIILCSKDDTESSKFAYKTIELPHTVDCLQGILSVIPLQLLSFHLAVLRGYDVDFPRNLAKSVTVE
|
2.6.1.16
| null |
cellular response to leukemia inhibitory factor [GO:1990830]; energy reserve metabolic process [GO:0006112]; fructose 6-phosphate metabolic process [GO:0006002]; glutamine metabolic process [GO:0006541]; protein N-linked glycosylation [GO:0006487]; UDP-N-acetylglucosamine biosynthetic process [GO:0006048]; UDP-N-acetylglucosamine metabolic process [GO:0006047]
|
cytosol [GO:0005829]
|
carbohydrate derivative binding [GO:0097367]; glutamine-fructose-6-phosphate transaminase (isomerizing) activity [GO:0004360]
|
PF13522;PF01380;
|
3.60.20.10;
| null | null | null |
CATALYTIC ACTIVITY: Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; Evidence={ECO:0000250|UniProtKB:P82808};
| null |
PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D-fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P82808}.
| null | null |
FUNCTION: Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
|
Homo sapiens (Human)
|
O94810
|
RGS11_HUMAN
|
MAAGPAPPPGRPRAQMPHLRKMERVVVSMQDPDQGVKMRSQRLLVTVIPHAVTGSDVVQWLAQKFCVSEEEALHLGAVLVQHGYIYPLRDPRSLMLRPDETPYRFQTPYFWTSTLRPAAELDYAIYLAKKNIRKRGTLVDYEKDCYDRLHKKINHAWDLVLMQAREQLRAAKQRSKGDRLVIACQEQTYWLVNRPPPGAPDVLEQGPGRGSCAASRVLMTKSADFHKREIEYFRKALGRTRVKSSVCLEAYLSFCGQRGPHDPLVSGCLPSNPWISDNDAYWVMNAPTVAAPTKLRVERWGFSFRELLEDPVGRAHFMDFLGKEFSGENLSFWEACEELRYGAQAQVPTLVDAVYEQFLAPGAAHWVNIDSRTMEQTLEGLRQPHRYVLDDAQLHIYMLMKKDSYPRFLKSDMYKALLAEAGIPLEMKRRVFPFTWRPRHSSPSPALLPTPVEPTAACGPGGGDGVA
| null | null |
G protein-coupled receptor signaling pathway [GO:0007186]; intracellular signal transduction [GO:0035556]; negative regulation of signal transduction [GO:0009968]; regulation of G protein-coupled receptor signaling pathway [GO:0008277]
|
cytoplasm [GO:0005737]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]
|
G-protein beta-subunit binding [GO:0031681]; GTPase activator activity [GO:0005096]; GTPase activity [GO:0003924]
|
PF00610;PF00631;PF00615;PF18148;
|
1.10.1240.60;1.10.167.10;4.10.260.10;1.10.10.10;
| null | null | null | null | null | null | null | null |
FUNCTION: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form.
|
Homo sapiens (Human)
|
O94811
|
TPPP_HUMAN
|
MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK
|
3.6.5.-
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21316364};
|
astral microtubule organization [GO:0030953]; cell division [GO:0051301]; microtubule bundle formation [GO:0001578]; microtubule nucleation by microtubule organizing center [GO:0051418]; microtubule polymerization [GO:0046785]; myelin assembly [GO:0032288]; negative regulation of tubulin deacetylation [GO:1904428]; oligodendrocyte development [GO:0014003]; oligodendrocyte differentiation [GO:0048709]; positive regulation of myelination [GO:0031643]; positive regulation of protein polymerization [GO:0032273]; positive regulation of protein-containing complex assembly [GO:0031334]; regulation of microtubule cytoskeleton organization [GO:0070507]
|
cytoplasm [GO:0005737]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; microtubule [GO:0005874]; microtubule organizing center [GO:0005815]; mitochondrion [GO:0005739]; mitotic spindle [GO:0072686]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; postsynaptic Golgi apparatus [GO:0150051]
|
GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; microtubule nucleator activity [GO:0140490]; protein dimerization activity [GO:0046983]; protein homodimerization activity [GO:0042803]; tubulin binding [GO:0015631]
|
PF05517;
|
1.10.238.10;
|
TPPP family
|
PTM: Phosphorylated by LIMK1 on serine residues; phosphorylation may alter the tubulin polymerization activity (PubMed:17693641, PubMed:18028908). Phosphorylation by LIMK2, but not LIMK1, regulates astral microtubule organization at early stage of mitosis (PubMed:22328514). Phosphorylation by ROCK1 at Ser-32, Ser-107 and Ser-159 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin, increased cell motility and entry into S-phase (PubMed:23093407, PubMed:23355470). Phosphorylation by CDK1 inhibits the microtubule polymerizing activity (PubMed:23355470). {ECO:0000269|PubMed:17693641, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:22328514, ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470}.; PTM: Degraded by the proteasome; zinc-binding inhibits degradation by the proteasome. {ECO:0000269|PubMed:25445539}.
|
SUBCELLULAR LOCATION: Golgi outpost {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17105200}. Nucleus {ECO:0000269|PubMed:18028908}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22328514}. Note=Specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (By similarity). Mainly localizes to the cytoskeleton (PubMed:18028908). Also found in the nucleus; however, nuclear localization is unclear and requires additional evidences (PubMed:18028908). Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies (PubMed:15590652, PubMed:17027006). During mitosis, colocalizes with LIMK2 at the mitotic spindle (PubMed:22328514). {ECO:0000250|UniProtKB:D3ZQL7, ECO:0000269|PubMed:15590652, ECO:0000269|PubMed:17027006, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:22328514}.
|
CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:21316364, ECO:0000269|PubMed:21995432}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:21316364, ECO:0000269|PubMed:21995432};
|
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=kcat is 0.018 min(-1) for GTP. {ECO:0000269|PubMed:21316364};
| null | null | null |
FUNCTION: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (PubMed:31522887). Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath (PubMed:31522887, PubMed:33831707). Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (PubMed:31522887). Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (PubMed:21316364, PubMed:21995432). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network (PubMed:17105200, PubMed:17693641, PubMed:18028908, PubMed:26289831). Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (PubMed:20308065, PubMed:23093407). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (PubMed:23093407). Plays a role in cell proliferation by regulating the G1/S-phase transition (PubMed:23355470). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (PubMed:22328514). {ECO:0000269|PubMed:17105200, ECO:0000269|PubMed:17693641, ECO:0000269|PubMed:18028908, ECO:0000269|PubMed:20308065, ECO:0000269|PubMed:21316364, ECO:0000269|PubMed:21995432, ECO:0000269|PubMed:22328514, ECO:0000269|PubMed:23093407, ECO:0000269|PubMed:23355470, ECO:0000269|PubMed:26289831, ECO:0000269|PubMed:31522887}.
|
Homo sapiens (Human)
|
O94812
|
BAIP3_HUMAN
|
MRPRGAAFAAGPPGDLHLGTAIGFAGAIWRSRSPAMSTLLDIKSSVLRQVQVCPSFRRRTEQDPGSASADPQEPATGAWKPGDGVEFFAHMRLMLKKGEGRQGLPCLEVPLRSGSPAPPEPVDPSLGLRALAPEEVEMLYEEALYTVLYRAGTMGPDQVDDEEALLSYLQQVFGTSLEEHTEAIERVRKAKAPTYALKVSVMRAKNLLAKDPNGFSDPYCMLGILPASDATREPRAQKEQRFGFRKGSKRGGPLPAKCIQVTEVKSSTLNPVWKEHFLFEIEDVSTDQLHLDIWDHDDDVSLVEACRKLNEVIGLKGMGRYFKQIVKSARANGTAGPTEDHTDDFLGCLNIPVREVPVAGVDRWFKLEPRSSASRVQGHCHLVLKLITTQRDTAMSQRGRSGFLSHLLLLSHLLRLEHSAEEPNSSSWRGELSTPAATILCLHGAQSNLSPLQLAVLHWQVSSRHHQTCTLDYSYLLGLLEDMQAHWEEAPSLPQEQEESLADSLSAFSEFGLQLLRQLRDYFPATNSTAVHRLELLLKCLGKLQLFQPSFEICPFESELNMDIAAALKRGNREWYDRILNDKSPREQPGPQRLPGLVVLADAVYDDLQFCYSVYASLFHSILNVDVFTLTFRQLERLVAEEAWVLTEELSPKMTLEVASGLFELYLTLADLQRFWDSIPGRDSRSLALAGIHAPFLPAVKLWFQVLRDQAKWRLQGAVDMDTLEPVDASSRHSSSAATAGLCLSHIQELWVRLAWPDPAQAQGLGTQLGQDVCEATLFYTELLRKKVDTQPGAAGEAVSEALCVVLNNVELVRKAAGQALKGLAWPEGATGPEGVLPRPLLSCTQALDDDLQREAHTVTAHLTSKMVGDIRKYVQHISLSPDSIQNDEAVAPLMKYLDEKLALLNASLVKGNLSRVLEALWELLLQAILQALGANRDVSADFYSRFHFTLEALVSFFHAEGQGLPLESLRDGSYKRLKEELRLHKCSTRECIEQFYLDKLKQRTLEQNRFGRLSVRCHYEAAEQRLAVEVLHAADLLPLDANGLSDPFVIVELGPPHLFPLVRSQRTQVKTRTLHPVYDELFYFSVPAEACRRRAACVLFTVMDHDWLSTNDFAGEAALGLGGVTGVARPQVGGGARAGQPVTLHLCRPRAQVRSALRRLEGRTSKEAQEFVKKLKELEKCMEADP
| null |
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per C2 domain. {ECO:0000255|PROSITE-ProRule:PRU00041};
|
dense core granule maturation [GO:1990502]; exocytosis [GO:0006887]; G protein-coupled receptor signaling pathway [GO:0007186]; positive regulation of insulin secretion involved in cellular response to glucose stimulus [GO:0035774]; positive regulation of neurotransmitter secretion [GO:0001956]; regulation of behavior [GO:0050795]; regulation of dense core granule exocytosis [GO:1905413]; regulation of synaptic transmission, GABAergic [GO:0032228]; retrograde transport, endosome to Golgi [GO:0042147]
|
cytosol [GO:0005829]; GABA-ergic synapse [GO:0098982]; late endosome membrane [GO:0031902]; plasma membrane [GO:0005886]; presynapse [GO:0098793]; recycling endosome membrane [GO:0055038]; secretory vesicle [GO:0099503]; trans-Golgi network membrane [GO:0032588]
|
calcium ion binding [GO:0005509]; phospholipid binding [GO:0005543]; SNARE binding [GO:0000149]; syntaxin binding [GO:0019905]
|
PF00168;PF06292;
|
1.10.357.50;2.60.40.150;
|
Unc-13 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28626000}. Recycling endosome membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein {ECO:0000305|PubMed:28626000}. Late endosome membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein {ECO:0000305|PubMed:28626000}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein {ECO:0000305|PubMed:28626000}. Cell membrane {ECO:0000269|PubMed:28626000}; Peripheral membrane protein {ECO:0000305|PubMed:28626000}. Note=Rapidly recruited to the plasma membrane and to Golgi structures in response to increased intracellular calcium concentration. {ECO:0000269|PubMed:28626000}.
| null | null | null | null | null |
FUNCTION: Functions in endosome to Golgi retrograde transport. In response to calcium influx, may interact with SNARE fusion receptors and membrane phospholipids to mediate endosome fusion with the trans-Golgi network. By promoting the recycling of secretory vesicle transmembrane proteins, it indirectly controls dense-core secretory vesicle biogenesis, maturation and their ability to mediate the constitutive and regulated secretion of neurotransmitters and hormones. May regulate behavior and food intake by controlling calcium-stimulated exocytosis of neurotransmitters including NPY and serotonin and hormones like insulin (PubMed:28626000). Proposed to play a role in hypothalamic neuronal firing by modulating gamma-aminobutyric acid (GABA)ergic inhibitory neurotransmission (By similarity). {ECO:0000250|UniProtKB:Q80TT2, ECO:0000269|PubMed:28626000}.
|
Homo sapiens (Human)
|
O94813
|
SLIT2_HUMAN
|
MRGVGWQMLSLSLGLVLAILNKVAPQACPAQCSCSGSTVDCHGLALRSVPRNIPRNTERLDLNGNNITRITKTDFAGLRHLRVLQLMENKISTIERGAFQDLKELERLRLNRNHLQLFPELLFLGTAKLYRLDLSENQIQAIPRKAFRGAVDIKNLQLDYNQISCIEDGAFRALRDLEVLTLNNNNITRLSVASFNHMPKLRTFRLHSNNLYCDCHLAWLSDWLRQRPRVGLYTQCMGPSHLRGHNVAEVQKREFVCSGHQSFMAPSCSVLHCPAACTCSNNIVDCRGKGLTEIPTNLPETITEIRLEQNTIKVIPPGAFSPYKKLRRIDLSNNQISELAPDAFQGLRSLNSLVLYGNKITELPKSLFEGLFSLQLLLLNANKINCLRVDAFQDLHNLNLLSLYDNKLQTIAKGTFSPLRAIQTMHLAQNPFICDCHLKWLADYLHTNPIETSGARCTSPRRLANKRIGQIKSKKFRCSAKEQYFIPGTEDYRSKLSGDCFADLACPEKCRCEGTTVDCSNQKLNKIPEHIPQYTAELRLNNNEFTVLEATGIFKKLPQLRKINFSNNKITDIEEGAFEGASGVNEILLTSNRLENVQHKMFKGLESLKTLMLRSNRITCVGNDSFIGLSSVRLLSLYDNQITTVAPGAFDTLHSLSTLNLLANPFNCNCYLAWLGEWLRKKRIVTGNPRCQKPYFLKEIPIQDVAIQDFTCDDGNDDNSCSPLSRCPTECTCLDTVVRCSNKGLKVLPKGIPRDVTELYLDGNQFTLVPKELSNYKHLTLIDLSNNRISTLSNQSFSNMTQLLTLILSYNRLRCIPPRTFDGLKSLRLLSLHGNDISVVPEGAFNDLSALSHLAIGANPLYCDCNMQWLSDWVKSEYKEPGIARCAGPGEMADKLLLTTPSKKFTCQGPVDVNILAKCNPCLSNPCKNDGTCNSDPVDFYRCTCPYGFKGQDCDVPIHACISNPCKHGGTCHLKEGEEDGFWCICADGFEGENCEVNVDDCEDNDCENNSTCVDGINNYTCLCPPEYTGELCEEKLDFCAQDLNPCQHDSKCILTPKGFKCDCTPGYVGEHCDIDFDDCQDNKCKNGAHCTDAVNGYTCICPEGYSGLFCEFSPPMVLPRTSPCDNFDCQNGAQCIVRINEPICQCLPGYQGEKCEKLVSVNFINKESYLQIPSAKVRPQTNITLQIATDEDSGILLYKGDKDHIAVELYRGRVRASYDTGSHPASAIYSVETINDGNFHIVELLALDQSLSLSVDGGNPKIITNLSKQSTLNFDSPLYVGGMPGKSNVASLRQAPGQNGTSFHGCIRNLYINSELQDFQKVPMQTGILPGCEPCHKKVCAHGTCQPSSQAGFTCECQEGWMGPLCDQRTNDPCLGNKCVHGTCLPINAFSYSCKCLEGHGGVLCDEEEDLFNPCQAIKCKHGKCRLSGLGQPYCECSSGYTGDSCDREISCRGERIRDYYQKQQGYAACQTTKKVSRLECRGGCAGGQCCGPLRSKRRKYSFECTDGSSFVDEVEKVVKCGCTRCVS
| null | null |
aortic valve morphogenesis [GO:0003180]; apoptotic process involved in luteolysis [GO:0061364]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; branching morphogenesis of an epithelial tube [GO:0048754]; cell migration involved in sprouting angiogenesis [GO:0002042]; cellular response to heparin [GO:0071504]; cellular response to hormone stimulus [GO:0032870]; chemorepulsion involved in postnatal olfactory bulb interneuron migration [GO:0021836]; corticospinal neuron axon guidance through spinal cord [GO:0021972]; induction of negative chemotaxis [GO:0050929]; motor neuron axon guidance [GO:0008045]; negative chemotaxis [GO:0050919]; negative regulation of actin filament polymerization [GO:0030837]; negative regulation of cell growth [GO:0030308]; negative regulation of cell migration [GO:0030336]; negative regulation of cellular response to growth factor stimulus [GO:0090288]; negative regulation of chemokine-mediated signaling pathway [GO:0070100]; negative regulation of endothelial cell migration [GO:0010596]; negative regulation of lamellipodium assembly [GO:0010593]; negative regulation of leukocyte chemotaxis [GO:0002689]; negative regulation of monocyte chemotaxis [GO:0090027]; negative regulation of mononuclear cell migration [GO:0071676]; negative regulation of neutrophil chemotaxis [GO:0090024]; negative regulation of protein phosphorylation [GO:0001933]; negative regulation of retinal ganglion cell axon guidance [GO:0090260]; negative regulation of small GTPase mediated signal transduction [GO:0051058]; negative regulation of smooth muscle cell chemotaxis [GO:0071672]; negative regulation of smooth muscle cell migration [GO:0014912]; negative regulation of vascular permeability [GO:0043116]; positive regulation of apoptotic process [GO:0043065]; positive regulation of axonogenesis [GO:0050772]; pulmonary valve morphogenesis [GO:0003184]; response to cortisol [GO:0051414]; retinal ganglion cell axon guidance [GO:0031290]; Roundabout signaling pathway [GO:0035385]; ureteric bud development [GO:0001657]; ventricular septum morphogenesis [GO:0060412]
|
cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020]
|
calcium ion binding [GO:0005509]; GTPase inhibitor activity [GO:0005095]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; laminin-1 binding [GO:0043237]; protein homodimerization activity [GO:0042803]; proteoglycan binding [GO:0043394]; Roundabout binding [GO:0048495]
|
PF00008;PF12661;PF00054;PF00560;PF13855;PF01463;PF01462;
|
2.60.120.200;2.10.25.10;3.80.10.10;
| null | null |
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10102268}. Note=The C-terminal cleavage protein is more diffusible than the larger N-terminal protein that is more tightly cell associated.
