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UB2D1_RAT
ID   UB2D1_RAT               Reviewed;         147 AA.
AC   D3ZDK2;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 D1;
DE            EC=2.3.2.23;
DE   AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme D1;
DE            EC=2.3.2.24;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme D1;
DE   AltName: Full=Ubiquitin carrier protein D1;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2(17)KB 1;
DE   AltName: Full=Ubiquitin-conjugating enzyme E2-17 kDa 1;
DE   AltName: Full=Ubiquitin-protein ligase D1;
GN   Name=Ube2d1;
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 [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=18359941; DOI=10.1074/jbc.m800402200;
RA   Grou C.P., Carvalho A.F., Pinto M.P., Wiese S., Piechura H., Meyer H.E.,
RA   Warscheid B., Sa-Miranda C., Azevedo J.E.;
RT   "Members of the E2D (UbcH5) family mediate the ubiquitination of the
RT   conserved cysteine of Pex5p, the peroxisomal import receptor.";
RL   J. Biol. Chem. 283:14190-14197(2008).
CC   -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-
CC       linked polyubiquitination. Mediates the selective degradation of short-
CC       lived and abnormal proteins. Functions in the E6/E6-AP-induced
CC       ubiquitination of p53/TP53. Mediates auto-ubiquitination of STUB1,
CC       TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-associated HSP90AB1 in
CC       vitro. Lacks inherent specificity for any particular lysine residue of
CC       ubiquitin. Essential for viral activation of IRF3. Mediates
CC       polyubiquitination of CYP3A4 (By similarity). Mediates ubiquitination
CC       of PEX5. {ECO:0000250|UniProtKB:P51668, ECO:0000269|PubMed:18359941}.
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:P51668, ECO:0000255|PROSITE-
CC         ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E1 ubiquitin-activating enzyme]-L-
CC         cysteine + N(6)-monoubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.24; Evidence={ECO:0000250|UniProtKB:P51668};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Component of a E3 ubiquitin ligase complex containing UBE2D1,
CC       SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts with RNF11.
CC       {ECO:0000250|UniProtKB:P51668}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P51668}.
CC   -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P51668}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; CH473988; EDL97256.1; -; Genomic_DNA.
DR   RefSeq; NP_001102000.1; NM_001108530.1.
DR   AlphaFoldDB; D3ZDK2; -.
DR   BMRB; D3ZDK2; -.
DR   SMR; D3ZDK2; -.
DR   BioGRID; 262993; 1.
DR   STRING; 10116.ENSRNOP00000000750; -.
DR   PeptideAtlas; D3ZDK2; -.
DR   PRIDE; D3ZDK2; -.
DR   Ensembl; ENSRNOT00000000750; ENSRNOP00000000750; ENSRNOG00000000611.
DR   GeneID; 361831; -.
DR   KEGG; rno:361831; -.
DR   UCSC; RGD:1307886; rat.
DR   CTD; 7321; -.
DR   RGD; 1307886; Ube2d1.
DR   eggNOG; KOG0417; Eukaryota.
DR   GeneTree; ENSGT00940000155109; -.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; D3ZDK2; -.
DR   OMA; FCELNRE; -.
DR   OrthoDB; 1337945at2759; -.
DR   PhylomeDB; D3ZDK2; -.
DR   TreeFam; TF101108; -.
DR   Reactome; R-RNO-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-RNO-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-RNO-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-RNO-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-RNO-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-RNO-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-RNO-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-RNO-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-RNO-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-RNO-176412; Phosphorylation of the APC/C.
DR   Reactome; R-RNO-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-RNO-201451; Signaling by BMP.
DR   Reactome; R-RNO-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR   Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR   Reactome; R-RNO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-RNO-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-RNO-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-RNO-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-RNO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-RNO-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-RNO-8951664; Neddylation.
DR   Reactome; R-RNO-9033241; Peroxisomal protein import.
DR   Reactome; R-RNO-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:D3ZDK2; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Proteomes; UP000234681; Chromosome 20.
DR   Bgee; ENSRNOG00000000611; Expressed in quadriceps femoris and 20 other tissues.
DR   Genevisible; D3ZDK2; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR   GO; GO:0000151; C:ubiquitin ligase complex; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:RGD.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:RGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:1902916; P:positive regulation of protein polyubiquitination; ISO:RGD.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISO:RGD.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; ISO:RGD.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; 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; Cytoplasm; Nucleotide-binding; Reference proteome;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..147
FT                   /note="Ubiquitin-conjugating enzyme E2 D1"
FT                   /id="PRO_0000396006"
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;  16602 MW;  2E96FD0179EE119D CRC64;
     MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF FLTVHFPTDY
     PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV
     PDIAQIYKSD KEKYNRHARE WTQKYAM
 
 
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