PUB3_SCHPO
ID PUB3_SCHPO Reviewed; 786 AA.
AC O14326; P79055;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=E3 ubiquitin-protein ligase pub3;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase pub3;
GN Name=pub3; ORFNames=SPBC16E9.11c;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 637-786.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
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.
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 -!- MISCELLANEOUS: A cysteine residue is required for ubiquitin-thioester
CC formation.
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DR EMBL; CU329671; CAB16903.1; -; Genomic_DNA.
DR EMBL; AB001023; BAA19217.1; -; mRNA.
DR PIR; T39585; T39585.
DR RefSeq; NP_595793.1; NM_001021694.2.
DR AlphaFoldDB; O14326; -.
DR SMR; O14326; -.
DR BioGRID; 276500; 79.
DR STRING; 4896.SPBC16E9.11c.1; -.
DR iPTMnet; O14326; -.
DR MaxQB; O14326; -.
DR PaxDb; O14326; -.
DR PRIDE; O14326; -.
DR EnsemblFungi; SPBC16E9.11c.1; SPBC16E9.11c.1:pep; SPBC16E9.11c.
DR GeneID; 2539956; -.
DR KEGG; spo:SPBC16E9.11c; -.
DR PomBase; SPBC16E9.11c; pub3.
DR VEuPathDB; FungiDB:SPBC16E9.11c; -.
DR eggNOG; KOG0940; Eukaryota.
DR HOGENOM; CLU_002173_0_0_1; -.
DR InParanoid; O14326; -.
DR OMA; DDWVIVP; -.
DR PhylomeDB; O14326; -.
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:O14326; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005543; F:phospholipid binding; ISM:PomBase.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISM: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; 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 2: Evidence at transcript level;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway.
FT CHAIN 1..786
FT /note="E3 ubiquitin-protein ligase pub3"
FT /id="PRO_0000120334"
FT DOMAIN 1..109
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 236..269
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 306..339
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 364..397
FT /note="WW 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 453..786
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT REGION 134..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 754
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT CONFLICT 637..649
FT /note="FNAFYSGFVELVS -> LMHFILVLLNWYP (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 786 AA; 89260 MW; 57B7A859F5497B9A CRC64;
MEQGAKRVRF YIVAADGLSK RDLFRQPDPF AILTVDGEQT HTTKVIKKSV NPYWNEGFEV
TVKPSSVISI RLFDQKKFKK KDQGFLGLVS FRMREVGSFR SNREVSLTRP LKKSSTTNLS
VLGNLVLKVA PSKIRAPAGN HSSTTANRTT STPTTTTART TRTTPRPTAT TNTSNQSTSN
STRNGTSAAT SNGTGTGAGT GASHRSSPVT NRQTNNTSAL SNSNAHIMSS FEDQYGRLPP
GWERRADSLG RTYYVDHNTR TTTWTRPASS TNPVHNTSSD SQRLNHQNRH LPDDSNPSLM
QSDSGNDLPF GWEMRYTDTG RPYFVDHNTR TTTWVDPRNP LVRPNGGSST VGSLMQPQSL
SHLGPLPSGW EMRLTNSARV YFVDHNTKTT TWDDPRLPSA LDQDVPQYKC DFRRKLIYFR
SQPGMRPLPG QCNVKVRRDH IFEDSYAEIM RYSAHDLKKR LMIRFDGEDG LDYGGLSREF
FFLLSHKMFD PIYCLFEYSA VDNYTLQINP HSSINPEHLN YFRFIGRVIG LAIFHRRFLD
AFFVVSLYKK LLRKKVSLAD MESIDAEFYR SLKWVLENDI TGILDLTFSV EEDHFGEVRT
VELITNGENI EVTEENKKKY VDLVTEWRVS KRVEQQFNAF YSGFVELVSP DLVNVFDERE
LELLIGGISD VDVEDWKSHT EYRTYIATDP VIKWFWEIIA GWKNEDRSKL LQFATGTSRI
PVNGFRDLQG SDGPRKFTIE KAGTPDQLPV AHTCFNRLDL PDYPSKDTLH EKLSLAVENT
VGFGNE
