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
O74423
ENT1_SCHPO
MKAAVRSVKNFSKGYTDTQIKVRNATTNDSWGPSGTAMAEIAELTYDQNEMLEVMDIIDRRLNDKGKNWRHVFKSLSLLEYCLHNGSENVVRWAKDNIYIITTLREFVYVDDNGHDQGQNVRTKAKEITSLLEDEHALKEARGDSRERDRDRDRTRSSRFDDDDDDRAPYEESRLSRAPSRASRYDDDDRDHRSRRRSRSRRPGRSRSRRRSRRPSPSAEHNSAEENDPELQRVIEESKRQAEEDAKRRNMANDSEAELQKAIQLSKEEDEARQRHQREREQQEQAFMGNQQNAYQPVDFFGNPVQPQPTGFLQQQPTGF...
null
null
actin cortical patch assembly [GO:0000147]; actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; endocytosis [GO:0006897]
actin cortical patch [GO:0030479]; clathrin vesicle coat [GO:0030125]; endosome [GO:0005768]; plasma membrane [GO:0005886]
clathrin binding [GO:0030276]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phospholipid binding [GO:0005543]
PF08226;PF01417;
1.25.40.90;
Epsin family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15659877}. Membrane {ECO:0000255|PROSITE-ProRule:PRU00243, ECO:0000269|PubMed:15659877}; Peripheral membrane protein {ECO:0000269|PubMed:15659877}. Note=Localizes in a punctate pattern. Colocalizes with F-actin.
null
null
null
null
null
FUNCTION: Binds to membranes enriched in phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2) and phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Required for endocytosis and localization of actin. {ECO:0000269|PubMed:15659877}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74424
NU211_SCHPO
MHDSSWTEADILGVCSFLDIPKTKIDPLLQVDAFTSILIPLISKSKDYESIKNDRIVTEVNYEQQLRNSEKKLLQSNERYDLLEDERKLLENELSQIKEYLREKSSSYDTVLHDCSSLKSVNEALKQAQDQNLKQTAQLQNLLSDKEKEVEKKITIIKDLKDALASSTHQVLELQHTQQEKASLQTNYEFELQKLTQKNSILENNNTWLSRELQGVNDKLLSLHQEASLEKSQLSSQLSDAVLEKDALQRKVSSLSQQFTESNLRYQNIVAELSEMRKQYEFSQVSFEKEISSQKQISELWMEKCEDCSLRLKELQNSNG...
null
null
mRNA export from nucleus [GO:0006406]; protein import into nucleus [GO:0006606]; regulation of mitotic spindle assembly [GO:1901673]
cytoplasm [GO:0005737]; nuclear periphery [GO:0034399]; nuclear pore [GO:0005643]; nuclear pore nuclear basket [GO:0044615]; nucleolar peripheral inclusion body [GO:0140602]; nucleus [GO:0005634]
structural constituent of nuclear pore [GO:0017056]
PF07926;
1.10.287.1490;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:15116432}. Note=Nuclear rim. {ECO:0000269|PubMed:15116432}.
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)
O74429
VIP1_SCHPO
MIQNASHLTSIDTESSTRTASPVSSIVTPTKRNVVGICAMDAKARSKPCRNILNRIIAEGEFEAIVFGDNMILDEAVENWPACDYLICFYSSGFPLKKAEKYVELRKPFCVNDVVFQELLWDRRLVLNILDAIRVSTPQRLICSRDGGPKINKVLEEKLRRKFGIEITEVPTPEVKMLDEDTLSVDGKIIKKPYVEKPVYGEDHNIYIYFPKSVGGGGRKLFRKVANKSSDYDPDLCAPRTEGSFIYEEFMNVDNAEDVKVYTVGPHYSHAETRKSPVVDGIVRRNPHGKEIRFITNLSEEEKNMASKISIAFEQPVCGF...
2.7.4.24
null
inositol metabolic process [GO:0006020]; inositol phosphate biosynthetic process [GO:0032958]; inositol phosphate catabolic process [GO:0071545]; inositol phosphate metabolic process [GO:0043647]; intracellular phosphate ion homeostasis [GO:0030643]; mitotic spindle assembly [GO:0090307]; phosphorylation [GO:0016310]; ...
cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634]
2 iron, 2 sulfur cluster binding [GO:0051537]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; diphosphoinositol-pentakisphosphate kinase activity [GO:0033857]; inositol heptakisphosphate kinase activity [GO:0000829]; inositol hexakisphosphate 1-kinase activity [GO:0052723]; inositol hexakisphosphate 3-...
PF00328;PF18086;PF08443;
3.40.50.11950;3.30.470.20;3.40.50.1240;
Histidine acid phosphatase family, VIP1 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10388810, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:10388810}.
CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q06685}; PhysiologicalDirection=left-to-rig...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=58.18 uM for inositol hexakisphosphate {ECO:0000269|PubMed:25254656}; Vmax=450.5 nmol/min/ug enzyme {ECO:0000269|PubMed:25254656};
null
null
null
FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. Phosphorylates inositol hexakisphosphate (InsP6) at position 1...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74435
CDC31_SCHPO
MFANARAKRRSRASSPTPARLGGYAPLRVEITEEQRQDINEAFKLFDSDKDNAIDYHELRAAMRALGFNAEKSEVLKILRDFDKTGKGYLQMEDFVRVMTEKIVERDPLEEIKRAFELFDDDETGKISLRNLRRVAKELNENIDDQELEAMIEEFDLDQDGEINEQEFIAIMMDEA
null
null
cell division [GO:0051301]; mitotic spindle pole body duplication [GO:1903087]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein localization to meiotic spindle pole body [GO:1902441]; spindle pole body duplication [GO:0030474]
cytosol [GO:0005829]; half bridge of mitotic spindle pole body [GO:0061496]; half bridge of spindle pole body [GO:0005825]; meiotic spindle pole body [GO:0035974]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]
calcium ion binding [GO:0005509]; microtubule binding [GO:0008017]
PF13499;
1.10.238.10;
Centrin family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12857865}. Note=Associates with the half-bridge structure of the SPB.
null
null
null
null
null
FUNCTION: Required for the proper coordination between exit from mitosis and the initiation of septation. Has a role in bipolar spindle formation during spindle pole body (SPB) duplication. Required for the localization of sad1 to the SPB (PubMed:12857865). {ECO:0000269|PubMed:12857865}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74441
CTL1_SCHPO
MFSDYASRFLAQSRFSSVDQRNFKYPTSRSNLQSVSIDRNSSIDSHETDLSAGSSSLHGLNSLIDSGSIHWQLREQEQSNSHISRNENELFSKENSIYNGNFSENLGVQPNPQTISHESVNEEYTELPYDAHLPSEQKVPDRKWGLTFGFLTLALFTYSFLMVWRTNPNIPPATSPYAAIQKAFPLFHKDAIICMMLSVIWLFCLVAIPRFLYFLLASVPLTMFAFAVYLLKASRIHLETSIQPKLMLLTGIILLVAPILLSYYVWRRRIHFETSFNIIRLACRVIADIPQITLIFISFLFSFYVLIFIWVRLFARLFLR...
null
null
macroautophagy [GO:0016236]; protein transport [GO:0015031]; transmembrane transport [GO:0055085]
endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]; plasma membrane [GO:0005886]
choline transmembrane transporter activity [GO:0015220]; transmembrane transporter activity [GO:0022857]
PF04515;
null
CTL (choline transporter-like) family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Multi-pass membrane protein. Preautophagosomal structure membrane; Multi-pass membrane protein.
null
null
null
null
null
FUNCTION: Required for the normal organization of the preautophagosomal structure (PAS) and for the correct subcellular location of atg9. {ECO:0000269|PubMed:23950735}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74456
PEF1_SCHPO
MNYQRLEKLGEGTYAHVYKGQNRVTGEIVALKVIRIDADEGTPSTAIREISLMKELRHPNIMSLSDVLQTENKLMLVFEYMEKDLKKYMDTYGNQGALPPSQVKNFTQQLLKGISFCHENRVLHRDLKPQNLLINSRGELKLADFGLARSIGIPVNTFSNEVVTLWYRAPDVLLGSRVYSTSIDIWSVGCIMAEMATGRPLFAGSNNEDQLLKIFRLLGTPTEQSWPGISLLPEYKPTFPIYKAQDLAYLFPTFDPLGLDLLRRMLRLQPELRTTGQDALQHAWFLTA
2.7.11.22
null
negative regulation of mitotic cohesin loading [GO:1905412]; phosphorylation [GO:0016310]; signal transduction [GO:0007165]; synaptic vesicle transport [GO:0048489]; traversing start control point of mitotic cell cycle [GO:0007089]; vesicle-mediated transport [GO:0016192]
ascospore-type prospore [GO:0042764]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
ATP binding [GO:0005524]; cyclin-dependent protein serine/threonine kinase activity [GO:0004693]; protein serine kinase activity [GO:0106310]
PF00069;
1.10.510.10;
Protein kinase superfamily, CMGC Ser/Thr protein kinase family, CDC2/CDKX subfamily
null
null
CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.22; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p...
null
null
null
null
null
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74465
HRR1_SCHPO
MEQVQDEIWKLSTLDAWEMVNKNTEVVFDEIPEPETLSEMKRHPLYSNIFNADNNTTSFTEQIETSETSKTQDSEGNKVDKNLKENKSIRRKRSIDNDYELSNVKRNDITSGKNREFENEHHPASDTSSWRELPSIPTLEELTSKSVELPSNNIYGGYKSFEDYLSIHYRLLREDAVSPLRESVLRYKVNPNYITGSSLAVYDHVRIDGYTISSSVIAAKLSFSVRAKKKIKWATSRRLISGSLVLLSNDDFQTFRIGTVCARPLSGLNKHPHEIDVKFEDISISLDPREEYVMIEATSGYWEAYKHVLRSLQRLSASTF...
3.6.4.13
null
chromosome segregation [GO:0007059]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]
cytosol [GO:0005829]; nuclear RNA-directed RNA polymerase complex [GO:0031380]; nucleus [GO:0005634]; RNA-directed RNA polymerase complex [GO:0031379]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]
PF13086;PF13087;
3.40.50.300;
null
null
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
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=3.6.4.13;
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-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-i...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74469
YQC7_SCHPO
MDPEYSELFERLNKQLDNVEDVLKPLKDAESIFELAEGKSELEQAKLYITMSYAINSTLYSFYKLNGIDASERPVMQELQRVKNYISKIQQAEKNVNPKTEAVNTSNAAISSSSSNRPKVAKDAATRIIKHHT
null
null
exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000467]; maturation of 5.8S rRNA [GO:0000460]; nonfunctional rRNA decay [GO:0070651]; nuclear mRNA surveillance [GO:0071028]; nuclear polyadenylation-dependent mRNA catabolic process [GO...
cytosol [GO:0005829]; exosome (RNase complex) [GO:0000178]; nuclear exosome (RNase complex) [GO:0000176]; nucleolus [GO:0005730]; nucleus [GO:0005634]
DNA binding [GO:0003677]; RNA binding [GO:0003723]
PF04000;
null
C1D family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites (By similarity). {ECO:0000250}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74473
CDC11_SCHPO
MEQLWLEHDLSEEWIPQPQEQGSDNSSEPPTTSNVNNTQSTGRGSSGTSTEHGTFKKGRNDAPDVPQWKQVNAKNPVARDIFARLDLENMFEESSKQSPPSKSPTKNPSKKSSNNSSRRSSSSVGKLSNVSNMQSSPSKDPFVSQDYEKESISSSQFSKKYSEGSLKSQQSNTRSNSVHEKQNTDHASNASSSSSVVSSPSLKPNNTSPLKLFQGASDPFTREHLNQLTQDVKSNSFENGEKQFSLPEPRRPQKPMRTTERKASLNTKDLYQEVEEVMARLRGRMPNSGRESTIFLPRKLSGLREEEEQDEISVEVSQED...
null
null
positive regulation of mitotic division septum assembly [GO:0140281]; regulation of mitotic cytokinesis [GO:1902412]; septation initiation signaling [GO:0031028]
cytoplasm [GO:0005737]; mitotic spindle pole body [GO:0044732]; outer plaque of mitotic spindle pole body [GO:0061499]; protein-containing complex [GO:0032991]
signaling adaptor activity [GO:0035591]
PF13855;
3.80.10.10;
null
PTM: Phosphorylated by cdc7 and cdk1. Hyperphosphorylated during anaphase. Dephosphorylated by par1. {ECO:0000269|PubMed:11676915, ECO:0000269|PubMed:12546793, ECO:0000269|PubMed:15062098, ECO:0000269|PubMed:18257517}.
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Note=Localizes at the spindle pole body and the barrier septum.
null
null
null
null
null
FUNCTION: Essential for the onset of septum formation. Involved in the organization of astral microtubules during mitosis. Acts as a bridge between sid4 and the other SIN proteins mediating their association with the spindle pole body (SPB). The sid4-cdc11 complex organizes a signaling hub on the SPB which coordinates ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74475
FKS4_SCHPO
MSGNNENVSGITGHDAVSDDQYAYDSEVYDDQNAYQRQPADAYSNEEFLDQADYDSMYGEGYNGYDYPTGVTESYGDEYTPVDTASSGINQYSTEKGKFTRPSDEYESEYSDYNAQPSDANNFYNLRGDGRYNAYDPSSDSLANVYNSVPYGSSPYDFSNSSFVGNSGSGTPLDGDSGSFYADSANLTNREPYPAWTPENELPLTKEEIEDIFIDLTNKLGFQRDSMRNMYDFFMCLLDSRASRMTPDQALLTLHADYIGSDIANYKKWYFASQMDREDAVGLANVGIYGGKVTSIKEKGKFFSRNKKAPKVVKPPRKSR...
2.4.1.34
null
(1->3)-beta-D-glucan biosynthetic process [GO:0006075]; fungal-type cell wall (1->3)-beta-D-glucan biosynthetic process [GO:0071970]; fungal-type cell wall polysaccharide biosynthetic process [GO:0051278]; secondary cell septum biogenesis [GO:1990344]
1,3-beta-D-glucan synthase complex [GO:0000148]; cell cortex of growing cell tip [GO:1902716]; cell division site [GO:0032153]; cell tip [GO:0051286]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; division septum [GO:0000935]; Golgi apparatus [GO:0005794]; mating projection tip [GO:0043332]; mitotic actomyosin ...
1,3-beta-D-glucan synthase activity [GO:0003843]; branched 1,3-beta-D-glucan synthase activity [GO:0140752]
PF14288;PF02364;
null
Glycosyltransferase 48 family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15615781}; Multi-pass membrane protein {ECO:0000255}. Cell septum {ECO:0000269|PubMed:15615781}. Spore wall {ECO:0000269|PubMed:15615781}. Note=Localizes to regions of active cell wall synthesis in an F-actin dependent manner. Following nuclear division and format...
CATALYTIC ACTIVITY: Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:21476, Rhea:RHEA-COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378, ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34; Evidence={ECO:0000305|PubMed:15615781};
null
null
null
null
FUNCTION: Alternate catalytic subunit of the 1,3-beta-glucan synthase (GS) complex. Synthesizes 1,3-beta-glucan, a major structural component of the yeast cell wall (By similarity). Required for maintaining cell integrity during cytokinesis and polarized growth (PubMed:15615781). {ECO:0000250|UniProtKB:P38631, ECO:0000...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74476
IMB3_SCHPO
MSSGFPPEVLSPLLNLVQGLSSPDNTVRNDAEKSLSSDWISQRADLLLNGLAILAYQSEDPAVRSFCLVLCRRISFRTLPGDSELEVFSSISNESKQSLQSQLLACFVKESVPTVRNKLCDTIAEIARSIYDCQGEWPELINVIFNAVNSPDESFRESVFRTITSLPRLLSGQDSAVTPLFTTGLADPSIRVRISAARAYSAVILESKQSTRDQVIPLLPSLMNILPPLQQDRDSDNLADCLMAITEIAEVFPKLFKPIFESVIAFGLGIIKDKELDNSARQAALELLVCFSEGAPAMCRKSSDYTDQLVLQCLLLMTDV...
null
null
protein import into nucleus [GO:0006606]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nuclear periphery [GO:0034399]; nucleus [GO:0005634]
nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139]
PF13513;PF18808;PF18816;PF18829;
1.25.10.10;
Importin beta family, Importin beta-3 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:12399381, ECO:0000269|PubMed:1682337...
null
null
null
null
null
FUNCTION: Involved in the nuclear import of cdc25 and mcs1. {ECO:0000269|PubMed:12399381}.; FUNCTION: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for nuclear localization signals (NLS) in cargo substrates. Involved in the nuclear import of cdc25 and mcs1 (PubMed:12399381). Medi...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74499
LSM7_SCHPO
MSSLQKRPGPGNSSQPTERPRKESILDLSRYQDQRIQATFTGGRQITGILKGFDQLMNLVLDDVEEQLRNPEDGKLTGAIRKLGLVVVRGTTLVLIAPMDGSEEIPNPFVQAE
null
null
mRNA cis splicing, via spliceosome [GO:0045292]; nuclear-transcribed mRNA catabolic process [GO:0000956]; rRNA processing [GO:0006364]; telomerase holoenzyme complex assembly [GO:1905323]; tRNA processing [GO:0008033]
catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; Lsm1-7-Pat1 complex [GO:1990726]; Lsm2-8 complex [GO:0120115]; nucleus [GO:0005634]; spliceosomal tri-snRNP complex [GO:0097526]; telomerase holoenzyme complex [GO:0005697]; U2 snRNP [GO:0005686]; U2-type prespliceosome [GO:0071004]; U4/U6 x U5 tri-snRNP ...
poly(U) RNA binding [GO:0008266]; U2 snRNA binding [GO:0030620]
PF01423;
2.30.30.100;
SnRNP Sm proteins family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. Probable component of the spliceosome.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74511
EKC1_SCHPO
MFWRLGQGFGFQSSSAIEAILDKPEDEINLKELLEENGVLDECKSHNPKLLEYLCKPEVLSQLIDYILEVDETEIPSADGGYEEPEHTRLSYIASEILSSDVWSICEACVENKTLMVKLWSFLDSEGPLNPLQASYFAKVNEHFLDKKTEETVAFIQSIDNFVEKILRHAETSAIMDLLLKFISMDRCNTAIGIADWLYSQGLIQSLLRLLSPYVDPDVQFTVADVIKAIIAISANSNEPGVIGPNSLSRELVSRQTITTLTDYMTDSKAPHSATSLINGVSIVIELIRKNNSDYDVTPVLQMPLDTHPPTTRDPIYLGT...
null
null
cell cycle [GO:0007049]; cell division [GO:0051301]; negative regulation of protein localization to kinetochore [GO:1905341]; signaling [GO:0023052]
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein serine/threonine phosphatase complex [GO:0008287]
protein phosphatase activator activity [GO:0072542]; protein phosphatase binding [GO:0019903]; protein phosphatase regulator activity [GO:0019888]
PF04499;
null
SAPS family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12773390}. Note=Associated with chromatin.
null
null
null
null
null
FUNCTION: Has a role in chromosome segregation. May provide a dynamic connection between kinetochore microtubules and kinetochore chromatin. {ECO:0000269|PubMed:12773390}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74518
CID12_SCHPO
MGKVLLELHSVPWNEEGLSDNARLYSFLEFVSPKIEELKYRKLLLEKLQTHIREVVLDAELQVYGSMYIGTTLSISDVDVSLKSPRVGELEKRRVTMVLRKYLDADADFHSSARVPRINLVDVSGIGVDLTFGNDKACRTAELQKAYNEEHPIFGRLLMLLKHWLFERDLENVHHGGIASCALSYMLIGWLEMRFHKKGIDSEVQPIRALLQKFFYFWGVEWTYELFVLRPLTGQIVPKLQKGWLNEVQPNLLSIEDPIDRNNDIGKQSFQISMIKAAFVASANELLSDKTWFSTFAITEDEMFLCKQFENVINTKRSLV...