| null | null | null | null | null |
FUNCTION: Thought to act as molecular guidance cue in cellular migration, and function appears to be mediated by interaction with roundabout homolog receptors. During neural development involved in axonal navigation at the ventral midline of the neural tube and projection of axons to different regions. SLIT1 and SLIT2 seem to be essential for midline guidance in the forebrain by acting as repulsive signal preventing inappropriate midline crossing by axons projecting from the olfactory bulb. In spinal cord development may play a role in guiding commissural axons once they reached the floor plate by modulating the response to netrin. In vitro, silences the attractive effect of NTN1 but not its growth-stimulatory effect and silencing requires the formation of a ROBO1-DCC complex. May be implicated in spinal cord midline post-crossing axon repulsion. In vitro, only commissural axons that crossed the midline responded to SLIT2. In the developing visual system appears to function as repellent for retinal ganglion axons by providing a repulsion that directs these axons along their appropriate paths prior to, and after passage through, the optic chiasm. In vitro, collapses and repels retinal ganglion cell growth cones. Seems to play a role in branching and arborization of CNS sensory axons, and in neuronal cell migration. In vitro, Slit homolog 2 protein N-product, but not Slit homolog 2 protein C-product, repels olfactory bulb (OB) but not dorsal root ganglia (DRG) axons, induces OB growth cones collapse and induces branching of DRG axons. Seems to be involved in regulating leukocyte migration. {ECO:0000269|PubMed:10102268, ECO:0000269|PubMed:10864954, ECO:0000269|PubMed:10975526, ECO:0000269|PubMed:11239147, ECO:0000269|PubMed:11309622, ECO:0000269|PubMed:11404413}.
|
Homo sapiens (Human)
|
O94817
|
ATG12_HUMAN
|
MAEEPQSVLQLPTSIAAGGEGLTDVSPETTTPEPPSSAAVSPGTEEPAGDTKKKIDILLKAVGDTPIMKTKKWAVERTRTIQGLIDFIKKFLKLVASEQLFIYVNQSFAPSPDQEVGTLYECFGSDGKLVLHYCKSQAWG
| null | null |
autophagosome assembly [GO:0000045]; autophagosome maturation [GO:0097352]; glycophagy [GO:0061723]; macroautophagy [GO:0016236]; negative regulation of defense response to virus [GO:0050687]; negative regulation of innate immune response [GO:0045824]; negative regulation of type I interferon production [GO:0032480]; piecemeal microautophagy of the nucleus [GO:0034727]; positive regulation of viral translation [GO:1904973]; regulation of autophagosome maturation [GO:1901096]
|
Atg12-Atg5-Atg16 complex [GO:0034274]; autophagosome [GO:0005776]; autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; phagocytic vesicle membrane [GO:0030670]; phagophore assembly site membrane [GO:0034045]; protein-containing complex [GO:0032991]; transferase complex [GO:1990234]
| null |
PF04110;
| null |
ATG12 family
|
PTM: Acetylated by EP300. {ECO:0000269|PubMed:19124466}.
|
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Preautophagosomal structure membrane {ECO:0000269|PubMed:22342342}; Peripheral membrane protein {ECO:0000269|PubMed:22342342}. Note=TECPR1 recruits the ATG12-ATG5 conjugate to the autolysosomal membrane.
| null | null | null | null | null |
FUNCTION: Ubiquitin-like protein involved in autophagy vesicles formation. Conjugation with ATG5 through a ubiquitin-like conjugating system involving also ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. {ECO:0000269|PubMed:12207896, ECO:0000269|PubMed:17999726, ECO:0000269|PubMed:19074260, ECO:0000269|PubMed:19164948, ECO:0000269|PubMed:23202584}.; FUNCTION: (Microbial infection) May act as a proviral factor. In association with ATG5, negatively regulates the innate antiviral immune response by impairing the type I IFN production pathway upon vesicular stomatitis virus (VSV) infection (PubMed:17709747). Required for the translation of incoming hepatitis C virus (HCV) RNA and, thereby, for the initiation of HCV replication, but not required once infection is established (PubMed:19666601). {ECO:0000269|PubMed:17709747, ECO:0000269|PubMed:19666601}.
|
Homo sapiens (Human)
|
O94818
|
NOL4_HUMAN
|
MESERDMYRQFQDWCLRTYGDSGKTKTVTRKKYERIVQLLNGSESSSTDNAKFKFWVKSKGFQLGQPDEVRGGGGGAKQVLYVPVKTTDGVGVDEKLSLRRVAVVEDFFDIIYSMHVETGPNGEQIRKHAGQKRTYKAISESYAFLPREAVTRFLMSCSECQKRMHLNPDGTDHKDNGKPPTLVTSMIDYNMPITMAYMKHMKLQLLNSQQDEDESSIESDEFDMSDSTRMSAVNSDLSSNLEERMQSPQNLHGQQDDDSAAESFNGNETLGHSSIASGGTHSREMGDSNSDGKTGLEQDEQPLNLSDSPLSAQLTSEYRIDDHNSNGKNKYKNLLISDLKMEREARENGSKSPAHSYSSYDSGKNESVDRGAEDLSLNRGDEDEDDHEDHDDSEKVNETDGVEAERLKAFNMFVRLFVDENLDRMVPISKQPKEKIQAIIDSCRRQFPEYQERARKRIRTYLKSCRRMKRSGFEMSRPIPSHLTSAVAESILASACESESRNAAKRMRLERQQDESAPADKQCKPEATQATYSTSAVPGSQDVLYINGNGTYSYHSYRGLGGGLLNLNDASSSGPTDLSMKRQLATSSGSSSSSNSRPQLSPTEINAVRQLVAGYRESAAFLLRSADELENLILQQN
| null | null | null |
nucleolus [GO:0005730]
|
RNA binding [GO:0003723]
| null | null | null | null |
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:9813152, ECO:0000269|PubMed:9853615}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
O94822
|
LTN1_HUMAN
|
MGGKNKQRTKGNLRPSNSGRAAELLAKEQGTVPGFIGFGTSQSDLGYVPAIQGAEEIDSLVDSDFRMVLRKLSKKDVTTKLKAMQEFGTMCTERDTETVKGVLPYWPRIFCKISLDHDRRVREATQQAFEKLILKVKKQLAPYLKSLMGYWLMAQCDTYTPAAFAAKDAFEAAFPPSKQPEAIAFCKDEITSVLQDHLIKETPDTLSDPQTVPEEEREAKFYRVVTCSLLALKRLLCLLPDNELDSLEEKFKSLLSQNKFWKYGKHSVPQIRSAYFELVSALCQRIPQLMKEEASKVSPSVLLSIDDSDPIVCPALWEAVLYTLTTIEDCWLHVNAKKSVFPKLSTVIREGGRGLATVIYPYLLPFISKLPQSITNPKLDFFKNFLTSLVAGLSTERTKTSSLESSAVISAFFECLRFIMQQNLGEEEIEQMLVNDQLIPFIDAVLKDPGLQHGQLFNHLAETLSSWEAKADTEKDEKTAHNLENVLIHFWERLSEICVAKISEPEADVESVLGVSNLLQVLQKPKSSLKSSKKKNGKVRFADEILESNKENEKCVSSEGEKIEGWELTTEPSLTHNSSGLLSPLRKKPLEDLVCKLADISINYVNERKSEQHLRFLSTLLDSFSSSRVFKMLLGDEKQSIVQAKPLEIAKLVQKNPAVQFLYQKLIGWLNEDQRKDFGFLVDILYSALRCCDNDMERKKVLDDLTKVDLKWNSLLKIIEKACPSSDKHALVTPWLKGDILGEKLVNLADCLCNEDLESRVSSESHFSERWTLLSLVLSQHVKNDYLIGDVYVERIIVRLHETLFKTKKLSEAESSDSSVSFICDVAYNYFSSAKGCLLMPSSEDLLLTLFQLCAQSKEKTHLPDFLICKLKNTWLSGVNLLVHQTDSSYKESTFLHLSALWLKNQVQASSLDINSLQVLLSAVDDLLNTLLESEDSYLMGVYIGSVMPNDSEWEKMRQSLPMQWLHRPLLEGRLSLNYECFKTDFKEQDIKTLPSHLCTSALLSKMVLIALRKETVLENNELEKIIAELLYSLQWCEELDNPPIFLIGFCEILQKMNITYDNLRVLGNTSGLLQLLFNRSREHGTLWSLIIAKLILSRSISSDEVKPHYKRKESFFPLTEGNLHTIQSLCPFLSKEEKKEFSAQCIPALLGWTKKDLCSTNGGFGHLAIFNSCLQTKSIDDGELLHGILKIIISWKKEHEDIFLFSCNLSEASPEVLGVNIEIIRFLSLFLKYCSSPLAESEWDFIMCSMLAWLETTSENQALYSIPLVQLFACVSCDLACDLSAFFDSTTLDTIGNLPVNLISEWKEFFSQGIHSLLLPILVTVTGENKDVSETSFQNAMLKPMCETLTYISKEQLLSHKLPARLVADQKTNLPEYLQTLLNTLAPLLLFRARPVQIAVYHMLYKLMPELPQYDQDNLKSYGDEEEEPALSPPAALMSLLSIQEDLLENVLGCIPVGQIVTIKPLSEDFCYVLGYLLTWKLILTFFKAASSQLRALYSMYLRKTKSLNKLLYHLFRLMPENPTYAETAVEVPNKDPKTFFTEELQLSIRETTMLPYHIPHLACSVYHMTLKDLPAMVRLWWNSSEKRVFNIVDRFTSKYVSSVLSFQEISSVQTSTQLFNGMTVKARATTREVMATYTIEDIVIELIIQLPSNYPLGSIIVESGKRVGVAVQQWRNWMLQLSTYLTHQNGSIMEGLALWKNNVDKRFEGVEDCMICFSVIHGFNYSLPKKACRTCKKKFHSACLYKWFTSSNKSTCPLCRETFF
|
2.3.2.27
| null |
protein autoubiquitination [GO:0051865]; rescue of stalled ribosome [GO:0072344]; ribosome-associated ubiquitin-dependent protein catabolic process [GO:1990116]
|
cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; RQC complex [GO:1990112]
|
ribosomal large subunit binding [GO:0043023]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
| null |
1.25.10.10;3.30.40.10;
|
LTN1 family
|
PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:Q6A009}.
