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
MATGFKLPELAPVKSAWGPPETEQIGGDIPYAPFSKGDRLGKIADWSVDQPKDGREQRGRQGAFAGRFRDQYQTYGYGASSIFGYQHSEDESSFSVIDRGSVNRTRTSARNGGTLLKVRGRGQNVQRGGRGGRYGSSGGRGAGDTVVSRSSGAGGARGRRFGWKDYDKHQRLRNASVTVGDDWQLLDEVEFSHLSKLNLAAAAPVTVDSYGYIYPYDKSFDKIHVKSEKPLQALDRVHYNPTTTEDPVIQKLALNSDANIFITDSILSLLMCSTRSVYPWDIVITHQSGKLFFDKREGGPFDYLTVNENAYDSPMDADNR...
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 transla...
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 specifica...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94244
HAT2_SCHPO
MSEEVVQDAPLENNELNAEIDLQKTIQEEYKLWKQNVPFLYDLVITHALEWPSLTIQWLPDKKTIPGTDYSIQRLILGTHTSGNDQNYLQIASVQLPNFDEDTTEFTPSTIRRAQATGSYTIEISQKIPHDGDVNRARYMPQKPEIIATMGEGGNAYIFDTTCHDALTTGEALPQAVLKGHTAEGFGLCWNPNLPGNLATGAEDQVICLWDVQTQSFTSSETKVISPIAKYHRHTDIVNDVQFHPQHEALLASVSDDCTLQIHDTRLNPEEEAPKVIQAHSKAINAVAINPFNDYLLATASADKTVALWDLRNPYQRLHT...
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 f...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94267
SPT16_SCHPO
MAEYEIDEITFHKRLGILLTSWKNEEDGKTLFQDCDSILVTVGAHDDTNPYQKSTALHTWLLGYEFPSTLILLEKHRITILTSVNKANMLTKLAETKGAAADVNILKRTKDAEENKKLFEKIIEYIRATNKKVGVFPKDKTQGKFINEWDSIFEPVKSEFNLVDASLGLAKCLAIKDEQELANIKGASRVSVAVMSKYFVDELSTYIDQGKKITHSKFSDQMESLIDNEAFFQTKSLKLGDIDLDQLEWCYTPIIQSGGSYDLKPSAITDDRNLHGDVVLCSLGFRYKSYCSNVGRTYLFDPDSEQQKNYSFLVALQKKL...
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 elon...
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...
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 ...
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
MSNKLCQLCNERRPALVRPKTGQKICKECFYYVFETEIHNVIIENKLFVRGERVGIGASGGKDSTVLAYVMKLLNERYDYGLELYLISVDEGIRGYRDDSLDTVKRNQQQYGLPMKIVSYADLYDGWTMDNVVARIGTKNNCTYCGVFRRQALDRAALSLDIHHLVTGHNADDIAETILMNLLRGDVARLPRSTEITTQSDSSPTKRSKPFKYSYEKEIVLYAHYKKLDYFSTECTYSPEAFRGTARAMIKQLENIRPSSILDIIYSGESMQLASSVQEQLPQQTTCERCGFISSNRICKACMLLEGLNKGITGLGLGSD...
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 f...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94284
HMT2_SCHPO
MLTLNSTIKSVTGSFQSASMLARFASTHHKVLVVGGGSAGISVAHQIYNKFSKYRFANDQGKDTSLKPGEIGIVDGAKYHYYQPGWTLTGAGLSSVAKTRRELASLVPADKFKLHPEFVKSLHPRENKIVTQSGQEISYDYLVMAAGIYTDFGRIKGLTEALDDPNTPVVTIYSEKYADAVYPWIEKTKSGNAIFTQPSGVLKCAGAPQKIMWMAEDYWRRHKVRSNIDVSFYTGMPTLFSVKRYSDALLRQNEQLHRNVKINYKDELVEVKGSERKAVFKNLNDGSLFERPFDLLHAVPSMRSHEFIAKSDLADKSGFV...
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
MARDVDNKQNAKRISRDEDEDEFAGESMVGRTLDNPFLGEDEFEDIFGSESQYISSSGQNSTNPFLADTRIENSPLGSESKANQLNKQGTNVNHIEIPLRDFNDPTQPESFLPPPKNTFTSRIKKIKNLFKKEKKQVKPEDLGPRQIILNDYSANHFLHNAVSTCKYSAFTFLPKFLKEQFSKYANLFFLFTAVVQQIPGITPVNRYTTIGPMLIVLSVSGIKEIMEDIKRKKQDQELNESPCYVLQGTGFVEKQWKDVVVGDIVKIVSETFFPADLVLLSSSEPEGLCYIETANLDGETNLKIKQALPETAGLLKPVEL...
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 [...
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; Xr...
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....
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94313
CARB_SCHPO
MALWATSMRRAIPGISKAFLGSNRVLETAGVSQLSKHLLPQWSGVPHRKISASATNFNDKVKESNTPDANAYIRSGHIKAAEHEKVKKVVVVGSGGLSIGQAGEFDYSGAQAIKALRESSVHTILINPNIATIQSSHSLADEIYFLPVTAEYLTHLIERENPDGILLTFGGQTALNVGIQLDDMGVFARNHVKVLGTPISTLKTSEDRDLFAKALNEINIPIAESVAVSTVDEALQAAEKVSYPVIIRSAYSLGGLGSGFANNKEELQSMAAKSLSLTPQILVEKSLKGWKEVEYEVVRDAANNCITVCNMENFDPLGIH...
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...
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)...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94316
SN114_SCHPO
MMEEDLYDEFGNYIGPENEEDEEELFPQAPSPTIAQVPSFEEVIPDEELEDVERAEEMALSHLEPQNAVVLHEDKQYYPSAEEVYGSNVDIMVQEQDTQPLSQPIIEPIRHKRIAIETTNVPDTVYKKEFLFGLLTGTDDVRSFIVAGHLHHGKSALLDLLVYYTHPDTKPPKRRSLRYTDTHYLERERVMSIKSTPLTLAVSDMKGKTFAFQCIDTPGHVDFVDEVAAPMAISDGVVLVVDVIEGVMINTTRIIKHAILHDMPIVLVLNKVDRLILELRLPPNDAYHKLRHVIDEVNDNICQISKDLKYRVSPELGNVC...
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 l...
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
MKRGKCKEKDNGLKRISSESEVWNFLDVTVSELNKQKRSPGQTVSKRLHKKQRVVSNPDLSLPSSPVKQILRNGLQNSKYGSHKTGLERSASCSSIDASANHSSTTYREQRSYLMEEGLDTQPIVPREVSSGRELDSTNHTIGTERAFLIEEDVSEDDEIQMKSIHELRFAGEQQRIVDEIEYLVDGVTFSGNSSASRYLSLIGIAEKMFDNSFRLCLKSIRDVFLRIFEEIDPKDTLHTFLQIYIFATMANEMDCMSSLLDAYSNNVKLLLQTAITLEPQVPVSILAKSLPKSVKGAVQEFVIKAELTFSFSNESLASS...
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
MESRYLSDRRSRFKSKGVFKADELRRQREEQQIEIRKQKREESLNKRRNLNAVLQNDIDVEEEADQSQVQMEQQMKDEFPKLTADVMSDDIELQLGAVTKFRKYLSKETHPPIDQVIACGVVDRFVQFLESEHHLLQFEAAWALTNIASGTTDQTRIVVDSGAVPRFIQLLSSPEKDVREQVVWALGNIAGDSSACRDYVLGNGVLQPLLNILQSSASDVSMLRNATWTLSNLCRGKNPPPNWSTISVAVPILAKLLYSEDVEIIVDACWAISYLSDGPNEKIGAILDVGCAPRLVELLSSPSVNIQTPALRSVGNIVTG...