2.7.7.19
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
chromosome segregation [GO:0007059]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; RNA 3'-end processing [GO:0031123]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]
cytosol [GO:0005829]; nuclear RNA-directed RNA polymerase complex [GO:0031380]; nucleolus [GO:0005730]; nucleus [GO:0005634]; RNA-directed RNA polymerase complex [GO:0031379]; TRAMP complex [GO:0031499]
ATP binding [GO:0005524]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; poly(A) RNA polymerase activity [GO:1990817]
PF03828;
1.10.1410.10;3.30.460.10;
DNA polymerase type-B-like family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:15607976, ECO:0000269|PubMed:16823372}.
CATALYTIC ACTIVITY: Reaction=ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide; Xref=Rhea:RHEA:11332, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17347, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:140395, ChEBI:CHEBI:173115; EC=2.7.7.19;
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-directed RNA polymerase complex (RDRC) which is involved in the generation of small interfering RNAs (siRNAs) and mediate their association with the RNA-i...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74536
SNF1_SCHPO
MQPQEVDLMENSTMRNGARVLPPEAISKRHIGPYIIRETLGEGSFGKVKLATHYKTQQKVALKFISRQLLKKSDMHMRVEREISYLKLLRHPHIIKLYDVITTPTDIVMVIEYAGGELFDYIVEKKRMTEDEGRRFFQQIICAIEYCHRHKIVHRDLKPENLLLDDNLNVKIADFGLSNIMTDGNFLKTSCGSPNYAAPEVINGKLYAGPEVDVWSCGIVLYVMLVGRLPFDDEFIPNLFKKVNSCVYVMPDFLSPGAQSLIRRMIVADPMQRITIQEIRRDPWFNVNLPDYLRPMEEVQGSYADSRIVSKLGEAMGFSE...
2.7.11.1
null
CAMKK-AMPK signaling cascade [GO:0061762]; induction of conjugation with cellular fusion [GO:0010514]; negative regulation of cytoplasmic translation [GO:2000766]; negative regulation of TORC1 signaling [GO:1904262]; phosphorylation [GO:0016310]; positive regulation of ascus development [GO:0075319]; positive regulatio...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle pole body [GO:0044732]; nucleotide-activated protein kinase complex [GO:0031588]; nucleus [GO:0005634]
ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF16579;PF00069;PF08587;
1.10.8.10;3.30.310.80;1.10.510.10;
Protein kinase superfamily, CAMK Ser/Thr protein kinase family, SNF1 subfamily
PTM: Phosphorylation at Thr-189 by ssp1 is required for nuclear entry in nutritionally stressed cells (PubMed:22375066). {ECO:0000269|PubMed:22375066}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22375066}. Nucleus {ECO:0000269|PubMed:22140232, ECO:0000269|PubMed:22375066}. Note=Nuclear translocation occurs under nitrogen and glucose starvation conditions and depends on Thr-189 phosphorylation by ssp1 (PubMed:22375066). {ECO:0000269|PubMed:22375066}.
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:0000250|UniProtKB:P06782}; CATALYTI...
null
null
null
null
FUNCTION: Serine/threonine protein kinase essential for release from glucose repression via the phosphorylation of scr1 upon glucose deprivation (PubMed:22140232). Catalytic subunit of the AMP-activated protein kinase complex also known as the SNF1 kinase complex (Snf1c), a central regulator of cellular energy homeosta...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74539
MAK3_SCHPO
MYSQHELRNKVSLALSSLLRYTFELTPFFELYEADFAYALYAGFELATNRKVVGKFSFQNVHLENEYNILTEIAKDERASKFSPTPIEFTSFPHIDLSACIAYDFGHGAELSTSYAYFRENPAEFVRFCIAICKCIEYLHSKGMVHGEIRLDSFIPISSYDNVYMLTVGSGASYFHNCLQAHNWRKYSEDSESMSRILFISPEQTGRTSYSVGYRTDIYSLGVLFFHYLSDCSPYTGSFVQRIRSILTEPLPDISKSCPKLPHLIFKIIEKMTRKNPDERYTSCSGIVNDLEACLDDIDKGLILNDHVLEKTGRTSLFYL...
2.7.13.3
null
phosphorelay signal transduction system [GO:0000160]; positive regulation of p38MAPK cascade [GO:1900745]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein histidine kinase complex [GO:0009365]
ATP binding [GO:0005524]; phosphorelay sensor kinase activity [GO:0000155]
PF13191;PF13185;PF00512;PF08447;PF00069;PF00072;
1.10.287.130;3.30.450.40;3.40.50.2300;3.30.565.10;3.30.450.20;1.10.510.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11179424}.
CATALYTIC ACTIVITY: Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.; EC=2.7.13.3;
null
null
null
null
FUNCTION: Involved in the control of the SAPK-dependent transcriptional response to peroxide stress. Regulates sty1 activity. {ECO:0000269|PubMed:11179424, ECO:0000269|PubMed:11758939}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74555
BBP_SCHPO
MLNSRSVGSTGSNNTPLGRRRFDEKPDSLPPLPDANGMSNGYRDSYKSNSRMDHRPDGYHDGRGRRAYRKHYWGHPTPIEEMLPSQMELETAVKSCMTMEQLELYSLNVRLEEITQKLRTGDVVPHHRERSPSPPPQYDNHGRRLNTREIRYKKKLEDERHRIIERAMKMVPGFRAPSDYRRPAKTQEKVYVPVKDYPEINFIGLLIGPRGHTLKDMEAKSGAKIAIRGKGSVKEGKGRSDPSVRGNMEEDLHCLVTADSEDKINHAIKLIDNVIQTAASVPEGQNDLKRNQLRQLATLNGTLRDDENQVCQNCGNVGHR...
null
null
mRNA cis splicing, via spliceosome [GO:0045292]; regulation of mRNA splicing, via spliceosome [GO:0048024]
commitment complex [GO:0000243]; cytosol [GO:0005829]; nucleus [GO:0005634]; U2-type prespliceosome [GO:0071004]
mRNA binding [GO:0003729]; RNA binding [GO:0003723]; zinc ion binding [GO:0008270]
PF00013;PF16275;PF00098;
6.10.140.1790;3.30.1370.10;4.10.60.10;
BBP/SF1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Necessary for the splicing of pre-mRNA. The BPB1(SF1)-u2af59-u2af23 complex has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns. {ECO:0000269|PubMed:12374752}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74558
MOB2_SCHPO
MFLLNSLSRITRGNRSKRHQNLSDASSSSGSFSKKSSTSQLVRTGSPSVEPTALYLQQPFVRTHLVKGNFSTIVSLPRFVDLDEWVALNVYELFTYLNHFYDVFATFCTVKTCPVMSAAANFDYTWLDNNRKPVHLPAPQYIEYVLAWIENRLHDQNVFPTKAGLPFPSNFLVIVKAIYKQMFRIFAHMYYAHYAEILHLSLEAHWNSFFAHFIAFGKEFQLLDKRDTAPLKDLIVVLENQGNI
null
null
cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of protein phosphorylation [GO:0001934]; RAM/MOR signaling [GO:0062200]; regulation of establishment or maintenance of bipolar cell polarity regulating cell shape [GO:2000100]; signal transduction [GO:0007165]
cell cortex [GO:0005938]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; nucleus [GO:0005634]
protein kinase activator activity [GO:0030295]
PF03637;
1.20.140.30;
MOB1/phocein family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12456722}. Cytoplasm, cell cortex {ECO:0000269|PubMed:12456722}. Note=Localizes to the cell periphery and to the division site during septation and cytokinesis.
null
null
null
null
null
FUNCTION: Required for coordinating polarized cell growth during interphase with the onset of mitosis. {ECO:0000269|PubMed:12456722}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74560
RAF2_SCHPO
MPPVRAEKKRKTDLIEQVCVTNKAGELVDLEDVLEYGPYSLTGILSSEKDEQEPLFDESIVLGYSIKISPVWTYNLKDVPEKETMSIWIVTPQRRYGILSPSSEYKAIYEQISEKNRLFYLIKTKFKDDMISGTLEDYDNYIEVLKEKLELPSCFQAILLVQKHIRFLLTQMVATSSLHVWSESPFFIRIRSSYEHLILQINKNIYNARQERKKSKLSSNNPSDNNTTMKSSLNQALTLINLPEQPFSISSPTATPQLGVVKRTSPLRFPLNDIWLSGLRIVDPNIESISLWKRIQVSTSPKHQRYISLQEVCSVIAQQL...
null
null
CENP-A containing chromatin assembly [GO:0034080]; 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]; CLRC complex [GO:0043494]; cytoplasm [GO:0005737]; heterochromatin island [GO:1990342]; mating-type region heterochromatin [GO:0031934]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
null
PF12047;
null
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Mitochondrion {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16040243, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18345014}. Chromosome {ECO:0000269|PubMed:16040243, ECO:0000269|PubMed:18345014}.
null
null
null
null
null
FUNCTION: Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me (PubMed:16024659, PubMed:16040243, PubMed:16157682). ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74562
SEC8_SCHPO
MDTRGYSETKKGRYPVGKKSLESPNGYSNYGTSMDNELSSEYASRGMHIGDLENLVNEIEDEWKDLGREDYQPISTALELLDDSSFGRDYKSFLNVYDRISAALQTIAHTHKDDFTRGISAYGEIMEGIQKCNSRIIALKQSLEASQECIGNTNSKELQQTLARSSQYKKVISVLKELNEANQLFDNFHTLVDSKQYYHASDLIRRVWDELSRSDFDGILVVEQFKSRMTGLLSHLEDILSEELVSITFLKDAVAYPIVSYCSPNPLRETSNPYFLRDFLKNNANTSTLGQSEQLRYLEEALSLKLSDCLKMDYGRDSLR...
null
null
ascospore-type prospore membrane formation [GO:0032120]; division septum assembly [GO:0000917]; endocytosis [GO:0006897]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; intracellular protein transport [GO:0006886]; vesicle docking involved in exocytosis [GO:0006904]; vesicle tethering involve...
cell cortex of growing cell tip [GO:1902716]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; exocyst [GO:0000145]; meiotic spindle pole [GO:0090619]; mitotic actomyosin contractile ring [GO:0110085]
null
PF20652;PF04048;
null
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16141239, ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:11854409}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11854409}. Cytoplasmic vesicle {ECO:0000269|PubMed:16141239}. Note=Associated with the actinomyosin ring at the division site and at the cell ti...
null
null
null
null
null
FUNCTION: Component of the exocyst complex involved in the delivery of secretory vesicles to the plasma membrane. Also required for polarized cell growth and division septum assembly. The exocyst complex plays an important role in the targeting of rho3, as well as the two main hydrolases required for cell separation, e...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74563
BRL2_SCHPO
MYQNGKPDAPTILGQKRELEDVEIQDDDIQEVSKEDLLKDVRVRSIQFDELESKIEGLQNLAEEKLKVLATLVSWWPEILQQFSVVFQGNELKDFESEGVFSILEKFPELSYFNDAVKNNKTKALSIIQKLLSTVDSSTNSVSRDPFSVLSIDDSALTEKLNTINLDIDKILDELDTTRSQLHSIIKLPDRSSSFTLQCINESVRPQSTKVKEEATTSSKGKDEEKKVSTVEQRTQLQQLSRLQDQQNGLMESRSQSLKILDSNVNEMDKLIMERENALNNVETTNLKKYSSFLALKEAVSMTSEQLRVLEHLLSECSHE...
2.3.2.27
null
epigenetic regulation of gene expression [GO:0040029]; protein ubiquitination [GO:0016567]; transcription elongation-coupled chromatin remodeling [GO:0140673]
HULC complex [GO:0033503]; nucleus [GO:0005634]
histone H2B C-terminal K residue ubiquitin ligase activity [GO:0140850]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF08647;PF13923;
3.30.40.10;
BRE1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
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};
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase which belongs to the histone H2B ubiquitin ligase complex (HULC) which mediates monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also a prerequisite for H3K4me and H3K79me formation. {ECO:0000269|...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74627
CG1C_SCHPO
MSEVIKSVPPGSQNTSQWIISKDQLVFTPSALDGIPLDQEEIQRSKGCNFIINVGLRLKLPQTALATANIYFHRFYLRFSLKNYHYYEVAATCIFLATKVEDSVRKLRDIVINCAKVAQKNSNVLVDEQTKEYWRWRDVILYTEEVLLEALCFDFTVEHPYPYVLSFIKKFVADDKNVTKVAWTYINDSTRSIACLLYSPKTIAAAAFQFALEKNEINLSTTTDGLPVWMEESQVSYEDVKGVLTLIDSLYKKINPSKQALPIDQKNGSHASSVAPGTPSSLASVSTQATPQHQNSSGRTDSFHSLNTETPSKSTVDDQI...
null
null
cell cycle [GO:0007049]; cell division [GO:0051301]; positive regulation of DNA-templated transcription, elongation [GO:0032786]; regulation of transcription by RNA polymerase II [GO:0006357]; signaling [GO:0023052]
cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cyclin/CDK positive transcription elongation factor complex [GO:0008024]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-TEFb complex [GO:0070691]
cyclin-dependent protein serine/threonine kinase activator activity [GO:0061575]
PF02984;PF00134;
1.10.472.10;
Cyclin family, Cyclin C subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
null
null
null
null
null
FUNCTION: Essential for progression through the whole cell cycle. {ECO:0000269|PubMed:9115279}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74630
ATM_SCHPO
MTSLNDIVNKLSSSKIKTRSDALQNLRSYIIYSRNGNSLNQEDALIIEKAIKRAFELEWQISANHGKRQISKASQEQKLQDISYLLRTCVESYILLFREPHILALLDIILRHTFTANGSICEVVCLNFSKALRLLLSHSPHLHHLRFSDWQSLVSYCCQAIEKLSIAEETYVSDSEEEPISQKNYQEISIWKSHDVIRVKQEVVELIYVMRSLVQWYAAPINFVSEQLLKFFEFFFYAYTEETDAHLPALQCLFQLCAYAIPNCNDYSASVVLLVFKILINSDKWKRLDLRLQLIQCLAISYPLWSNSETWDPHRSIRSF...
2.7.11.1
null
DNA damage checkpoint signaling [GO:0000077]; DNA repair [GO:0006281]; mitotic DNA damage checkpoint signaling [GO:0044773]; negative regulation of TORC1 signaling [GO:1904262]; phosphorylation [GO:0016310]; positive regulation of initiation of premeiotic DNA replication [GO:1904514]; spatial regulation of meiotic DNA ...
chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; nucleus [GO:0005634]
ATP binding [GO:0005524]; histone H2AS121 kinase activity [GO:0072371]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]
PF02259;PF02260;PF00454;PF11640;
1.10.1070.11;
PI3/PI4-kinase family, ATM subfamily
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000250}. Note=Localizes to nuclear DNA repair foci with other DNA repair proteins in response to DNA double strand breaks. {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: Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates histone H2A to form H2AS1...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74641
INUA_ASPNG
MLNPKVAYMVWMTCLGLMLPSQAQSNDYRPSYHFTPDQYWMNEPNGLIKIGSTWHLFFQHNPTANVWGNICWGHATSTDLMHWAHKPTAIADENGVEAFTGTAYYDPNNTSGLGDSANPPYLAWFTGYTTSSQTQDQRLAFSVDNGATWTKFQGNPIISTSQEAPHDITGGLESRDPKVFFHRQSGNWIMVLAHGGQDKLSFWTSADTINWTWQSDLKSTSINGLSSDITGWEVPDMFELPVEGTEETTWVVMMTPAEGSPAGGNGVLAITGSFDGKSFTADPVDASTMWLDNGRDFDGALSWVNVPASDGRRIIAAVMN...
3.2.1.7
null
polysaccharide catabolic process [GO:0000272]; sucrose catabolic process [GO:0005987]
cytoplasm [GO:0005737]; extracellular region [GO:0005576]
inulinase activity [GO:0051670]; sucrose alpha-glucosidase activity [GO:0004575]
PF08244;PF00251;
null
Glycosyl hydrolase 32 family
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (2->1)-beta-D-fructosidic linkages in inulin.; EC=3.2.1.7; Evidence={ECO:0000269|PubMed:15135402};
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.57 mM for inulin {ECO:0000269|PubMed:15135402};
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:15135402};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius. {ECO:0000269|PubMed:15135402};
FUNCTION: Endo-inulinase involved in utilization of the plant storage polymer inulin, consisting of fructooligosaccharides with a degree of polymerization (DP) value from 2 to 60. {ECO:0000269|PubMed:15135402}.
Aspergillus niger
O74653
POB1_SCHPO
MASQRFVIALHSFPGKSSDELPLVEGRKYLLIKMDEEFGDGWWEGEDEQGNRGIFPASHVELISDERSDSSDSRRGKEDFSISTAEVTRSSLSSSRSTSSRSDKDSEKLYSNNSLSSSHSSILNGPLDSLSKPSVPSNFNSMFPSSKQEGPSPLLDNQPSSDLSNFNTIDADYNNASASTSAPATSASLKKVLSAEDSVRETITDIETALQNMSTSASRTPNDSSPLPYIENRPASSLAVSEKIQNVPNWSTEEVVEWLMNAGLGSVAPNFAENEITGEILLGLDSNVLKELNITSFGKRFEVLRKIQQLKDSYEQSLYE...
null
null
endosome organization [GO:0007032]; exocytosis [GO:0006887]; receptor recycling [GO:0001881]; retrograde transport, endosome to Golgi [GO:0042147]
cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cell tip [GO:0051286]; cytosol [GO:0005829]; early endosome [GO:0005769]; medial cortex [GO:0031097]; membrane [GO:0016020]; recycling endosome [GO:0055037]; trans-Golgi network [GO:0005802]
lipid binding [GO:0008289]
PF00169;PF07647;PF00018;
2.30.29.30;2.30.30.40;1.10.150.50;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10436025}. Membrane {ECO:0000269|PubMed:10436025}; Peripheral membrane protein {ECO:0000269|PubMed:10436025}. Note=Membrane-associated at the cell tips during interphase.
null
null
null
null
null
FUNCTION: Has a role in cell elongation and separation. {ECO:0000269|PubMed:10436025}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74700
TIM9_YEAST
MDALNSKEQQEFQKVVEQKQMKDFMRLYSNLVERCFTDCVNDFTTSKLTNKEQTCIMKCSEKFLKHSERVGQRFQEQNAALGQGLGR
null
null
protein insertion into mitochondrial inner membrane [GO:0045039]
mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial intermembrane space protein transporter complex [GO:0042719]; mitochondrion [GO:0005739]; TIM22 mitochondrial import inner membrane insertion complex [GO:0042721]
metal ion binding [GO:0046872]; protein transporter activity [GO:0140318]; unfolded protein binding [GO:0051082]
PF02953;
1.10.287.810;
Small Tim family
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:9822593, ECO:0000269|PubMed:9889188}; Peripheral membrane protein {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:9822593, ECO:0000269|PubMed:9889188}; Intermembrane side {ECO:0000269|PubMed:16823961, ECO:0000269|PubMed...
null
null
null
null
null
FUNCTION: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membran...
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
O74718
ERF3_SCHPO
MASNQPNNGEQDEQLAKQTSKLSMSAKAPTFTPKAAPFIPSFQRPGFVPVNNIAGGYPYAQYTGQGQNSNSPHPTKSYQQYYQKPTGNTVDEDKSRVPDFSKKKSFVPPKPAIPKGKVLSLGGNTSAPKSTKPISISLGGTKAPTTTKPAAPAAQSKTETPAPKVTSESTKKETAAPPPQETPTKSADAELAKTPSAPAAALKKAAEAAEPATVTEDATDLQNEVDQELLKDMYGKEHVNIVFIGHVDAGKSTLGGNILFLTGMVDKRTMEKIEREAKEAGKESWYLSWALDSTSEEREKGKTVEVGRAYFETEHRRFSL...
