UBC15_SCHPO
ID UBC15_SCHPO Reviewed; 167 AA.
AC Q9Y818;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 15;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 15;
DE AltName: Full=Ubiquitin carrier protein 15;
DE AltName: Full=Ubiquitin-protein ligase 15;
GN Name=ubc15; ORFNames=SPBC1105.09;
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.
RX PubMed=12456009; DOI=10.1128/ec.1.4.613-625.2002;
RA Nielsen I.S., Nielsen O., Murray J.M., Thon G.;
RT "The fission yeast ubiquitin-conjugating enzymes UbcP3, Ubc15, and Rhp6
RT affect transcriptional silencing of the mating-type region.";
RL Eukaryot. Cell 1:613-625(2002).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC proteins. Has a role in the formation of chromatin structures that
CC influence the localization of transcriptional silencing factors.
CC {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:12456009}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROSITE-
CC ProRule:PRU10133};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; CU329671; CAB50972.1; -; Genomic_DNA.
DR PIR; T39286; T39286.
DR RefSeq; NP_596465.1; NM_001022384.2.
DR PDB; 5KNL; X-ray; 2.50 A; C/F=1-167.
DR PDBsum; 5KNL; -.
DR AlphaFoldDB; Q9Y818; -.
DR SMR; Q9Y818; -.
DR BioGRID; 276539; 32.
DR STRING; 4896.SPBC1105.09.1; -.
DR MaxQB; Q9Y818; -.
DR PaxDb; Q9Y818; -.
DR EnsemblFungi; SPBC1105.09.1; SPBC1105.09.1:pep; SPBC1105.09.
DR GeneID; 2539995; -.
DR KEGG; spo:SPBC1105.09; -.
DR PomBase; SPBC1105.09; ubc15.
DR VEuPathDB; FungiDB:SPBC1105.09; -.
DR eggNOG; KOG0425; Eukaryota.
DR HOGENOM; CLU_030988_10_1_1; -.
DR InParanoid; Q9Y818; -.
DR OMA; GFFKCHL; -.
DR PhylomeDB; Q9Y818; -.
DR Reactome; R-SPO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q9Y818; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005634; C:nucleus; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO: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:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR Pfam; PF00179; UQ_con; 1.
DR SUPFAM; SSF54495; SSF54495; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Nucleotide-binding; Reference proteome;
KW Transferase; Ubl conjugation pathway.
FT CHAIN 1..167
FT /note="Ubiquitin-conjugating enzyme E2 15"
FT /id="PRO_0000082589"
FT DOMAIN 5..165
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 90
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT HELIX 5..17
FT /evidence="ECO:0007829|PDB:5KNL"
FT STRAND 25..31
FT /evidence="ECO:0007829|PDB:5KNL"
FT STRAND 34..43
FT /evidence="ECO:0007829|PDB:5KNL"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:5KNL"
FT STRAND 54..60
FT /evidence="ECO:0007829|PDB:5KNL"
FT TURN 63..66
FT /evidence="ECO:0007829|PDB:5KNL"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5KNL"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5KNL"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:5KNL"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:5KNL"
FT HELIX 117..129
FT /evidence="ECO:0007829|PDB:5KNL"
FT HELIX 139..147
FT /evidence="ECO:0007829|PDB:5KNL"
FT HELIX 149..167
FT /evidence="ECO:0007829|PDB:5KNL"
SQ SEQUENCE 167 AA; 19106 MW; 2289FD04069E1707 CRC64;
MPSSASEQLL RKQLKEIQKN PPQGFSVGLV DDKSIFEWEV MIIGPEDTLY EGGFFHATLS
FPQDYPLMPP KMKFTTEIWH PNVHPNGEVC ISILHPPGDD KYGYEDAGER WLPVHSPETI
LISVISMLSS PNDESPANID AAKEFRENPQ EFKKRVRRLV RRSIEMI
