UBC13_SCHPO
ID UBC13_SCHPO Reviewed; 148 AA.
AC O13685;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 148.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 13;
DE EC=2.3.2.23;
DE AltName: Full=E2 ubiquitin-conjugating enzyme 13;
DE AltName: Full=Ubiquitin carrier protein 13;
DE AltName: Full=Ubiquitin-protein ligase 13;
GN Name=ubc13; Synonyms=spu13; ORFNames=SPAC11E3.04c;
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 [MRNA], FUNCTION, AND INTERACTION WITH SPM2.
RX PubMed=12531016; DOI=10.1016/s1568-7864(02)00111-8;
RA Brown M., Zhu Y., Hemmingsen S.M., Xiao W.;
RT "Structural and functional conservation of error-free DNA postreplication
RT repair in Schizosaccharomyces pombe.";
RL DNA Repair 1:869-880(2002).
RN [2]
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).
CC -!- FUNCTION: Has a role in the DNA error-free postreplication repair (PRR)
CC pathway. The ubc13/spm2 heterodimer catalyzes the synthesis of non-
CC canonical poly-ubiquitin chains that are linked through 'Lys-63'.
CC {ECO:0000269|PubMed:12531016}.
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 -!- SUBUNIT: Heterodimer with spm2.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AF470232; AAL79844.1; -; mRNA.
DR EMBL; CU329670; CAB11183.1; -; Genomic_DNA.
DR PIR; T37532; T37532.
DR RefSeq; NP_594929.1; NM_001020360.2.
DR AlphaFoldDB; O13685; -.
DR SMR; O13685; -.
DR BioGRID; 279366; 46.
DR STRING; 4896.SPAC11E3.04c.1; -.
DR MaxQB; O13685; -.
DR PaxDb; O13685; -.
DR EnsemblFungi; SPAC11E3.04c.1; SPAC11E3.04c.1:pep; SPAC11E3.04c.
DR GeneID; 2542925; -.
DR KEGG; spo:SPAC11E3.04c; -.
DR PomBase; SPAC11E3.04c; ubc13.
DR VEuPathDB; FungiDB:SPAC11E3.04c; -.
DR eggNOG; KOG0417; Eukaryota.
DR HOGENOM; CLU_030988_13_2_1; -.
DR InParanoid; O13685; -.
DR OMA; PDDYPME; -.
DR PhylomeDB; O13685; -.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-SPO-9020702; Interleukin-1 signaling.
DR Reactome; R-SPO-9646399; Aggrephagy.
DR Reactome; R-SPO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR PRO; PR:O13685; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; 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:0006301; P:postreplication repair; IMP:PomBase.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:PomBase.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0070914; P:UV-damage excision repair; IMP:PomBase.
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 ATP-binding; Nucleotide-binding; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..148
FT /note="Ubiquitin-conjugating enzyme E2 13"
FT /id="PRO_0000082564"
FT DOMAIN 2..148
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 86
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 148 AA; 16856 MW; 4BD0FAC35A571B9C CRC64;
MALPKRIIKE IETLTRDPPP GIVAAPTEDN LRYFKITMEG PQQSAYEGGK FHLELFLPDE
YPMMPPNVRF LTKIYHPNVD KLGRICLSTL KKDWSPALQI RTVLLSIQAL MGAPNPDDPL
DNDVAKIWKE NEPQAIANAR EWTKKYAV
