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UB2D1_BOVIN
ID   UB2D1_BOVIN             Reviewed;         147 AA.
AC   Q2TA10;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 117.
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-protein ligase D1;
GN   Name=UBE2D1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Liver;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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 ubiquitination of PEX5 and auto-
CC       ubiquitination of STUB1, TRAF6 and TRIM63/MURF1. Ubiquitinates STUB1-
CC       associated HSP90AB1 in vitro. Lacks inherent specificity for any
CC       particular lysine residue of ubiquitin. Essential for viral activation
CC       of IRF3. Mediates polyubiquitination of CYP3A4.
CC       {ECO:0000250|UniProtKB:P51668}.
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; BC111175; AAI11176.1; -; mRNA.
DR   RefSeq; NP_001033256.1; NM_001038167.1.
DR   AlphaFoldDB; Q2TA10; -.
DR   BMRB; Q2TA10; -.
DR   SMR; Q2TA10; -.
DR   STRING; 9913.ENSBTAP00000051358; -.
DR   PaxDb; Q2TA10; -.
DR   PRIDE; Q2TA10; -.
DR   Ensembl; ENSBTAT00000055368; ENSBTAP00000051358; ENSBTAG00000020796.
DR   GeneID; 535287; -.
DR   KEGG; bta:535287; -.
DR   CTD; 7321; -.
DR   VEuPathDB; HostDB:ENSBTAG00000020796; -.
DR   VGNC; VGNC:36579; UBE2D1.
DR   eggNOG; KOG0417; Eukaryota.
DR   GeneTree; ENSGT00940000155109; -.
DR   HOGENOM; CLU_030988_13_3_1; -.
DR   InParanoid; Q2TA10; -.
DR   OMA; FCELNRE; -.
DR   OrthoDB; 1337945at2759; -.
DR   TreeFam; TF101108; -.
DR   Reactome; R-BTA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR   Reactome; R-BTA-5689896; Ovarian tumor domain proteases.
DR   Reactome; R-BTA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-BTA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-BTA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR   Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 26.
DR   Bgee; ENSBTAG00000020796; Expressed in supraspinatus muscle and 103 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; 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; 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_0000245033"
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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