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 ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94383
SMC1_SCHPO
MGRLLRLEVENFKSYRGHQIIGPFEDFTSIIGPNGAGKSNLMDAISFVLGVKSSHLRSTNVKELIYRGKILQRDNTDFTDSSNPTTAYVKLMYELDNGEQREYKRAITPSGATEYKIDEEIVTFSEYCGSLQKENILVRARNFLVFQGDVETIASQSPLELSKLVEQISGSLEYKSEYDKSKDEQDKAVNLSAHSFNKKRGINAELRQYQEQKTEAERYQSQKEKRDSAQLVYLLWKLFHLEKSISSNMAEVTRLKADSIQLIERRDENTKEIEKLKEKEGSIRRNLLAFDRKVRKQEKLIASKRPELISIAEKALESKS...
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, all...
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....
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94395
KU70_SCHPO
MENDEQIDETENFAIGKYAILFVIEVSPSMLDPVDEFTPSSLQMALICAYQLAAQRVITNPSDIMGVLLYGTESSTGRFANQMMLLDIDPPDAERIKSLQSFEKDFQFSKEKFKPCSCQVSLSSVLYHCSVIFTTKAENFEKRLFLITDNDHPAWDATERDIILQRAKDLRDLDIQVHPVFLDPPTHSFRINIFYSDFLYIVYGRQDVSNLVNRGQAQLQHMLNMITALQKPKRAHFHLKMDLGNDVRIGVEAFILLKRLESAKTNWVYAKGERFAVAVPQSKQVSFATKKELKKDEIRRSYSYGGSSVVFGSDELNKVR...
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 ther...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94396
PUS1_SCHPO
MGRGGKRTWYNGDRREAKRNRPNSIYNGEGRPENLVVGEKKPKRKVACLVGYCGSGYHGMQLNPPSKTIEGDLFDAFVKAGAVSSYNADDPKKVALARAARTDKGVHAAGNVISLKLIMEDEKLIEKVNEHLPPSIRLWDVIRTINSFNPRTYCESRIYEYMVPTYAFVPPKPSSILGNCIMKNSPMPAEPINKENINQLSRSLFYEEGKEFWDDYDIAAKEILSLYEQDPEGFVNPYSKRGAAALANSENNKGSEAGVSAKTNPDMDSDSSAIVNEFLKPDSVEDESAGSKIDPSYRLERALKHIEVLKLKNYRISADR...
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:RHE...
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). Al...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94399
TWF1_SCHPO
MSASVELKPTEKFSKFLEEYSSVPVRAAIISISNENSFDVKTMVEKSESIESDFKKVRECLLGSEEPAFVLVYDDSKKNLLQLISYVPENANVRRKMLYASSRAAFVRCVTLAKLDESYFASTPEELDYQQIMKSLSKQEDQSPLRQDELERKEYNESMQSSVTHKRPLVTRGVAMSIDDKALKALSDLKSSTENNLVILSIDKEVISLSQEKQNIPPSDVKSFFSSTEPNFAFYSLPKDGSSKILFIYICPMQATVKHRMVYSSSKLGLLDSIKAELGIVIDGKIESNDAADITEKEILHAAGISSPQAETSTTKTGFS...
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]; s...
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
MFAVQGNQKFPKGLTKDNIQSLYQQWQVMRNQGATEENNPEFAQISSILRMVQRAHYARMQQMRNQSSEFPDAENTNLRKQQDTLPTTGFNNLPEGKAGMQTLPGRPASNGPTPPNPGNGNVGLNNPSYMNSQASPNIMNAPLQRDTSVPPAPSMVHPHTNTNANSNNLKVYANQLSQQNTSNPTYHNAYDMASMMKNGSRMNNSFPPTTPYPPANDTTVNSSLPHSFASPSSTFEQPHTVQSRAPSVDTTSSSHSFSARNIPANVSMQQQMGRRGSIPVNPSTFSASSPPSGSMLASPYNGYQNDAASFAHSKLPSSAN...
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 nuc...
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...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94446
ESA1_SCHPO
MSNDVDDESKIETKSYEAKDIVYKSKVFAFKDGEYRKAEILMIQKRTRGVVYYVHYNDYNKRLDEWITIDNIDLSKGIEYPPPEKPKKAHGKGKSSKRPKAVDRRRSITAPSKTEPSTPSTEKPEPSTPSGESDHGSNAGNESLPLLEEDHKPESLSKEQEVERLRFSGSMVQNPHEIARIRNINKICIGDHEIEPWYFSPYPKEFSEVDIVYICSFCFCYYGSERQFQRHREKCTLQHPPGNEIYRDDYISFFEIDGRKQRTWCRNICLLSKLFLDHKMLYYDVDPFLFYCMCRRDEYGCHLVGYFSKEKESSENYNLA...
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 poly...
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 activit...
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) (Pu...
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}; P...
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, H4K12a...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94449
RFC4_SCHPO
MSNAVSSSVFGEKNNSVAYELPWVEKYRPIVLDDIVGNEETIDRLKVIAKEGNMPHLVISGMPGIGKTTSILCLAHALLGPAYKEGVLELNASDERGIDVVRNRIKAFAQKKVILPPGRHKIIILDEADSMTAGAQQALRRTMEIYSNTTRFALACNQSNKIIEPIQSRCAILRYSRLTDQQVLQRLLNICKAEKVNYTDDGLAALIMTAEGDMRQAVNNLQSTVAGFGLVNGENVFRVADQPSPVAIHAMLTACQSGNIDVALEKLQGIWDLGFSAVDIVTNMFRVVKTMDSIPEFSRLEMLKEIGQTHMIILEGVQTL...
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
MNQANFLQELPNVLKRLETGLIIPQLKDILRVFGLRLSGTKAELITRIKQLIERIAIENNTTSWEALKKAIDGDVTSAVCILKYNTYQIYSAAAPIAPPSSASGNRSYSRPFAPVVHSRIRFRKSPFYDILEQFNAPFVVPACVGTRNTISFSFHVTPPALSKLLNDPKQYRVYLFSTPSETIGFGNCLMEFPTPQMELRINNQVAHANYRRLKGKPGTTNPADITDLVSKYAGPPGNNVVIYYMNSTKSYSVVVCFVKVYTIENLVDQIKSRKAESKEKIIERIKNDNQDADIIATSTDISLKCPLSFSRISLPVRSVF...
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 localiz...
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, Ch...
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 invo...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94459
SCC4_SCHPO
MTGLNETDARILVTSRHLFLWPLAETYFKNAEKVLQDCGVCDSFGRLLSTGLQCLYSVLMDTKMEPRVELLTRKRICEVLLSHTVEYADVEAILNRALIIAEQHNLTEYKFSLQLLLSRVFCRTSPKAAKVLLTRCVREAEEYAKVAEIYHSNNQSNPHRWVYEFLLATLEFQNVSQVANSIHNYANHHKHQHLQLLAMILNQSLPMDEISTDSDQISILCLVTQIAQCLRKGEILLAREILPKIHSKLESETFVWPSSYIDFFIDDTSKISIKWMSINQLYLLIYLISGFCYISDSTSGRASRFLQEGLRITGDFKHQE...
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
MLSAPSSSTTPASPPTSPPNTTSSDDFAVLKEPKVEAILNSELGLAILNDRIKDYLLTCKELAGFFKKRSILEEESGKNLQKLAKSYLETFQSKHHSPQSFSASVITSMEIHEQLANHSLTLQKTLSAFSDQVIEFHKNAERKRKSIKEYAKKQENAYLEAVMQMDKSKSRFKGAETEYNRALDNKNTGDSQKKVGFFKPKSNAQLTKLEDEARLKAENAESDMHSKIENAQNVQKQLLCIHRPNYIKQFFSLQREIESSLIANYLRYTKLCESNTLLNGLTIRPQKPTPTNCGLQHALDNINANTDFVQYVLHASIKHE...