3.6.5.-
null
cytoplasmic translational termination [GO:0002184]; nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; translation [GO:0006412]
cytosol [GO:0005829]; translation release factor complex [GO:0018444]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; magnesium ion binding [GO:0000287]; translation release factor activity [GO:0003747]
PF00009;PF03143;
3.40.50.300;2.40.30.10;
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, ERF3 subfamily
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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:19417105}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:19417105}...
null
null
null
null
FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons (PubMed:19417105). Sup35/eRF3 mediates sup45/ERF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in the ribosomal A-site (PubMed:194171...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74736
ING2_SCHPO
MGTSGIEIFAALNDFTDAIVSVPESVCGKFTSLKEIDAQVRDIRQNVIQEIGVVLKNEKNDELSGEERCERLQKTLKEILPYSDSKICLATDAMNNIKSCIDRLDAGFEYVELEIPQQLRLGYPDDRALMNYHSTVTPQTSERRRETRRHQNNQHSQQYSSQERSSSYNNFEDASSPQSSYHTPTKRRKNAVPRKSSSPPLSSTKHAPQSTERRPVRRSESRLKQTNGEPLVKHDTLDSSDISREGEQLYCYCQQVSYGQMIGCDNENCKREWFHLPCVGLVEPPKGIWYCKECEELAKSSESRQ
null
null
DNA repair-dependent chromatin remodeling [GO:0140861]; regulation of DNA-templated transcription [GO:0006355]
cytosol [GO:0005829]; NuA4 histone acetyltransferase complex [GO:0035267]; nucleus [GO:0005634]; Rpd3L complex [GO:0033698]
histone acetyltransferase activity [GO:0004402]; metal ion binding [GO:0046872]; methylated histone binding [GO:0035064]
PF12998;
6.10.140.1740;3.30.40.10;
ING family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Component of the clr6 histone deacetylase complex I' responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progres...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74739
PNG1_SCHPO
MDFHAISQRFIDMMRSKNSQNASQPPETYPFYHEVRQMSQHPWMYEDPELQDYALSILPLDKLFQDASELEKEGDGSWGYQDYVIQALLKWFKREFFVWVNQPPCEKCGGETHMTGNGPPNEEEKWNGVRNVELYQCNVCGHNQRFPRYNRIRALLDSRKGRCGEWANCFTFLCRALGSRARWIWNAEDHVWTEVYSNKQQRWVHVDSGEESFDEPLIYEQGWGKKMSYCLGFGIDSVRDVSHRYIRHPENGLPRDRCPESVLQQALHEINIEFRSRLTDSERKALEEEDKREKDELDGYMRPVSQATPTNTDLPARQTG...
3.5.1.52
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
ERAD pathway [GO:0036503]; glycoprotein catabolic process [GO:0006516]; protein quality control for misfolded or incompletely synthesized proteins [GO:0006515]
cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; misfolded protein binding [GO:0051787]; peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity [GO:0000224]
PF01841;
2.20.25.10;3.10.620.30;
Transglutaminase-like superfamily, PNGase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CATALYTIC ACTIVITY: Reaction=Hydrolysis of an N(4)-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue.; EC=3.5.1.52;
null
null
null
null
FUNCTION: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74752
MAS5_SCHPO
MVKETKLYEVLNVDVTASQAELKKAYRKLALKYHPDKNPNAGDKFKEISRAYEILADEEKRATYDRFGEEGLQGGGADGGMSADDLFASFFGGGMFGGGMPRGPRKGKDLVHTIKVTLEDLYRGKTTKLALQKKVICPKCSGRGGKEGSVKSCASCNGSGVKFITRAMGPMIQRMQMTCPDCNGAGETIRDEDRCKECDGAKVISQRKILTVHVEKGMHNGQKIVFKEEGEQAPGIIPGDVIFVIDQKEHPRFKRSGDHLFYEAHVDLLTALAGGQIVVEHLDDRWLTIPIIPGECIRPNELKVLPGQGMLSQRHHQPGN...
null
null
cellular response to heat [GO:0034605]; cytoplasm protein quality control [GO:0140455]; protein aggregate center assembly [GO:0140454]; protein refolding [GO:0042026]; protein transport [GO:0015031]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; protein aggregate center [GO:0140453]
ATP binding [GO:0005524]; Hsp70 protein binding [GO:0030544]; metal ion binding [GO:0046872]; protein sequestering activity [GO:0140311]; protein-folding chaperone binding [GO:0051087]; unfolded protein binding [GO:0051082]
PF00226;PF01556;PF00684;
1.10.287.110;2.10.230.10;2.60.260.20;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Probably involved in mitochondrial protein import (By similarity). Plays a role in microtubule cytoskeleton organization. {ECO:0000250, ECO:0000269|PubMed:15797925}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74757
HRD1_SCHPO
MKFILYVLASLVLFGLSVLLSLYSSANVYSATVMISQSPVHITIGLNVCLCLFFAIANALKTLLFGSLQTFELELLYEQFWITLTEIMLAITVFREAISISFFMLLSTLMFARVFHSICSFRTERLQIQLTDQRFHIFSRLTCAYFVLSILDASLIYLCFTSEHLGDKSTRMLFVCEFSVLLLNLTIEASKLCIYLYEARHLDQVWDEKSTYLFRLEVCRDGLRLLAYSLLFMYQFPYVSVPIYSIRQMYTCFYSLFRRIREHARFRQATRDMNAMYPTATEEQLTNSDRTCTICREEMFHPDHPPENTDEMEPLPRGLD...
2.3.2.27
null
ERAD pathway [GO:0036503]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511]
cell cortex [GO:0005938]; cytoplasm [GO:0005737]; endomembrane system [GO:0012505]; Hrd1p ubiquitin ligase complex [GO:0000836]
ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270]
PF12678;
3.30.40.10;
HRD1 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
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;
null
PATHWAY: Protein modification; protein ubiquitination.
null
null
FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of endoplasmic reticulum proteins (ERQC), also called ER-associated degradation (ERAD). Component of the hrd1 ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74760
EIF3A_SCHPO
MAPPQGKPENVLRLADELIALDQHSSALQSLHETIVLKRSRNAQGFSLEPIMMRFIELCVHLRKGKIAKEGLYTYKNAVQNTSVTAIENVVKHFIELANKRVQEAQEKADKISVEYVDDLEATETPESIMMSLVSGDLSKSRTDRALVTPWLKFLWDAYRTVLDILRNNARLEVMYQLIANSAFQFCLKYQRKTEFRRLCELLRSHLGNASKFSNAPHSINLNDAETMQRHLDMRFSQLNVAVELELWQEAFRSIEDIHSLLTFSKRAPAAVMLGNYYRKLIKIFLVCDNYLLHAAAWNRYFTFTNVQKPATANFVILSA...
null
null
formation of cytoplasmic translation initiation complex [GO:0001732]; translation reinitiation [GO:0002188]
cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; 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 trans...
mRNA binding [GO:0003729]; translation initiation factor activity [GO:0003743]
null
1.25.40.860;4.10.860.10;
EIF-3 subunit A family
null
SUBCELLULAR LOCATION: Cytoplasm.
null
null
null
null
null
FUNCTION: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically t...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74774
HBS1_SCHPO
MSRHRDVKNLDLDDYELDEEPGEEELTEEQEEEFRSAVATVRETLLGVPISEKEIADTVWYYYFDVEKSVNYLLQKASSKAGAKEKQNTDSQKEKKQNKSKEALADAKDPLDESSNGIKNLSLNKNDEPAFQTNGEVKMKNSSESDNQPEKKKIKKQNPTDLVSVPEIFEQSNPKPVVHLVVTGHVDSGKSTMLGRIMFELGEINSRSMQKLHNEAANSGKGSFSYAWLLDTTEEERARGVTMDVASTTFESDKKIYEIGDAPGHRDFISGMIAGASSADFAVLVVDSSQNNFERGFLENGQTREHAYLLRALGISEIVV...
3.6.5.-
null
cytoplasmic translational termination [GO:0002184]; endoplasmic reticulum unfolded protein response [GO:0030968]; nuclear-transcribed mRNA catabolic process, no-go decay [GO:0070966]; translation [GO:0006412]
cytosol [GO:0005829]; Dom34-Hbs1 complex [GO:1990533]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746]; translation release factor activity [GO:0003747]
PF00009;PF08938;
3.40.50.300;2.40.30.10;
TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
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:0000250|UniProtKB:P32769}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P3276...
null
null
null
null
FUNCTION: GTPase component of the Dom34-Hbs1 complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway (PubMed:20890290). The Dom34-Hbs1 complex recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel (By similar...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74791
GRN1_SCHPO
MVSLKKKSKRRTTRLRSRIEKKAAESKRKQKRADKKNPQWKSRIPKDPGIPNSFPYKDKILAEIEEQKRIREEEKLARRASGQVDAAMEEEDAVDENGSLMISKIAEAAQASNPDDEEEFVMEEDNLGEAPLLVDSESYEASVKADTSRKAYDKEFKKVVEASDVILYVLDARDPEGTRSKDVERQVLASSAEEKRLIFVINKIDLVPSEVLNKWVTYLRNFFPTIPMRSASGSGNSNLKHQSASASSTISNLLKSLKSYSAKKKLKSSLTVGVIGYPNVGKSSVINALVNRSANGRSAPCPAGNVAGMTTSLREVKLDN...
null
null
protein transport [GO:0015031]; rRNA processing [GO:0006364]
nucleolus [GO:0005730]; nucleus [GO:0005634]
GTP binding [GO:0005525]; GTPase activity [GO:0003924]; RNA binding [GO:0003723]
PF08701;PF01926;
1.10.1580.10;3.40.50.300;
TRAFAC class YlqF/YawG GTPase family
null
SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16251348, ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Required for optimal growth. Required for normal processing of ribosomal pre-rRNA. Required for nuclear export of ribosomal protein rpl2501. {ECO:0000269|PubMed:16251348}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74803
RHP23_SCHPO
MNLTFKNLQQQKFVISDVSADTKISELKEKIQTQQNYEVERQKLIYSGRILADDKTVGEYNIKEQDFIVCMVSRPKTSTSTPKSAASPAPNPPASVPEKKVEAPSSTVAESTSTTQTVAAAAPSNPDTTATSEAPIDANTLAVGAQRNVAVENMVEMGYERSEVERAMRAAFNNPDRAVEYLLTGIPEDILNRQREESAAALAAQQQQSEALAPTSTGQPANLFEQAALSENENQEQPSNTVGDDPLGFLRSIPQFQQLRQIVQQNPQMLETILQQIGQGDPALAQAITQNPEAFLQLLAEGAEGESALPSGGIQIQITQ...
null
null
ERAD pathway [GO:0036503]; nucleotide-excision repair [GO:0006289]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]
cytosol [GO:0005829]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
damaged DNA binding [GO:0003684]; polyubiquitin modification-dependent protein binding [GO:0031593]; proteasome binding [GO:0070628]; ubiquitin binding [GO:0043130]
PF00627;PF00240;PF09280;
1.10.8.10;1.10.10.540;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11788722}.
null
null
null
null
null
FUNCTION: Involved in postreplication repair of UV-damaged DNA. Postreplication repair functions in gap-filling of a daughter strand on replication of damaged DNA. {ECO:0000269|PubMed:12560082}.; FUNCTION: Protects ubiquitin chains against dissambly by deubiquitinating enzymes thereby promoting protein degradation. {EC...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74804
EST1_SCHPO
MSQQLSSNEICEEQGKLVKALCEAAQGGFKHDLYEKIIAIEIEVEKKLLNRLKSIQTNTFERPDIIWSCCHYKIIQHFRSRFREIHPRHVVEKKKTKKVFFKFLKTCAIFYQTCISELISKFQLDSYRPFFCKWTSSATVSSTISNDEMSSIPEASYSRNHMEALECVYNCFIYLGDMARYSSTCLKKRGAYDRALGFYDLAHRTLPGNGMHRNQIAVVWASDECIVESIYWFSSALCSEDPPKSALLNLLKQLIAFYRRCFAVHFEFVSPMMILLFIISDCCIHSLKEIQPFKCPSIMVKDLENSLLQSNIRNVGYEKK...
null
null
nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; telomere maintenance via telomerase [GO:0007004]; telomere-telomerase complex assembly [GO:1905324]
chromosome, telomeric repeat region [GO:0140445]; nuclear periphery [GO:0034399]; nucleus [GO:0005634]; telomerase holoenzyme complex [GO:0005697]
single-stranded telomeric DNA binding [GO:0043047]; telomerase RNA binding [GO:0070034]
PF10374;PF10373;
1.25.40.10;
EST1 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12676088}. Chromosome, telomere {ECO:0000305|PubMed:12676088}.
null
null
null
null
null
FUNCTION: Directly involved in telomere replication. Associates with telomerase and during its interaction with trt1, telomerase activity is promoted. {ECO:0000269|PubMed:12676088}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74805
MYO51_SCHPO
MSHARLSVGSECWVSNNNGHWDAARLIEIKDNGGGKVVATVAKSSGVLETVNYQQLQNRNIGQSESPSDLTNLPYLNEPSVLHALHNRYNNKQIYTYSGIVLVSINPYQNLPEFYNDNLIKHFHKDPEAAKVPHLYSIASSCYHALTTDSKNQTIIVSGESGAGKTVAAKYIMRYLTSVQGVDHNGVVKRSVENQVLATNPIMEAFGNAKTIRNDNSSRFGKYVTISFDENLLITGANVNTYLLERSRVVSLLKGERNYHIFYQLITGCTEEQRDKWFLESASSFNYLSQGNCDEISGVDDSNDFTITCRALSTIGISES...
null
null
actin filament bundle organization [GO:0061572]; actin filament organization [GO:0007015]; actomyosin contractile ring assembly actin filament bundle convergence [GO:0071520]; formin-nucleated actin cable assembly [GO:0070649]; mitotic actomyosin contractile ring assembly [GO:1903475]; protein transport to mating proje...
actin cytoskeleton [GO:0015629]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; formin-nucleated actin cable [GO:0070648]; mating projection actin fusion focus [GO:1990819]; membrane [GO:0016020]; mitotic actomyosin contractile ring [GO:0110085]; mitotic actomyosin contractile ring, prox...
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;1.20.58.530;6.20.240.20;3.40.850.10;1.20.120.720;
TRAFAC class myosin-kinesin ATPase superfamily, Myosin family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11112691}. Note=Component of the cytokinetic actin ring (CAR).
null
null
null
null
null
FUNCTION: Involved in cytokinesis. {ECO:0000269|PubMed:11112691}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74808
CLR1_SCHPO
MAEPDISSSETLTELQQLRLLYFFCFYHAAPFNVKTLVHSLIPPGALSYLLSTYDILRPWLMALRVREGPVNDISTIVQLYEEIVKTGFFINPPPFESYSQTLVARITTLGRPKLQVQQEAQSEVYQRASTNTQQQVSNVSHGNFKPNSSVNTEPNTSILSNSKYAGIKPFDFQSSSQNPGLVCEQKTFYQHQFRPFSNLPSNKSSPVKHVSPNVKNNSKKTASSVNSNHSSIPSSITKSNISSLDVYGSEKLISSGSQQPGHGMVQTTSDKVNASASLYDRSPSKKDITSSRNTSSYNLGSMRNPSTLKNAAHANPFEG...
null
null
chromatin organization [GO:0006325]; heterochromatin formation [GO:0031507]; silent mating-type cassette heterochromatin formation [GO:0030466]
chromosome, subtelomeric region [GO:0099115]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; rDNA heterochromatin [GO:0033553]; SHREC complex [GO:0070824]
metal ion binding [GO:0046872]
null
null
null
null
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome, telomere. Note=Associates with major heterochromatin, centromeres, sub-telomeres, rDNA and the mat locus.
null
null
null
null
null
FUNCTION: Regulates silencing of the mat2 and mat3 loci. Organizes the chromatin structure of the mating-type region where it also participates in establishing the 'cold spot' for recombination. Required for proper positioning of nucleosomes at heterochromatic loci and for transcriptional gene silencing (TGS) function ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74833
DNLI4_SCHPO
MDEAKETVFTKPQNHSSTLEFYDFVTTLLEPLSRIGKTRKSKTSNLDPYELKRKILLDYFNKWRQHVGPDLYPLLRLMLPDLDRERGSYGFKEFGLGKLFIRAMHLSPTSEDAKSLKNWRGSESKHTGDFSTMLQDILQRRAYRTFPGAFTVGDVNALLDQLADASSEDTRVNILEQFYRSLSPLELRWLIPILLKVRKYGTSEKFILSVFHPDAARLYRLCSSLKRICWELYDPSRSLDETETDVEVFSCFQPQLANFKKKDLHQTLEAMGNKPFWIEEKLDGERIQLHMSSGKFQFYSRNARSYTYAYGSSYFDEQSR...
6.5.1.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P49917};
DNA biosynthetic process [GO:0071897]; DNA ligation involved in DNA repair [GO:0051103]; DNA recombination [GO:0006310]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; double-strand break repair via nonhomologous end joining [GO:0006303]; nucleotide-excision repair, DNA gap filling [GO...
chromatin [GO:0000785]; DNA ligase IV complex [GO:0032807]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; nucleolus [GO:0005730]; nucleus [GO:0005634]
ATP binding [GO:0005524]; DNA binding [GO:0003677]; DNA ligase (ATP) activity [GO:0003910]; metal ion binding [GO:0046872]
PF04679;PF01068;PF04675;
3.40.50.10190;1.10.3260.10;3.30.470.30;2.40.50.140;
ATP-dependent DNA ligase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q08387}.
CATALYTIC ACTIVITY: Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.; EC=6.5.1.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10135};
null
null
null
null
FUNCTION: DNA ligase involved in DNA non-homologous end joining (NHEJ); required for double-strand break (DSB) repair. {ECO:0000269|PubMed:11029034, ECO:0000269|PubMed:11172711, ECO:0000269|PubMed:15226425}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74839
MSY1_SCHPO
MSSPTSPTSSPGRHHWSNSKDGMPPEYTNQDPNSDQADNENSDAKAHQPQHSPQHSTENQGHTGTSDTSSLEMELSKLHPESKQRQLPHSPEHERSRSPIASVVSYRSHMTLEDENQIFNAEMAVRGSQSLQRRPTGRSVRGSMRRLSSHRSKSMRTSKSKKSGDYERTAENEEAAQEAENHLDNFGVVTFGTEAPIKAPDHPVTIFGRIFKFIQQRSFYLRSLIYIIPLGVLLLIPVFIGRFYHPQPPYRDELGHEYERHLHVGGVDLMWMAIWWEIIWLSIWAARYAAKVIPYFFAFFVSFISNNVTKWRCMAVALEF...
null
null
calcium ion transmembrane transport [GO:0070588]; cell volume homeostasis [GO:0006884]; intracellular calcium ion homeostasis [GO:0006874]
endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; perinuclear endoplasmic reticulum [GO:0097038]
calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; stretch-activated, monoatomic cation-selective, calcium channel activity [GO:0015275]
PF00924;
2.30.30.60;
MscS (TC 1.A.23) family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22910366}; Multi-pass membrane protein {ECO:0000305}. Note=Perinuclear endoplasmic reticulum. {ECO:0000269|PubMed:22910366}.
null
null
null
null
null
FUNCTION: Regulates intracellular calcium levels and cell volume for survival in response to hypo-osmotic shock. Acts as a mechanosensitive calcium channel in response to membrane stretch. The conductance is about 0.25 nanosiemens (PubMed:22910366). Involved in maintaining vacuole integrity and protecting the nuclear e...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74844
CENPQ_SCHPO
MEMKRRVRAVRRDQIQKRWRPLEDKQRQEIIIIFRTCSRLVLNTIKSETRKSLAEEWFMNILLKIEAPLRNLPVPRKRKESILFSQLLSSNMQLEQQLYSDLDHINVLQQELKVETARLENEQKSYEEMKQNMAINNSRLADLKSKLHPYLKKGLKISHDNFSDSNDFSFQKKLNTEDSNTSKTSTLDMYKEKLKPFTKTMQIHANKTVQLSQTIQKATLLLQRLNNTKNIGLNKSSKLKIKNI
null
null
cell division [GO:0051301]; mitotic sister chromatid segregation [GO:0000070]
condensed chromosome, centromeric region [GO:0000779]; cytoplasm [GO:0005737]; inner kinetochore [GO:0000939]; kinetochore [GO:0000776]; microtubule [GO:0005874]; Mis6-Sim4 complex [GO:0031511]; nucleus [GO:0005634]; spindle pole body [GO:0005816]
null
PF13094;
null
CENP-Q/OKP1 family
null
SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
null
null
null
null
null
FUNCTION: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore COMA complex, which connects centromere-asso...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74846
SEC6_SCHPO
MTAAASDDAVYNKVADILRQCEDFHRLSTHIERFEREQASLNMHVKTELEKHVEAVELGKLALHDAQTKRVKLLQELHNMLTLCESAREMVDEFPLISRMSRIYKNCYATKQMISQLNNLVKETDVIEDMLREDLELDSDMPNLLRAHYKLSKLREFREEALYQASLEGQSDLPITLENSFSNLNTLSDNFDRLVLNFCRNIFQLVKSGHIKTIVQIFKIVEAEESSDEVLKSIRDAKSSLPDSQDGPFLSLQGMTRQLRNFRLRVLEEFQGAAAENFQRAWVSYLEDGSGELNLDFIFEDLKVAFYVLPDLTPPSYNIA...
null
null
exocyst localization [GO:0051601]; exocytosis [GO:0006887]; intracellular protein transport [GO:0006886]; vesicle tethering involved in exocytosis [GO:0090522]
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]; exocyst [GO:0000145]; lateral cell cortex [GO:0097575]; nucleus [GO:0005634]; spindle pole [GO:0000922]
SNARE binding [GO:0000149]
PF06046;
1.10.357.50;1.10.357.70;
SEC6 family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cell tip {ECO:0000269|PubMed:11854409}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. {ECO:0000269|PubMed:11854409}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74850
DGAT2_SCHPO
MSEETSIPGIIASTPPISKDSRRNVSHWLQALAVFLHSVSLTLTASWYTVLWAFLPFWPFLIVYLIWLIYDDGFVTGKDRQKRWLRNAPPYRWFCHYFPIRLHKTTELDSEKNYIFGYHPHGIISLGAFGGFASEGADFSKLFPGINVSVLTLNSNFYVPVYRDYLMALNINSVSKKSCVSILSRKPGDSVLIVIGGAQESLLSRPGQNNLVLKKRFGFVKLAFLTGSSLVPCFAFGESDIFEQVDNNPRTRIYKFQEIVKKIAGFTVPFFYGRGLLNKTFGLMPWRKPINIVVGEPIDVPKKSHPTNQEIYEVHEEYIR...
