UBC9_CHICK
ID UBC9_CHICK Reviewed; 158 AA.
AC P63283; P50550; Q15698; Q547R1; Q86VB3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RX PubMed=12413887; DOI=10.1006/excr.2002.5634;
RA Hayashi T., Seki M., Maeda D., Wang W., Kawabe Y., Seki T., Saitoh H.,
RA Fukagawa T., Yagi H., Enomoto T.;
RT "Ubc9 is essential for viability of higher eukaryotic cells.";
RL Exp. Cell Res. 280:212-221(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Inner ear;
RA Venkataramu C.R., Sokolowski B.H.A.;
RT "Protein-protein interactions of Kvbeta.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH SOX9.
RX PubMed=23382206; DOI=10.1073/pnas.1211747110;
RA Liu J.A., Wu M.H., Yan C.H., Chau B.K., So H., Ng A., Chan A., Cheah K.S.,
RA Briscoe J., Cheung M.;
RT "Phosphorylation of Sox9 is required for neural crest delamination and is
RT regulated downstream of BMP and canonical Wnt signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2882-2887(2013).
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:12413887}.
CC -!- PATHWAY: Protein modification; protein sumoylation.
CC -!- SUBUNIT: Interacts with SOX9. {ECO:0000269|PubMed:23382206}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P63280}. Cytoplasm
CC {ECO:0000250|UniProtKB:P63280}.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR EMBL; AB069964; BAB68210.1; -; mRNA.
DR EMBL; AF461016; AAL85282.1; -; mRNA.
DR RefSeq; NP_989596.1; NM_204265.1.
DR RefSeq; XP_015149596.1; XM_015294110.1.
DR RefSeq; XP_015149597.1; XM_015294111.1.
DR RefSeq; XP_015149598.1; XM_015294112.1.
DR RefSeq; XP_015149599.1; XM_015294113.1.
DR RefSeq; XP_015149601.1; XM_015294115.1.
DR AlphaFoldDB; P63283; -.
DR BMRB; P63283; -.
DR SMR; P63283; -.
DR BioGRID; 675156; 1.
DR STRING; 9031.ENSGALP00000010363; -.
DR PaxDb; P63283; -.
DR Ensembl; ENSGALT00000010377; ENSGALP00000010363; ENSGALG00000006428.
DR GeneID; 374123; -.
DR KEGG; gga:374123; -.
DR CTD; 7329; -.
DR VEuPathDB; HostDB:geneid_374123; -.
DR eggNOG; KOG0424; Eukaryota.
DR GeneTree; ENSGT00550000075088; -.
DR HOGENOM; CLU_030988_12_0_1; -.
DR InParanoid; P63283; -.
DR OMA; QEPAWRA; -.
DR OrthoDB; 1522509at2759; -.
DR PhylomeDB; P63283; -.
DR Reactome; R-GGA-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-GGA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-GGA-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-GGA-3232118; SUMOylation of transcription factors.
DR Reactome; R-GGA-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-GGA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-GGA-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-GGA-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-GGA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-GGA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-GGA-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-GGA-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-GGA-4755510; SUMOylation of immune response proteins.
DR Reactome; R-GGA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-GGA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-GGA-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-GGA-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR UniPathway; UPA00886; -.
DR PRO; PR:P63283; -.
DR Proteomes; UP000000539; Chromosome 14.
DR Bgee; ENSGALG00000006428; Expressed in spermatid and 12 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0016605; C:PML body; IEA:Ensembl.
DR GO; GO:0106068; C:SUMO ligase complex; IEA:Ensembl.
DR GO; GO:1990356; C:sumoylated E2 ligase complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043398; F:HLH domain binding; IEA:Ensembl.
DR GO; GO:0071535; F:RING-like zinc finger domain binding; IEA:Ensembl.
DR GO; GO:0044388; F:small protein activating enzyme binding; IEA:Ensembl.
DR GO; GO:0061656; F:SUMO conjugating enzyme activity; IBA:GO_Central.
DR GO; GO:0001221; F:transcription coregulator binding; IEA:Ensembl.
DR GO; GO:0008134; F:transcription factor binding; IPI:AgBase.
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:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:1903755; P:positive regulation of SUMO transferase activity; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; 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 ATP-binding; Cell cycle; Cell division; Chromosome partition; Cytoplasm;
KW Mitosis; Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..158
FT /note="SUMO-conjugating enzyme UBC9"
FT /id="PRO_0000082459"
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; 18007 MW; E2C826E9C8D0683D CRC64;
MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL
RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS