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:000716...
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...
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
MTSGIYYKGLQCWIPDEQSQWIPGSIKDCRVEGEKAFLTVQDENENETVITVKPDDLNYEGRNGLPFLRSINSDADDLTDLSYLNEPSVLDALSTRYNQLQIYTYSGIVLIAVNPFQRLPNLYTHEIVRAYSEKSRDELDPHLYAIAEDSYKCMNQEHKNQTIIISGESGAGKTVSARYIMRYFASVQALIQSTDSNFHEAPQLTAVENEILATNPIMEAFGNSKTSRNDNSSRFGKYIQILFDGNATIIGAKIQTYLLERSRLVFQPNQERNYHIFYQILAGSSSEQLEKWKLVENSQEFNYLKQGNCSTIEGVNDKEE...
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 ce...
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 p...
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
MDLLGLKELDNNKLVSKAKENGVEFSDLFLLSSGYLRDRENASASVSSKNERMVLNEERQNCWTKRNDPKGLTYYQLLKPSEVEILSRPETRRKRMACQVFFLNYYISTIEYHKLRKERLEEFTACTSSLKQSKQKRLWKEHCGRERAFLRKKRTKIQCSHFDLLVKLGQGGYGSVWLAKKRNTHELLAMKMMKKSTLQQLNEVKHILNERDILTNTNSEWLVKLYYAFQDKEKVYLAMEYVPGGDFRTFLTTKGLLHENQTRFYLAEMVAAISAVHKLGYMHRDLKPENFLIDQKGHIKLSDFGLSTAIVTSNQVNRLQ...
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-[pr...
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
MEENSSELDSNNFNVLVDNLAGLSLTDEEVRRILSPRKEGSRQLPSSTSKDEDSEEASHKYDFEIDRDSLKSDSGSPRLHQNATAPTSSTPLQSPDESVNKLNSEDEEGNSSVAPFFLDTTNFDRLNDNITTDDEQLSPVLTANQGFQSQEQYEEDSYNNYDYTSDPSSPNYISSSLDQLPHLDDEDDLQLTPIKEERNYLHSQDAPTTNALSKKISDILIPASAMKDLKDRKNALAKEFEESQPGSSLTLKEQANVIDNLRKEVFGLKLKCYFLYDQLNKFHDQEVQDIMKQNIDLKTLTMELQRAVAGYEKKISGLES...
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]; micr...
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 ...
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:15...
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 mi...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94489
EF3_SCHPO
MSAKSENKQSVKALEELLKHLTVCDAAEEADAAKALASFVNGPIEEQDAPSQVFSAISKQLNDKNATARERVLKGLEAVANHGSVAADVEPYLVELLPAVIAKVADKQNAVRDAAIAASKAIVRCTTPYAVKAIVPSVLESIHTTGKWNEKMNSLQLLDVLVEVAPSQLSYSLPQIIPVVSESMWDTKAEVKKQSKETMTKVCTLIANADIDRFIPELINCIAHPEEVPETIHSLGATTFVTEVQAPTLSIMVPLLARGLNERSTPIKRKTAVIIDNMSKLVEDPQVVAPFLPKLLPGLYHIKDTIGDPECRSVVQRAIT...
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, w...
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, EC...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94505
DPNP_SCHPO
MSFDAEKQLAIAAVRRASYLTEKVFNQLIKEKSAAGALTKDDKSPVTIGDFGAQAIVISMLKDAFPNDPIVGEEDSDFLRENTQTCSRVWELVQETIQHATEYKELGQIKSAEEMMSIIDQGSYHGGRNGRMWTLDPIDGTKGFLRGAQYAICLALIENGKPVVSAIGCPNLPYDFNQPETSPKGIIMSAVRNHGCFQYSLHNEKLEPVQVHMQDVQNTKDSKFCEGVEAGHSMQGTQEEIAKYLGITRGPTKMDSQAKYASLARGDGDIYLRLPTKMTFEEKIWDHAGGSLLVEEAGGVVSDMFGKPLDFGVGRTLKNN...
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; Evide...
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 ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94510
AGN2_SCHPO
MASLTTALPNKAVVAHFMMGLTYNYAQSDFQNDIQNAISLGLDGFVLNFGNDSWMMSKLTLMYNAADALNLQFLLYLNLDMSEMSTVPASTLVTYVQTFANRGHQARINNNVVVGTFLGQDINFGQSSVNQGWQVAFKNALASAGINIFFMPTWPLDASTIYQTYPVADGFCKWNCWPYYTSSPTSDAEDLVYIQNSKATNKKYMATVSPIFYTHFTSKNYSFFSEGLWFTRWMQLIKDQPNYVQVLTWNDYGESTYIGPTNYAADFPVIGSNSHEWVDSFTHAPLSYSLPLFIQMYKQNTTGLPSNFSGISQLYVTYRV...
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 wit...
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
MGSELKSTSPLAVKYDLSQKIMQHLDRHLIFPLLEFLSLRQTHDPKELLQAKYDLLKDTNMTDYVANLWTNLHGGHTDEDMANAFAEKRRSVLQELSELEEEVQGILGVLENPDLIAALRQDKGQNLQHLQEHYNITPERIAVLYKFAQFQYNCGNYGGASDLLYHFRAFSKDPELNASATWGKFASEILTVDWDGAMEELGKLREMVDSKSFKDSAVQLRNRTWLLHWSLFPLFNHANGCDTLCDLFFYTPYLNTIQTSCPWLLRYLTVAVVTNQNNANQKPRNPRQSYQRRMRDLVRIISQENYEYSDPVTSFISALY...
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 i...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94529
POB3_SCHPO
MAAKTVQYDNIYLNLSEKPGKLRIAPSGLGWKSPSLAEPFTLPISEIRRFCWSRFARGYELKIILKSKDPVSLDGFSQEDLDDLINVIKQNFDMGIEQKEFSIKGWNWGEANFLGSELVFDVNSRPAFEIPISAVTNTNLSGKNEVALEFSTTDDKQIPSAQVDELVEMRLYVPGTTAKEDAADGEEVEQNAANLFYESLKERADIGQAAGDAIVSFSEILLLTPRGRYDIDMYETCMRLRGKTYDYKVEYSSINSLFLLPKPDEQHVVFVIGLEPPLRQGQTRYPFLVTQFVRDEDMEVDLNIEETVLKEKYADKVKAS...
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:014067...
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...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94532
FOR3_SCHPO
MASKMPEGSPPTSRSIQSRNSSYSTSSNERIGTPSTISLSENSDLSKLQSTNDFESREDLSLTSDDNNDPEYVMCYNTVYHQKTKINDKLLSETEQLRKIYPLESRVFPKPTIVKEITNERTKRYTFYDDDAPLTNQHTVLDEATYNRILKRIDFFIEKVVEVPPTYHFLSLLNVQLRIQPIWWMDEFAERNGIESLLSALRNLGHYPERASKTPLESQIIQSLFHCLNSENCRRRYQSSAKCSVPGFNALGTIAETVLSKSLNSARMATFLLKFLCNKKGLSYFKAVIRAFEWLVEQKLSKTRFSAWMHSFNDVITGVR...
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]; prote...
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 ...
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
MSQDQEEDYSKLPLESRIVHKVWKVRLSAYEECSKSFSLSADGSDNCFELWNNQSELWKSVLTDSNVAAQEAGTAAFVAYCRFSDPSHLLKAREISVLSISEKCLTSPRAGTRENALEALMLLVEADSAAPVIESIIPSLSARSPKVIASNVAAIASLVEQFGAKVIPSKMIIPHISNLFGHADKNVRKEASRLTVNIYRWTGDPLKDLLFKDLRPVQTKELESLFAELPTEPPKQTRFLKSQQPTSEPNVETQVEEQPALENEESEPEPSDDQFDLVEEVDVLPNVDPNLETLMASSKWKDRKEALDKLLPVLSQPKIK...