2.3.1.20
null
diacylglycerol metabolic process [GO:0046339]; glycerol metabolic process [GO:0006071]; 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]; lipid droplet [GO:0005811]; perinuclear endoplasmic reticulum [GO:0097038]
2-acylglycerol O-acyltransferase activity [GO:0003846]; diacylglycerol O-acyltransferase activity [GO:0004144]
PF03982;
null
Diacylglycerol acyltransferase family
null
SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q08650}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12963726, ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to sites of lipid droplet biogenesis in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q08650}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycerol + an acyl-CoA = a triacyl-sn-glycerol + CoA; Xref=Rhea:RHEA:10868, ChEBI:CHEBI:17815, ChEBI:CHEBI:57287, ChEBI:CHEBI:58342, ChEBI:CHEBI:64615; EC=2.3.1.20; Evidence={ECO:0000269|PubMed:12963726}; CATALYTIC ACTIVITY: Reaction=a 2-acylglycerol + an acyl-CoA = a 1,2-di...
null
PATHWAY: Glycerolipid metabolism; triacylglycerol biosynthesis. {ECO:0000305|PubMed:12963726}.
null
null
FUNCTION: Catalyzes the terminal and only committed step in triacylglycerol (TAG) synthesis by using diacylglycerol (DAG) and fatty acyl-CoA as substrates. Required for storage lipid synthesis (PubMed:12963726, PubMed:26990381). Major DAG esterifying enzyme in stationary phase when TAG production is particularly active...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74854
POF6_SCHPO
MKPSEAREHAIRKIKEYLERRHKQQFKALFGCLTINIYLKIFTLISTPDLCNCRLVCRKFQQLCDYNSIYVKKLLLMNAWDVTLSRKLYYESQDGMSQANMSSNTSKGFHLQSSDKKYADSDRPKLSSSSLLSLPDQKIPFPVDYSTVQGKQVVLTVLDCVSQRVEFARLDYIKVWRALAPIYRNLAYASNTIDPIAFSAFRTPEEQSKVLKYLIRFGNSYPYGTYRQAMQNAILDMASLFEQACLDEFELGLHSRNLDLLRKFSHVLHDFSGPNAYVSMYLAKQTDFVRSFFHFDPYSLFISNNLEEIHINWNILESVV...
null
null
cell cycle [GO:0007049]; endocytic recycling [GO:0032456]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; septum digestion after cytokinesis [GO:0000920]
cell division site [GO:0032153]; cell septum [GO:0030428]; cell tip [GO:0051286]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; exocyst [GO:0000145]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
protein-macromolecule adaptor activity [GO:0030674]
PF12937;PF07393;
1.20.1280.50;
null
null
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Constantly expressed throughout the cell cycle. Expressed in nucleus except the nucleolus and is localized at cell tips on both sides of the septum in septated cells.
null
null
null
null
null
FUNCTION: Together with skp1, essential for septum processing and cell separation. {ECO:0000269|PubMed:12511573}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74856
CAF1_SCHPO
MTAMNSNFSYPALGVDGISSQISPIRDVWSTNLQQEMNLIMSLIERYPVVSMDTEFPGVVARPLGVFKSSDDYHYQTLRANVDSLKIIQIGLALSDEEGNAPVEACTWQFNFTFNLQDDMYAPESIELLTKSGIDFKKHQEVGIEPADFAELLIGSGLVLQEEVTWITFHSGYDFAYLLKAMTQIPLPAEYEEFYKILCIYFPKNYDIKYIMKSVLNNSKGLQDIADDLQIHRIGPQHQAGSDALLTARIFFEIRSRYFDGSIDSRMLNQLYGLGSTGSVLWHNNSSTPQIQFRDLPGAHPSPTPSNAGIPTTLTNTSSA...
3.1.13.4
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19307292}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:19307292}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:19307292}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19307292}; N...
exonucleolytic catabolism of deadenylated mRNA [GO:0043928]; nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]; regulatory ncRNA-mediated gene silencing [GO:0031047]
CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]
chromatin binding [GO:0003682]; manganese ion binding [GO:0030145]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA nuclease activity [GO:0004540]; zinc ion binding [GO:0008270]
PF04857;
3.30.420.10;
CAF1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
null
null
null
null
FUNCTION: Acts as the catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vivo and in vitro, caf1 has 3'-exoribonuclease activity with a preference for poly(A) RNAs. {ECO:0000269|...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74859
APTX_SCHPO
MSVHKTNDAFKVLMNSAKEPIVEDIPKKYRKQSFRDNLKVYIESPESYKNVIYYDDDVVLVRDMFPKSKMHLLLMTRDPHLTHVHPLEIMMKHRSLVEKLVSYVQGDLSGLIFDEARNCLSQQLTNEALCNYIKVGFHAGPSMNNLHLHIMTLDHVSPSLKNSAHYISFTSPFFVKIDTPTSNLPTRGTLTSLFQEDLKCWRCGETFGRHFTKLKAHLQEEYDDWLDKSVSM
3.6.1.71; 3.6.1.72
null
mismatch repair [GO:0006298]; single strand break repair [GO:0000012]
cytosol [GO:0005829]; nucleus [GO:0005634]
DNA 5'-adenosine monophosphate hydrolase activity [GO:0033699]; DNA-3'-diphospho-5'-guanosine diphosphatase [GO:0120108]; double-stranded DNA binding [GO:0003690]; double-stranded RNA binding [GO:0003725]; GMP binding [GO:0019002]; guanosine binding [GO:1905108]; mismatched DNA binding [GO:0030983]; single-strand break...
PF01230;PF16278;
3.30.428.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
CATALYTIC ACTIVITY: Reaction=a 5'-end adenosine-5'-diphospho-5'-2'-deoxyribonucleoside-DNA + H2O = a 5'-end 5'-phospho-2'-deoxyribonucleoside-DNA + AMP + 2 H(+); Xref=Rhea:RHEA:52128, Rhea:RHEA-COMP:13180, Rhea:RHEA-COMP:13181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:136413, ChEBI:CHEBI:45...
null
null
null
null
FUNCTION: DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species (PubMed:2198...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74866
RIFK_SCHPO
MTVNLEEKRPEIVGPEKVQSPYPIRFEGKVVHGFGRGSKELGIPTANISEDAIQELLRYRDSGVYFGYAMVQKRVFPMVMSVGWNPYYKNKLRSAEVHLIERQGEDFYEEIMRVIVLGYIRPELNYAGLDKLIEDIHTDIRVALNSMDRPSYSSYKKDPFFKV
2.7.1.26
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.;
FMN biosynthetic process [GO:0009398]; phosphorylation [GO:0016310]; riboflavin biosynthetic process [GO:0009231]; riboflavin metabolic process [GO:0006771]
cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; nucleus [GO:0005634]
ATP binding [GO:0005524]; riboflavin kinase activity [GO:0008531]; zinc ion binding [GO:0008270]
PF01687;
2.40.30.30;
Flavokinase family
null
null
CATALYTIC ACTIVITY: Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
null
PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.
null
null
FUNCTION: Catalyzes the phosphorylation of riboflavin (vitamin B2) to form flavin mononucleotide (FMN) coenzyme.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74874
CCR4_SCHPO
MFNPRYTQGTIYPGAHPGLLTPDHQHAAILSVQNSPALENSNISEHWKQQIALATQSRSFSSPHQRAHNAAALARSGGPGFSMNYNARTGAFTGGPNAAGLSSLGGKYNTSSTTTTLTTSTTLNTSSGTTLNSTSKTTTSSVAVDDQKSKSDSKKERRDWTCLDLGGIGLRNVSTDLFKFSFLTELYINHNNLTRLPPEIGKLKNLVILDASGNSIKTIPPELGLLTELREVLLFDNMISVIPAELGTLFQLKILGIEGNPLQDVYKNQIMESGTAGLIAALRDGCPVGPPPPERGWEKLVSDDDDDVNDNVSTSVRDLT...
3.1.13.4
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
nuclear-transcribed mRNA poly(A) tail shortening [GO:0000289]
CCR4-NOT complex [GO:0030014]; CCR4-NOT core complex [GO:0030015]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; P-body [GO:0000932]
metal ion binding [GO:0046872]; poly(A)-specific ribonuclease activity [GO:0004535]; RNA binding [GO:0003723]
PF03372;PF12799;
3.60.10.10;3.80.10.10;
CCR4/nocturin family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
CATALYTIC ACTIVITY: Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
null
null
null
null
FUNCTION: Acts as a catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover (By similarity). Ccr4 has 3'-5' RNase activity with a strong preference for polyadenylated substrates and also ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74880
MCES_SCHPO
MSSSNSRVHEEQPPTENRRYARPTAQMNRVIEQQPRRRDYFQNNDNSGRRGYNRHENNGNAQDVVRSHYNARPDLGYKKRQFSPIIQLKRFNNWIKSVLIQKFAPHASDYPILVLDMGCGKGGDLIKWDKAGIDGYIGIDIAEVSVNQAKKRYREMHASFDALFYAGDCFSSSINELLPPDQRKFDVVSLQFCMHYAFESEEKVRVLLGNVSKCLPRGGVMIGTIPNSDVIVKHIKMLKPGEKEWGNDIYKVRFPESPPRSFRPPYGIQYYFYLEDAVTDVPEYVVPFEAFRAVAEGYNLELIWVKPFLDILNEEKNSET...
2.1.1.56
null
7-methylguanosine mRNA capping [GO:0006370]
cytosol [GO:0005829]; nucleus [GO:0005634]; P-TEFb-cap methyltransferase complex [GO:0070693]
mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA binding [GO:0003723]
PF03291;
3.40.50.150;
Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0 methyltransferase family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CATALYTIC ACTIVITY: Reaction=a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:67008, Rhea:RHEA-COMP:17166, Rhea:RHEA-COMP:17167, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEB...
null
null
null
null
FUNCTION: Responsible for methylating the 5'-cap structure of mRNAs. {ECO:0000269|PubMed:10347220}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74887
TPX1_SCHPO
MSLQIGKPAPDFKGTAVVNGAFEEIKLADYKGKWVFLGFYPLDFTFVCPTEIVAFSEAASKFAERNAQVILTSTDSEYSHLAFINTPRKEGGLGGINIPLLADPSHKVSRDYGVLIEDAGVAFRGLFLIDPKGVLRQITINDLPVGRSVDEALRLLDAFQFVEEHGEVCPANWHKGSDTIDTKNPEKYFSKH
1.11.1.24
null
cell redox homeostasis [GO:0045454]; cellular detoxification of hydrogen peroxide [GO:0061692]; hydrogen peroxide catabolic process [GO:0042744]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; removal of superoxide radicals...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
peroxidase activity [GO:0004601]; peroxiredoxin activity [GO:0051920]; thioredoxin peroxidase activity [GO:0008379]; thioredoxin-dependent peroxiredoxin activity [GO:0140824]; unfolded protein binding [GO:0051082]
PF10417;PF00578;
3.40.30.10;
Peroxiredoxin family, AhpC/Prx1 subfamily
PTM: The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin srx1, which reduces the cysteine sulfinic acid in an ATP- and Mg-d...
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:24316080}. 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:0000269|PubMed:2...
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 (PubMed:17409354, PubMed:20...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74910
RAF1_SCHPO
MTNSSPRVKRRTDTQYLHSVSSKLPKVDFDTNNEEFFEEEFEIYDPFYRAELPCPKPSLSISKHSIAKVPSNVNKRLELQLLLTSGTFLPNSRPYLSERVRKHTHLLSNSITGDDKPSLIHVDFTPEECFILQEAKLKFGPVNSVQFNDAYSTHISPKLPGRAYEDCQKFEIDNPSLSPVDKHGAIILRTYKKNKKLLPDYLKSFYNAGSSYFQREQVHQLMDGESVFFLKPWKHFNETSGDTVCVAYNPLCEKFALGSTAQDGAYNRLGNLWIGDFHSETIQSLESHYKLNQVGEKEYSTISDLCFSKGNLFLYTGAFD...
null
null
CENP-A containing chromatin assembly [GO:0034080]; meiotic telomere clustering [GO:0045141]; regulatory ncRNA-mediated heterochromatin formation [GO:0031048]; silent mating-type cassette heterochromatin formation [GO:0030466]; siRNA-mediated pericentric heterochromatin formation [GO:0140727]; subtelomeric heterochromat...
chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; CLRC complex [GO:0043494]; cytosol [GO:0005829]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]
null
PF00400;
2.130.10.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:18345014}. Chromosome {ECO:0000269|PubMed:18345014}.
null
null
null
null
null
FUNCTION: Component of the Clr4 methyltransferase complex (ClrC) which contributes to the establishment of heterochromatin by specifically methylating histone H3 to form H3K9me (PubMed:16024659, PubMed:16040243, PubMed:16157682). ClrC preferentially ubiquitylates H3K14 and ClrC-mediated H3 ubiquitination promotes clr4 ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74919
RNC1_SCHPO
MAYNHFSIPKNIEEKENSFFDVTFQDEPDETTSTATGIAKVSIPTPKPSTPLSTLTNGSTIQQSMTNQPEPTSQVPPISAKPPMDDATYATQQLTLRALLSTREAGIIIGKAGKNVAELRSTTNVKAGVTKAVPNVHDRVLTISGPLENVVRAYRFIIDIFAKNSTNPDGTPSDANTPRKLRLLIAHSLMGSIIGRNGLRIKLIQDKCSCRMIASKDMLPQSTERTVEIHGTVDNLHAAIWEIGKCLIDDWERGAGTVFYNPVSRLTQPLPSLASTASPQQVSPPAAPSTTSGEAIPENFVSYGAQVFPATQMPFLQQPK...
null
null
3'-UTR-mediated mRNA destabilization [GO:0061158]; 3'-UTR-mediated mRNA stabilization [GO:0070935]; mRNA splicing, via spliceosome [GO:0000398]; negative regulation of cell wall integrity MAPK cascade [GO:1903138]; negative regulation of p38MAPK cascade [GO:1903753]; regulation of alternative mRNA splicing, via spliceo...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]
mRNA 3'-UTR AU-rich region binding [GO:0035925]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]
PF00013;
3.30.1370.10;
null
PTM: Phosphorylated by pmk1. Phosphorylation causes enhancement of the RNA-binding activity. {ECO:0000269|PubMed:12931193}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Binds and stabilizes pmp1 mRNA and hence acts as a negative regulator of pmk1 signaling. Overexpression suppresses the Cl(-) sensitivity of calcineurin deletion. {ECO:0000269|PubMed:12931193}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74926
RBD2_SCHPO
MIFMILGRSKEFILKLPIWTQIITYIAILVYALSFFGISTGVLSLSWIGLLQKRQLYEIITYVTLHLSMLHIVFNFVSLLPAMSQFEKKQGTLACILVTVIPYTLFPGIMHLIVYHFFLRKDYVSIAGLSGWAFAFISASCVHSPQRLISFFNLFSIPAYCFPIIYLIMTTILVPKASFIGHASGAVMGYCTPFMLGSIPLKSWAQNVDPIFQSWVKNYHSFDQLSHAQLPIAEPLSTFSSFPGKGTRLGG
3.4.21.105
null
proteolysis [GO:0006508]; SREBP signaling pathway [GO:0032933]
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]
protein-macromolecule adaptor activity [GO:0030674]; serine-type endopeptidase activity [GO:0004252]
PF01694;
1.20.1540.10;
Peptidase S54 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:27655872}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
CATALYTIC ACTIVITY: Reaction=Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.; EC=3.4.21.105; Evidence={ECO:0000269|PubMed:26545776, ECO:0000269|PubMed:27655872};
null
null
null
null
FUNCTION: Rhomboid-type serine protease that catalyzes intramembrane proteolysis (PubMed:26545776, PubMed:27655872). Upon binding to cdc48, required for sterol regulatory element-binding protein sre1 activation by mediating its release from the membrane and thereby regulating its activity under hypoxic conditions (PubM...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74944
POLK_SCHPO
MENAKDFIGETIKENGLLTIEDDGSSSSDEEATLKRRLAGPSVLKSGQENVNQKKINEIIYEASKGSKFFEAEQKRDRELRLRIEKVQVEVEKYQSKLRFDKAFQREWTIRQESVDTTVEDFRAKRDLTQIIVHVDCDAFYASIEELKNPKLKSLPMAVGKSVLCTANYVARKFGVRSAMPEFIARKICPDLVVIPLNLSEYAIKSKEIQNVLAQYDSNLCPASIDEFYMNLTSHLRLQELAFTVENITMVVEKIRKQVHEETGVTVSCGIAANKLLAKIASNKRKPNNQFFIPFDEIGISKFMNDLPVREVSGIGRVLE...
2.7.7.7
null
DNA damage response [GO:0006974]; DNA replication [GO:0006260]; error-free translesion synthesis [GO:0070987]; error-prone translesion synthesis [GO:0042276]; meiotic cell cycle [GO:0051321]; translesion synthesis [GO:0019985]
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]
damaged DNA binding [GO:0003684]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]
PF00817;PF11799;
1.10.150.810;3.30.70.270;3.40.1170.60;3.30.160.60;3.30.1490.100;
null
null
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Associates with chromatin.
CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7;
null
null
null
null
FUNCTION: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Has a role in meiosis. {ECO:0000269|PubMed:12514100, ECO:0000269|PubMed:16303567}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74954
CBF11_SCHPO
MGDYFAWDFANISGSNTSGSLNLNQLNLDNINNGLHNQEDGAGGRNENSERVGSGSPGSVSMQVLSLFSAVNSALATLEKSEEFPSVVKDEQSIFPAVAKASNSLDELAQNIIPAPSPPGFNRKRKTFDEDSSVEMIRRAISDHLDLLNNCCIGIANLNEDSVHKISLTRSGKPSQLVTVSCRHSSVIQKSYGSEKRYLCPPPMVYINGNYSSIFNQSFRTEISIMNDFGQCSQPISEEYTGQGCMIFRSLHISSLVAAKSKNLRLSLDMFSNVNNQLLSHLVTSSISIVSKPSKKGSKLKISNITLRSGSVVSLYNRIN...
null
null
cell adhesion [GO:0007155]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of lipid metabolic process [GO:0019216]
chromatin [GO:0000785]; cytosol [GO:0005829]; nucleus [GO:0005634]
DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polym...
