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   28-JUN-2011, entry version 93.
DE   RecName: Full=E3 ubiquitin-protein ligase pub1;
DE            EC=6.3.2.-;
GN   Name=pub1; ORFNames=SPAC11G7.02;
OS   Schizosaccharomyces pombe (strain ATCC 38366 / 972) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX   MEDLINE=96205868; PubMed=8635463;
RA   Nefsky B., Beach D.;
RT   "Pub1 acts as an E6-AP-like protein ubiquitiin ligase in the
RT   degradation of cdc25.";
RL   EMBO J. 15:1301-1312(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=J227;
RX   MEDLINE=97340937; 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
RT   functioning pub1 ubiquitin ligase.";
RL   Mol. Gen. Genet. 254:520-528(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 38366 / 972;
RX   MEDLINE=21848401; 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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., 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
RP   THR-180, AND 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
CC       an E2 ubiquitin-conjugating enzyme in the form of a thioester and
CC       then directly transfers the ubiquitin to targeted substrates.
CC       Regulates ubiquitination of cdc25.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Membrane; Peripheral membrane protein.
CC       Cytoplasm.
CC   -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-
CC       thioester formation.
CC   -!- SIMILARITY: Contains 1 C2 domain.
CC   -!- SIMILARITY: Contains 1 HECT (E6AP-type E3 ubiquitin-protein
CC       ligase) domain.
CC   -!- SIMILARITY: Contains 3 WW domains.
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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_001019819.1.
DR   ProteinModelPortal; Q92462; -.
DR   SMR; Q92462; 7-132, 201-377, 388-759.
DR   STRING; Q92462; -.
DR   EnsemblFungi; SPAC11G7.02-1; SPAC11G7.02-1; SPAC11G7.02.
DR   GeneID; 2541818; -.
DR   GenomeReviews; CU329670_GR; pub1.
DR   KEGG; spo:SPAC11G7.02; -.
DR   NMPDR; fig|4896.1.peg.4366; -.
DR   GeneDB_Spombe; SPAC11G7.02; -.
DR   eggNOG; fuNOG04992; -.
DR   GeneTree; EFGT00050000000432; -.
DR   HOGENOM; HBG607874; -.
DR   OMA; EYSAHDN; -.
DR   OrthoDB; EOG4SXRMK; -.
DR   PhylomeDB; Q92462; -.
DR   BioCyc; SPOM-XXX-01:SPOM-XXX-01-002501-MONOMER; -.
DR   ArrayExpress; Q92462; -.
DR   GO; GO:0071944; C:cell periphery; IDA:GeneDB_Spombe.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:GeneDB_Spombe.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004842; F:ubiquitin-protein ligase activity; IMP:GeneDB_Spombe.
DR   GO; GO:0060360; P:negative regulation of leucine import in response to ammonium ion; IMP:GeneDB_Spombe.
DR   GO; GO:0051453; P:regulation of intracellular pH; IGI:GeneDB_Spombe.
DR   GO; GO:0034762; P:regulation of transmembrane transport; IMP:GeneDB_Spombe.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IGI:GeneDB_Spombe.
DR   InterPro; IPR000008; C2_Ca-dep.
DR   InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB.
DR   InterPro; IPR018029; C2_membr_targeting.
DR   InterPro; IPR000569; HECT.
DR   InterPro; IPR001202; WW_Rsp5_WWP.
DR   Gene3D; G3DSA:2.20.70.10; G3DSA:2.20.70.10; 3.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF00397; WW; 3.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 3.
DR   SUPFAM; SSF49562; C2_CaLB; 1.
DR   SUPFAM; SSF56204; HECT; 1.
DR   SUPFAM; SSF51045; WW_Rsp5_WWP; 3.
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   Complete proteome; Cytoplasm; Ligase; Membrane; Phosphoprotein;
KW   Repeat; Ubl conjugation pathway.
FT   CHAIN         1    767       E3 ubiquitin-protein ligase pub1.
FT                                /FTId=PRO_0000120332.
FT   DOMAIN       17     32       C2.
FT   DOMAIN      211    236       WW 1.
FT   DOMAIN      294    319       WW 2.
FT   DOMAIN      351    376       WW 3.
FT   DOMAIN      463    767       HECT.
FT   COMPBIAS    242    247       Poly-Ala.
FT   ACT_SITE    735    735       Glycyl thioester intermediate (By
FT                                similarity).
FT   MOD_RES     156    156       Phosphothreonine.
FT   MOD_RES     178    178       Phosphoserine.
FT   MOD_RES     180    180       Phosphothreonine.
FT   CONFLICT    163    163       Q -> K (in Ref. 1; CAA68867/AAB07514).
FT   CONFLICT    609    609       Missing (in Ref. 1; CAA68867/AAB07514).
FT   CONFLICT    661    661       T -> K (in Ref. 1; CAA68867/AAB07514).
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
//