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 [...
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]; nucleu...
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
MKSLKGRLLFLRKFVFFSLLILLFAHGASSSSSSFNYFDKRTNGKANNELALFSPTADSPSSVDGVLELPSAENVFAESSLYNAFIVATVDGSLHSYDRITGQELWSLFTNANPGLSYTKDENSLLSSKFLSQSNFKSYNSTHGEFYSDSTLNISYLSDDDTVWFVEPIDGGILYAFNLQTGLVRLPHSIKDLVHASPIRLLNNNVFVGSKNTTLFTIDVSNGDIVSQYPSGHRYETHHSVHNLGTKRDSVPSGADSDLSFKDPSGKKLSESLDLLDDFNYQVTVSNKSFVDIARTEYFITIYSDSNVILDLVYIDWTPT...
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...
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-re...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94544
LKHA4_SCHPO
MKLRLDPSTQSNYHDVSISKLDWHARIDFDQELLHGKVSFVIQSARVSQALSHIILDTSYLEIKNVTINDIPTPFRVDKRRGFLGSALHIVPADEIPSSKSCILTILYSTTKDCTALQFLKPEQTIGGKFPYVFSECQAIHARSFIPCQDTPSVKVPCTFKIRSKLPVIASGIPCGTANFCNGSLEYLFEQKNPIPSYLFCILSGDLASTNIGPRSSVYTEPGNLLACKYEFEHDMENFMEAAEQLTLPYCWTRYDFVILPPSFPYGGMENPNATFATPTLIAGDRSNVNVIAHELAHSWSGNLVTNESWQCFWLNEGMT...
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 ho...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94547
SRK1_SCHPO
MRFKSIQQNIEDEGKVNVREVNPDSYAERDHGYTAGIFSDAEENFGITQQVADSTQNPTSKPKSRHAHFHETVHENPSEYSRSKCKQPTNEKEYDKAIEALVAKAIVEEHSGQQFPVYKGLEQYTLLQKMGDGAFSNVYKAIHNRTGEKVAIKVVQRAQPNTDPRDPRKRQGVESHNILKEVQIMRRVKHPNIIQLLEFIQTPEYYYLVLELADGGELFHQIVRLTYFSEDLSRHVITQVAHAIRYLHEDCGVVHRDIKPENLLFDSIDFVPSRVRKYRAGDDPDKVDEGEFIPGVGAGTIGRIRLADFGLSKVVWDSHT...
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 cel...
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....
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...
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:000...
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 fo...
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|UniProtK...
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 ...
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 reac...
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 ...
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:1936...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94603
JHD1_SCHPO
MDSWLEYDDIINQDIDIPSNDLSGSGTLCVGVHSSLLENSLNSIDSFISSKEEISWCGNQSTPIATKSHLSCINPQYVNPFDTSPVSVDTEFQDTYLLDAPSFAQPHFSERQSVDKTRSRCLSRNRRRKRHPNLHKNHQRLLGMSFPQDGFRRMPAESVNFSYFRDTGFNEPTIFPSSDTQNTRQLNLSKIATLIGYDCPLALVDVVTQKQIPNKMDMESWVKYMSLEPSKRGRIYDVLSLEVSTTKLAYYVRKPNIVRDLDLVNTVWPPGSFALGEYPHVDTYCLMSAENSYTEFHIEFGGSSAYYNILDGCKIFYLIP...
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:29...
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
MSNNMNIDQTDQNTIDEGLYSRQLYVLGHEAMKQMSQSNVLIIGCKGLGVEIAKNVCLAGVKSVTLYDPQPTRIEDLSSQYFLTEDDIGVPRAKVTVSKLAELNQYVPVSVVDELSTEYLKNFKCVVVTETSLTKQLEINDFTHKNHIAYIAADSRGLFGSIFCDFGENFICTDTDGNEPLTGMIASITDDGVVTMLEETRHGLENGDFVKFTEVKGMPGLNDGTPRKVEVKGPYTFSIGSVKDLGSAGYNGVFTQVKVPTKISFKSLRESLKDPEYVYPDFGKMMRPPQYHIAFQALSAFADAHEGSLPRPRNDIDAAE...
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 u...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94614
CHR4_SCHPO
MDSASSMRNRSPLGVPEFSYSSQSVNNIRGIKSRNRSSIGHSITDPQVASRINAFYLSNVQSSIPFETDAIGPAYGIGDMIAPEMNDTQSLSASVTNMKKENFYSRPNVSSSSILLTIKRATSSQETKRDRPLPNIRNSAPSATRSHSTPCVAPGYLRTSNEAADVVFPHEEAHFSNHNPKPNNGSPLQKQVVADLPFPLPVSDEEQLDWIRANEDLVHSQDIDEALEWAEYVLRFTQSHLPYLQTYESENLHEINYLESMCENALYKIREFSELENAKAMYFDAYVYETGAFDVESDIQRAWDLYSSSANLGYTRSLYR...
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
MAFNQRKRRRPVGIADFDEANDEAYESVGFHDYADYFSRKQRKLQNQNAALYKSIDEDSKSDLFHGLAIAINGYTKPSYTELRQMIVSNGGTFIQYVDGKTSISYLVCSFLTPSKARQWKHQKVVKPEWIVDCIKQKKILPWINYRTFQASSAQATLSFVASKPSQPEGNLEDIQTSSQEEEHDNEKDKTKESKAKGFLDDLSGLSASSLHNYQLLKNPNVRNSTTQNQDFLENFFSSSRLHHLSTWKADFKNEIQAMTTASEPVRPIMKDKSKKSRFLLHVDFDCFFASVSTRFSHELRLKPVAVAHGIKNSEIASCNY...
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 p...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94632
EGT1_SCHPO
MTEIENIGALEVLFSPESIEQSLKRCQLPSTLLYDEKGLRLFDEITNLKEYYLYESELDILKKFSDSIANQLLSPDLPNTVIELGCGNMRKTKLLLDAFEKKGCDVHFYALDLNEAELQKGLQELRQTTNYQHVKVSGICGCFERLLQCLDRFRSEPNSRISMLYLGASIGNFDRKSAASFLRSFASRLNIHDNLLISFDHRNKAELVQLAYDDPYRITEKFEKNILASVNAVFGENLFDENDWEYKSVYDEDLGVHRAYLQAKNEVTVIKGPMFFQFKPSHLILIEESWKNSDQECRQIIEKGDFKLVSKYESTIADYS...
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]; sele...
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...
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:...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94640
SIR2_SCHPO
MASNPLDNNMPTTPVEEKIPVASYSPSSSGSSSGASLLVDIMCGSKETEDEEVDSDEWDKPETENISDLDERSEMVRYLRASGYAKFLEKYLIEEELPVRSILKKLGINLPSALEEFEDIDLLPLLKEVLKREVARRIKLPHFNTFEDVVNLLKKAKNVVVLVGAGISTSLGILDFRSDNGFYARLARHGLSEPSEMFDIHTFRENPEIFYTFARDLLPETNHYSPSHAFIRLLEKKNKLSTLFTQNIDNLEKKTGLSDNKIIQCHGSFATATCIKCKHKVDGSELYEDIRNQRVSYCNECGKPPLKLRRVGQNKKEKHY...
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:01407...
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 H3...
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=...
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:1...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94641
HS104_SCHPO
MADYPFTDKAAKTLSDAYSIAQSYGHSQLTPIHIAAALLSDSDSNGTTLLRTIVDKAGGDGQKFERSVTSRLVRLPAQDPPPEQVTLSPESAKLLRNAHELQKTQKDSYIAQDHFIAVFTKDDTLKSLLAEAGVTPKAFEFAVNNVRGNKRIDSKNAEEGFDALNKFTVDLTELARNGQLDPVIGREDEIRRTIRVLSRRTKNNPVLIGEPGVGKTSIAEGLARRIIDDDVPANLSNCKLLSLDVGSLVAGSKFRGEFEERIKSVLKEVEESETPIILFVDEMHLLMGAGSGGEGGMDAANLLKPMLARGKLHCIGATTL...