PF09270;PF09271;
2.80.10.50;2.60.40.1450;
Su(H) family
null
SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
null
null
null
null
null
FUNCTION: Transcription factor that behaves as a negative regulator of adhesion. Recognizes specifically the canonical CSL response element GTGA/GGAA. May also play a cbf12-antagonistic role in the regulation of a number of other important processes such as extracellular material production, colony morphogenesis, ploid...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74957
AGO1_SCHPO
MSYKPSSEIALRPGYGGLGKQITLKANFFQIISLPNETINQYHVIVGDGSRVPRKQSQLIWNSKEVKQYFGSSWMNSVYDGRSMCWSKGDIADGTIKVNIGSESHPREIEFSIQKSSKINLHTLSQFVNSKYSSDPQVLSSIMFLDLLLKKKPSETLFGFMHSFFTGENGVSLGGGVEAWKGFYQSIRPNQGFMSVNVDISSSAFWRNDSLLQILMEYTDCSNVRDLTRFDLKRLSRKFRFLKVTCQHRNNVGTDLANRVYSIEGFSSKSASDSFFVRRLNGEEQKISVAEYFLENHNVRLQYPNLPCILVKNGAMLPIE...
null
null
chromosome segregation [GO:0007059]; co-transcriptional gene silencing by RNA interference machinery [GO:0033562]; negative regulation of G0 to G1 transition [GO:0070317]; nuclear polyadenylation-dependent antisense transcript catabolic process [GO:0071040]; priRNA 3'-end processing [GO:1990431]; regulatory ncRNA-media...
ARC complex [GO:0033167]; chromosome, subtelomeric region [GO:0099115]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; heterochromatin island [GO:1990342]; mating-type region heterochromatin [GO:0031934]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721]; RITS complex [GO:0030958]
miRNA binding [GO:0035198]; protein-macromolecule adaptor activity [GO:0030674]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; RNA endonuclease activity, producing 5'-phosphomonoesters [GO:0016891]; single-stranded RNA binding [GO:0003727]
PF08699;PF16488;PF16487;PF16486;PF02170;PF02171;
3.40.50.2300;2.170.260.10;3.30.420.10;
Argonaute family, Ago subfamily
null
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Chromosome, centromere. Chromosome, telomere. Note=Associates with telomeric and mating-type region heterochromatin.
null
null
null
null
null
FUNCTION: Required for G1 arrest and mating in response to nitrogen starvation. Ago1 regulation of cytokinesis and cell cycle checkpoints occurs downstream of dcr1. Required, indirectly, for regulated hyperphosphorylation of cdc2. Has a role in the RNA interference (RNAi) pathway which is important for heterochromatin ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74958
MMI1_SCHPO
MSNTNFSTSRSSKSIPELPNLEALRSLWPPPSLNESGDTRSVWTTHTGEPVASSVLSTSGSNNFSSPLKRPAPESHDAPIGRRLMVDDPRLIKHGKYDFSRHCTDYGHSYEWPYFRSLRRESMLYHTSGSYPESQPPYSSYSTDAPHYYHAGSESSAYYDSRSRLHGIQPPPKRRTLSPPPRRLADPVVVGSSRYVEEEVYRRPPYTLASEVPSSASAYQAGYSSYPVRSSPQLSHEDTRHGIASSGSTRYPFVPANTRASHSPSLLEPYAHSLPSSVAPVGAYPEKSSYLLSNSSNDSASRKEKPKARASTPPPLNFSR...
null
null
lncRNA catabolic process [GO:0110064]; mRNA destabilization [GO:0061157]; nuclear mRNA surveillance of mRNA 3'-end processing [GO:0071031]; nuclear mRNA surveillance of spliceosomal pre-mRNA splicing [GO:0071030]; nuclear ncRNA surveillance [GO:0071029]; nuclear RNA surveillance [GO:0071027]; nuclear-transcribed mRNA c...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; heterochromatin island [GO:1990342]; Mei2 nuclear dot complex [GO:0033620]; nuclear exosome focus [GO:1990251]; nucleus [GO:0005634]
CCR4-NOT complex binding [GO:1905762]; DNA binding [GO:0003677]; lncRNA binding [GO:0106222]; mRNA binding [GO:0003729]; N6-methyladenosine-containing RNA reader activity [GO:1990247]; pre-mRNA binding [GO:0036002]; pre-mRNA intronic binding [GO:0097157]; protein-RNA adaptor activity [GO:0140517]; RNA binding [GO:00037...
PF04146;
3.10.590.10;
null
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16823445}.
null
null
null
null
null
FUNCTION: RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs (By similarity). Functions alone and as part of the erh1-mmi1 complex, to recruit the CCR4-NOT complex and the NURS complex to target RNAs (PubMed:...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74966
RUXG_SCHPO
MSKAGAPDLKKYLDRQVFVQLNGSRKVYGVLRGYDIFLNIVLEDSIEEKVDGEKVKIGSVAIRGNSVIMIETLDKMT
null
null
mRNA 5'-splice site recognition [GO:0000395]; mRNA splicing, via spliceosome [GO:0000398]; spliceosomal snRNP assembly [GO:0000387]
catalytic step 2 spliceosome [GO:0071013]; cytosol [GO:0005829]; nucleus [GO:0005634]; post-mRNA release spliceosomal complex [GO:0071014]; precatalytic spliceosome [GO:0071011]; SMN-Sm protein complex [GO:0034719]; spliceosomal tri-snRNP complex [GO:0097526]; U1 snRNP [GO:0005685]; U2 snRNP [GO:0005686]; U2-type presp...
RNA binding [GO:0003723]
PF01423;
2.30.30.100;
SnRNP Sm proteins family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}. Cytoplasm {ECO:0000269|PubMed:16823372}.
null
null
null
null
null
FUNCTION: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome (By similarity). {ECO:0000250|UniProtKB:P62308}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74971
ATG5_SCHPO
MNVDNNKGNIPELLWNGTISVRIDYEGNSLAYLANVPRQSYFAQILPNVQRLLAPSIPLSECWLDYNGVPLKWHWPVGLLFDLLTVFDPDTPRAPVLWRIQLRSGLFPTTKILQMETMDTFRTYFFNCLKESDYVRNGSSSGIIALSKAETDTYWNAILNHDYYDFRPIAIKILFSKSKFIPLKIYLGANAPIIQTSAPLGSSLGEFLNKRLPDLFPSCDKFLIVKPVIHGITIFLQSVLDELNRDFCYIDGFLHIVLMKV
null
null
autophagosome assembly [GO:0000045]; cellular response to nitrogen starvation [GO:0006995]; macroautophagy [GO:0016236]; meiotic cell cycle [GO:0051321]; mitophagy [GO:0000423]; piecemeal microautophagy of the nucleus [GO:0034727]; protein transport [GO:0015031]; reticulophagy [GO:0061709]
Atg12-Atg5-Atg16 complex [GO:0034274]; autophagosome [GO:0005776]; cytosol [GO:0005829]; mitochondria-associated endoplasmic reticulum membrane [GO:0044233]; nucleus [GO:0005634]; phagophore [GO:0061908]; phagophore assembly site [GO:0000407]; phagophore assembly site membrane [GO:0034045]
Atg8-family ligase activity [GO:0019776]
PF20637;PF20638;PF04106;
3.10.20.620;1.10.246.190;
ATG5 family
PTM: Conjugated to atg12; which is essential for autophagy.
SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Preautophagosomal structure membrane; Peripheral membrane protein.
null
null
null
null
null
FUNCTION: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which elimina...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74986
COM1_SCHPO
MNEEEHNKSVHWSIVYRQLGNLLEQYEVEIARLKSQLVLEKKLRIQVEKELESVKTKQISSSASSKVSSNTIQELDSTTDEDEIPGSDTVDEEDPSLNAPFSEKNQSVKIPPHSPTLPVQNASAFVKPISVPLGNVKEEKFLDTNPIGAESFESSDGEMHLRARSPEDMILLRETQPLAPLDINTLGVSDNRQKKGTEKKRPFEPEFLNDDVIRGNKRKALPAYECPDCQKFYELHGPVKESSVAPTWNDENRLGGGSLPNCKHQPLVQKVGRHRKLNIPKPIPNGFWESDFVD
3.1.-.-
null
DNA double-strand break processing [GO:0000729]; double-strand break repair involved in meiotic recombination [GO:1990918]; double-strand break repair via homologous recombination [GO:0000724]; double-strand break repair via nonhomologous end joining [GO:0006303]; gene conversion at mating-type locus [GO:0007534]; meio...
nucleus [GO:0005634]; site of double-strand break [GO:0035861]
bubble DNA binding [GO:0000405]; DNA end binding [GO:0045027]; DNA-DNA tethering activity [GO:0106260]; double-strand/single-strand DNA junction binding [GO:0000406]; double-stranded DNA binding [GO:0003690]; endodeoxyribonuclease activator activity [GO:0140656]; endonuclease activity [GO:0004519]; flap-structured DNA ...
PF08573;
null
COM1/SAE2/CtIP family
PTM: Phosphorylated by tel1 in response to DNA damage; promoting interaction with nbs1 and recruitment to DSBs. {ECO:0000269|PubMed:18378696, ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:19804756, ECO:0000269|PubMed:33836577}.
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19804755}. Chromosome {ECO:0000269|PubMed:19804755}. Note=Accumulates at DSBs; recruited to DSBs following phosphorylation and interaction with nbs1. {ECO:0000269|PubMed:19804755, ECO:0000269|PubMed:33836577}.
null
null
null
null
null
FUNCTION: Endonuclease that cooperates with the MRN complex in processing meiotic and mitotic double-strand breaks by allowing the endonucleolytic removal of rec12 from the break sites and ensuring both resection and intrachromosomal association of the broken ends (PubMed:16303567, PubMed:17936710, PubMed:18378696, Pub...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O74991
POF3_SCHPO
MNNYQVKAIKEKTQQYLSKRKFEDALTFITKTIEQEPNPTIDLFELRAQVYEKSGQYSQAELDAKRMIHLNARNARGYLRLGKLLQLDGFDKKADQLYTQGLRMVHKMDPLRPVLKKVSQRLNERILRTRPVLDLFRILPREVLLCILQQLNFKSIVQCMQVCKHWRDCIKKEPSLFCCLDFSCASPRSVNSRDRNVMAVARYSVYSKDNIQEVIGLEKLGILTPTKALLRSVKSLKVYKTISPLHTQSTDKLYTIWTPFSELHYFYCATPITFSIASKILSCCKKLKQVELVDLIPDLIFDSMDWDKLFNAESVPLALK...
null
null
negative regulation of mitotic cell cycle DNA replication [GO:1903464]; SCF-dependent proteasomal ubiquitin-dependent protein catabolic process [GO:0031146]; telomere maintenance [GO:0000723]; ubiquitin-dependent protein catabolic process [GO:0006511]
mitochondrion [GO:0005739]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151]
ubiquitin ligase-substrate adaptor activity [GO:1990756]
PF12937;
1.20.1280.50;3.80.10.10;1.25.40.10;
null
null
SUBCELLULAR LOCATION: Mitochondrion. Nucleus.
null
null
null
null
null
FUNCTION: Has a role in substrate recognition in the Skp1-Cullin-1/Cdc53-F-box (SCF) ubiquitin ligase complex. Required for the maintenance of telomere length and transcriptional silencing at the telomere. Also required for chromosome segregation. {ECO:0000269|PubMed:11809834}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O75001
MCM7_SCHPO
MALPTIDLKIPEYEECQHKITDFLSHFKQEQVQDGQQNQDISMSDAGDEPFLKSKYMDILQKISNRESNVINVDLNDLYEFDPSDTQLLHNIESNAKRFVELFSQCADALMPPPTVEINYRNEVLDVIMQQRVQRNENIDPEHKGFPPELTRGYDLYFRPVTRNKKPFSVRDLRGENLGSLLTVRGIVTRTSDVKPSLTVNAYTCDRCGYEVFQEIRQKTFLPMSECPSDECKKNDAKGQLFMSTRASKFLPFQEVKIQELTNQVPIGHIPRSLTVHLYGAITRSVNPGDIVDISGIFLPTPYTGFRAMRAGLLTDTYLE...
3.6.4.12
null
DNA replication initiation [GO:0006270]; DNA strand elongation involved in DNA replication [GO:0006271]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via break-induced replication [GO:0000727]; mitotic DNA replication initiation [GO:1902975]; premeiotic DNA replication [GO:0006279]
chromatin [GO:0000785]; DNA replication preinitiation complex [GO:0031261]; MCM complex [GO:0042555]; MCM core complex [GO:0097373]; nuclear pre-replicative complex [GO:0005656]; nuclear replication fork [GO:0043596]; nucleus [GO:0005634]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; single-stranded DNA binding [GO:0003697]; single-stranded DNA helicase activity [GO:0017116]
PF00493;PF17855;PF14551;PF17207;
2.20.28.10;3.30.1640.10;2.40.50.140;3.40.50.300;
MCM family
null
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11606526}.
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; Evidence={ECO:0000250|UniProtKB:P33993}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000250|U...
null
null
null
null
FUNCTION: Acts as a component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ...
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O75003
TREPH_GRIFR
MAPPHQFQSKPSDVIRRRLSSAVSSKRPNIPGYTSLTPMWAGIAGAVVNNNTQFEVAISIHDSVYNTDFASSVVPYSPNEPEAQAGIIEKHVLETLRKFSTEHMCKFLGAGVTVILLREAPNLCTRLWLDMDIVPIVFNIKPFHTDSITRPNVRHRISSTTGSYVPSGAETPTVYYDPAQLQDPNKLSANVQTRLPIPRTVDEQADSAARKCIMYFGPGNNPRLQIGPRNQVAVDAGGKIHLIDDIDEYRKTVGKGTWNSVIKLADELREKKIKIGFFSSTPQGGGVALMRHAIIRFFTALDVDAAWYVPNPSPSVFRTT...
2.4.1.231
null
glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; trehalose metabolic process [GO:0005991]
null
alpha,alpha-trehalose phosphorylase (configuration-retaining) activity [GO:0033832]
PF00534;PF21269;
3.40.50.2000;
Glycosyltransferase group 1 family, Glycosyltransferase 4 subfamily
null
null
CATALYTIC ACTIVITY: Reaction=alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate; Xref=Rhea:RHEA:16257, ChEBI:CHEBI:16551, ChEBI:CHEBI:17925, ChEBI:CHEBI:43474, ChEBI:CHEBI:58601; EC=2.4.1.231; Evidence={ECO:0000269|PubMed:9763690, ECO:0000269|PubMed:9797287};
null
null
BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5 for trehalose phosphorolysis activity, 6.5-6.8 for trehalose synthesis activity. {ECO:0000269|PubMed:9797287};
BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 32.5 degrees Celsius for trehalose phosphorolysis activity, 37.5 degrees Celsius for trehalose synthesis activity. Stable up to 35 degrees Celsius for trehalose phosphorolysis activity, 32.5 degrees Celsius for trehalose synthesis activity. ...
FUNCTION: Reversibly catalyzes the synthesis and degradation of trehalose from glucose and alpha-D-glucose 1-phosphate. The equilibrium lies in the direction of trehalose synthesis. {ECO:0000269|PubMed:9763690, ECO:0000269|PubMed:9797287}.
Grifola frondosa (Maitake) (Polyporus frondosus)
O75011
NAK1_SCHPO
MENNTASSPYTKLELVGRGSYGAVYRGICNLTKETVAIKILNLDTDEDEVSDIQKEVAVLSELKQSDVENIIKYHGSYLVGTNLWIIMDYCHGGSVRTLMEAGPISEPCISLILRETLQALKFIHHAGIIHRDIKAANILVSMSGNVKLCDFGVAAELNINRRKRITFIGTPYWMAPEVIRDGQEYNVMADIWSLGITAYEIATGSPPHAKEDPFRAVYLIAHTAPPRLNGNFSALLKEFIASCLQDVPQRRLDSSELLKSKFIKQYSRMSISELTNVVKRYDTWQAAGGIPQTLLLGEEADDGSDPDQETSDTAASDDG...
2.7.11.1
null
establishment or maintenance of actin cytoskeleton polarity [GO:0030950]; establishment or maintenance of cell polarity [GO:0007163]; phosphorylation [GO:0016310]; positive regulation of establishment or maintenance of bipolar cell polarity regulating cell shape [GO:2000247]; protein localization to medial cortex [GO:0...
actin cortical patch [GO:0030479]; cell division site [GO:0032153]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic actomyosin contractile ring [GO:0110085]; mitotic spindle pole body [GO:0044732]; new mitotic spindle pole body [GO:0071958]
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, Ser/Thr protein kinase family
PTM: Autophosphorylated. {ECO:0000305|PubMed:18257517}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12427731}.
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 the regulation of cell polarity, growth and division. {ECO:0000269|PubMed:12427731}.
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
O75015
FCG3B_HUMAN
MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYSVLEKDSVTLKCQGAYSPEDNSTQWFHNENLISSQASSYFIDAATVNDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKNVSSETVNITITQGLAVSTISSFSPPGYQVSFCLVMVLLFAVDTGLYFSVKTNI
null
null
antibody-dependent cellular cytotoxicity [GO:0001788]; cell surface receptor signaling pathway [GO:0007166]; immune response [GO:0006955]
external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]
GPI anchor binding [GO:0034235]; IgG binding [GO:0019864]; IgG receptor activity [GO:0019770]
PF13895;
2.60.40.10;
null
PTM: Glycosylated. Glycosylation plays an inhibitory role in the interaction with IgG3.; PTM: The soluble form is produced by a proteolytic cleavage.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1825220}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1825220}. Secreted. Note=Secreted after cleavage.
null
null
null
null
null
FUNCTION: Receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does...
Homo sapiens (Human)
O75019
LIRA1_HUMAN
MTPIVTVLICLRLSLGPRTHVQAGTLPKPTLWAEPGSVITQGSPVTLWCQGILETQEYRLYREKKTAPWITRIPQEIVKKGQFPIPSITWEHTGRYRCFYGSHTAGWSEPSDPLELVVTGAYIKPTLSALPSPVVTSGGNVTLHCVSQVAFGSFILCKEGEDEHPQCLNSQPRTHGWSRAIFSVGPVSPSRRWSYRCYAYDSNSPHVWSLPSDLLELLVLGVSKKPSLSVQPGPIVAPGESLTLQCVSDVSYDRFVLYKEGERDFLQLPGPQPQAGLSQANFTLGPVSRSYGGQYRCSGAYNLSSEWSAPSDPLDILIAG...
null
null
adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response [GO:0006952]
plasma membrane [GO:0005886]
antigen binding [GO:0003823]; inhibitory MHC class I receptor activity [GO:0032396]; transmembrane signaling receptor activity [GO:0004888]
PF13895;PF13927;
2.60.40.10;
null
null
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: May act as receptor for class I MHC antigens.
Homo sapiens (Human)
O75022
LIRB3_HUMAN
MTPALTALLCLGLSLGPRTRVQAGPFPKPTLWAEPGSVISWGSPVTIWCQGSQEAQEYRLHKEGSPEPLDRNNPLEPKNKARFSIPSMTEHHAGRYRCHYYSSAGWSEPSDPLEMVMTGAYSKPTLSALPSPVVASGGNMTLRCGSQKGYHHFVLMKEGEHQLPRTLDSQQLHSRGFQALFPVGPVTPSHRWRFTCYYYYTNTPWVWSHPSDPLEILPSGVSRKPSLLTLQGPVLAPGQSLTLQCGSDVGYNRFVLYKEGERDFLQRPGQQPQAGLSQANFTLGPVSPSNGGQYRCYGAHNLSSEWSAPSDPLNILMAGQ...
null
null
adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response [GO:0006952]; negative regulation of osteoclast differentiation [GO:0045671]
plasma membrane [GO:0005886]; secretory granule membrane [GO:0030667]
inhibitory MHC class I receptor activity [GO:0032396]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]
PF00047;PF13895;
2.60.40.10;
null
PTM: Phosphorylated on tyrosine residues by LYN. Phosphorylation at Tyr-595 and Tyr-625 is important for interaction with PTPN6/SHP-1 and PTPN11/SHP-2. {ECO:0000250|UniProtKB:P97484}.
