PUB1_SCHPO
ID PUB1_SCHPO Reviewed; 767 AA.
AC Q92462; O14454;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=E3 ubiquitin-protein ligase pub1;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase pub1;
GN Name=pub1; ORFNames=SPAC11G7.02;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=8635463; DOI=10.1002/j.1460-2075.1996.tb00472.x;
RA Nefsky B., Beach D.;
RT "Pub1 acts as an E6-AP-like protein ubiquitiin ligase in the degradation of
RT cdc25.";
RL EMBO J. 15:1301-1312(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=J227;
RX PubMed=9197411; DOI=10.1007/s004380050447;
RA Saleki R., Jia Z., Karagiannis J., Young P.G.;
RT "Tolerance of low pH in Schizosaccharomyces pombe requires a functioning
RT pub1 ubiquitin ligase.";
RL Mol. Gen. Genet. 254:520-528(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11956316; DOI=10.1242/jcs.115.9.1847;
RA Tamai K.K., Shimoda C.;
RT "The novel HECT-type ubiquitin-protein ligase Pub2p shares partially
RT overlapping function with Pub1p in Schizosaccharomyces pombe.";
RL J. Cell Sci. 115:1847-1857(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-156; SER-178 AND THR-180, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Regulates
CC ubiquitination of cdc25.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:11956316};
CC Peripheral membrane protein {ECO:0000269|PubMed:11956316}. Cytoplasm
CC {ECO:0000269|PubMed:11956316}.
CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester
CC formation.
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DR EMBL; Y07592; CAA68867.1; -; mRNA.
DR EMBL; U66716; AAB07514.1; -; mRNA.
DR EMBL; CU329670; CAB16207.1; -; Genomic_DNA.
DR EMBL; U62795; AAB63350.1; -; Genomic_DNA.
DR PIR; S66562; S66562.
DR PIR; T37545; T37545.
DR RefSeq; NP_594396.1; NM_001019819.2.
DR AlphaFoldDB; Q92462; -.
DR SMR; Q92462; -.
DR BioGRID; 278309; 76.
DR STRING; 4896.SPAC11G7.02.1; -.
DR iPTMnet; Q92462; -.
DR MaxQB; Q92462; -.
DR PaxDb; Q92462; -.
DR PRIDE; Q92462; -.
DR EnsemblFungi; SPAC11G7.02.1; SPAC11G7.02.1:pep; SPAC11G7.02.
DR GeneID; 2541818; -.
DR KEGG; spo:SPAC11G7.02; -.
DR PomBase; SPAC11G7.02; pub1.
DR VEuPathDB; FungiDB:SPAC11G7.02; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR InParanoid; Q92462; -.
DR OMA; FNAFITG; -.
DR PhylomeDB; Q92462; -.
DR Reactome; R-SPO-8948747; Regulation of PTEN localization.
DR Reactome; R-SPO-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-SPO-9013420; RHOU GTPase cycle.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q92462; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0071944; C:cell periphery; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005794; C:Golgi apparatus; HDA:PomBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005543; F:phospholipid binding; ISM:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:PomBase.
DR GO; GO:0120113; P:cytoplasm to vacuole transport by the NVT pathway; IMP:PomBase.
DR GO; GO:1905533; P:negative regulation of leucine import across plasma membrane; IMP:PomBase.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IMP:PomBase.
DR GO; GO:1905530; P:negative regulation of uracil import across plasma membrane; IMP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:PomBase.
DR GO; GO:0070647; P:protein modification by small protein conjugation or removal; IC:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051453; P:regulation of intracellular pH; IGI:PomBase.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:PomBase.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51045; SSF51045; 3.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 3.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..767
FT /note="E3 ubiquitin-protein ligase pub1"
FT /id="PRO_0000120332"
FT DOMAIN 1..111
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 211..236
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 294..319
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 351..376
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 463..767
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 138..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 735
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 156
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 180
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 163
FT /note="Q -> K (in Ref. 1; CAA68867/AAB07514)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="Missing (in Ref. 1; CAA68867/AAB07514)"
FT /evidence="ECO:0000305"
FT CONFLICT 661
FT /note="T -> K (in Ref. 1; CAA68867/AAB07514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 767 AA; 87268 MW; F1455A155EB9ACF7 CRC64;
MSNSAQSRRI RVTIVAADGL YKRDVFRFPD PFAVLTVDGE QTHTTTAIKK TLNPYWNETF
EVNVTDNSTI AIQVFDQKKF KKKGQGFLGV INLRVGDVLD LAIGGDEMLT RDLKKSNENT
VVHGKIIINL STTAQSTLQV PSSAASGART QRTSITNDPQ SSQSSSVSRN PASSRAGSPT
RDNAPAASPA SSEPRTFSSF EDQYGRLPPG WERRTDNLGR TYYVDHNTRS TTWIRPNLSS
VAGAAAAELH SSASSANVTE GVQPSSSNAA RRTEASVLTS NATTAGSGEL PPGWEQRYTP
EGRPYFVDHN TRTTTWVDPR RQQYIRSYGG PNNATIQQQP VSQLGPLPSG WEMRLTNTAR
VYFVDHNTKT TTWDDPRLPS SLDQNVPQYK RDFRRKLIYF LSQPALHPLP GQCHIKVRRN
HIFEDSYAEI MRQSATDLKK RLMIKFDGED GLDYGGLSRE YFFLLSHEMF NPFYCLFEYS
SVDNYTLQIN PHSGINPEHL NYFKFIGRVI GLAIFHRRFV DAFFVVSFYK MILQKKVTLQ
DMESMDAEYY RSLVWILDND ITGVLDLTFS VEDNCFGEVV TIDLKPNGRN IEVTEENKRE
YVDLVTVWRI QKRIEEQFNA FHEGFSELIP QELINVFDER ELELLIGGIS EIDMEDWKKH
TDYRSYSEND QIIKWFWELM DEWSNEKKSR LLQFTTGTSR IPVNGFKDLQ GSDGPRKFTI
EKAGEPNKLP KAHTCFNRLD LPPYTSKKDL DHKLSIAVEE TIGFGQE
