UBC9A_DANRE
ID UBC9A_DANRE Reviewed; 158 AA.
AC Q9W6H5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=SUMO-conjugating enzyme UBC9-A;
DE EC=2.3.2.-;
DE AltName: Full=RING-type E3 SUMO transferase UBC9-A;
DE AltName: Full=SUMO-protein ligase A;
DE AltName: Full=Ubiquitin carrier protein 9-A;
DE AltName: Full=Ubiquitin carrier protein I-A;
DE AltName: Full=Ubiquitin-conjugating enzyme E2 I-A;
DE AltName: Full=Ubiquitin-protein ligase I-A;
GN Name=ube2ia; Synonyms=ubc9a, ube2i;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH VSX1, AND FUNCTION.
RX PubMed=11331779; DOI=10.1073/pnas.101129698;
RA Kurtzman A.L., Schechter N.;
RT "Ubc9 interacts with a nuclear localization signal and mediates nuclear
RT localization of the paired-like homeobox protein Vsx-1 independent of SUMO-
RT 1 modification.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:5602-5607(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=17035631; DOI=10.1091/mbc.e06-05-0413;
RA Nowak M., Hammerschmidt M.;
RT "Ubc9 regulates mitosis and cell survival during Zebrafish development.";
RL Mol. Biol. Cell 17:5324-5336(2006).
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 (By similarity). Mediates nuclear localization of vsx1.
CC Required for progression through mitosis during organogenesis.
CC {ECO:0000250, ECO:0000269|PubMed:11331779,
CC ECO:0000269|PubMed:17035631}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Forms a tight complex with rangap1 and ranbp2 (By similarity).
CC Interacts with vsx1. {ECO:0000250, ECO:0000269|PubMed:11331779}.
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; AF128240; AAD28601.1; -; mRNA.
DR EMBL; BC059506; AAH59506.1; -; mRNA.
DR RefSeq; NP_571426.1; NM_131351.2.
DR RefSeq; XP_005174251.1; XM_005174194.3.
DR AlphaFoldDB; Q9W6H5; -.
DR SMR; Q9W6H5; -.
DR STRING; 7955.ENSDARP00000011487; -.
DR PaxDb; Q9W6H5; -.
DR DNASU; 30622; -.
DR Ensembl; ENSDART00000022999; ENSDARP00000011487; ENSDARG00000007438.
DR GeneID; 30622; -.
DR KEGG; dre:30622; -.
DR CTD; 30622; -.
DR ZFIN; ZDB-GENE-990614-17; ube2ib.
DR eggNOG; KOG0424; Eukaryota.
DR GeneTree; ENSGT00550000075088; -.
DR InParanoid; Q9W6H5; -.
DR OMA; KWICKVP; -.
DR OrthoDB; 1522509at2759; -.
DR PhylomeDB; Q9W6H5; -.
DR TreeFam; TF101122; -.
DR Reactome; R-DRE-196791; Vitamin D (calciferol) metabolism.
DR Reactome; R-DRE-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DRE-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-DRE-3232118; SUMOylation of transcription factors.
DR Reactome; R-DRE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-DRE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DRE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-DRE-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-DRE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DRE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DRE-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-DRE-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-DRE-4755510; SUMOylation of immune response proteins.
DR Reactome; R-DRE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-DRE-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-DRE-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DRE-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-DRE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR UniPathway; UPA00886; -.
DR PRO; PR:Q9W6H5; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 24.
DR Bgee; ENSDARG00000007438; Expressed in mature ovarian follicle and 38 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0019789; F:SUMO transferase activity; IDA:ZFIN.
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:0060216; P:definitive hemopoiesis; IGI:ZFIN.
DR GO; GO:0036306; P:embryonic heart tube elongation; IGI:ZFIN.
DR GO; GO:0001947; P:heart looping; IGI:ZFIN.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IMP:ZFIN.
DR GO; GO:0016925; P:protein sumoylation; IDA:ZFIN.
DR GO; GO:0031099; P:regeneration; IMP:ZFIN.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:ZFIN.
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 Developmental protein; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Ubl conjugation pathway.
FT CHAIN 1..158
FT /note="SUMO-conjugating enzyme UBC9-A"
FT /id="PRO_0000268876"
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 ECO:0000255|PROSITE-ProRule:PRU10133"
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"
SQ SEQUENCE 158 AA; 18053 MW; CFC0339EF8D0682A CRC64;
MSGIALSRLA QERKAWRKDH PFGFVAVPMK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFSPS