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM). {ECO:0000250|UniProt...
Homo sapiens (Human)
O75023
LIRB5_HUMAN
MTLTLSVLICLGLSVGPRTCVQAGTLPKPTLWAEPASVIARGKPVTLWCQGPLETEEYRLDKEGLPWARKRQNPLEPGAKAKFHIPSTVYDSAGRYRCYYETPAGWSEPSDPLELVATGFYAEPTLLALPSPVVASGGNVTLQCDTLDGLLTFVLVEEEQKLPRTLYSQKLPKGPSQALFPVGPVTPSCRWRFRCYYYYRKNPQVWSNPSDLLEILVPGVSRKPSLLIPQGSVVARGGSLTLQCRSDVGYDIFVLYKEGEHDLVQGSGQQPQAGLSQANFTLGPVSRSHGGQYRCYGAHNLSPRWSAPSDPLDILIAGLI...
null
null
adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; cytokine-mediated signaling pathway [GO:0019221]; defense response [GO:0006952]
plasma membrane [GO:0005886]
inhibitory MHC class I receptor activity [GO:0032396]; transmembrane signaling receptor activity [GO:0004888]
PF00047;PF13895;
2.60.40.10;
null
null
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: May act as receptor for class I MHC antigens.
Homo sapiens (Human)
O75027
ABCB7_HUMAN
MALLAMHSWRWAAAAAAFEKRRHSAILIRPLVSVSGSGPQWRPHQLGALGTARAYQIPESLKSITWQRLGKGNSGQFLDAAKALQVWPLIEKRTCWHGHAGGGLHTDPKEGLKDVDTRKIIKAMLSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRI...
null
null
intracellular iron ion homeostasis [GO:0006879]; iron ion transmembrane transport [GO:0034755]; iron-sulfur cluster assembly [GO:0016226]; iron-sulfur cluster export from the mitochondrion [GO:0140466]; negative regulation of reactive oxygen species biosynthetic process [GO:1903427]; positive regulation of heme biosynt...
mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]
ABC-type iron-sulfur cluster transporter activity [GO:0140481]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled transmembrane transporter activity [GO:0042626]; heme transmembrane transporter activity [GO:0015232]; identical protein binding [GO:0042802]; protein homodimerization activity ...
PF00664;PF00005;
1.20.1560.10;3.40.50.300;
ABC transporter superfamily, ABCB family, Heavy Metal importer (TC 3.A.1.210) subfamily
null
SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P40416}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40416}.
CATALYTIC ACTIVITY: Reaction=(glutathione)4[2Fe(III)-2S] cluster(in) + ATP + H2O = (glutathione)4[2Fe(III)-2S] cluster(out) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:67028, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:167627, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:331...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.3 mM for Mg-ATP {ECO:0000269|PubMed:33157103}; KM=0.54 mM for Mg-ATP (in the presence of the [2Fe-2S](GS)4 cluster) {ECO:0000269|PubMed:33157103};
null
null
null
FUNCTION: Exports glutathione-coordinated iron-sulfur clusters such as [2Fe-2S]-(GS)4 cluster from the mitochondria to the cytosol in an ATP-dependent manner allowing the assembly of the cytosolic iron-sulfur (Fe/S) cluster-containing proteins and participates in iron homeostasis (PubMed:10196363, PubMed:17192393, PubM...
Homo sapiens (Human)
O75030
MITF_HUMAN
MQSESGIVPDFEVGEEFHEEPKTYYELKSQPLKSSSSAEHPGASKPPISSSSMTSRILLRQQLMREQMQEQERREQQQKLQAAQFMQQRVPVSQTPAINVSVPTTLPSATQVPMEVLKVQTHLENPTKYHIQQAQRQQVKQYLSTTLANKHANQVLSLPCPNQPGDHVMPPVPGSSAPNSPMAMLTLNSNCEKEGFYKFEEQNRAESECPGMNTHSRASCMQMDDVIDDIISLESSYNEEILGLMDPALQMANTLPVSGNLIDLYGNQGLPPPGLTISNSCPANLPNIKRELTACIFPTESEARALAKERQKKDNHNLIE...
null
null
bone remodeling [GO:0046849]; camera-type eye development [GO:0043010]; cell fate commitment [GO:0045165]; melanocyte apoptotic process [GO:1902362]; melanocyte differentiation [GO:0030318]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cell migration [GO:0030336]; negative regulation of...
chromatin [GO:0000785]; cytoplasm [GO:0005737]; lysosomal membrane [GO:0005765]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]
chromatin binding [GO:0003682]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; E-box binding [GO:0070888]; pr...
PF11851;PF00010;PF15951;
4.10.280.10;
MiT/TFE family
PTM: When nutrients are present, phosphorylation by MTOR at Ser-5 via non-canonical mTORC1 pathway promotes ubiquitination by the SCF(BTRC) complex, followed by degradation (PubMed:36608670). Phosphorylation at Ser-405 significantly enhances the ability to bind the tyrosinase promoter (PubMed:10587587). Phosphorylation...
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16822840, ECO:0000269|PubMed:27889061, ECO:0000269|PubMed:28842328, ECO:0000269|PubMed:36608670}. Cytoplasm {ECO:0000269|PubMed:16822840, ECO:0000269|PubMed:28842328, ECO:0000269|PubMed:36608670}. Lysosome membrane {ECO:0000269|PubMed:23401004, ECO:0000269|PubMed:366086...
null
null
null
null
null
FUNCTION: Transcription factor that acts as a master regulator of melanocyte survival and differentiation as well as melanosome biogenesis (PubMed:10587587, PubMed:22647378, PubMed:27889061, PubMed:9647758). Binds to M-boxes (5'-TCATGTG-3') and symmetrical DNA sequences (E-boxes) (5'-CACGTG-3') found in the promoter of...
Homo sapiens (Human)
O75031
HSF2B_HUMAN
MGEAGAAEEACRHMGTKEEFVKVRKKDLERLTTEVMQIRDFLPRILNGEVLESFQKLKIVEKNLERKEQELEQLKMDCEHFKARLETVQADNIREKKEKLALRQQLNEAKQQLLQQAEYCTEMGAAACTLLWGVSSSEEVVKAILGGDKALKFFSITGQTMESFVKSLDGDVQELDSDESQFVFALAGIVTNVAAIACGREFLVNSSRVLLDTILQLLGDLKPGQCTKLKVLMLMSLYNVSINLKGLKYISESPGFIPLLWWLLSDPDAEVCLHVLRLVQSVVLEPEVFSKSASEFRSSLPLQRILAMSKSRNPRLQTAA...
null
null
double-strand break repair involved in meiotic recombination [GO:1990918]; female meiosis I [GO:0007144]; male meiosis I [GO:0007141]; spermatogenesis [GO:0007283]; transcription by RNA polymerase II [GO:0006366]
chromosome [GO:0005694]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]
null
null
1.25.10.10;
null
PTM: Sumoylated by UBE2I in response to MEKK1-mediated stimuli. {ECO:0000269|PubMed:17709345}.
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D4G2}. Chromosome {ECO:0000269|PubMed:31242413}. Note=Localizes on double-strand breaks (DSBs) in mitotic and meiotic chromosomes. {ECO:0000269|PubMed:31242413}.
null
null
null
null
null
FUNCTION: Meiotic recombination factor component of recombination bridges involved in meiotic double-strand break repair. Modulates the localization of recombinases DMC1:RAD51 to meiotic double-strand break (DSB) sites through the interaction with BRCA2 and its recruitment during meiotic recombination (By similarity) (...
Homo sapiens (Human)
O75037
KI21B_HUMAN
MAGQGDCCVKVAVRIRPQLSKEKIEGCHICTSVTPGEPQVLLGKDKAFTYDFVFDLDTWQEQIYSTCVSKLIEGCFEGYNATVLAYGQTGAGKTYTMGTGFDMATSEEEQGIIPRAIAHLFGGIAERKRRAQEQGVAGPEFKVSAQFLELYNEEILDLFDSTRDPDTRHRRSNIKIHEDANGGIYTTGVTSRLIHSQEELIQCLKQGALSRTTASTQMNVQSSRSHAIFTIHLCQMRMCTQPDLVNEAVTGLPDGTPPSSEYETLTAKFHFVDLAGSERLKRTGATGERAKEGISINCGLLALGNVISALGDQSKKVVHV...
null
null
microtubule-based movement [GO:0007018]; mitotic spindle organization [GO:0007052]; spindle elongation [GO:0051231]
cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; growth cone [GO:0030426]; kinesin complex [GO:0005871]; microtubule [GO:0005874]
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]
PF00225;PF00400;
3.40.850.10;2.130.10.10;
TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family
null
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, growth cone {ECO:0000250|UniProtKB:Q9QXL1}. Cell projection, axon {ECO:0000250|UniProtKB:Q9QXL1}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:F1M5N7}.
null
null
null
null
null
FUNCTION: Plus-end directed microtubule-dependent motor protein which displays processive activity. Is involved in regulation of microtubule dynamics, synapse function and neuronal morphology, including dendritic tree branching and spine formation. Plays a role in lerning and memory. Involved in delivery of gamma-amino...
Homo sapiens (Human)
O75038
PLCH2_HUMAN
MSGPWPSPDSRTKGTVAWLAEVLLWVGGSVVLSSEWQLGPLVERCMGAMQEGMQMVKLRGGSKGLVRFYYLDEHRSCIRWRPSRKNEKAKISIDSIQEVSEGRQSEVFQRYPDGSFDPNCCFSIYHGSHRESLDLVSTSSEVARTWVTGLRYLMAGISDEDSLARRQRTRDQWLKQTFDEADKNGDGSLSIGEVLQLLHKLNVNLPRQRVKQMFREADTDDHQGTLGFEEFCAFYKMMSTRRDLYLLMLTYSNHKDHLDAASLQRFLQVEQKMAGVTLESCQDIIEQFEPCPENKSKGLLGIDGFTNYTRSPAGDIFNPE...
3.1.4.11
COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
lipid catabolic process [GO:0016042]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; release of sequestered calcium ion into cytosol [GO:0051209]
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
calcium ion binding [GO:0005509]; phosphatidylinositol phospholipase C activity [GO:0004435]
PF00168;PF09279;PF16457;PF00388;PF00387;
2.60.40.150;1.10.238.10;3.20.20.190;2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A2AP18}. Cell membrane {ECO:0000250|UniProtKB:A2AP18}. Note=Localized predominantly at the plasma membrane. {ECO:0000250|UniProtKB:A2AP18}.
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=14.4 uM for 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) {ECO:0000269|PubMed:18361507}; Vmax=12.6 umol/min/mg enzyme {ECO:0000269|PubMed:18361507};
null
null
null
FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (PubMed:18361507). This phospholipase activity is very sensitive to calcium. May be important for formation and maintenanc...
Homo sapiens (Human)
O75044
SRGP2_HUMAN
MTSPAKFKKDKEIIAEYDTQVKEIRAQLTEQMKCLDQQCELRVQLLQDLQDFFRKKAEIEMDYSRNLEKLAERFLAKTRSTKDQQFKKDQNVLSPVNCWNLLLNQVKRESRDHTTLSDIYLNNIIPRFVQVSEDSGRLFKKSKEVGQQLQDDLMKVLNELYSVMKTYHMYNADSISAQSKLKEAEKQEEKQIGKSVKQEDRQTPRSPDSTANVRIEEKHVRRSSVKKIEKMKEKRQAKYTENKLKAIKARNEYLLALEATNASVFKYYIHDLSDLIDQCCDLGYHASLNRALRTFLSAELNLEQSKHEGLDAIENAVENL...
null
null
actin filament severing [GO:0051014]; dendritic spine development [GO:0060996]; excitatory synapse assembly [GO:1904861]; extension of a leading process involved in cell motility in cerebral cortex radial glia guided migration [GO:0021816]; filopodium assembly [GO:0046847]; inhibitory synapse assembly [GO:1904862]; lam...
cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic spine head [GO:0044327]; lamellipodium [GO:0030027]; nucleus [GO:0005634]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic membrane [GO:0045211]
GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; small GTPase binding [GO:0031267]
PF00611;PF00620;PF00018;
1.20.1270.60;1.10.555.10;2.30.30.40;
null
PTM: Methylation at Arg-927 is required for the stimulation of cell migration, dimerization and localization at the plasma membrane protrusions. {ECO:0000269|PubMed:20810653}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21148482}. Cell projection, dendritic spine {ECO:0000303|PubMed:22559944}. Postsynaptic density {ECO:0000250|UniProtKB:Q91Z67}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q91Z67}. Cell projection, lamellipodium {ECO:0000269|PubMed:20810653}. Cytoplasmic ves...
null
null
null
null
null
FUNCTION: Postsynaptic RAC1 GTPase activating protein (GAP) that plays a key role in neuronal morphogenesis and migration mainly during development of the cerebral cortex (PubMed:20810653, PubMed:27373832, PubMed:28333212). Regulates excitatory and inhibitory synapse maturation and density in cortical pyramidal neurons...
Homo sapiens (Human)
O75051
PLXA2_HUMAN
MEQRRPWPRALEVDSRSVVLLSVVWVLLAPPAAGMPQFSTFHSENRDWTFNHLTVHQGTGAVYVGAINRVYKLTGNLTIQVAHKTGPEEDNKSCYPPLIVQPCSEVLTLTNNVNKLLIIDYSENRLLACGSLYQGVCKLLRLDDLFILVEPSHKKEHYLSSVNKTGTMYGVIVRSEGEDGKLFIGTAVDGKQDYFPTLSSRKLPRDPESSAMLDYELHSDFVSSLIKIPSDTLALVSHFDIFYIYGFASGGFVYFLTVQPETPEGVAINSAGDLFYTSRIVRLCKDDPKFHSYVSLPFGCTRAGVEYRLLQAAYLAKPGD...
null
null
centrosome localization [GO:0051642]; cerebellar granule cell precursor tangential migration [GO:0021935]; limb bud formation [GO:0060174]; negative regulation of cell adhesion [GO:0007162]; neural tube development [GO:0021915]; pharyngeal system development [GO:0060037]; positive regulation of axonogenesis [GO:0050772...
plasma membrane [GO:0005886]; semaphorin receptor complex [GO:0002116]
identical protein binding [GO:0042802]; semaphorin receptor activity [GO:0017154]
PF08337;PF20170;PF01437;PF01403;PF01833;PF18020;PF17960;
2.60.40.10;2.130.10.10;
Plexin family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
null
null
null
null
null
FUNCTION: Coreceptor for SEMA3A and SEMA6A. Necessary for signaling by SEMA6A and class 3 semaphorins and subsequent remodeling of the cytoskeleton. Plays a role in axon guidance, invasive growth and cell migration. Class 3 semaphorins bind to a complex composed of a neuropilin and a plexin. The plexin modulates the af...
Homo sapiens (Human)
O75052
CAPON_HUMAN
MPSKTKYNLVDDGHDLRIPLHNEDAFQHGICFEAKYVGSLDVPRPNSRVEIVAAMRRIRYEFKAKNIKKKKVSIMVSVDGVKVILKKKKKLLLLQKKEWTWDESKMLVMQDPIYRIFYVSHDSQDLKIFSYIARDGASNIFRCNVFKSKKKSQAMRIVRTVGQAFEVCHKLSLQHTQQNADGQEDGESERNSNSSGDPGRQLTGAERASTATAEETDIDAVEVPLPGNDVLEFSRGVTDLDAVGKEGGSHTGSKVSHPQEPMLTASPRMLLPSSSSKPPGLGTETPLSTHHQMQLLQQLLQQQQQQTQVAVAQVHLLKDQ...
null
null
nitric oxide biosynthetic process [GO:0006809]; positive regulation of membrane repolarization during ventricular cardiac muscle cell action potential [GO:1905026]; positive regulation of peptidyl-cysteine S-nitrosylation [GO:2000170]; positive regulation of potassium ion transmembrane transport [GO:1901381]; postsynap...
anchoring junction [GO:0070161]; caveola [GO:0005901]; cytosol [GO:0005829]; filopodium [GO:0030175]; glutamatergic synapse [GO:0098978]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; podosome [GO:0002102]; sarcolemma [GO:0042383]; sarcoplasmic reticulum membrane [GO:00...
nitric-oxide synthase binding [GO:0050998]; nitric-oxide synthase regulator activity [GO:0030235]; signaling adaptor activity [GO:0035591]
PF00640;
2.30.29.30;
null
null
SUBCELLULAR LOCATION: Cell projection, filopodium {ECO:0000250|UniProtKB:O54960}. Cell projection, podosome {ECO:0000250|UniProtKB:O54960}.
null
null
null
null
null
FUNCTION: Adapter protein involved in neuronal nitric-oxide (NO) synthesis regulation via its association with nNOS/NOS1. The complex formed with NOS1 and synapsins is necessary for specific NO and synapsin functions at a presynaptic level. Mediates an indirect interaction between NOS1 and RASD1 leading to enhance the ...
Homo sapiens (Human)
O75054
IGSF3_HUMAN
MKCFFPVLSCLAVLGVVSAQRQVTVQEGPLYRTEGSHITIWCNVSGYQGPSEQNFQWSIYLPSSPEREVQIVSTMDSSFPYAIYTQRVRGGKIFIERVQGNSTLLHITDLQARDAGEYECHTPSTDKQYFGSYSAKMNLVVIPDSLQTTAMPQTLHRVEQDPLELTCEVASETIQHSHLSVAWLRQKVGEKPVEVISLSRDFMLHSSSEYAQRQSLGEVRLDKLGRTTFRLTIFHLQPSDQGEFYCEAAEWIQDPDGSWYAMTRKRSEGAVVNVQPTDKEFTVRLETEKRLHTVGEPVEFRCILEAQNVPDRYFAVSWAF...
null
null
lacrimal gland development [GO:0032808]
cell surface [GO:0009986]; membrane [GO:0016020]
null
PF07686;
2.60.40.10;
null
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
null
null
null
null
null
null
Homo sapiens (Human)
O75056
SDC3_HUMAN
MKPGPPHRAGAAHGAGAGAGAAAGPGARGLLLPPLLLLLLAGRAAGAQRWRSENFERPVDLEGSGDDDSFPDDELDDLYSGSGSGYFEQESGIETAMRFSPDVALAVSTTPAVLPTTNIQPVGTPFEELPSERPTLEPATSPLVVTEVPEEPSQRATTVSTTMATTAATSTGDPTVATVPATVATATPSTPAAPPFTATTAVIRTTGVRRLLPLPLTTVATARATTPEAPSPPTTAAVLDTEAPTPRLVSTATSRPRALPRPATTQEPDIPERSTLPLGTTAPGPTEVAQTPTPETFLTTIRDEPEVPVSGGPSGDFELP...
null
null
cell migration [GO:0016477]
cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; membrane [GO:0016020]; microspike [GO:0044393]; plasma membrane [GO:0005886]
identical protein binding [GO:0042802]
PF01034;
null
Syndecan proteoglycan family
PTM: O-glycosylated within the Thr/Ser-rich region which could interact with lectin domains on other molecules. {ECO:0000305}.
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
null
null
null
null
null
FUNCTION: Cell surface proteoglycan that may bear heparan sulfate (By similarity). May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism. {ECO:0000250, ECO:0000269|PubMed:11527150}.
Homo sapiens (Human)
O75061
AUXI_HUMAN
MKDSENKGASSPDMEPSYGGGLFDMVKGGAGRLFSNLKDNLKDTLKDTSSRVIQSVTSYTKGDLDFTYVTSRIIVMSFPLDNVDIGFRNQVDDIRSFLDSRHLDHYTVYNLSPKSYRTAKFHSRVSECSWPIRQAPSLHNLFAVCRNMYNWLLQNPKNVCVVHCLDGRAASSILVGAMFIFCNLYSTPGPAIRLLYAKRPGIGLSPSHRRYLGYMCDLLADKPYRPHFKPLTIKSITVSPIPFFNKQRNGCRPYCDVLIGETKIYSTCTDFERMKEYRVQDGKIFIPLNITVQGDVVVSMYHLRSTIGSRLQAKVTNTQI...
