UBC9_SCHPO
ID UBC9_SCHPO Reviewed; 157 AA.
AC P40984;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 25-MAY-2022, entry version 174.
DE RecName: Full=SUMO-conjugating enzyme ubc9;
DE EC=2.3.2.-;
DE AltName: Full=Ubiquitin carrier protein 9;
DE AltName: Full=Ubiquitin carrier protein hus5;
DE AltName: Full=Ubiquitin-conjugating enzyme E2-18 kDa;
GN Name=hus5; Synonyms=ubc9; ORFNames=SPAC30D11.13;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=7768995; DOI=10.1242/jcs.108.2.475;
RA Al-Khodairy F., Enoch T., Hagman I.M., Carr A.M.;
RT "The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating
RT enzyme required for normal mitosis.";
RL J. Cell Sci. 108:475-486(1995).
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).
RN [3]
RP FUNCTION.
RX PubMed=12597774; DOI=10.1042/bj20021645;
RA Ho J.C., Watts F.Z.;
RT "Characterization of SUMO-conjugating enzyme mutants in Schizosaccharomyces
RT pombe identifies a dominant-negative allele that severely reduces SUMO
RT conjugation.";
RL Biochem. J. 372:97-104(2003).
CC -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin-like protein
CC SUMO/Smt3 to other proteins. Required for efficient recovery from DNA
CC damage or S-phase arrest and normal mitosis. This may be as part of a
CC checkpoint independent recovery process. {ECO:0000269|PubMed:12597774,
CC ECO:0000269|PubMed:7768995}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- INTERACTION:
CC P40984; Q9USX3: rad60; NbExp=2; IntAct=EBI-966468, EBI-3650521;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7768995}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; X81846; CAA57438.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA91899.1; -; Genomic_DNA.
DR PIR; S62571; S62571.
DR RefSeq; NP_593204.1; NM_001018600.2.
DR PDB; 3RCZ; X-ray; 1.90 A; B=2-157.
DR PDBsum; 3RCZ; -.
DR AlphaFoldDB; P40984; -.
DR SMR; P40984; -.
DR BioGRID; 278671; 15.
DR DIP; DIP-35488N; -.
DR IntAct; P40984; 4.
DR STRING; 4896.SPAC30D11.13.1; -.
DR MaxQB; P40984; -.
DR PaxDb; P40984; -.
DR EnsemblFungi; SPAC30D11.13.1; SPAC30D11.13.1:pep; SPAC30D11.13.
DR GeneID; 2542196; -.
DR KEGG; spo:SPAC30D11.13; -.
DR PomBase; SPAC30D11.13; hus5.
DR VEuPathDB; FungiDB:SPAC30D11.13; -.
DR eggNOG; KOG0424; Eukaryota.
DR HOGENOM; CLU_030988_12_0_1; -.
DR InParanoid; P40984; -.
DR OMA; QEPAWRA; -.
DR PhylomeDB; P40984; -.
DR Reactome; R-SPO-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-SPO-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-SPO-3232118; SUMOylation of transcription factors.
DR Reactome; R-SPO-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SPO-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SPO-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-SPO-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-SPO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SPO-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR UniPathway; UPA00886; -.
DR PRO; PR:P40984; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019948; F:SUMO activating enzyme activity; EXP:PomBase.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; IDA:PomBase.
DR GO; GO:0006281; P:DNA repair; IGI:PomBase.
DR GO; GO:0016925; P:protein sumoylation; IDA:PomBase.
DR GO; GO:1903379; P:regulation of mitotic chromosome condensation; IGI:PomBase.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 3.10.110.10; -; 1.
DR InterPro; IPR027230; Ubc9.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR24067:SF248; PTHR24067:SF248; 1.
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; DNA damage; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..157
FT /note="SUMO-conjugating enzyme ubc9"
FT /id="PRO_0000082568"
FT DOMAIN 4..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT ACT_SITE 93
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT ECO:0000255|PROSITE-ProRule:PRU10133"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:3RCZ"
FT STRAND 25..30
FT /evidence="ECO:0007829|PDB:3RCZ"
FT STRAND 34..46
FT /evidence="ECO:0007829|PDB:3RCZ"
FT TURN 52..55
FT /evidence="ECO:0007829|PDB:3RCZ"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3RCZ"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:3RCZ"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:3RCZ"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:3RCZ"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:3RCZ"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:3RCZ"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:3RCZ"
FT HELIX 131..139
FT /evidence="ECO:0007829|PDB:3RCZ"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:3RCZ"
SQ SEQUENCE 157 AA; 17989 MW; 4BF3A6389203D27F CRC64;
MSSLCKTRLQ EERKQWRRDH PFGFYAKPCK SSDGGLDLMN WKVGIPGKPK TSWEGGLYKL
TMAFPEEYPT RPPKCRFTPP LFHPNVYPSG TVCLSILNEE EGWKPAITIK QILLGIQDLL
DDPNIASPAQ TEAYTMFKKD KVEYEKRVRA QARENAP