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 o...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94649
ATG2_SCHPO
MRLPSWLKNSSSWLWTAALSRTVQRRLLAFALRKLIGSILLENVQPEDIDILFSKGVLMLSNLQLNCSFLNAVVSLPMINFTKGTLRRLILRLNVTDIVNLNVELEVNGLSLEIELVPPDESLSSTTYEDAPSQLDILDNVVEYMNKTASQDFEDEVINEGLESEIDGSSHNLLDSILQKCLASTSVLMQDALVYIGTANMSTRLEAKLDFMSFSSVKSNSTSRLLNINGITVSMVRPISKSNAGSSSPPRSEESFVSMDSSSSIVEGFENDLSPSQVTLNESSIISSNREEESFYSVHDSVTQKKTRTSWLIFQCSGEF...
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:00304...
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...
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-se...
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 ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94652
GLE1_SCHPO
MDTKTTPLIHAKLDEKIISSYNDANGLDIDDLWDIYNEKTRRMIHIISQRYKPKKQSPFPVIADENVRIFPPLHKTIDWAKKRNVEEQNLIEQSITESQRIFSEKQRLEQERFNRELLEKKRIEAERQRLKDEEERRKKELMEKEKKEKERIRLIEEQKHKENEQRRLKQEQIDAKRKEEEAREKRMKETFKDDPEEDSNMAWSIIHKIKTEVVAPISEKKELKNYCFTQKRKITPRLGQITKSNSQIMKITQLLQQTFQEARNTDPLVYKWVLNFFCKSVVKQAEAEVAVNPISAYPLAKVCLLLQTQNADLKDLLFAR...
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}; Periphera...
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 termina...
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 fus...
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 i...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94679
CND1_SCHPO
MSLDLLSRLKKYIHDEENSDLDSIYAECENAGLTAVVNDVIDTLLLGTSSCFDEDCLEKLFAICSHFADLSSSVRNKVYDLLTSNISSESAILEDMISANATDFTVPQTNLETTGIAFQLTVNSLSSSNQLSVIRSSTNTVKGRKKNPTTNSNWNGISHVNALLDAIITLFQKKLSRVWTTSSERDMFLSLFLKPIYTLMESEINIKNASFRSRLFNIIGLAVQFHNHTTAAETNIIQNLQYFEHLSEYAADLVHIVTVQFNSVTLAEGIIRTLCSLEFNDNDVKGPKQVALFLVRLSSLIPNLCLKQLTQLVKLLDSES...
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 mitosi...
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 f...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94680
PDAT_SCHPO
MASSKKSKTHKKKKEVKSPIDLPNSKKPTRALSEQPSASETQSVSNKSRKSKFGKRLNFILGAILGICGAFFFAVGDDNAVFDPATLDKFGNMLGSSDLFDDIKGYLSYNVFKDAPFTTDKPSQSPSGNEVQVGLDMYNEGYRSDHPVIMVPGVISSGLESWSFNNCSIPYFRKRLWGSWSMLKAMFLDKQCWLEHLMLDKKTGLDPKGIKLRAAQGFEAADFFITGYWIWSKVIENLAAIGYEPNNMLSASYDWRLSYANLEERDKYFSKLKMFIEYSNIVHKKKVVLISHSMGSQVTYYFFKWVEAEGYGNGGPTWVN...
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, Pu...
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 f...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94687
TAS3_SCHPO
MEKGIKKYLPSLPFLACISDFPENHGTSRRSATVSLERVHELFTEHWLSNLKNRREKRQELAEEAVYCRSEMLSQRKLLAAVDFPQQLKNSPAKAKATHTSSGVTKEVRASKKYTSSNVEFPLVTDGKEKPVKSKQLRKNSVTEFEKPIETKKSKHRKSRNKFLDKSSGSMEIESWDNSTSDSIIESSSRLHESISLRENDIRSSDSKSVGWDDNSTGFRESSKSLDHTDTSMFMELDSNSDPQFRPKYQAKSSWFAPDDPEASWGNLDDGWGETNGSWSSTDDTKHYKNEWAESINLDNFNRPSQQEDYDKPKNTQVSR...
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:...
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 polyme...
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:19...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94720
FIL1_SCHPO
MNYNDTTEFCFPFGQPSFPTSAMTEGSFDGQFSEFDPTFTSPADTALSDIANLPIDLHKDALFANAPGKGDVDFDSVSMLQLLSDYPLAFNSTENNQKLQTNPSARWSLLDSMDFDNQRQCSDLESAQLGDSGLLKSTILSNSHIDIAALSSSKTSEPTPPFSYVQTPCIPTPSSALIDTPFPGALDSEFGFDESQAPLFPASDGDCQRAFASISYPTNYGCKLSNLGFMSPQSPVKRELNDSTSPSKLSESSSSLTGSSSALLSQSEFLGSVPSLSDSIATVDPFFSFESFETDEKARSLLMDASLKLPQFSTPNLSSN...
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
MDSKHSVFNVMGQEFVLQKGYEVIKGLGKGSYGVVCSAKNIEVEDNNKVAIKKITNIFSKKMLAKRALREIMLLQHFRNHKNITTLYDMDIVDPSKFNELYLYEELMQANLNSIIRSDQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPSNLLINADCKLKICDFGLSRGISVNQGQGTEYMTEYVTTRWYRAPEVMLSFQSYSKAIDLWSVGCILAELLGRKPFFKGSNYVDQLNQIFCILGTPNENIISKIKSASAQSYIRSLPTLPKMPYSKIFPYANPDALDLLNCLLTFDPYDRISCEEALEHPYLIIWHDP...
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}; CATALYTI...
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
MAIDYSKWDKLELSDDSDIEVHPNVDKKSFIRWRQRDIHEKRAVRKQKMEDIKGAMAMNRRLLSRISEMETVLEKESPSDPYVLLGSFLEAKKSEDMDSAIPGGMSYHHMLMSLLKVIKDAEDTTEEKSMDDSDKCLRRLKSHKERLLKLLEDAQKEYDTLEAESKNYITSEDLHLGFDSTYVQKKEPEKPKKTKTKKETIQVIESLNNPTPPTDFPGAKEQASTGNAPKNPVNENESEDEEGLSLSEDGKKFANIDFGDYSSSEEFLKEHLNILADEEESDAILLEAFNAELEGKPSLAKQYVHQALLISYCRQLGPNG...
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-mediat...
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 i...
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
O94751
BUB1_SCHPO
MSDWRLTENVLDQNIPETKPRESKTRLEEIQRLALFQEELDIIEELDDPVDVWYRCIEWLLETRFLGMETVNKMLDDAIQYLERCRFALNDVRHLLIQLAKIKQSYETPDELQQAAKQFYQLASKGIGLELALFYEEYGSLLIRMQRWKEASEVFHAAVSREARPLVRLLRNAAEFSRAYDLHNAHPSIHDAPYSSPFPPPRIVLGSKPVSSSTLPSKPKSFQVFSDASSSRDSQNASDLPQAKSLESEANTPNLPLLYDKSSGKRVEYSAFNFLALYENGEERSMEECRAQRYLSSIQPNTAASFPKVVPKNEISVHHD...
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, centrom...
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-[pr...