3.1.3.-
null
clathrin coat disassembly [GO:0072318]; clathrin-dependent endocytosis [GO:0072583]; dephosphorylation [GO:0016311]; intracellular transport [GO:0046907]; regulation of clathrin coat assembly [GO:1905443]; regulation of clathrin-dependent endocytosis [GO:2000369]; synaptic vesicle recycling [GO:0036465]; synaptic vesic...
clathrin-coated vesicle [GO:0030136]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extrinsic component of presynaptic endocytic zone membrane [GO:0098894]; intracellular membrane-bounded organelle [GO:0043231]; postsynaptic density [GO:0014069]; vesicle [GO:0031982]
clathrin binding [GO:0030276]; clathrin heavy chain binding [GO:0032050]; heat shock protein binding [GO:0031072]; protein tyrosine phosphatase activity [GO:0004725]; SH3 domain binding [GO:0017124]
PF10409;
2.60.40.1110;1.10.287.110;3.90.190.10;
null
PTM: Phosphorylation at Ser-570 modulates its ability to bind CLTC and therefore the synaptic vesicle endocytosis (SVE). {ECO:0000269|PubMed:29735704}.; PTM: The N-terminus is blocked. {ECO:0000250|UniProtKB:Q27974}.
SUBCELLULAR LOCATION: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q27974}. Note=Appears on coated vesicles in successive transient bursts, immediately after the vesicle release from the plasma membrane. Recruitment to clathrin-coated vesicles depends on temporal variations in phosphoinositide co...
null
null
null
null
null
FUNCTION: May act as a protein phosphatase and/or a lipid phosphatase. Co-chaperone that recruits HSPA8/HSC70 to clathrin-coated vesicles (CCVs) and promotes the ATP-dependent dissociation of clathrin from CCVs and participates in clathrin-mediated endocytosis of synaptic vesicles and their recycling and also in intrac...
Homo sapiens (Human)
O75063
XYLK_HUMAN
MKLKQRVVLLAILLVIFIFTKVFLIDNLDTSAANREDQRAFHRMMTGLRVELAPKLDHTLQSPWEIAAQWVVPREVYPEETPELGAVMHAMATKKIIKADVGYKGTQLKALLILEGGQKVVFKPKRYSRDHVVEGEPYAGYDRHNAEVAAFHLDRILGFHRAPLVVGRFVNLRTEIKPVATEQLLSTFLTVGNNTCFYGKCYYCRETEPACADGDIMEGSVTLWLPDVWPLQKHRHPWGRTYREGKLARWEYDESYCDAVKKTSPYDSGPRLLDIIDTAVFDYLIGNADRHHYESFQDDEGASMLILLDNAKSFGNPSLD...
2.7.1.-
COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9XTW2};
phosphorylation [GO:0016310]; proteoglycan biosynthetic process [GO:0030166]
Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleoplasm [GO:0005654]
ATP binding [GO:0005524]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; phosphotransferase activity, alcohol group as acceptor [GO:0016773]
PF06702;
null
FAM20 family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:19473117}; Single-pass type II membrane protein {ECO:0000269|PubMed:19473117}.
CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + ATP = 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-2-O-phosphoxylosyl)-L-seryl-[protein] + ADP + H(+); Xref=Rhea:RHEA:19461, Rhea:RHEA-COMP:12571, Rhea:RHEA-COMP:14558, ChEBI:CHEBI:15...
null
null
null
null
FUNCTION: Responsible for the 2-O-phosphorylation of xylose in the glycosaminoglycan-protein linkage region of proteoglycans thereby regulating the amount of mature GAG chains. Sulfated glycosaminoglycans (GAGs), including heparan sulfate and chondroitin sulfate, are synthesized on the so-called common GAG-protein link...
Homo sapiens (Human)
O75069
TMCC2_HUMAN
MKRCRSDELQQQQGEEDGAGLEDAASHLPGADLRPGETTGANSAGGPTSDAGAAAAPNPGPRSKPPDLKKIQQLSEGSMFGHGLKHLFHSRRRSREREHQTSQDSQQHQQQQGMSDHDSPDEKERSPEMHRVSYAMSLHDLPARPTAFNRVLQQIRSRPSIKRGASLHSSSGGGSSGSSSRRTKSSSLEPQRGSPHLLRKAPQDSSLAAILHQHQCRPRSSSTTDTALLLADGSNVYLLAEEAEGIGDKVDKGDLVALSLPAGHGDTDGPISLDVPDGAPDPQRTKAAIDHLHQKILKITEQIKIEQEARDDNVAEYLKL...
null
null
amyloid precursor protein metabolic process [GO:0042982]
endomembrane system [GO:0012505]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]
null
PF10267;
null
TEX28 family
null
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:21593558, ECO:0000269|PubMed:24454821, ECO:0000269|PubMed:30220460}; Multi-pass membrane protein {ECO:0000255}. Note=Concentrates in discrete patches along peripheral endoplasmic reticulum tubules. {ECO:0000269|PubMed:30220460}.
null
null
null
null
null
FUNCTION: May be involved in the regulation of the proteolytic processing of the amyloid precursor protein (APP) possibly also implicating APOE. {ECO:0000269|PubMed:21593558}.
Homo sapiens (Human)
O75072
FKTN_HUMAN
MSRINKNVVLALLTLTSSAFLLFQLYYYKHYLSTKNGAGLSKSKGSRIGFDSTQWRAVKKFIMLTSNQNVPVFLIDPLILELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGFQCLKIESKDPRLDGIDSLSGTEIPLHYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFDRPELQQVTVDGLEVLIPKDPMHFVEEVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAKELLQLAAKTLNKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDL...
2.7.8.-
null
muscle organ development [GO:0007517]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of JNK cascade [GO:0046329]; nervous system development [GO:0007399]; protein glycosylation [GO:0006486]; protein O-linked glycosylation [GO:0006493]; protein O-linked mannosylation [GO:0035269]...
cis-Golgi network [GO:0005801]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; nucleus [GO:0005634]
phosphotransferase activity, for other substituted phosphate groups [GO:0016780]
PF19737;PF04991;
null
LicD transferase family
null
SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:29477842, ECO:0000305|PubMed:26923585}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q8R507}. Nucleus {ECO:0000250|UniProtKB:Q8R507}. Note=In retinal tissue, does not localize with the...
CATALYTIC ACTIVITY: Reaction=3-O-[beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + CDP-L-ribitol = 3-O-[Rib-ol-P-3-beta-D-GalNAc-(1->3)-beta-D-GlcNAc-(1->4)-(O-6-P-alpha-D-Man)]-Thr-[protein] + CMP + H(+); Xref=Rhea:RHEA:36551, Rhea:RHEA-COMP:13309, Rhea:RHEA-COMP:17480, ChEBI:CHEBI:15378,...
null
PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:25279699, ECO:0000269|PubMed:26923585, ECO:0000269|PubMed:27194101, ECO:0000269|PubMed:29477842}.
null
null
FUNCTION: Catalyzes the transfer of a ribitol-phosphate from CDP-ribitol to the distal N-acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) (PubMed:26923585, Pub...
Homo sapiens (Human)
O75074
LRP3_HUMAN
MEKRAAAGLEGAPGARAQLAVVCLVNIFLTGRLSSAVPALAACSGKLEQHTERRGVIYSPAWPLNYPPGTNCSWYIQGDRGDMITISFRNFDVEESHQCSLDWLLLGPAAPPRQEAFRLCGSAIPPAFISARDHVWIFFHSDASSSGQAQGFRLSYIRGKLGQASCQADEFRCDNGKCLPGPWQCNTVDECGDGSDEGNCSAPASEPPGSLCPGGTFPCSGARSTRCLPVERRCDGLQDCGDGSDEAGCPDLACGRRLGSFYGSFASPDLFGAARGPSDLHCTWLVDTQDSRRVLLQLELRLGYDDYVQVYEGLGERGDR...
null
null
negative regulation of fat cell differentiation [GO:0045599]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; positive regulation of osteoblast differentiation [GO:0045669]; receptor-mediated endocytosis [GO:0006898]; transport across blood-brain barrier [GO:015...
clathrin-coated pit [GO:0005905]; membrane [GO:0016020]; plasma membrane [GO:0005886]
null
PF00431;PF00057;
4.10.400.10;2.60.120.290;
LDLR family
null
SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Membrane, coated pit {ECO:0000250}.
null
null
null
null
null
FUNCTION: Probable receptor, which may be involved in the internalization of lipophilic molecules and/or signal transduction. Its precise role is however unclear, since it does not bind to very low density lipoprotein (VLDL) or to LRPAP1 in vitro.
Homo sapiens (Human)
O75077
ADA23_HUMAN
MKPPGSSSRQPPLAGCSLAGASCGPQRGPAGSVPASAPARTPPCRLLLVLLLLPPLAASSRPRAWGAAAPSAPHWNETAEKNLGVLADEDNTLQQNSSSNISYSNAMQKEITLPSRLIYYINQDSESPYHVLDTKARHQQKHNKAVHLAQASFQIEAFGSKFILDLILNNGLLSSDYVEIHYENGKPQYSKGGEHCYYHGSIRGVKDSKVALSTCNGLHGMFEDDTFVYMIEPLELVHDEKSTGRPHIIQKTLAGQYSKQMKNLTMERGDQWPFLSELQWLKRRKRAVNPSRGIFEEMKYLELMIVNDHKTYKKHRSSHA...
null
null
cell adhesion [GO:0007155]; cellular response to leukemia inhibitory factor [GO:1990830]; central nervous system development [GO:0007417]; proteolysis [GO:0006508]
extracellular region [GO:0005576]; glutamatergic synapse [GO:0098978]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
integrin binding [GO:0005178]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
PF08516;PF00200;PF07974;PF01562;PF01421;
3.40.390.10;4.10.70.10;2.10.25.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform Gamma]: Secreted.
null
null
null
null
null
FUNCTION: May play a role in cell-cell and cell-matrix interactions. This is a non-catalytic metalloprotease-like protein.
Homo sapiens (Human)
O75078
ADA11_HUMAN
MRLLRRWAFAALLLSLLPTPGLGTQGPAGALRWGGLPQLGGPGAPEVTEPSRLVRESSGGEVRKQQLDTRVRQEPPGGPPVHLAQVSFVIPAFNSNFTLDLELNHHLLSSQYVERHFSREGTTQHSTGAGDHCYYQGKLRGNPHSFAALSTCQGLHGVFSDGNLTYIVEPQEVAGPWGAPQGPLPHLIYRTPLLPDPLGCREPGCLFAVPAQSAPPNRPRLRRKRQVRRGHPTVHSETKYVELIVINDHQLFEQMRQSVVLTSNFAKSVVNLADVIYKEQLNTRIVLVAMETWADGDKIQVQDDLLETLARLMVYRREGL...
null
null
behavioral response to acetic acid induced pain [GO:0061367]; behavioral response to formalin induced pain [GO:0061368]; establishment of protein localization [GO:0045184]; integrin-mediated signaling pathway [GO:0007229]; multicellular organismal response to stress [GO:0033555]; proteolysis [GO:0006508]
axon [GO:0030424]; collagen-containing extracellular matrix [GO:0062023]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; presynaptic membrane [GO:0042734]
integrin binding [GO:0005178]; metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]
PF08516;PF00200;PF07974;PF01562;PF01421;
3.40.390.10;4.10.70.10;2.10.25.10;
null
PTM: The precursor is cleaved by a furin endopeptidase. {ECO:0000250}.
SUBCELLULAR LOCATION: Presynaptic cell membrane {ECO:0000250|UniProtKB:Q9R1V4}; Single-pass type I membrane protein. Perikaryon {ECO:0000250|UniProtKB:Q9R1V4}. Cell projection, axon {ECO:0000250|UniProtKB:Q9R1V4}. Note=Localizes to basket cell terminals and pinceaux. {ECO:0000250|UniProtKB:Q9R1V4}.
null
null
null
null
null
FUNCTION: Probable ligand for integrin in the brain. This is a non catalytic metalloprotease-like protein. Required for localization of the potassium channel subunit proteins KCNA1/KV1.1 and KCNA2/KV1.2 at cerebellar cortex basket cell distal terminals, is thereby involved in ephaptic inhibitory synchronization of Purk...
Homo sapiens (Human)
O75081
MTG16_HUMAN
MPASRLRDRAASSASGSTCGSMSQTHPVLESGLLASAGCSAPRGPRKGGPAPVDRKAKASAMPDSPAEVKTQPRSTPPSMPPPPPAASQGATRPPSFTPHTHREDGPATLPHGRFHGCLKWSMVCLLMNGSSHSPTAINGAPCTPNGFSNGPATSSTASLSTQHLPPACGARQLSKLKRFLTTLQQFGSDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQTPAQYLAQHEQLLLDASASSPIDSSELLLEVNENGKRRTPDRTKENGSDRDPLHPEHLSKRPCT...
null
null
DNA-templated transcription [GO:0006351]; granulocyte differentiation [GO:0030851]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of glycolytic process [GO:0045820]; positive regulation of proteasomal ubiquitin-dep...
Golgi membrane [GO:0000139]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]
metal ion binding [GO:0046872]; transcription corepressor activity [GO:0003714]
PF08788;PF07531;PF01753;
6.10.140.2220;6.10.250.230;1.20.120.1110;
CBFA2T family
null
SUBCELLULAR LOCATION: [Isoform 1]: Nucleus, nucleolus. Note=The RUNX1-CBFA2T3 fusion protein localizes to the nucleoplasm.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus, nucleoplasm {ECO:0000269|PubMed:11823486}. Golgi apparatus membrane {ECO:0000269|PubMed:11823486}.
null
null
null
null
null
FUNCTION: Transcriptional corepressor which facilitates transcriptional repression via its association with DNA-binding transcription factors and recruitment of other corepressors and histone-modifying enzymes (PubMed:12559562, PubMed:15203199). Can repress the expression of MMP7 in a ZBTB33-dependent manner (PubMed:23...
Homo sapiens (Human)
O75083
WDR1_HUMAN
MPYEIKKVFASLPQVERGVSKIIGGDPKGNNFLYTNGKCVILRNIDNPALADIYTEHAHQVVVAKYAPSGFYIASGDVSGKLRIWDTTQKEHLLKYEYQPFAGKIKDIAWTEDSKRIAVVGEGREKFGAVFLWDSGSSVGEITGHNKVINSVDIKQSRPYRLATGSDDNCAAFFEGPPFKFKFTIGDHSRFVNCVRFSPDGNRFATASADGQIYIYDGKTGEKVCALGGSKAHDGGIYAISWSPDSTHLLSASGDKTSKIWDVSVNSVVSTFPMGSTVLDQQLGCLWQKDHLLSVSLSGYINYLDRNNPSKPLHVIKGHS...
null
null
actin filament depolymerization [GO:0030042]; actin filament fragmentation [GO:0030043]; apical junction assembly [GO:0043297]; cortical cytoskeleton organization [GO:0030865]; establishment of planar polarity of follicular epithelium [GO:0042247]; locomotion [GO:0040011]; maintenance of epithelial cell apical/basal po...
cell junction [GO:0030054]; cell projection [GO:0042995]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; podosome [GO:0002102]
actin filament binding [GO:0051015]
PF00400;
2.130.10.10;
WD repeat AIP1 family
null
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27994071}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5RKI0}. Cell projection, podosome {ECO:0000269|PubMed:22721921}. Cell junction {ECO:0000269|PubMed:25792565}.
null
null
null
null
null
FUNCTION: Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins (PubMed:15629458, PubMed:27557945, PubMed:29751004). Enhances cofilin-mediated actin severing (By similarity). Involved in cytokinesis. Involved in chemotactic cell migration by restricting lamellipodial membrane protrusion...
Homo sapiens (Human)
O75084
FZD7_HUMAN
MRDPGAAAPLSSLGLCALVLALLGALSAGAGAQPYHGEKGISVPDHGFCQPISIPLCTDIAYNQTILPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLDQAIPPCRSLCERARQGCEALMNKFGFQWPERLRCENFPVHGAGEICVGQNTSDGSGGPGGGPTAYPTAPYLPDLPFTALPPGASDGRGRPAFPFSCPRQLKVPPYLGYRFLGERDCGAPCEPGRANGLMYFKEEERRFARLWVGVWSVLCCASTLFTVLTYLVDMRRFSYPERPIIFLSGCYFMVAVAHVAGFLLEDRAVCVERFS...
null
null
canonical Wnt signaling pathway [GO:0060070]; cellular response to retinoic acid [GO:0071300]; mesenchymal to epithelial transition [GO:0060231]; negative regulation of cardiac muscle cell differentiation [GO:2000726]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of ectodermal cell f...
intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020]; plasma membrane [GO:0005886]; recycling endosome membrane [GO:0055038]
frizzled binding [GO:0005109]; G protein-coupled receptor activity [GO:0004930]; PDZ domain binding [GO:0030165]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; Wnt receptor activity [GO:0042813]; Wnt-protein binding [GO:0017147]
PF01534;PF01392;
1.10.2000.10;1.20.1070.10;
G-protein coupled receptor Fz/Smo family
PTM: Ubiquitinated by ZNRF3, leading to its degradation by the proteasome. {ECO:0000250}.
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27386966}; Multi-pass membrane protein {ECO:0000269|PubMed:27386966}. Endosome membrane {ECO:0000269|PubMed:27386966}; Multi-pass membrane protein {ECO:0000269|PubMed:27386966}. Note=Associated to the plasma membrane in the presence of FZD7 and phosphatidylinosito...
null
null
null
null
null
FUNCTION: Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC an...
Homo sapiens (Human)
O75093
SLIT1_HUMAN
MALTPGWGSSAGPVRPELWLLLWAAAWRLGASACPALCTCTGTTVDCHGTGLQAIPKNIPRNTERLELNGNNITRIHKNDFAGLKQLRVLQLMENQIGAVERGAFDDMKELERLRLNRNQLHMLPELLFQNNQALSRLDLSENAIQAIPRKAFRGATDLKNLQLDKNQISCIEEGAFRALRGLEVLTLNNNNITTIPVSSFNHMPKLRTFRLHSNHLFCDCHLAWLSQWLRQRPTIGLFTQCSGPASLRGLNVAEVQKSEFSCSGQGEAGRVPTCTLSSGSCPAMCTCSNGIVDCRGKGLTAIPANLPETMTEIRLELNG...
null
null
axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; dorsal/ventral axon guidance [GO:0033563]; forebrain morphogenesis [GO:0048853]; motor neuron axon guidance [GO:0008045]; negative chemotaxis [GO:0050919]; negative regulation of axon extension involved in axon guidance [GO:0048843]; neg...
extracellular space [GO:0005615]
calcium ion binding [GO:0005509]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; Roundabout binding [GO:0048495]
PF00008;PF12661;PF02210;PF13855;PF01463;PF01462;
2.60.120.200;2.10.25.10;3.80.10.10;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
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 (By similarity). ...
Homo sapiens (Human)
O75094
SLIT3_HUMAN
MAPGWAGVGAAVRARLALALALASVLSGPPAVACPTKCTCSAASVDCHGLGLRAVPRGIPRNAERLDLDRNNITRITKMDFAGLKNLRVLHLEDNQVSVIERGAFQDLKQLERLRLNKNKLQVLPELLFQSTPKLTRLDLSENQIQGIPRKAFRGITDVKNLQLDNNHISCIEDGAFRALRDLEILTLNNNNISRILVTSFNHMPKIRTLRLHSNHLYCDCHLAWLSDWLRQRRTVGQFTLCMAPVHLRGFNVADVQKKEYVCPAPHSEPPSCNANSISCPSPCTCSNNIVDCRGKGLMEIPANLPEGIVEIRLEQNSIK...
null
null
aortic valve morphogenesis [GO:0003180]; apoptotic process involved in luteolysis [GO:0061364]; atrioventricular valve morphogenesis [GO:0003181]; axon extension involved in axon guidance [GO:0048846]; axon guidance [GO:0007411]; cellular response to hormone stimulus [GO:0032870]; negative chemotaxis [GO:0050919]; nega...
extracellular space [GO:0005615]; mitochondrion [GO:0005739]
calcium ion binding [GO:0005509]; heparin binding [GO:0008201]; Roundabout binding [GO:0048495]
PF00008;PF12661;PF02210;PF13855;PF01463;PF01462;
2.60.120.200;2.10.25.10;3.80.10.10;
null
null
SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
null
null
null
null
null
FUNCTION: May act as molecular guidance cue in cellular migration, and function may be mediated by interaction with roundabout homolog receptors.
Homo sapiens (Human)
O75096
LRP4_HUMAN
MRRQWGALLLGALLCAHGLASSPECACGRSHFTCAVSALGECTCIPAQWQCDGDNDCGDHSDEDGCILPTCSPLDFHCDNGKCIRRSWVCDGDNDCEDDSDEQDCPPRECEEDEFPCQNGYCIRSLWHCDGDNDCGDNSDEQCDMRKCSDKEFRCSDGSCIAEHWYCDGDTDCKDGSDEENCPSAVPAPPCNLEEFQCAYGRCILDIYHCDGDDDCGDWSDESDCSSHQPCRSGEFMCDSGLCINAGWRCDGDADCDDQSDERNCTTSMCTAEQFRCHSGRCVRLSWRCDGEDDCADNSDEENCENTGSPQCALDQFLCW...
null
null
amyloid-beta clearance by cellular catabolic process [GO:0150094]; dendrite morphogenesis [GO:0048813]; dorsal/ventral pattern formation [GO:0009953]; embryonic digit morphogenesis [GO:0042733]; enzyme-linked receptor protein signaling pathway [GO:0007167]; generation of neurons [GO:0048699]; hair follicle development ...
apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; dendrite [GO:0030425]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; plasma membrane raft [GO:0044853]; postsynaptic density [GO:0014069]; receptor complex [GO:0043235]; synaptic membrane [GO:0097060]
apolipoprotein binding [GO:0034185]; calcium ion binding [GO:0005509]; coreceptor activity [GO:0015026]; hormone binding [GO:0042562]; protein homodimerization activity [GO:0042803]; receptor tyrosine kinase binding [GO:0030971]; scaffold protein binding [GO:0097110]
PF12662;PF14670;PF00057;PF00058;
2.10.25.10;4.10.400.10;2.120.10.30;
LDLR family
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VI56}; Single-pass type I membrane protein {ECO:0000255}.
null
null
null
null
null
FUNCTION: Mediates SOST-dependent inhibition of bone formation. Functions as a specific facilitator of SOST-mediated inhibition of Wnt signaling. Plays a key role in the formation and the maintenance of the neuromuscular junction (NMJ), the synapse between motor neuron and skeletal muscle. Directly binds AGRIN and recr...
Homo sapiens (Human)
O75106
AOC2_HUMAN
MHLKIVLAFLALSLITIFALAYVLLTSPGGSSQPPHCPSVSHRAQPWPHPGQSQLFADLSREELTAVMRFLTQRLGPGLVDAAQAQPSDNCIFSVELQLPPKAAALAHLDRGSPPPAREALAIVLFGGQPQPNVSELVVGPLPHPSYMRDVTVERHGGPLPYHRRPVLRAEFTQMWRHLKEVELPKAPIFLSSTFNYNGSTLAAVHATPRGLRSGDRATWMALYHNISGVGLFLHPVGLELLLDHRALDPAHWTVQQVFYLGHYYADLGQLEREFKSGRLEVVRVPLPPPNGASSLRSRNSPGPLPPLQFSPQGSQYSVQ...
1.4.3.21
COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 1 copper ion per subunit. {ECO:0000250|UniProtKB:Q16853}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:Q16853}; Note=Binds 2 calcium ions per subunit. {ECO:0000250|UniProtKB:Q16853}; COFA...
amine metabolic process [GO:0009308]; catecholamine metabolic process [GO:0006584]; visual perception [GO:0007601]; xenobiotic metabolic process [GO:0006805]
cytoplasm [GO:0005737]; plasma membrane [GO:0005886]
aliphatic amine oxidase activity [GO:0052595]; copper ion binding [GO:0005507]; electron transfer activity [GO:0009055]; primary amine oxidase activity [GO:0008131]; quinone binding [GO:0048038]
PF01179;PF02727;PF02728;
3.10.450.40;2.70.98.20;
Copper/topaquinone oxidase family
PTM: Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue. {ECO:0000250|UniProtKB:Q16853}.
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:19588076}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16853}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:19588076}. Note=Either not translocated to the plasma membrane or below detection level. {ECO:0000269|Pub...
CATALYTIC ACTIVITY: Reaction=2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 + NH4(+); Xref=Rhea:RHEA:25265, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16424, ChEBI:CHEBI:28938, ChEBI:CHEBI:225237; EC=1.4.3.21; Evidence={ECO:0000269|PubMed:19588076}; PhysiologicalDirection=left-to-...
BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.056 mM for tryptamine {ECO:0000269|PubMed:19588076}; KM=0.077 mM for 2-phenylethylamine {ECO:0000269|PubMed:19588076}; KM=0.167 mM for benzylamine {ECO:0000269|PubMed:19588076}; KM=0.178 mM for p-tyramine {ECO:0000269|PubMed:19588076}; KM=1.7 mM for methylamine {...
null
null
null
FUNCTION: Catalyzes the oxidative deamination of primary amines to the corresponding aldehydes with the concomitant production of hydrogen peroxide and ammonia (PubMed:19588076). Has a preference for 2-phenylethylamine, tryptamine and tyramine (PubMed:19588076). Could also act on methylamine and benzylamine but much le...
Homo sapiens (Human)
O75110
ATP9A_HUMAN
MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINNQKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIREAVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSEKNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFTREDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEVNCLTKILFGALVVVSLVMVA...
7.6.2.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P40527};
endocytosis [GO:0006897]; negative regulation of exosomal secretion [GO:1903542]; neuron projection morphogenesis [GO:0048812]; phospholipid translocation [GO:0045332]; regulation of endocytic recycling [GO:2001135]; regulation of retrograde transport, endosome to Golgi [GO:1905279]; retrograde vesicle-mediated transpo...
early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; trans-Golgi ne...
ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATPase-coupled intramembrane lipid transporter activity [GO:0140326]; magnesium ion binding [GO:0000287]; protease binding [GO:0002020]
PF13246;PF00122;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: Early endosome membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620, ECO:0000269|PubMed:30213940}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000269|PubMed:21914794, ECO:0000269|PubMed:27733620}; Multi-pass membrane protein {ECO:0000255}. Late endoso...
CATALYTIC ACTIVITY: Reaction=ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.; EC=7.6.2.1; Evidence={ECO:0000305|PubMed:30213940};
null
null
null
null
FUNCTION: Plays a role in regulating membrane trafficking of cargo proteins, namely endosome to plasma membrane recycling, probably acting through RAB5 and RAB11 activation (PubMed:27733620, PubMed:30213940, PubMed:36604604). Also involved in endosome to trans-Golgi network retrograde transport (PubMed:27733620, PubMed...
Homo sapiens (Human)
O75112
LDB3_HUMAN
MSYSVTLTGPGPWGFRLQGGKDFNMPLTISRITPGSKAAQSQLSQGDLVVAIDGVNTDTMTHLEAQNKIKSASYNLSLTLQKSKRPIPISTTAPPVQTPLPVIPHQKDPALDTNGSLVAPSPSPEARASPGTPGTPELRPTFSPAFSRPSAFSSLAEASDPGPPRASLRAKTSPEGARDLLGPKALPGSSQPRQYNNPIGLYSAETLREMAQMYQMSLRGKASGVGLPGGSLPIKDLAVDSASPVYQAVIKSQNKPEDEADEWARRSSNLQSRSFRILAQMTGTEFMQDPDEEALRRSSTPIEHAPVCTSQATTPLLPAS...
null
null
actin cytoskeleton organization [GO:0030036]; heart development [GO:0007507]; muscle structure development [GO:0061061]; sarcomere organization [GO:0045214]
adherens junction [GO:0005912]; cytoskeleton [GO:0005856]; filamentous actin [GO:0031941]; perinuclear region of cytoplasm [GO:0048471]; pseudopodium [GO:0031143]; stress fiber [GO:0001725]; Z disc [GO:0030018]
actin binding [GO:0003779]; cytoskeletal protein binding [GO:0008092]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371]; protein kinase C binding [GO:0005080]
PF15936;PF00412;PF00595;
2.30.42.10;2.10.110.10;
null
null
SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000269|PubMed:10427098}. Cell projection, pseudopodium {ECO:0000269|PubMed:10427098}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10427098}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10427098}. Note=Localized to the cytoplasm around nuclei and ...
null
null
null
null
null
FUNCTION: May function as an adapter in striated muscle to couple protein kinase C-mediated signaling via its LIM domains to the cytoskeleton. {ECO:0000305}.
Homo sapiens (Human)
O75113
N4BP1_HUMAN
MAARAVLDEFTAPAEKAELLEQSRGRIEGLFGVSLAVLGALGAEEPLPARIWLQLCGAQEAVHSAKEYIKGICEPELEERECYPKDMHCIFVGAESLFLKSLIQDTCADLCILDIGLLGIRGSAEAVVMARSHIQQFVKLFENKENLPSSQKESEVKREFKQFVEAHADNYTMDLLILPTSLKKELLTLTQGEENLFETGDDEVIEMRDSQQTEFTQNAATGLNISRDETVLQEEARNKAGTPVSELTKQMDTVLSSSPDVLFDPINGLTPDEEALSNERICQKRRFSDSEERHTKKQFSLENVQEGEILHDAKTLAGNV...
3.1.-.-
null
cellular response to UV [GO:0034644]; innate immune response [GO:0045087]; negative regulation of cytokine production [GO:0001818]; negative regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032435]; negative regulation of protein ubiquitination [GO:0031397]; negative regulation of viral geno...
cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634]; PML body [GO:0016605]
mRNA binding [GO:0003729]; RNA nuclease activity [GO:0004540]; ubiquitin binding [GO:0043130]
PF11977;
3.40.50.11980;
N4BP1 family
PTM: Proteolytically cleaved by CASP8 downstream of TLR3 or TLR4, leading to its inactivation. Mainly cleaved at Asp-490 by CASP8 (By similarity). Cleaved by caspase-like protein MALT1 in T-cells following TCR-mediated activation, leading to its inactivation and subsequent viral reactivation during HIV-1 infection (Pub...
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6A037}. Nucleus {ECO:0000250|UniProtKB:Q6A037}. Nucleus, nucleolus {ECO:0000250|UniProtKB:Q6A037}. Nucleus, PML body {ECO:0000250|UniProtKB:Q6A037}. Note=Primarily localizes to the nucleolus. Also localizes to the PML nuclear bodies, when desumoylated. {E...
null
null
null
null
null
FUNCTION: Potent suppressor of cytokine production that acts as a regulator of innate immune signaling and inflammation. Acts as a key negative regulator of select cytokine and chemokine responses elicited by TRIF-independent Toll-like receptors (TLRs), thereby limiting inflammatory cytokine responses to minor insults....
Homo sapiens (Human)
O75116
ROCK2_HUMAN
MSRPPPTGKMPGAPETAPGDGAGASRQRKLEALIRDPRSPINVESLLDGLNSLVLDLDFPALRKNKNIDNFLNRYEKIVKKIRGLQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKHGHLKLADFGTCMKMDETGMVHCDTAVGTPDYISPEVLKSQGGDGFYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMDHKNSLCFPEDAE...
2.7.11.1
COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
actin cytoskeleton organization [GO:0030036]; actomyosin structure organization [GO:0031032]; aortic valve morphogenesis [GO:0003180]; blood vessel diameter maintenance [GO:0097746]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to acetylcholine [GO:1905145]; cellular response to testosterone ...
centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
ATP binding [GO:0005524]; endopeptidase activator activity [GO:0061133]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; Rho-dependent protein serine/threonine kinase activity [GO:0072518]; RNA binding [GO...
PF00069;PF08912;
1.20.5.340;3.30.60.20;2.30.29.30;1.20.5.730;1.10.510.10;
Protein kinase superfamily, AGC Ser/Thr protein kinase family
PTM: Phosphorylation at Tyr-722 reduces its binding to RHOA and is crucial for focal adhesion dynamics. Dephosphorylation by PTPN11 stimulates its RHOA binding activity. {ECO:0000269|PubMed:18559669, ECO:0000269|PubMed:20826462}.; PTM: Cleaved by granzyme B during apoptosis. This leads to constitutive activation of the...
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Cytoplasmic, and associated with actin microfilaments and 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: Protein kinase which is a key regulator of actin cytoskeleton and cell polarity. Involved in regulation of smooth muscle contraction, actin cytoskeleton organization, stress fiber and focal adhesion formation, neurite retraction, cell adhesion and motility via phosphorylation of ADD1, BRCA2, CNN1, EZR, DPYSL2...
Homo sapiens (Human)
O75121
MFA3L_HUMAN
MDRLKSHLTVCFLPSVPFLILVSTLATAKSVTNSTLNGTNVVLGSVPVIIARTDHIIVKEGNSALINCSVYGIPDPQFKWYNSIGKLLKEEEDEKERGGGKWQMHDSGLLNITKVSFSDRGKYTCVASNIYGTVNNTVTLRVIFTSGDMGVYYMVVCLVAFTIVMVLNITRLCMMSSHLKKTEKAINEFFRTEGAEKLQKAFEIAKRIPIITSAKTLELAKVTQFKTMEFARYIEELARSVPLPPLIMNCRTIMEEIMEVVGLEEQGQNFVRHTPEGQEAADRDEVYTIPNSLKRSDSPAADSDASSLHEQPQQIAIKVS...
null
null
null
cell junction [GO:0030054]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]
null
PF07679;
2.60.40.10;
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:24735981}; Single-pass type I membrane protein {ECO:0000305}. Nucleus {ECO:0000269|PubMed:24735981}. Cytoplasm {ECO:0000269|PubMed:24735981}. Note=Mainly localized in the nucleus (PubMed:24735981). {ECO:0000269|PubMed:24735981}.
null
null
null
null
null
FUNCTION: May participate in the nuclear signaling of EGFR and MAPK1/ERK2. May a have a role in metastasis. {ECO:0000269|PubMed:24735981}.
Homo sapiens (Human)
O75122
CLAP2_HUMAN
MAMGDDKSFDDEESVDGNRPSSAASAFKVPAPKTSGNPANSARKPGSAGGPKVGGASKEGGAGAVDEDDFIKAFTDVPSIQIYSSRELEETLNKIREILSDDKHDWDQRANALKKIRSLLVAGAAQYDCFFQHLRLLDGALKLSAKDLRSQVVREACITVAHLSTVLGNKFDHGAEAIVPTLFNLVPNSAKVMATSGCAAIRFIIRHTHVPRLIPLITSNCTSKSVPVRRRSFEFLDLLLQEWQTHSLERHAAVLVETIKKGIHDADAEARVEARKTYMGLRNHFPGEAETLYNSLEPSYQKSLQTYLKSSGSVASLPQS...
null
null
cell division [GO:0051301]; establishment of mitotic spindle localization [GO:0040001]; establishment or maintenance of cell polarity [GO:0007163]; exit from mitosis [GO:0010458]; Golgi organization [GO:0007030]; microtubule anchoring [GO:0034453]; microtubule cytoskeleton organization [GO:0000226]; microtubule nucleat...
axonal growth cone [GO:0044295]; basal cortex [GO:0045180]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; centrosome [GO:0005813]; cortical microtubule plus-end [GO:1903754]; cytoplasm [GO:0005737]; cytoplasmic microtubule [GO:0005881]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; kinetochore [GO:000...
actin filament binding [GO:0051015]; dystroglycan binding [GO:0002162]; microtubule binding [GO:0008017]; microtubule plus-end binding [GO:0051010]; protein tyrosine kinase binding [GO:1990782]
PF21040;PF12348;
1.25.10.10;
CLASP family
PTM: Phosphorylated by GSK3B. Phosphorylation reduces MAPRE1 binding (PubMed:26003921). Phosphorylation by GSK3B may negatively regulate binding to microtubule lattices in lamella. {ECO:0000269|PubMed:15955847, ECO:0000305|PubMed:26003921}.
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:20937854}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:16914514}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:16866869, ECO:0000269|PubMed:16914514}. Cytoplasm, cytoskele...
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null
null
null
null
FUNCTION: Microtubule plus-end tracking protein that promotes the stabilization of dynamic microtubules (PubMed:26003921). Involved in the nucleation of noncentrosomal microtubules originating from the trans-Golgi network (TGN). Required for the polarization of the cytoplasmic microtubule arrays in migrating cells towa...
Homo sapiens (Human)
O75127
PTCD1_HUMAN
MDFVRLARLFARARPMGLFILQHLDPCRARWAGGREGLMRPMWAPFSSSSSQLPLGQERQENTGSLGSDPSHSNSTATQEEDEEEEESFGTLSDKYSSRRLFRKSAAQFHNLRFGERRDEQMEPEPKLWRGRRNTPYWYFLQCKHLIKEGKLVEALDLFERQMLKEERLQPMESNYTVLIGGCGRVGYLKKAFNLYNQMKKRDLEPSDATYTALFNVCAESPWKDSALQSALKLRQQLQAKNFELNLKTYHALLKMAAKCADLRMCLDVFKEIIHKGHVVTEETFSFLLMGCIQDKKTGFRYALQVWRLMLSLGLQPSRD...
null
null
mitochondrial translation [GO:0032543]; tRNA 3'-end processing [GO:0042780]
mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]
RNA binding [GO:0003723]; tRNA binding [GO:0000049]
PF13812;PF17177;
1.25.40.10;
PTCD1 family
null
SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:19651879, ECO:0000269|PubMed:21857155}. Mitochondrion matrix {ECO:0000250}.
null
null
null
null
null
FUNCTION: Mitochondrial protein implicated in negative regulation of leucine tRNA levels, as well as negative regulation of mitochondria-encoded proteins and COX activity. Affects also the 3'-processing of mitochondrial tRNAs. {ECO:0000269|PubMed:21857155}.
Homo sapiens (Human)
O75128
COBL_HUMAN
MDAPRASAAKPPTGRKMKARAPPPPGKAATLHVHSDQKPPHDGALGSQQNLVRMKEALRASTMDVTVVLPSGLEKRSVLNGSHAMMDLLVELCLQNHLNPSHHALEIRSSETQQPLSFKPNTLIGTLNVHTVFLKEKVPEEKVKPGPPKVPEKSVRLVVNYLRTQKAVVRVSPEVPLQNILPVICAKCEVSPEHVVLLRDNIAGEELELSKSLNELGIKELYAWDNRRETFRKSSLGNDETDKEKKKFLGFFKVNKRSNSKGCLTTPNSPSMHSRSLTLGPSLSLGSISGVSVKSEMKKRRAPPPPGSGPPVQDKASEKV...
null
null
actin filament network formation [GO:0051639]; actin filament polymerization [GO:0030041]; collateral sprouting in absence of injury [GO:0048669]; digestive tract development [GO:0048565]; embryonic axis specification [GO:0000578]; floor plate development [GO:0033504]; liver development [GO:0001889]; neural tube closur...
actin filament [GO:0005884]; axon [GO:0030424]; axonal growth cone [GO:0044295]; cell cortex [GO:0005938]; dendrite [GO:0030425]; dendritic growth cone [GO:0044294]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; ruffle [GO:0001726]; t...
actin monomer binding [GO:0003785]
PF09469;PF02205;
null
null
null
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cell projection, ruffle {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Recruited to the cell membrane via interaction with PACSIN1. Colocalizes with the acti...
null
null
null
null
null
FUNCTION: Plays an important role in the reorganization of the actin cytoskeleton. Regulates neuron morphogenesis and increases branching of axons and dendrites. Regulates dendrite branching in Purkinje cells (By similarity). Binds to and sequesters actin monomers (G actin). Nucleates actin polymerization by assembling...
Homo sapiens (Human)