UBC9_XENLA
ID UBC9_XENLA Reviewed; 158 AA.
AC P63282; P50550; Q15698; Q5D0B2; Q86VB3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=SUMO-conjugating enzyme UBC9;
DE EC=2.3.2.-;
DE AltName: Full=RING-type E3 SUMO transferase UBC9;
DE AltName: Full=SUMO-protein ligase;
DE AltName: Full=Ubiquitin carrier protein 9;
DE AltName: Full=Ubiquitin carrier protein I;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 I;
DE AltName: Full=Ubiquitin-protein ligase I;
GN Name=ube2i; Synonyms=ubc9, ubce9;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-28 AND 60-64, AND
RP INTERACTION WITH RANBP2 AND RANGAP1.
RC TISSUE=Oocyte;
RX PubMed=9108047; DOI=10.1073/pnas.94.8.3736;
RA Saitoh H., Pu R., Cavenagh M., Dasso M.;
RT "RanBP2 associates with Ubc9p and a modified form of RanGAP1.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:3736-3741(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND MUTAGENESIS OF CYS-93.
RX PubMed=9427648; DOI=10.1016/s0960-9822(98)70044-2;
RA Saitoh H., Sparrow D.B., Shiomi T., Pu R.T., Nishimoto T., Mohun T.J.,
RA Dasso M.;
RT "Ubc9p and the conjugation of SUMO-1 to RanGAP1 and RanBP2.";
RL Curr. Biol. 8:121-124(1998).
RN [4]
RP FUNCTION.
RX PubMed=14597774; DOI=10.1083/jcb.200304088;
RA Azuma Y., Arnaoutov A., Dasso M.;
RT "SUMO-2/3 regulates topoisomerase II in mitosis.";
RL J. Cell Biol. 163:477-487(2003).
RN [5]
RP INTERACTION WITH SOX9 AND SOX10.
RX PubMed=16256735; DOI=10.1016/j.devcel.2005.09.016;
RA Taylor K.M., Labonne C.;
RT "SoxE factors function equivalently during neural crest and inner ear
RT development and their activity is regulated by SUMOylation.";
RL Dev. Cell 9:593-603(2005).
CC -!- FUNCTION: Accepts the ubiquitin-like proteins sumo1, sumo2 and sumo3
CC from the uble1a-uble1b E1 complex and catalyzes their covalent
CC attachment to other proteins with the help of an E3 ligase such as
CC ranbp2 or cbx4. Essential for nuclear architecture and chromosome
CC segregation. {ECO:0000269|PubMed:14597774, ECO:0000269|PubMed:9427648}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Forms a tight complex with rangap1 and ranbp2. Interacts with
CC sox9 and sox10. {ECO:0000269|PubMed:16256735,
CC ECO:0000269|PubMed:9108047}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; U88561; AAB57736.1; -; mRNA.
DR EMBL; BC046273; AAH46273.1; -; mRNA.
DR RefSeq; NP_001080758.1; NM_001087289.1.
DR RefSeq; XP_018094631.1; XM_018239142.1.
DR RefSeq; XP_018094632.1; XM_018239143.1.
DR AlphaFoldDB; P63282; -.
DR BMRB; P63282; -.
DR SMR; P63282; -.
DR BioGRID; 98692; 4.
DR MaxQB; P63282; -.
DR DNASU; 380450; -.
DR GeneID; 108703134; -.
DR GeneID; 380450; -.
DR KEGG; xla:108703134; -.
DR KEGG; xla:380450; -.
DR CTD; 108703134; -.
DR CTD; 380450; -.
DR Xenbase; XB-GENE-974023; ube2i.L.
DR Xenbase; XB-GENE-17341858; ube2i.S.
DR OrthoDB; 1522509at2759; -.
DR UniPathway; UPA00886; -.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 108703134; Expressed in egg cell and 19 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
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; Cell cycle; Cell division; Chromosome partition;
KW Direct protein sequencing; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..158
FT /note="SUMO-conjugating enzyme UBC9"
FT /id="PRO_0000082458"
FT DOMAIN 4..157
FT /note="UBC core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT REGION 13..18
FT /note="Interaction with sumo1"
FT /evidence="ECO:0000250"
FT ACT_SITE 93
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT SITE 4
FT /note="Interaction with ranbp2"
FT /evidence="ECO:0000250"
FT SITE 25
FT /note="Interaction with ranbp2"
FT /evidence="ECO:0000250"
FT SITE 57
FT /note="Interaction with ranbp2"
FT /evidence="ECO:0000250"
FT SITE 100..101
FT /note="Substrate binding"
FT /evidence="ECO:0000250"
FT MUTAGEN 93
FT /note="C->A: Abolishes enzymatic activity."
FT /evidence="ECO:0000269|PubMed:9427648"
SQ SEQUENCE 158 AA; 18007 MW; E2C826E9C8D0683D CRC64;
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS
