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UBC9B_DANRE
ID   UBC9B_DANRE             Reviewed;         157 AA.
AC   Q9DDJ0;
DT   12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=SUMO-conjugating enzyme UBC9-B;
DE            EC=2.3.2.-;
DE   AltName: Full=RING-type E3 SUMO transferase UBC9-B;
DE   AltName: Full=SUMO-protein ligase B;
DE   AltName: Full=Ubiquitin carrier protein 9-B;
DE   AltName: Full=Ubiquitin carrier protein I-B;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2 I-B;
DE   AltName: Full=Ubiquitin-protein ligase I-B;
GN   Name=ube2ib; Synonyms=ubc9b, ube2i2;
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=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (FEB-2004) 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; AF332623; AAG48365.1; -; mRNA.
DR   EMBL; BC066609; AAH66609.1; -; mRNA.
DR   EMBL; BC058302; AAH58302.1; -; mRNA.
DR   RefSeq; NP_571908.1; NM_131833.2.
DR   AlphaFoldDB; Q9DDJ0; -.
DR   SMR; Q9DDJ0; -.
DR   STRING; 7955.ENSDARP00000052745; -.
DR   PaxDb; Q9DDJ0; -.
DR   Ensembl; ENSDART00000052746; ENSDARP00000052745; ENSDARG00000052649.
DR   Ensembl; ENSDART00000187282; ENSDARP00000151619; ENSDARG00000052649.
DR   GeneID; 114445; -.
DR   KEGG; dre:114445; -.
DR   CTD; 114445; -.
DR   ZFIN; ZDB-GENE-010607-1; ube2ia.
DR   eggNOG; KOG0424; Eukaryota.
DR   GeneTree; ENSGT00550000075088; -.
DR   InParanoid; Q9DDJ0; -.
DR   OMA; QEPAWRA; -.
DR   OrthoDB; 1522509at2759; -.
DR   PhylomeDB; Q9DDJ0; -.
DR   TreeFam; TF101122; -.
DR   UniPathway; UPA00886; -.
DR   PRO; PR:Q9DDJ0; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 3.
DR   Bgee; ENSDARG00000052649; Expressed in early embryo and 27 other tissues.
DR   ExpressionAtlas; Q9DDJ0; 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: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: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;
KW   Developmental protein; Mitosis; Nucleotide-binding; Nucleus;
KW   Reference proteome; Transferase; Ubl conjugation pathway.
FT   CHAIN           1..157
FT                   /note="SUMO-conjugating enzyme UBC9-B"
FT                   /id="PRO_0000268877"
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   157 AA;  17936 MW;  F83E89C8D0683DFA CRC64;
     MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL
     RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL
     NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFSP
 
 
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