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U2D2B_RAT
ID   U2D2B_RAT               Reviewed;         147 AA.
AC   P70711;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 D2B;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme D2B;
DE   AltName: Full=Ubiquitin carrier protein D2B;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2(17)KB 2B;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 2B;
DE   AltName: Full=Ubiquitin-protein ligase D2B;
GN   Name=Ube2d2b; Synonyms=Ube2d2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Testis;
RX   PubMed=8754804; DOI=10.1128/mcb.16.8.4064;
RA   Wing S.S., Bedard N., Morales C., Hingamp P., Trasler J.;
RT   "A novel rat homolog of the Saccharomyces cerevisiae ubiquitin-conjugating
RT   enzymes UBC4 and UBC5 with distinct biochemical features is induced during
RT   spermatogenesis.";
RL   Mol. Cell. Biol. 16:4064-4072(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Catalyzes the covalent attachment of ubiquitin to other
CC       proteins. Mediates the selective degradation of short-lived and
CC       abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of
CC       p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of
CC       STUB1 and TRAF6. Involved in the signal-induced conjugation and
CC       subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination
CC       and degradation, MDM2-dependent degradation of p53/TP53 and the
CC       activation of MAVS in the mitochondria by DDX58/RIG-I in response to
CC       viral infection Plays a role in early maturation of the testis.
CC       {ECO:0000250|UniProtKB:P62837, ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-
CC         activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-
CC         conjugating enzyme]-L-cysteine.; EC=2.3.2.23;
CC         Evidence={ECO:0000250|UniProtKB:P62837, ECO:0000255|PROSITE-
CC         ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with CNOT4 (via RING domain).
CC       {ECO:0000250|UniProtKB:P62837}.
CC   -!- TISSUE SPECIFICITY: Testis-specific. Mainly expressed in the round
CC       spermatids (at protein level). {ECO:0000269|PubMed:8754804}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; U56407; AAC52942.1; -; mRNA.
DR   EMBL; BC078808; AAH78808.1; -; mRNA.
DR   RefSeq; NP_112263.1; NM_031001.2.
DR   AlphaFoldDB; P70711; -.
DR   SMR; P70711; -.
DR   STRING; 10116.ENSRNOP00000039621; -.
DR   iPTMnet; P70711; -.
DR   PhosphoSitePlus; P70711; -.
DR   PaxDb; P70711; -.
DR   GeneID; 79435; -.
DR   KEGG; rno:79435; -.
DR   UCSC; RGD:69425; rat.
DR   CTD; 73318; -.
DR   RGD; 69425; RGD69425.
DR   eggNOG; KOG0417; Eukaryota.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; P70711; -.
DR   OMA; ISEANMY; -.
DR   OrthoDB; 1337945at2759; -.
DR   PhylomeDB; P70711; -.
DR   TreeFam; TF101108; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P70711; -.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000034016; Expressed in testis and 2 other tissues.
DR   Genevisible; P70711; RN.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:RGD.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISO:RGD.
DR   GO; GO:1903841; P:cellular response to arsenite(3-); IEP:RGD.
DR   GO; GO:0071276; P:cellular response to cadmium ion; IEP:RGD.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; ISO:RGD.
DR   GO; GO:0044314; P:protein K27-linked ubiquitination; ISO:RGD.
DR   GO; GO:0035519; P:protein K29-linked ubiquitination; ISO:RGD.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISO:RGD.
DR   GO; GO:0085020; P:protein K6-linked ubiquitination; ISO:RGD.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISO:RGD.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; ISO:RGD.
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; Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   CHAIN           1..147
FT                   /note="Ubiquitin-conjugating enzyme E2 D2B"
FT                   /id="PRO_0000082469"
FT   DOMAIN          1..147
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        85
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
SQ   SEQUENCE   147 AA;  16659 MW;  E950720AEC2AB2B2 CRC64;
     MALKRIHKEL NDLAQDPPAQ CSAGPVGEDM FHWQATIMGP NDSPYQGGAF FLTIDFPTEY
     PFKPPKVEFT TRIYHPNVNS NGSICLDILR SQWSPALTIS KVLLSISSLL CDPNPDDPLV
     PEIAQIYKTD RDKYNRTARE WTQKYAM
 
 
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