|
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:28757607}.
|
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:0000305|PubMed:25578875};
| null |
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:25578875}.
| null | null |
FUNCTION: E3 ubiquitin-protein ligase component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation (PubMed:23685075, PubMed:25132172, PubMed:25578875, PubMed:28757607). Within the RQC complex, LTN1 is recruited to stalled 60S ribosomal subunits by NEMF and mediates ubiquitination of stalled nascent chains (PubMed:25578875). Ubiquitination leads to VCP/p97 recruitment for extraction and degradation of the incomplete translation product (By similarity). {ECO:0000250|UniProtKB:Q04781, ECO:0000269|PubMed:23685075, ECO:0000269|PubMed:25132172, ECO:0000269|PubMed:25578875, ECO:0000269|PubMed:28757607}.
|
Homo sapiens (Human)
|
O94823
|
AT10B_HUMAN
|
MALSVDSSWHRWQWRVRDGFPHCPSETTPLLSPEKGRQSYNLTQQRVVFPNNSIFHQDWEEVSRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFLPSALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNIAEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLETPKELDSDGEEWTQYQCLSFSARWAQDPATMRSQKGAQPLRRSQSARVPIQGHYRQRSMGHRESSQPPVAFSSSIEKDVTPDKNLLTKVRDAALWLETLSDSRPAKASLSTTSSIADFFLALTICNSVMVSTTTEPRQRVTIKPSSKALGTSLEKIQQLFQKLKLLSLSQSFSSTAPSDTDLGESLGANVATTDSDERDDASVCSGGDSTDDGGYRSSMWDQGDILESGSGTSLEEALEAPATDLARPEFCYEAESPDEAALVHAAHAYSFTLVSRTPEQVTVRLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHPLTGEIVVYTKGADSVIMDLLEDPACVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIAKKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDTIATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEELKQFRELQKPDRKLFGFRLPSKTPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQYCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQAVMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSSTMIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMVDAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTIFHGVVLLGSFLMYFLVSLLYNATCVICNSPTNPYWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQGTCGKSLISKAQKIDKLPPDKRNLEIQSWRSRQRPAPVPEVARPTHHPVSSITGQDFSASTPKSSNPPKRKHVEESVLHEQRCGTECMRDDSCSGDSSAQLSSGEHLLGPNRIMAYSRGQTDMCRCSKRSSHRRSQSSLTI
|
7.6.2.1
|
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9Y2Q0};
|
lysosomal membrane organization [GO:0097212]; phospholipid translocation [GO:0045332]
|
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; phospholipid-translocating ATPase complex [GO:1990531]; plasma membrane [GO:0005886]
|
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; glycosylceramide flippase activity [GO:0140351]; magnesium ion binding [GO:0000287]; phosphatidylcholine flippase activity [GO:0140345]
|
PF13246;PF16212;PF16209;
|
3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000;
|
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IV subfamily
|
PTM: Autophosphorylated at the conserved aspartate of the P-type ATPase signature sequence. {ECO:0000269|PubMed:32172343}.
|
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:32172343}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:25947375, ECO:0000269|PubMed:32172343}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25947375}; Multi-pass membrane protein {ECO:0000255}. Note=Exit from the endoplasmic reticulum requires the presence of TMEM30A, but not TMEM30B.
|
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000269|PubMed:32172343}; CATALYTIC ACTIVITY: Reaction=a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:66036, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:22801, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:32172343}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66037; Evidence={ECO:0000305|PubMed:32172343};
| null | null | null | null |
FUNCTION: Catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of lysosome membranes. Plays an important role in the maintenance of lysosome membrane integrity and function in cortical neurons. {ECO:0000269|PubMed:32172343}.
|
Homo sapiens (Human)
|
O94826
|
TOM70_HUMAN
|
MAASKPVEAAVVAAAVPSSGSGVGGGGTAGPGTGGLPRWQLALAVGAPLLLGAGAIYLWSRQQRRREARGRGDASGLKRNSERKTPEGRASPAPGSGHPEGPGAHLDMNSLDRAQAAKNKGNKYFKAGKYEQAIQCYTEAISLCPTEKNVDLSTFYQNRAAAFEQLQKWKEVAQDCTKAVELNPKYVKALFRRAKAHEKLDNKKECLEDVTAVCILEGFQNQQSMLLADKVLKLLGKEKAKEKYKNREPLMPSPQFIKSYFSSFTDDIISQPMLKGEKSDEDKDKEGEALEVKENSGYLKAKQYMEEENYDKIISECSKEIDAEGKYMAEALLLRATFYLLIGNANAAKPDLDKVISLKEANVKLRANALIKRGSMYMQQQQPLLSTQDFNMAADIDPQNADVYHHRGQLKILLDQVEEAVADFDECIRLRPESALAQAQKCFALYRQAYTGNNSSQIQAAMKGFEEVIKKFPRCAEGYALYAQALTDQQQFGKADEMYDKCIDLEPDNATTYVHKGLLQLQWKQDLDRGLELISKAIEIDNKCDFAYETMGTIEVQRGNMEKAIDMFNKAINLAKSEMEMAHLYSLCDAAHAQTEVAKKYGLKPPTL
| null | null |
activation of innate immune response [GO:0002218]; cellular response to virus [GO:0098586]; negative regulation of cell growth involved in cardiac muscle cell development [GO:0061052]; positive regulation of defense response to virus by host [GO:0002230]; positive regulation of interferon-beta production [GO:0032728]; positive regulation of protein targeting to mitochondrion [GO:1903955]; protein import into mitochondrial matrix [GO:0030150]; protein insertion into mitochondrial inner membrane [GO:0045039]; protein insertion into mitochondrial outer membrane [GO:0045040]; protein targeting to mitochondrion [GO:0006626]; regulation of apoptotic process [GO:0042981]; response to thyroxine [GO:0097068]
|
extracellular exosome [GO:0070062]; membrane [GO:0016020]; mitochondrial membrane [GO:0031966]; mitochondrial outer membrane [GO:0005741]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739]; TOM complex [GO:0140596]
|
mitochondrion targeting sequence binding [GO:0030943]; molecular adaptor activity [GO:0060090]; protein transmembrane transporter activity [GO:0008320]
|
PF00515;PF13181;
|
1.25.40.10;
|
Tom70 family
| null |
SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:33723040}; Single-pass membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: Note=(Microbial infection) During parasite T.gondii-mediated infection, enriched at the interface between the host mitochondria and the parasitopharous vacuole. {ECO:0000269|PubMed:33723040}.
| null | null | null | null | null |
FUNCTION: Acts as a receptor of the preprotein translocase complex of the outer mitochondrial membrane (TOM complex) (PubMed:12526792). Recognizes and mediates the translocation of mitochondrial preproteins from the cytosol into the mitochondria in a chaperone dependent manner (PubMed:12526792, PubMed:35025629). Mediates TBK1 and IRF3 activation induced by MAVS in response to Sendai virus infection and promotes host antiviral responses during virus infection (PubMed:20628368, PubMed:25609812, PubMed:32728199). Upon Sendai virus infection, recruits HSP90AA1:IRF3:BAX in mitochondrion and the complex induces apoptosis (PubMed:25609812). {ECO:0000269|PubMed:12526792, ECO:0000269|PubMed:20628368, ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:32728199, ECO:0000269|PubMed:35025629}.
|
Homo sapiens (Human)
|
O94827
|
PKHG5_HUMAN
|
MHYDGHVRFDLPPQGSVLARNVSTRSCPPRTSPAVDLEEEEEESSVDGKGDRKSTGLKLSKKKARRRHTDDPSKECFTLKFDLNVDIETEIVPAMKKKSLGEVLLPVFERKGIALGKVDIYLDQSNTPLSLTFEAYRFGGHYLRVKAPAKPGDEGKVEQGMKDSKSLSLPILRPAGTGPPALERVDAQSRRESLDILAPGRRRKNMSEFLGEASIPGQEPPTPSSCSLPSGSSGSTNTGDSWKNRAASRFSGFFSSGPSTSAFGREVDKMEQLEGKLHTYSLFGLPRLPRGLRFDHDSWEEEYDEDEDEDNACLRLEDSWRELIDGHEKLTRRQCHQQEAVWELLHTEASYIRKLRVIINLFLCCLLNLQESGLLCEVEAERLFSNIPEIAQLHRRLWASVMAPVLEKARRTRALLQPGDFLKGFKMFGSLFKPYIRYCMEEEGCMEYMRGLLRDNDLFRAYITWAEKHPQCQRLKLSDMLAKPHQRLTKYPLLLKSVLRKTEEPRAKEAVVAMIGSVERFIHHVNACMRQRQERQRLAAVVSRIDAYEVVESSSDEVDKLLKEFLHLDLTAPIPGASPEETRQLLLEGSLRMKEGKDSKMDVYCFLFTDLLLVTKAVKKAERTRVIRPPLLVDKIVCRELRDPGSFLLIYLNEFHSAVGAYTFQASGQALCRGWVDTIYNAQNQLQQLRAQEPPGSQQPLQSLEEEEDEQEEEEEEEEEEEEGEDSGTSAASSPTIMRKSSGSPDSQHCASDGSTETLAMVVVEPGDTLSSPEFDSGPFSSQSDETSLSTTASSATPTSELLPLGPVDGRSCSMDSAYGTLSPTSLQDFVAPGPMAELVPRAPESPRVPSPPPSPRLRRRTPVQLLSCPPHLLKSKSEASLLQLLAGAGTHGTPSAPSRSLSELCLAVPAPGIRTQGSPQEAGPSWDCRGAPSPGSGPGLVGCLAGEPAGSHRKRCGDLPSGASPRVQPEPPPGVSAQHRKLTLAQLYRIRTTLLLNSTLTASEV
| null | null |
endothelial cell chemotaxis [GO:0035767]; endothelial cell migration [GO:0043542]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; regulation of small GTPase mediated signal transduction [GO:0051056]; Rho protein signal transduction [GO:0007266]
|
axon [GO:0030424]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; lamellipodium [GO:0030027]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]
|
guanyl-nucleotide exchange factor activity [GO:0005085]
|
PF00621;
|
1.20.900.10;2.30.29.30;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q66T02}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q66T02}. Cell membrane {ECO:0000250|UniProtKB:Q66T02}. Cell junction {ECO:0000250|UniProtKB:Q66T02}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q66T02}. Note=Predominantly cytoplasmic, however when endothelial cells are stimulated with lysophosphatidic acid, PLEKHG5 is found in perinuclear regions and at the cell membrane. Localizes at cell-cell junctions in quiescent endothelial cells, and relocalizes to cytoplasmic vesicle and the leading edge of lamellipodia in migrating endothelial cells. {ECO:0000250|UniProtKB:Q66T02}.
| null | null | null | null | null |
FUNCTION: Functions as a guanine exchange factor (GEF) for RAB26 and thus regulates autophagy of synaptic vesicles in axon terminal of motoneurons (By similarity). Involved in the control of neuronal cell differentiation (PubMed:11704860). Plays a role in angiogenesis through regulation of endothelial cells chemotaxis. Affects also the migration, adhesion, and matrix/bone degradation in macrophages and osteoclasts (PubMed:23777631). {ECO:0000250|UniProtKB:Q66T02, ECO:0000269|PubMed:11704860, ECO:0000269|PubMed:23777631}.
|
Homo sapiens (Human)
|
O94829
|
IPO13_HUMAN
|
MERREEQPGAAGAGAAPALDFTVENVEKALHQLYYDPNIENKNLAQKWLMQAQVSPQAWHFSWQLLQPDKVPEIQYFGASALHIKISRYWSDIPTDQYESLKAQLFTQITRFASGSKIVLTRLCVALASLALSMMPDAWPCAVADMVRLFQAEDSPVDGQGRCLALLELLTVLPEEFQTSRLPQYRKGLVRTSLAVECGAVFPLLEQLLQQPSSPSCVRQKVLKCFSSWVQLEVPLQDCEALIQAAFAALQDSELFDSSVEAIVNAISQPDAQRYVNTLLKLIPLVLGLQEQLRQAVQNGDMETSHGICRIAVALGENHSRALLDQVEHWQSFLALVNMIMFCTGIPGHYPVNETTSSLTLTFWYTLQDDILSFEAEKQAVYQQVYRPVYFQLVDVLLHKAQFPSDEEYGFWSSDEKEQFRIYRVDISDTLMYVYEMLGAELLSNLYDKLGRLLTSSEEPYSWQHTEALLYGFQSIAETIDVNYSDVVPGLIGLIPRISISNVQLADTVMFTIGALSEWLADHPVMINSVLPLVLHALGNPELSVSSVSTLKKICRECKYDLPPYAANIVAVSQDVLMKQIHKTSQCMWLMQALGFLLSALQVEEILKNLHSLISPYIQQLEKLAEEIPNPSNKLAIVHILGLLSNLFTTLDISHHEDDHEGPELRKLPVPQGPNPVVVVLQQVFQLIQKVLSKWLNDAQVVEAVCAIFEKSVKTLLDDFAPMVPQLCEMLGRMYSTIPQASALDLTRQLVHIFAHEPAHFPPIEALFLLVTSVTLTLFQQGPRDHPDIVDSFMQLLAQALKRKPDLFLCERLDVKAVFQCAVLALKFPEAPTVKASCGFFTELLPRCGEVESVGKVVQEDGRMLLIAVLEAIGGQASRSLMDCFADILFALNKHCFSLLSMWIKEALQPPGFPSARLSPEQKDTFSQQILRERVNKRRVKEMVKEFTLLCRGLHGTDYTADY
| null | null |
protein import into nucleus [GO:0006606]
|
cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
small GTPase binding [GO:0031267]
|
PF03810;PF18773;PF18786;PF18806;PF08389;
|
1.25.10.10;
|
Importin beta family
| null |
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
| null | null | null | null | null |
FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Is thought to mediate docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to nucleoporin and the complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, Ran binds to the importin, the importin/substrate complex dissociates and importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus (By similarity). Mediates the nuclear import of UBC9, the RBM8A/MAGOH complex, PAX6 and probably other members of the paired homeobox family. Also mediates nuclear export of eIF-1A, and the cytoplasmic release of eIF-1A is triggered by the loading of import substrates onto IPO13. {ECO:0000250, ECO:0000269|PubMed:11447110, ECO:0000269|PubMed:15143176}.
|
Homo sapiens (Human)
|
O94830
|
DDHD2_HUMAN
|
MSSVQSQQEQLSQSDPSPSPNSCSSFELIDMDAGSLYEPVSPHWFYCKIIDSKETWIPFNSEDSQQLEEAYSSGKGCNGRVVPTDGGRYDVHLGERMRYAVYWDELASEVRRCTWFYKGDKDNKYVPYSESFSQVLEETYMLAVTLDEWKKKLESPNREIIILHNPKLMVHYQPVAGSDDWGSTPTEQGRPRTVKRGVENISVDIHCGEPLQIDHLVFVVHGIGPACDLRFRSIVQCVNDFRSVSLNLLQTHFKKAQENQQIGRVEFLPVNWHSPLHSTGVDVDLQRITLPSINRLRHFTNDTILDVFFYNSPTYCQTIVDTVASEMNRIYTLFLQRNPDFKGGVSIAGHSLGSLILFDILTNQKDSLGDIDSEKDSLNIVMDQGDTPTLEEDLKKLQLSEFFDIFEKEKVDKEALALCTDRDLQEIGIPLGPRKKILNYFSTRKNSMGIKRPAPQPASGANIPKESEFCSSSNTRNGDYLDVGIGQVSVKYPRLIYKPEIFFAFGSPIGMFLTVRGLKRIDPNYRFPTCKGFFNIYHPFDPVAYRIEPMVVPGVEFEPMLIPHHKGRKRMHLELREGLTRMSMDLKNNLLGSLRMAWKSFTRAPYPALQASETPEETEAEPESTSEKPSDVNTEETSVAVKEEVLPINVGMLNGGQRIDYVLQEKPIESFNEYLFALQSHLCYWESEDTVLLVLKEIYQTQGIFLDQPLQ
|
3.1.1.-
| null |
lipid droplet organization [GO:0034389]; locomotory behavior [GO:0007626]; mitochondrial fission [GO:0000266]; positive regulation of mitochondrial fission [GO:0090141]; triglyceride catabolic process [GO:0019433]; visual learning [GO:0008542]
|
centriolar satellite [GO:0034451]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytosol [GO:0005829]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]
|
metal ion binding [GO:0046872]; phospholipase activity [GO:0004620]; triglyceride lipase activity [GO:0004806]
|
PF02862;PF00536;PF02825;
|
1.10.150.50;
|
PA-PLA1 family
| null |
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum-Golgi intermediate compartment. Golgi apparatus, cis-Golgi network. Note=Cycles between the Golgi apparatus and the cytosol. DDHD2 recruitment to the Golgi/endoplasmic reticulum-Golgi intermediate compartment (ERGIC) is regulated by the levels of phosphoinositides, including PI(4)P.
|
CATALYTIC ACTIVITY: Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+); Xref=Rhea:RHEA:45128, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:74546, ChEBI:CHEBI:77593; Evidence={ECO:0000269|PubMed:22922100}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45129; Evidence={ECO:0000305|PubMed:22922100}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H(+) + hexadecanoate; Xref=Rhea:RHEA:40943, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:64839, ChEBI:CHEBI:77593; Evidence={ECO:0000269|PubMed:11788596}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40944; Evidence={ECO:0000305|PubMed:11788596}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine + H(+) + hexadecanoate; Xref=Rhea:RHEA:45132, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73007, ChEBI:CHEBI:76088; Evidence={ECO:0000269|PubMed:11788596}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45133; Evidence={ECO:0000305|PubMed:11788596}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phospho-L-serine + H(+) + hexadecanoate; Xref=Rhea:RHEA:43968, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75029, ChEBI:CHEBI:77342; Evidence={ECO:0000269|PubMed:11788596}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43969; Evidence={ECO:0000305|PubMed:11788596}; CATALYTIC ACTIVITY: Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate; Xref=Rhea:RHEA:38783, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:73001, ChEBI:CHEBI:76071; Evidence={ECO:0000269|PubMed:11788596}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38784; Evidence={ECO:0000305|PubMed:11788596};
| null | null | null | null |
FUNCTION: Phospholipase that hydrolyzes preferentially phosphatidic acid, including 1,2-dioleoyl-sn-phosphatidic acid, and phosphatidylethanolamine. Specifically binds to phosphatidylinositol 3-phosphate (PI(3)P), phosphatidylinositol 4-phosphate (PI(4)P), phosphatidylinositol 5-phosphate (PI(5)P) and possibly phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2). May be involved in the maintenance of the endoplasmic reticulum and/or Golgi structures. May regulate the transport between Golgi apparatus and plasma membrane. {ECO:0000269|PubMed:11788596, ECO:0000269|PubMed:20932832, ECO:0000269|PubMed:22922100}.
|
Homo sapiens (Human)
|
O94832
|
MYO1D_HUMAN
|
MAEQESLEFGKADFVLMDTVSMPEFMANLRLRFEKGRIYTFIGEVVVSVNPYKLLNIYGRDTIEQYKGRELYERPPHLFAIADAAYKAMKRRSKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIVQQPGERSFHSFYQLLQGGSEQMLRSLHLQKSLSSYNYIHVGAQLKSSINDAAEFRVVADAMKVIGFKPEEIQTVYKILAAILHLGNLKFVVDGDTPLIENGKVVSIIAELLSTKTDMVEKALLYRTVATGRDIIDKQHTEQEASYGRDAFAKAIYERLFCWIVTRINDIIEVKNYDTTIHGKNTVIGVLDIYGFEIFDNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIIAILDDACMNVGKVTDEMFLEALNSKLGKHAHFSSRKLCASDKILEFDRDFRIRHYAGDVVYSVIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERCGFQDDVAYGKTKIFIRTPRTLFTLEELRAQMLIRIVLFLQKVWRGTLARMRYKRTKAALTIIRYYRRYKVKSYIHEVARRFHGVKTMRDYGKHVKWPSPPKVLRRFEEALQTIFNRWRASQLIKSIPASDLPQVRAKVAAVEMLKGQRADLGLQRAWEGNYLASKPDTPQTSGTFVPVANELKRKDKYMNVLFSCHVRKVNRFSKVEDRAIFVTDRHLYKMDPTKQYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGELVGVLVNHFKSEKRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPQPDFTKNRSGFILSVPGN
| null | null |
actin filament organization [GO:0007015]; actin filament-based movement [GO:0030048]; cellular localization [GO:0051641]; early endosome to recycling endosome transport [GO:0061502]; endocytosis [GO:0006897]; protein transport [GO:0015031]; vesicle transport along actin filament [GO:0030050]
|
actin cytoskeleton [GO:0015629]; apical dendrite [GO:0097440]; axolemma [GO:0030673]; axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; brush border [GO:0005903]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; early endosome [GO:0005769]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; microvillus [GO:0005902]; myelin sheath [GO:0043209]; myosin complex [GO:0016459]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; smooth endoplasmic reticulum [GO:0005790]
|
actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calcium-dependent protein binding [GO:0048306]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; protein domain specific binding [GO:0019904]
|
PF00612;PF00063;PF06017;
|
1.10.10.820;1.20.5.4820;1.20.58.530;3.40.850.10;1.20.120.720;
|
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
| null |
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q63357}. Perikaryon {ECO:0000250|UniProtKB:Q63357}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q63357}. Early endosome {ECO:0000250|UniProtKB:F1PRN2}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q63357}. Note=Colocalizes with the actin cytoskeleton in the cell cortex close to the apical cell membrane. Colocalizes with cytoplasmic puncta that are reminiscent of transport vesicles. {ECO:0000250|UniProtKB:Q63357}.
| null | null | null | null | null |
FUNCTION: Unconventional myosin that functions as actin-based motor protein with ATPase activity (By similarity). Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (By similarity). Required for normal planar cell polarity in ciliated tracheal cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement in the trachea. Required for normal, polarized cilia organization in brain ependymal epithelial cells (By similarity). {ECO:0000250|UniProtKB:F1PRN2, ECO:0000250|UniProtKB:Q63357}.
|
Homo sapiens (Human)
|
O94842
|
TOX4_HUMAN
|
MEFPGGNDNYLTITGPSHPFLSGAETFHTPSLGDEEFEIPPISLDSDPSLAVSDVVGHFDDLADPSSSQDGSFSAQYGVQTLDMPVGMTHGLMEQGGGLLSGGLTMDLDHSIGTQYSANPPVTIDVPMTDMTSGLMGHSQLTTIDQSELSSQLGLSLGGGTILPPAQSPEDRLSTTPSPTSSLHEDGVEDFRRQLPSQKTVVVEAGKKQKAPKKRKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAAYKDNQECQATVETVELDPAPPSQTPSPPPMATVDPASPAPASIEPPALSPSIVVNSTLSSYVANQASSGAGGQPNITKLIITKQMLPSSITMSQGGMVTVIPATVVTSRGLQLGQTSTATIQPSQQAQIVTRSVLQAAAAAAAAASMQLPPPRLQPPPLQQMPQPPTQQQVTILQQPPPLQAMQQPPPQKVRINLQQQPPPLQIKSVPLPTLKMQTTLVPPTVESSPERPMNNSPEAHTVEAPSPETICEMITDVVPEVESPSQMDVELVSGSPVALSPQPRCVRSGCENPPIVSKDWDNEYCSNECVVKHCRDVFLAWVASRNSNTVVFVK
| null | null |
regulation of transcription by RNA polymerase II [GO:0006357]
|
chromatin [GO:0000785]; nucleus [GO:0005634]; PTW/PP1 phosphatase complex [GO:0072357]
|
chromatin DNA binding [GO:0031490]
|
PF00505;
|
1.10.30.10;
| null | null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:20516061}. Note=Associated with chromatin.
| null | null | null | null | null |
FUNCTION: Transcription factor that modulates cell fate reprogramming from the somatic state to the pluripotent and neuronal fate (By similarity). Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase (PubMed:20516061). In liver, controls the expression of hormone-regulated gluconeogenic genes such as G6PC1 and PCK1. This regulation is independent of the insulin receptor activation (By similarity). {ECO:0000250|UniProtKB:Q8BU11, ECO:0000269|PubMed:20516061}.
|
Homo sapiens (Human)
|
O94844
|
RHBT1_HUMAN
|
MDADMDYERPNVETIKCVVVGDNAVGKTRLICARACNTTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHHKDRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPEKGREVAKELGLPYYETSVFDQFGIKDVFDNAIRAALISRRHLQFWKSHLKKVQKPLLQAPFLPPKAPPPVIKIPECPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESPNGSEGACEKEKQSRDFQGRILSVDPEEEREEGPPRIPQADQWKSSNKSLVEALGLEAEGAVPETQTLTGWSKGFIGMHREMQVNPISKRMGPMTVVRMDASVQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMNQEITKAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAATSGVGIDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREKEDIALNKHRSRRKWCFWNSSPAVA
| null | null |
actin filament organization [GO:0007015]; Cdc42 protein signal transduction [GO:0032488]; cortical cytoskeleton organization [GO:0030865]; endocytosis [GO:0006897]; engulfment of apoptotic cell [GO:0043652]; establishment or maintenance of cell polarity [GO:0007163]; regulation of actin cytoskeleton organization [GO:0032956]; regulation of cell shape [GO:0008360]
|
cell projection [GO:0042995]; cytoskeleton [GO:0005856]; endosome membrane [GO:0010008]; plasma membrane [GO:0005886]
|
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901]
|
PF00651;PF00071;
|
3.40.50.300;
|
Small GTPase superfamily, Rho family
| null | null | null | null | null | null | null | null |
Homo sapiens (Human)
|
O94850
|
DEND_HUMAN
|
MLDGPLFSEGPDSPRELQDEESGSCLWVQKSKLLVIEVKTISCHYSRRAPSRQPMDFQASHWARGFQNRTCGPRPGSPQPPPRRPWASRVLQEATNWRAGPLAEVRAREQEKRKAASQEREAKETERKRRKAGGARRSPPGRPRPEPRNAPRVAQLAGLPAPLRPERLAPVGRAPRPSAQPQSDPGSAWAGPWGGRRPGPPSYEAHLLLRGSAGTAPRRRWDRPPPYVAPPSYEGPHRTLGTKRGPGNSQVPTSSAPAATPARTDGGRTKKRLDPRIYRDVLGAWGLRQGQGLLGGSPGCGAARARPEPGKGVVEKSLGLAAADLNSGSDSHPQAKATGSAGTEIAPAGSATAAPCAPHPAPRSRHHLKGSREGKEGEQIWFPKCWIPSPKKQPPRHSQTLPRPWAPGGTGWRESLGLGEGAGPETLEGWKATRRAHTLPRSSQGLSRGEGVFVIDATCVVIRSQYVPTPRTQQVQLLPSGVTRVVGDSPSQSKPGKEEGEGATVFPSPCQKRLSSSRLLHQPGGGRGGEAEGGRPGDSTLEERTFRILGLPAPEVNLRDAPTQPGSPEHQALGPAASGAQGRAEGSEVAVVQRRAGRGWARTPGPYAGALREAVSRIRRHTAPDSDTDEAEELSVHSGSSDGSDTEAPGASWRNERTLPEVGNSSPEEDGKTAELSDSVGEILDVISQTEEVLFGVRDIRGTQQGNRKRQ
| null | null |
positive regulation of transcription by RNA polymerase II [GO:0045944]
|
cell projection [GO:0042995]; cytoplasm [GO:0005737]; dendritic spine membrane [GO:0032591]; endoplasmic reticulum membrane [GO:0005789]; nucleus [GO:0005634]; perikaryon [GO:0043204]; postsynaptic membrane [GO:0045211]
|
DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]
|
PF15498;
| null | null | null |
SUBCELLULAR LOCATION: Cell projection, dendritic spine membrane; Peripheral membrane protein. Cytoplasm. Endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Perikaryon {ECO:0000250}. Nucleus {ECO:0000250}. Note=Enriched at the cytoplasmic insertion of the slit diaphragm into the foot process of podocytes and associated with polyribosomes in dendrites. {ECO:0000250}.
| null | null | null | null | null |
FUNCTION: Promotes apoptosis of kidney glomerular podocytes. Podocytes are highly specialized cells essential to the ultrafiltration of blood, resulting in the extraction of urine and the retention of protein (By similarity). {ECO:0000250}.
|
Homo sapiens (Human)
|
O94851
|
MICA2_HUMAN
|
MGENEDEKQAQAGQVFENFVQASTCKGTLQAFNILTRHLDLDPLDHRNFYSKLKSKVTTWKAKALWYKLDKRGSHKEYKRGKSCTNTKCLIVGGGPCGLRTAIELAYLGAKVVVVEKRDSFSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGSIDHISIRQLQLILFKVALMLGVEIHVNVEFVKVLEPPEDQENQKIGWRAEFLPTDHSLSEFEFDVIIGADGRRNTLEGFRRKEFRGKLAIAITANFINRNSTAEAKVEEISGVAFIFNQKFFQDLKEETGIDLENIVYYKDCTHYFVMTAKKQSLLDKGVIINDYIDTEMLLCAENVNQDNLLSYAREAADFATNYQLPSLDFAMNHYGQPDVAMFDFTCMYASENAALVRERQAHQLLVALVGDSLLEPFWPMGTGCARGFLAAFDTAWMVKSWNQGTPPLELLAERESLYRLLPQTTPENINKNFEQYTLDPGTRYPNLNSHCVRPHQVKHLYITKELEHYPLERLGSVRRSVNLSRKESDIRPSKLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTGKEMASAQEPDKLSMVMYLSKFYELFRGTPLRPVDSWRKNYGENADLSLAKSSISNNYLNLTFPRKRTPRVDGQTGENDMNKRRRKGFTNLDEPSNFSSRSLGSNQECGSSKEGGNQNKVKSMANQLLAKFEESTRNPSLMKQERRVSGIGKPVLCSSSGPPVHSCCPKPEEATPSPSPPLKRQFPSVVVTGHVLRELKQVSAGSECLSRPWRARAKSDLQLGGTENFATLPSTRPRAQALSGVLWRLQQVEEKILQKRAQNLANREFHTKNIKEKAAHLASMFGHGDFPQNKLLSKGLSHTHPPSPPSRLPSPDPAASSSPSTVDSASPARKEKKSPSGFHFHPSHLRTVHPQLTVGKVSSGIGAAAEVLVNLYMNDHRPKAQATSPDLESMRKSFPLNLGGSDTCYFCKKRVYVMERLSAEGHFFHRECFRCSICATTLRLAAYTFDCDEGKFYCKPHFIHCKTNSKQRKRRAELKQQREEEATWQEQEAPRRDTPTESSCAVAAIGTLEGSPPDEPTSPKRPKSISEPQHSDAEGDAASPLPSEWTSVRISPGEEAAGQDVLAVRVLVTSEDSSSDTESDYGGSEGSHTEPCEEKPWRPGSPHLPHTSLGEALSRAVSPQCPEEPRAVHAALQRANSFQSPTPSKYQNWRREFWWSLTPVNKRTMSPPKDPSPSLPLPSSSSHSSSPPSSSSTSVSGNAPDGSSPPQMTASEPLSQVSRGHPSPPTPNFRRRAVAQGAPREIPLYLPHHPKPEWAEYCLVSPGEDGLSDPAEMTSDECQPAEAPLGDIGSNHRDPHPIWGKDRSWTGQELSPLAGEDREKGSTGARKEEEGGPVLVKEKLGLKKLVLTQEQKTMLLDWNDSIPESVHLKAGERISQKSAENGRGGRVLKPVRPLLLPRAAGEPLPTQRGAQEKMGTPAEQAQGERNVPPPKSPLRLIANAIRRSLEPLLSNSEGGKKAWAKQESKTLPAQACTRSFSLRKTNSNKDGDQHSPGRNQSSAFSPPDPALRTHSLPNRPSKVFPALRSPPCSKIEDVPTLLEKVSLQENFPDASKPPKKRISLFSSLRLKDKSFESFLQESRQRKDIRDLFGSPKRKVLPEDSAQALEKLLQPFKSTSLRQAAPPPPPPPPPPPPPPTAGGADSKNFPLRAQVTEASSSASSTSSSSADEEFDPQLSLQLKEKKTLRRRKKLEKAMKQLVKQEELKRLYKAQAIQRQLEEVEERQRASEIQGVRLEKALRGEADSGTQDEAQLLQEWFKLVLEKNKLMRYESELLIMAQELELEDHQSRLEQKLREKMLKEESQKDEKDLNEEQEVFTELMQVIEQRDKLVDSLEEQRIREKAEDQHFESFVFSRGCQLSRT
|
1.14.13.225
|
COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250|UniProtKB:Q8TDZ2};
|
actin filament depolymerization [GO:0030042]; cytoskeleton organization [GO:0007010]; heart development [GO:0007507]; heart looping [GO:0001947]; positive regulation of transcription by RNA polymerase II [GO:0045944]; sulfur oxidation [GO:0019417]
|
actin filament [GO:0005884]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
|
actin binding [GO:0003779]; FAD binding [GO:0071949]; metal ion binding [GO:0046872]; mitogen-activated protein kinase binding [GO:0051019]; monooxygenase activity [GO:0004497]; NAD(P)H oxidase H2O2-forming activity [GO:0016174]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]
|
PF12130;PF00307;PF01494;PF00412;
|
1.10.418.10;2.10.110.10;3.50.50.60;
|
Mical family
| null |
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24440334}. Cytoplasm {ECO:0000250|UniProtKB:Q8BML1}.
|
CATALYTIC ACTIVITY: Reaction=H(+) + L-methionyl-[F-actin] + NADPH + O2 = H2O + L-methionyl-(R)-S-oxide-[F-actin] + NADP(+); Xref=Rhea:RHEA:51308, Rhea:RHEA-COMP:12953, Rhea:RHEA-COMP:12956, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16044, ChEBI:CHEBI:45764, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.225; Evidence={ECO:0000269|PubMed:24440334, ECO:0000269|PubMed:29343822, ECO:0000269|PubMed:34106209};
| null | null | null | null |
FUNCTION: Methionine monooxygenase that promotes depolymerization of F-actin by mediating oxidation of residues 'Met-44' and 'Met-47' on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization (PubMed:24440334, PubMed:29343822). Regulates the disassembly of branched actin networks also by oxidizing ARP3B-containing ARP2/3 complexes leading to ARP3B dissociation from the network (PubMed:34106209). Acts as a key regulator of the SRF signaling pathway elicited by nerve growth factor and serum: mediates oxidation and subsequent depolymerization of nuclear actin, leading to increase MKL1/MRTF-A presence in the nucleus and promote SRF:MKL1/MRTF-A-dependent gene transcription. Does not activate SRF:MKL1/MRTF-A through RhoA (PubMed:24440334). {ECO:0000269|PubMed:24440334, ECO:0000269|PubMed:29343822, ECO:0000269|PubMed:34106209}.