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:1552...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O94753
VPL2_PLEER
MSFKTLSALALALGAAVQFASAAVPLVQKRATCDDGRTTANAACCILFPILDDIQENLFDGAQCGEEVHESLRLTFHDAIGFSPTLGGGGADGSIIAFDTIETNFPANAGIDEIVSAQKPFVAKHNISAGDFIQFAGAVGVSNCPGGVRIPFFLGRPDAVAASPDHLVPEPFDSVDSILARMGDAGFSPVEVVWLLASHSIAAADKVDPSIPGTPFDSTPGVFDSQFFIETQLKGRLFPGTADNKGEAQSPLQGEIRLQSDHLLARDPQTACEWQSMVNNQPKIQNRFAATMSKMALLGQDKTKLIDCSDVIPTPPALVG...
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={E...
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...
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:12...
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
MEPSALRKAGSEQEEGFEGLPRRVTDLGMVSNLRRSNSSLFKSWRLQCPFGNNDKQESLSSWIPENIKKKECVYFVESSKLSDAGKVVCQCGYTHEQHLEEATKPHTFQGTQWDPKKHVQEMPTDAFGDIVFTGLSQKVKKYVRVSQDTPSSVIYHLMTQHWGLDVPNLLISVTGGAKNFNMKPRLKSIFRRGLVKVAQTTGAWIITGGSHTGVMKQVGEAVRDFSLSSSYKEGELITIGVATWGTVHRREGLIHPTGSFPAEYILDEDGQGNLTCLDSNHSHFILVDDGTHGQYGVEIPLRTRLEKFISEQTKERGGVA...
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:00712...
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 activ...
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:224...
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:2...
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]; nit...
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:000...
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...
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
MERLRDVRERLQAWERAFRRQRGRRPSQDDVEAAPEETRALYREYRTLKRTTGQAGGGLRSSESLPAAAEEAPEPRCWGPHLNRAATKSPQSTPGRSRQGSVPDYGQRLKANLKGTLQAGPALGRRPWPLGRASSKASTPKPPGTGPVPSFAEKVSDEPPQLPEPQPRPGRLQHLQASLSQRLGSLDPGWLQRCHSEVPDFLGAPKACRPDLGSEESQLLIPGESAVLGPGAGSQGPEASAFQEVSIRVGSPQPSSSGGEKRRWNEEPWESPAQVQQESSQAGPPSEGAGAVAVEEDPPGEPVQAQPPQPCSSPSNPRYH...
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:003...
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:3061...
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)....
Homo sapiens (Human)
O94762
RECQ5_HUMAN
MSSHHTTFPFDPERRVRSTLKKVFGFDSFKTPLQESATMAVVKGNKDVFVCMPTGAGKSLCYQLPALLAKGITIVVSPLIALIQDQVDHLLTLKVRVSSLNSKLSAQERKELLADLEREKPQTKILYITPEMAASSSFQPTLNSLVSRHLLSYLVVDEAHCVSQWGHDFRPDYLRLGALRSRLGHAPCVALTATATPQVQEDVFAALHLKKPVAIFKTPCFRANLFYDVQFKELISDPYGNLKDFCLKALGQEADKGLSGCGIVYCRTREACEQLAIELSCRGVNAKAYHAGLKASERTLVQNDWMEEKVPVIVATISFG...
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...
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...
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. R...
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:3061...
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 trans...
Homo sapiens (Human)
O94763
RMP_HUMAN
MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEKVVTNCQERIQHWKKVDNDYNALRERLSTLPDKLSYNIMVPFGPFAFMPGKLVHTNEVTVLLGDNWFAKCSAKQAVGLVEHRKEHVRKTIDDLKKVMKNFESRVEFTEDLQKMSDAAGDIVDIREEIKCDFEFKAKHRIAHKPHSKPKTSDIFEADIANDVKSKDLLADKELWARLEELERQEELLGELDSKPDTVIANGEDTTSSEEEKEDRNTNVNAMHQVTDSHTPCHKDVASSEPFSGQVNSQLNCSVNGSSSYHSDDDDDDDDDDDDDNIDDDDGDN...
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...
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 g...
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. Req...
Homo sapiens (Human)
O94766
B3GA3_HUMAN
MKLKLKNVFLAYFLVSIAGLLYALVQLGQPCDCLPPLRAAAEQLRQKDLRISQLQAELRRPPPAPAQPPEPEALPTIYVVTPTYARLVQKAELVRLSQTLSLVPRLHWLLVEDAEGPTPLVSGLLAASGLLFTHLVVLTPKAQRLREGEPGWVHPRGVEQRNKALDWLRGRGGAVGGEKDPPPPGTQGVVYFADDDNTYSRELFEEMRWTRGVSVWPVGLVGGLRFEGPQVQDGRVVGFHTAWEPSRPFPVDMAGFAVALPLLLDKPNAQFDSTAPRGHLESSLLSHLVDPKDLEPRAANCTRVLVWHTRTEKPKMKQEE...
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 ca...
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, ChEB...
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,...
Homo sapiens (Human)
O94768
ST17B_HUMAN
MSRRRFDCRSISGLLTTTPQIPIKMENFNNFYILTSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSCPRVINLHEVYENTSEIILILEYAAGGEIFSLCLPELAEMVSENDVIRLIKQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGHACELREIMGTPEYLAPEILNYDPITTATDMWNIGIIAYMLLTHTSPFVGEDNQETYLNISQVNVDYSEETFSSVSQLATDFIQSLLVKNPEKRPTAEICLSHSWLQQWDFENLFHPEETSSSSQTQDHSVRS...
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-[pr...
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
MKIAVLFCFFLLIIFQTDFGKNEEIPRKQRRKIYHRRLRKSSTSHKHRSNRQLGIQQTTVFTPVARLPIVNFDYSMEEKFESFSSFPGVESSYNVLPGKKGHCLVKGITMYNKAVWSPEPCTTCLCSDGRVLCDETMCHPQRCPQTVIPEGECCPVCSATVSYSLLSGIALNDRNEFSGDSSEQREPTNLLHKQLPPPQVGMDRIVRKEALQSEEDEEVKEEDTEQKRETPESRNQGQLYSEGDSRGGDRKQRPGEERRLAHQQQRQGREEEEDEEEEGEEGEEDEEDEEDPVRGDMFRMPSRSPLPAPPRGTLRLPSGC...
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
MAANMYRVGDYVYFENSSSNPYLVRRIEELNKTANGNVEAKVVCLFRRRDISSSLNSLADSNAREFEEESKQPGVSEQQRHQLKHRELFLSRQFESLPATHIRGKCSVTLLNETDILSQYLEKEDCFFYSLVFDPVQKTLLADQGEIRVGCKYQAEIPDRLVEGESDNRNQQKMEMKVWDPDNPLTDRQIDQFLVVARAVGTFARALDCSSSIRQPSLHMSAAAASRDITLFHAMDTLQRNGYDLAKAMSTLVPQGGPVLCRDEMEEWSASEAMLFEEALEKYGKDFNDIRQDFLPWKSLASIVQFYYMWKTTDRYIQQK...
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 po...
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:000371...
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 (...
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...
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 [...
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 leadin...
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:P5640...
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, E...
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:1894...
Homo sapiens (Human)
O94779
CNTN5_HUMAN
MASSWKLMLFLSVTMCLSEYSKSLPGLSTSYAALLRIKKSSSSSLFGSKTRPRYSSPSLGTLSASSPSWLGAAQNYYSPINLYHSSDAFKQDESVDYGPVFVQEPDDIIFPTDSDEKKVALNCEVRGNPVPSYRWLRNGTEIDLESDYRYSLIDGTFIISNPSEAKDSGHYQCLATNTVGSILSREATLQFAYLGNFSGRTRSAVSVREGQGVVLMCSPPPHSPEIIYSWVFNEFPSFVAEDSRRFISQETGNLYISKVQTSDVGSYICLVKNTVTNARVLSPPTPLTLRNDGVMGEYEPKIEVHFPFTVTAAKGTTVKM...
