PUB2_SCHPO
ID PUB2_SCHPO Reviewed; 671 AA.
AC Q9UTG2;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=E3 ubiquitin-protein ligase pub2;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase pub2;
GN Name=pub2; ORFNames=SPAC1805.15c;
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 [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 [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-639.
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).
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. Has a role in
CC the G2/M transition. {ECO:0000269|PubMed:11956316}.
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}. Note=Predominantly found at the cell
CC surface of the polar regions.
CC -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester
CC formation.
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DR EMBL; CU329670; CAB55856.1; -; Genomic_DNA.
DR PIR; T37900; T37900.
DR RefSeq; NP_593926.1; NM_001019355.2.
DR AlphaFoldDB; Q9UTG2; -.
DR SMR; Q9UTG2; -.
DR BioGRID; 278894; 8.
DR STRING; 4896.SPAC1805.15c.1; -.
DR iPTMnet; Q9UTG2; -.
DR MaxQB; Q9UTG2; -.
DR PaxDb; Q9UTG2; -.
DR PRIDE; Q9UTG2; -.
DR EnsemblFungi; SPAC1805.15c.1; SPAC1805.15c.1:pep; SPAC1805.15c.
DR GeneID; 2542432; -.
DR KEGG; spo:SPAC1805.15c; -.
DR PomBase; SPAC1805.15c; pub2.
DR VEuPathDB; FungiDB:SPAC1805.15c; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR InParanoid; Q9UTG2; -.
DR OMA; AIFHRRY; -.
DR PhylomeDB; Q9UTG2; -.
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:Q9UTG2; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IMP:PomBase.
DR GO; GO:0120113; P:cytoplasm to vacuole transport by the NVT pathway; IMP:PomBase.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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 CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 1.
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; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 1.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Membrane; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..671
FT /note="E3 ubiquitin-protein ligase pub2"
FT /id="PRO_0000120333"
FT DOMAIN 1..112
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 242..275
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 338..671
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ACT_SITE 639
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000305"
FT MUTAGEN 639
FT /note="C->A: No growth arrest or cell elongation."
FT /evidence="ECO:0000269|PubMed:11956316"
SQ SEQUENCE 671 AA; 77195 MW; 3629F82D4B47F594 CRC64;
MENIRFEVQL TILHVEGLWK NGLLRSLKPY LLISVDDDQF IKTNVASGTL RLSWGFTQKL
TVSPQSIILL QLFDEKQKNE TSDGFVGLGA AVVNSFLPFN NPKDDYKTRI TLRSPSGSYR
GSVVCLFKRS KFLPEELPAD KSQICTDIID DASGCAWETR IDEFGHVYYL KSPQLSVISA
ISHEKLENLT PKQLKEVFSQ FLFNNQSKSS LKINLEYKVI KHLLEHYPLA LSVRQQVAVE
KGPLPAGWEM RLSEDYHVYF VDHSTKTTTW SDPRDNVVAS DSVSENTDSI QQINDEYQRK
IAYMYDRPEM AVNDAQLQLK VSRATTFEDA YDIISKLSVS DMKKKLLIRF RNEDGLDYGG
VSREFFYILS HAIFNPGYSL FEYATDDNYG LQISPLSSVN PDFRSYFRFV GRVMGLAIYH
RRYLDVQFVL PFYKRILQKP LCLEDVKDVD EVYYESLKWI KNNDVDESLC LNFSVEENRF
GESVTVDLIP NGRNIAVNNQ NKMNYLKALT EHKLVTSTEE QFNALKGGLN ELIPDSVLQI
FNENELDTLL NGKRDIDVQD WKRFTDYRSY TETDDIVIWF WELLSEWSPE KKAKLLQFAT
GTSRLPLSGF KDMHGSDGPR KFTIEKVGHI SQLPKAHTCF NRLDIPPYNS KEELEQKLTI
AIQETAGFGT E