|
Homo sapiens (Human)
|
O94854
|
K0754_HUMAN
|
MGKPLSRPDCLRRNPSCLGKGEEEDGYIEDCYVPQRSIYDTMRINEQIDQGSKLNQTSKSTMEKMEGSTISSNGTLGAASNVFESRAPEGKKLDERIIFDALKLSSDVQKSAPVPPRRRPNAERKDNVNRRSWKSFMPPNFPEFAERIEASLSEVSEAGASNPSLQEKKESSSALTESSGHLDHREPQSESVTLEHVSKSIGIPEVQDFKNLSGDCQDFRFQQHSANPPHEFQPVESEAVATSGNTDVMQESRFSSATWPRATKSLAKGGFSEKQHPLGDTACTVEMPPLSPCLSEELLDPELHVLITPSLREKTESELKFEEDERWIMMEAEGEWEEEKLSDREKTFLMADEKNSLADIFEEREQANTAVVEDGSDCLAAVLRTFGHLSLGQICCPDDPQPAKDQLATVPKDIPLDCDCVLTGEDILGEVANRTAQGLEGLVSDSACTVGTIDAEQLSDTDSVQMFLELEKECLCEEGVTPLVELQNQISSEGLAASQDAENLLVISHFSGAALEKEQHLGLLHVRAKDYDTRLDCGYFNTLDSSQVPNAVELIAHVDIMRDTSTVSKEECEKVPFSPRTAEFKSRQPADLDSLEKLDPGGLLNSDHRVSHEEKLSGFIASELAKDNGSLSQGDCSQTEGNGEECIERVTFSFAFNHELTDVTSGPEVEVLYESNLLTDEIHLESGNVTVNQENNSLTSMGNVVTCELSVEKVCDEDGEAKELDYQATLLEDQAPAHFHRNFPEQVFQDLQRKSPESEILSLHLLVEELRLNPDGVETVNDTKPELNVASSEGGEMERRDSDSFLNIFPEKQVTKAGNTEPVLEEWIPVLQRPSRTAAVPTVKDALDAALPSPEEGTSIAAVPAPEGTAVVAALVPFPHEDILVASIVSLEEEDVTAAAVSAPERATVPAVTVSVPEGTAAVAAVSSPEETAPAVAAAITQEGMSAVAGFSPEWAALAITVPITEEDGTPEGPVTPATTVHAPEEPDTAAVRVSTPEEPASPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPPPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPTSPAAAVPTPEEPASPAAAVPTPEEPASPAAAVPTPEEPAFPAPAVPTPEESASAAVAVPTPEESASPAAAVPTPAESASFAAVVATLEEPTSPAASVPTPAAMVATLEEFTSPAASVPTSEEPASLAAAVSNPEEPTSPAAAVPTLEEPTSSAAAVLTPEELSSPAASVPTPEEPASPAAAVSNLEEPASPAAAVPTPEVAAIPAASVPTPEVPAIPAAAVPPMEEVSPIGVPFLGVSAHTDSVPISEEGTPVLEEASSTGMWIKEDLDSLVFGIKEVTSTVLHGKVPLAATAGLNSDEMFQKEQVDPLQMKLQQVNGLGQGLIQSAGKDCDVQGLEHDMEEINARWNTLNKKVAQRIAQLQEALLHCGKFQDALEPLLSWLADTEELIANQKPPSAEYKVVKAQIQEQKLLQRLLDDRKATVDMLQAEGGRIAQSAELADREKITGQLESLESRWTELLSKAAARQKQLEDILVLAKQFHETAEPISDFLSVTEKKLANSEPVGTQTAKIQQQIIRHKALNEEIVNRKKNVDQAIKNGQALLKQTTGEEVLLIQEKLDGIKTRYADITVTSSKALRTLEQARQLATKFQSTYEELTGWLREVEEELATSGGQSPTGEQIPQFQQRQKELKKEVMEHRLVLDTVNEVSRALLELVPWRAREGLDKLVSDANEQYKLVSDTIGQRVDEIDAAIQRSQQYEQAADAELAWVAETKRKLMALGPIRLEQDQTTAQLQVQKAFSIDIIRHKDSMDELFSHRSEIFGTCGEEQKTVLQEKTESLIQQYEAISLLNSERYARLERAQVLVNQFWETYEELSPWIEETRALIAQLPSPAIDHEQLRQQQEEMRQLRESIAEHKPHIDKLLKIGPQLKELNPEEGEMVEEKYQKAENMYAQIKEEVRQRALALDEAVSQSTQITEFHDKIEPMLETLENLSSRLRMPPLIPAEVDKIRECISDNKSATVELEKLQPSFEALKRRGEELIGRSQGADKDLAAKEIQDKLDQMVFFWEDIKARAEEREIKFLDVLELAEKFWYDMAALLTTIKDTQDIVHDLESPGIDPSIIKQQVEAAETIKEETDGLHEELEFIRILGADLIFACGETEKPEVRKSIDEMNNAWENLNKTWKERLEKLEDAMQAAVQYQDTLQAMFDWLDNTVIKLCTMPPVGTDLNTVKDQLNEMKEFKVEVYQQQIEMEKLNHQGELMLKKATDETDRDIIREPLTELKHLWENLGEKIAHRQHKLEGALLALGQFQHALEELMSWLTHTEELLDAQRPISGDPKVIEVELAKHHVLKNDVLAHQATVETVNKAGNELLESSAGDDASSLRSRLEAMNQCWESVLQKTEEREQQLQSTLQQAQGFHSEIEDFLLELTRMESQLSASKPTGGLPETAREQLDTHMELYSQLKAKEETYNQLLDKGRLMLLSRDDSGSGSKTEQSVALLEQKWHVVSSKMEERKSKLEEALNLATEFQNSLQEFINWLTLAEQSLNIASPPSLILNTVLSQIEEHKVFANEVNAHRDQIIELDQTGNQLKFLSQKQDVVLIKNLLVSVQSRWEKVVQRSIERGRSLDDARKRAKQFHEAWKKLIDWLEDAESHLDSELEISNDPDKIKLQLSKHKEFQKTLGGKQPVYDTTIRTGRALKEKTLLPEDSQKLDNFLGEVRDKWDTVCGKSVERQHKLEEALLFSGQFMDALQALVDWLYKVEPQLAEDQPVHGDLDLVMNLMDAHKVFQKELGKRTGTVQVLKRSGRELIENSRDDTTWVKGQLQELSTRWDTVCKLSVSKQSRLEQALKQAEVFRDTVHMLLEWLSEAEQTLRFRGALPDDTEALQSLIDTHKEFMKKVEEKRVDVNSAVAMGEVILAVCHPDCITTIKHWITIIRARFEEVLTWAKQHQQRLETALSELVANAELLEELLAWIQWAETTLIQRDQEPIPQNIDRVKALIAEHQTFMEEMTRKQPDVDRVTKTYKRKNIEPTHAPFIEKSRSGGRKSLSQPTPPPMPILSQSEAKNPRINQLSARWQQVWLLALERQRKLNDALDRLEELKEFANFDFDVWRKKYMRWMNHKKSRVMDFFRRIDKDQDGKITRQEFIDGILASKFPTTKLEMTAVADIFDRDGDGYIDYYEFVAALHPNKDAYRPTTDADKIEDEVTRQVAQCKCAKRFQVEQIGENKYRFGDSQQLRLVRILRSTVMVRVGGGWMALDEFLVKNDPCRARGRTNIELREKFILPEGASQGMTPFRSRGRRSKPSSRAASPTRSSSSASQSNHSCTSMPSSPATPASGTKVIPSSGSKLKRPTPTFHSSRTSLAGDTSNSSSPASTGAKTNRADPKKSASRPGSRAGSRAGSRASSRRGSDASDFDLLETQSACSDTSESSAAGGQGNSRRGLNKPSKIPTMSKKTTTASPRTPGPKR
| null | null |
intermediate filament cytoskeleton organization [GO:0045104]; regulation of focal adhesion assembly [GO:0051893]; regulation of microtubule-based process [GO:0032886]; wound healing [GO:0042060]
|
actin cytoskeleton [GO:0015629]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; membrane [GO:0016020]; microtubule [GO:0005874]
|
cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; microtubule binding [GO:0008017]; structural molecule activity [GO:0005198]
|
PF13499;PF02187;PF00435;
|
1.20.58.60;1.10.238.10;3.30.920.20;
| null | null |
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000255|PROSITE-ProRule:PRU00792}.
| null | null | null | null | null | null |
Homo sapiens (Human)
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.