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
MPGVIPSESNGLSRGSPSKKNRLSLKFFQKKETKRALDFTDSQENEEKASEYRASEIDQVVPAAQSSPINCEKRENLLPFVGLNNLGNTCYLNSILQVLYFCPGFKSGVKHLFNIISRKKEALKDEANQKDKGNCKEDSLASYELICSLQSLIISVEQLQASFLLNPEKYTDELATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETCQLLKKEEVKNVAELPTKVEEIPHPKEEMNGINSIEMDSMRHSEDFKEKLPKGNGKRKSDTEFGNMKKKVKLSKEHQSLEENQRQTRSKRKATSDTLESPPKIIPK...
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 ...
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...
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, ...
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...
Homo sapiens (Human)
O94788
AL1A2_HUMAN
MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVYNPATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVLATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVCGQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILPGYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADADLDYAVEQAHQGVFFNQGQCC...
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 developme...
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}; PhysiologicalDirectio...
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 th...
Homo sapiens (Human)
O94804
STK10_HUMAN
MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNEVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYHDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHSKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLEHPFVSSITSNKALRELVAEAKAEVMEEIED...
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...
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 b...
Homo sapiens (Human)
O94805
ACL6B_HUMAN
MSGGVYGGDEVGALVFDIGSFSVRAGYAGEDCPKADFPTTVGLLAAEEGGGLELEGDKEKKGKIFHIDTNALHVPRDGAEVMSPLKNGMIEDWECFRAILDHTYSKHVKSEPNLHPVLMSEAPWNTRAKREKLTELMFEQYNIPAFFLCKTAVLTAFANGRSTGLVLDSGATHTTAIPVHDGYVLQQGIVKSPLAGDFISMQCRELFQEMAIDIIPPYMIAAKEPVREGAPPNWKKKEKLPQVSKSWHNYMCNEVIQDFQASVLQVSDSPYDEQVAAQMPTVHYEMPNGYNTDYGAERLRIPEGLFDPSNVKGLSGNTML...
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 c...
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:00165...
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 ...
Homo sapiens (Human)
O94806
KPCD3_HUMAN
MSANNSPPSAQKSVLPTAIPAVLPAASPCSSPKTGLSARLSNGSFSAPSLTNSRGSVHTVSFLLQIGLTRESVTIEAQELSLSAVKDLVCSIVYQKFPECGFFGMYDKILLFRHDMNSENILQLITSADEIHEGDLVEVVLSALATVEDFQIRPHTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLPGPGLSVPRPLQPEYVALPSEESHVHQEPSKRIPSWSGRPIWMEKMVMCRVKVPHTFAVHSYTRPTICQYCKRLLKGLFRQGMQCKDCKFNCHKRCASKVPRD...
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-[p...
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
MCGIFAYMNYRVPRTRKEIFETLIKGLQRLEYRGYDSAGVAIDGNNHEVKERHIQLVKKRGKVKALDEELYKQDSMDLKVEFETHFGIAHTRWATHGVPSAVNSHPQRSDKGNEFVVIHNGIITNYKDLRKFLESKGYEFESETDTETIAKLIKYVFDNRETEDITFSTLVERVIQQLEGAFALVFKSVHYPGEAVATRRGSPLLIGVRSKYKLSTEQIPILYRTCTLENVKNICKTRMKRLDSSACLHAVGDKAVEFFFASDASAIIEHTNRVIFLEDDDIAAVADGKLSIHRVKRSASDDPSRAIQTLQMELQQIMKG...
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-acetyl...
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
MAAGPAPPPGRPRAQMPHLRKMERVVVSMQDPDQGVKMRSQRLLVTVIPHAVTGSDVVQWLAQKFCVSEEEALHLGAVLVQHGYIYPLRDPRSLMLRPDETPYRFQTPYFWTSTLRPAAELDYAIYLAKKNIRKRGTLVDYEKDCYDRLHKKINHAWDLVLMQAREQLRAAKQRSKGDRLVIACQEQTYWLVNRPPPGAPDVLEQGPGRGSCAASRVLMTKSADFHKREIEYFRKALGRTRVKSSVCLEAYLSFCGQRGPHDPLVSGCLPSNPWISDNDAYWVMNAPTVAAPTKLRVERWGFSFRELLEDPVGRAHFMDF...
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]; oli...
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 a...
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=Sp...
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=...
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 microtub...
Homo sapiens (Human)
O94812
BAIP3_HUMAN
MRPRGAAFAAGPPGDLHLGTAIGFAGAIWRSRSPAMSTLLDIKSSVLRQVQVCPSFRRRTEQDPGSASADPQEPATGAWKPGDGVEFFAHMRLMLKKGEGRQGLPCLEVPLRSGSPAPPEPVDPSLGLRALAPEEVEMLYEEALYTVLYRAGTMGPDQVDDEEALLSYLQQVFGTSLEEHTEAIERVRKAKAPTYALKVSVMRAKNLLAKDPNGFSDPYCMLGILPASDATREPRAQKEQRFGFRKGSKRGGPLPAKCIQVTEVKSSTLNPVWKEHFLFEIEDVSTDQLHLDIWDHDDDVSLVEACRKLNEVIGLKGMGR...
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 ...
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, ...
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-...
Homo sapiens (Human)
O94813
SLIT2_HUMAN
MRGVGWQMLSLSLGLVLAILNKVAPQACPAQCSCSGSTVDCHGLALRSVPRNIPRNTERLDLNGNNITRITKTDFAGLRHLRVLQLMENKISTIERGAFQDLKELERLRLNRNHLQLFPELLFLGTAKLYRLDLSENQIQAIPRKAFRGAVDIKNLQLDYNQISCIEDGAFRALRDLEVLTLNNNNITRLSVASFNHMPKLRTFRLHSNNLYCDCHLAWLSDWLRQRPRVGLYTQCMGPSHLRGHNVAEVQKREFVCSGHQSFMAPSCSVLHCPAACTCSNNIVDCRGKGLTEIPTNLPETITEIRLEQNTIKVIPPGAF...
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...
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 ...
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]; p...
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 comp...
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 w...
Homo sapiens (Human)
O94818
NOL4_HUMAN
MESERDMYRQFQDWCLRTYGDSGKTKTVTRKKYERIVQLLNGSESSSTDNAKFKFWVKSKGFQLGQPDEVRGGGGGAKQVLYVPVKTTDGVGVDEKLSLRRVAVVEDFFDIIYSMHVETGPNGEQIRKHAGQKRTYKAISESYAFLPREAVTRFLMSCSECQKRMHLNPDGTDHKDNGKPPTLVTSMIDYNMPITMAYMKHMKLQLLNSQQDEDESSIESDEFDMSDSTRMSAVNSDLSSNLEERMQSPQNLHGQQDDDSAAESFNGNETLGHSSIASGGTHSREMGDSNSDGKTGLEQDEQPLNLSDSPLSAQLTSEYR...
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
MGGKNKQRTKGNLRPSNSGRAAELLAKEQGTVPGFIGFGTSQSDLGYVPAIQGAEEIDSLVDSDFRMVLRKLSKKDVTTKLKAMQEFGTMCTERDTETVKGVLPYWPRIFCKISLDHDRRVREATQQAFEKLILKVKKQLAPYLKSLMGYWLMAQCDTYTPAAFAAKDAFEAAFPPSKQPEAIAFCKDEITSVLQDHLIKETPDTLSDPQTVPEEEREAKFYRVVTCSLLALKRLLCLLPDNELDSLEEKFKSLLSQNKFWKYGKHSVPQIRSAYFELVSALCQRIPQLMKEEASKVSPSVLLSIDDSDPIVCPALWEAV...
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...
Homo sapiens (Human)
O94823
AT10B_HUMAN
MALSVDSSWHRWQWRVRDGFPHCPSETTPLLSPEKGRQSYNLTQQRVVFPNNSIFHQDWEEVSRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITMLPLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKCNEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELFHNTIVCEKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNSGPRYKRSKIERRMNIDIFFC...
