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   10-FEB-2021, entry version 168.
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;
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   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; TYWEKPT; -.
DR   PhylomeDB; Q92462; -.
DR   BRENDA; 6.3.2.19; 5613.
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:0045732; P:positive regulation of protein catabolic process; IBA:GO_Central.
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; 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   COMPBIAS        242..247
FT                   /note="Poly-Ala"
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
//