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UBC9_XENTR
ID   UBC9_XENTR              Reviewed;         158 AA.
AC   Q28CQ4;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, 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; ORFNames=TEgg019l14.1, TEgg096h05.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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:0000250}.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC   -!- SUBUNIT: Forms a tight complex with rangap1 and ranbp2. Interacts with
CC       sox9 and sox10 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CR761123; CAJ81669.1; -; mRNA.
DR   EMBL; CR926257; CAJ81434.1; -; mRNA.
DR   RefSeq; NP_001016408.1; NM_001016408.2.
DR   RefSeq; XP_012825871.1; XM_012970417.2.
DR   RefSeq; XP_012825872.1; XM_012970418.2.
DR   RefSeq; XP_012825873.1; XM_012970419.2.
DR   AlphaFoldDB; Q28CQ4; -.
DR   SMR; Q28CQ4; -.
DR   STRING; 8364.ENSXETP00000054232; -.
DR   PaxDb; Q28CQ4; -.
DR   GeneID; 549162; -.
DR   KEGG; xtr:549162; -.
DR   CTD; 7329; -.
DR   Xenbase; XB-GENE-974017; ube2i.
DR   eggNOG; KOG0424; Eukaryota.
DR   HOGENOM; CLU_030988_12_0_1; -.
DR   InParanoid; Q28CQ4; -.
DR   OrthoDB; 1522509at2759; -.
DR   PhylomeDB; Q28CQ4; -.
DR   Reactome; R-XTR-196791; Vitamin D (calciferol) metabolism.
DR   Reactome; R-XTR-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR   Reactome; R-XTR-3108214; SUMOylation of DNA damage response and repair proteins.
DR   Reactome; R-XTR-3108232; SUMO E3 ligases SUMOylate target proteins.
DR   Reactome; R-XTR-3232118; SUMOylation of transcription factors.
DR   Reactome; R-XTR-3232142; SUMOylation of ubiquitinylation proteins.
DR   Reactome; R-XTR-3899300; SUMOylation of transcription cofactors.
DR   Reactome; R-XTR-4085377; SUMOylation of SUMOylation proteins.
DR   Reactome; R-XTR-4090294; SUMOylation of intracellular receptors.
DR   Reactome; R-XTR-4551638; SUMOylation of chromatin organization proteins.
DR   Reactome; R-XTR-4570464; SUMOylation of RNA binding proteins.
DR   Reactome; R-XTR-4615885; SUMOylation of DNA replication proteins.
DR   Reactome; R-XTR-4655427; SUMOylation of DNA methylation proteins.
DR   Reactome; R-XTR-4755510; SUMOylation of immune response proteins.
DR   Reactome; R-XTR-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-XTR-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000008143; Chromosome 9.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000004027; Expressed in ovary and 15 other tissues.
DR   ExpressionAtlas; Q28CQ4; baseline.
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: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; 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   2: Evidence at transcript level;
KW   ATP-binding; Cell cycle; Cell division; Chromosome partition; Mitosis;
KW   Nucleotide-binding; Nucleus; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..158
FT                   /note="SUMO-conjugating enzyme UBC9"
FT                   /id="PRO_0000269463"
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
 
 
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