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:...
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(+) + phos...
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...
Homo sapiens (Human)
O94826
TOM70_HUMAN
MAASKPVEAAVVAAAVPSSGSGVGGGGTAGPGTGGLPRWQLALAVGAPLLLGAGAIYLWSRQQRRREARGRGDASGLKRNSERKTPEGRASPAPGSGHPEGPGAHLDMNSLDRAQAAKNKGNKYFKAGKYEQAIQCYTEAISLCPTEKNVDLSTFYQNRAAAFEQLQKWKEVAQDCTKAVELNPKYVKALFRRAKAHEKLDNKKECLEDVTAVCILEGFQNQQSMLLADKVLKLLGKEKAKEKYKNREPLMPSPQFIKSYFSSFTDDIISQPMLKGEKSDEDKDKEGEALEVKENSGYLKAKQYMEEENYDKIISECSKE...
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]; ...
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 hos...
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). Mediat...
Homo sapiens (Human)
O94827
PKHG5_HUMAN
MHYDGHVRFDLPPQGSVLARNVSTRSCPPRTSPAVDLEEEEEESSVDGKGDRKSTGLKLSKKKARRRHTDDPSKECFTLKFDLNVDIETEIVPAMKKKSLGEVLLPVFERKGIALGKVDIYLDQSNTPLSLTFEAYRFGGHYLRVKAPAKPGDEGKVEQGMKDSKSLSLPILRPAGTGPPALERVDAQSRRESLDILAPGRRRKNMSEFLGEASIPGQEPPTPSSCSLPSGSSGSTNTGDSWKNRAASRFSGFFSSGPSTSAFGREVDKMEQLEGKLHTYSLFGLPRLPRGLRFDHDSWEEEYDEDEDEDNACLRLEDSW...
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...
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....
Homo sapiens (Human)
O94829
IPO13_HUMAN
MERREEQPGAAGAGAAPALDFTVENVEKALHQLYYDPNIENKNLAQKWLMQAQVSPQAWHFSWQLLQPDKVPEIQYFGASALHIKISRYWSDIPTDQYESLKAQLFTQITRFASGSKIVLTRLCVALASLALSMMPDAWPCAVADMVRLFQAEDSPVDGQGRCLALLELLTVLPEEFQTSRLPQYRKGLVRTSLAVECGAVFPLLEQLLQQPSSPSCVRQKVLKCFSSWVQLEVPLQDCEALIQAAFAALQDSELFDSSVEAIVNAISQPDAQRYVNTLLKLIPLVLGLQEQLRQAVQNGDMETSHGICRIAVALGENHS...
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 tra...
Homo sapiens (Human)
O94830
DDHD2_HUMAN
MSSVQSQQEQLSQSDPSPSPNSCSSFELIDMDAGSLYEPVSPHWFYCKIIDSKETWIPFNSEDSQQLEEAYSSGKGCNGRVVPTDGGRYDVHLGERMRYAVYWDELASEVRRCTWFYKGDKDNKYVPYSESFSQVLEETYMLAVTLDEWKKKLESPNREIIILHNPKLMVHYQPVAGSDDWGSTPTEQGRPRTVKRGVENISVDIHCGEPLQIDHLVFVVHGIGPACDLRFRSIVQCVNDFRSVSLNLLQTHFKKAQENQQIGRVEFLPVNWHSPLHSTGVDVDLQRITLPSINRLRHFTNDTILDVFFYNSPTYCQTIV...
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 phosphoin...
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}; Physio...
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 phosphat...
Homo sapiens (Human)
O94832
MYO1D_HUMAN
MAEQESLEFGKADFVLMDTVSMPEFMANLRLRFEKGRIYTFIGEVVVSVNPYKLLNIYGRDTIEQYKGRELYERPPHLFAIADAAYKAMKRRSKDTCIVISGESGAGKTEASKYIMQYIAAITNPSQRAEVERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIVQQPGERSFHSFYQLLQGGSEQMLRSLHLQKSLSSYNYIHVGAQLKSSINDAAEFRVVADAMKVIGFKPEEIQTVYKILAAILHLGNLKFVVDGDTPLIENGKVVSIIAELLSTKTDMVEKALLYRTV...
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]; extracellu...
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 c...
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 trache...
Homo sapiens (Human)
O94842
TOX4_HUMAN
MEFPGGNDNYLTITGPSHPFLSGAETFHTPSLGDEEFEIPPISLDSDPSLAVSDVVGHFDDLADPSSSQDGSFSAQYGVQTLDMPVGMTHGLMEQGGGLLSGGLTMDLDHSIGTQYSANPPVTIDVPMTDMTSGLMGHSQLTTIDQSELSSQLGLSLGGGTILPPAQSPEDRLSTTPSPTSSLHEDGVEDFRRQLPSQKTVVVEAGKKQKAPKKRKKKDPNEPQKPVSAYALFFRDTQAAIKGQNPNATFGEVSKIVASMWDSLGEEQKQVYKRKTEAAKKEYLKALAAYKDNQECQATVETVELDPAPPSQTPSPPPMA...
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 int...
Homo sapiens (Human)
O94844
RHBT1_HUMAN
MDADMDYERPNVETIKCVVVGDNAVGKTRLICARACNTTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHHKDRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPEKGREVAKELGLPYYETSVFDQFGIKDVFDNAIRAALISRRHLQFWKSHLKKVQKPLLQAPFLPPKAPPPVIKIPECPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESPNGSEGACEKEKQSRDF...
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:00...
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
MLDGPLFSEGPDSPRELQDEESGSCLWVQKSKLLVIEVKTISCHYSRRAPSRQPMDFQASHWARGFQNRTCGPRPGSPQPPPRRPWASRVLQEATNWRAGPLAEVRAREQEKRKAASQEREAKETERKRRKAGGARRSPPGRPRPEPRNAPRVAQLAGLPAPLRPERLAPVGRAPRPSAQPQSDPGSAWAGPWGGRRPGPPSYEAHLLLRGSAGTAPRRRWDRPPPYVAPPSYEGPHRTLGTKRGPGNSQVPTSSAPAATPARTDGGRTKKRLDPRIYRDVLGAWGLRQGQGLLGGSPGCGAARARPEPGKGVVEKSLGL...
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...
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
MGENEDEKQAQAGQVFENFVQASTCKGTLQAFNILTRHLDLDPLDHRNFYSKLKSKVTTWKAKALWYKLDKRGSHKEYKRGKSCTNTKCLIVGGGPCGLRTAIELAYLGAKVVVVEKRDSFSRNNVLHLWPFTIHDLRGLGAKKFYGKFCAGSIDHISIRQLQLILFKVALMLGVEIHVNVEFVKVLEPPEDQENQKIGWRAEFLPTDHSLSEFEFDVIIGADGRRNTLEGFRRKEFRGKLAIAITANFINRNSTAEAKVEEISGVAFIFNQKFFQDLKEETGIDLENIVYYKDCTHYFVMTAKKQSLLDKGVIINDYID...
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, wi...
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:5834...
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 a...
Homo sapiens (Human)
O94854
K0754_HUMAN
MGKPLSRPDCLRRNPSCLGKGEEEDGYIEDCYVPQRSIYDTMRINEQIDQGSKLNQTSKSTMEKMEGSTISSNGTLGAASNVFESRAPEGKKLDERIIFDALKLSSDVQKSAPVPPRRRPNAERKDNVNRRSWKSFMPPNFPEFAERIEASLSEVSEAGASNPSLQEKKESSSALTESSGHLDHREPQSESVTLEHVSKSIGIPEVQDFKNLSGDCQDFRFQQHSANPPHEFQPVESEAVATSGNTDVMQESRFSSATWPRATKSLAKGGFSEKQHPLGDTACTVEMPPLSPCLSEELLDPELHVLITPSLREKTESELK...
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)