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UB2G1_RAT
ID   UB2G1_RAT               Reviewed;         170 AA.
AC   P62255; Q99462;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 G1;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme G1;
DE   AltName: Full=E217K;
DE   AltName: Full=UBC7;
DE   AltName: Full=Ubiquitin carrier protein G1;
DE   AltName: Full=Ubiquitin-protein ligase G1;
DE   Contains:
DE     RecName: Full=Ubiquitin-conjugating enzyme E2 G1, N-terminally processed;
GN   Name=Ube2g1; Synonyms=Ubc7, Ube2g;
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.
RX   PubMed=10329663; DOI=10.1074/jbc.274.21.14685;
RA   Lin H., Wing S.S.;
RT   "Identification of rabbit reticulocyte E217K as a UBC7 homologue and
RT   functional characterization of its core domain loop.";
RL   J. Biol. Chem. 274:14685-14691(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
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: Accepts ubiquitin from the E1 complex and catalyzes its
CC       covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-, as
CC       well as 'Lys-63'-linked polyubiquitination. May be involved in
CC       degradation of muscle-specific proteins. Mediates polyubiquitination of
CC       CYP3A4. {ECO:0000250|UniProtKB:P62253}.
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:P62253, ECO:0000255|PROSITE-
CC         ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- TISSUE SPECIFICITY: Widely expressed, with higher level in testis.
CC       {ECO:0000269|PubMed:10329663}.
CC   -!- DEVELOPMENTAL STAGE: Induced from days 15 to 30.
CC   -!- PTM: Autoubiquitinated. {ECO:0000250|UniProtKB:P62253}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AF099093; AAC69605.1; -; mRNA.
DR   EMBL; BC086980; AAH86980.1; -; mRNA.
DR   RefSeq; NP_073181.1; NM_022690.2.
DR   AlphaFoldDB; P62255; -.
DR   SMR; P62255; -.
DR   IntAct; P62255; 1.
DR   STRING; 10116.ENSRNOP00000013486; -.
DR   PhosphoSitePlus; P62255; -.
DR   jPOST; P62255; -.
DR   PaxDb; P62255; -.
DR   PRIDE; P62255; -.
DR   Ensembl; ENSRNOT00000013486; ENSRNOP00000013486; ENSRNOG00000010041.
DR   GeneID; 64631; -.
DR   KEGG; rno:64631; -.
DR   CTD; 7326; -.
DR   RGD; 620392; Ube2g1.
DR   eggNOG; KOG0425; Eukaryota.
DR   GeneTree; ENSGT00940000155228; -.
DR   HOGENOM; CLU_030988_10_1_1; -.
DR   InParanoid; P62255; -.
DR   OMA; GFFKCHL; -.
DR   OrthoDB; 1317014at2759; -.
DR   PhylomeDB; P62255; -.
DR   TreeFam; TF101118; -.
DR   Reactome; R-RNO-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-RNO-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:P62255; -.
DR   Proteomes; UP000002494; Chromosome 10.
DR   Bgee; ENSRNOG00000010041; Expressed in quadriceps femoris and 20 other tissues.
DR   Genevisible; P62255; RN.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; ISO:RGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:RGD.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; TAS:RGD.
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   Acetylation; ATP-binding; Nucleotide-binding; Reference proteome;
KW   Transferase; Ubl conjugation; Ubl conjugation pathway.
FT   CHAIN           1..170
FT                   /note="Ubiquitin-conjugating enzyme E2 G1"
FT                   /id="PRO_0000424517"
FT   INIT_MET        1
FT                   /note="Removed; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62253"
FT   CHAIN           2..170
FT                   /note="Ubiquitin-conjugating enzyme E2 G1, N-terminally
FT                   processed"
FT                   /id="PRO_0000082482"
FT   DOMAIN          5..166
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        90
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P62253"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine; in Ubiquitin-conjugating enzyme
FT                   E2 G1, N-terminally processed"
FT                   /evidence="ECO:0000250|UniProtKB:P62253"
SQ   SEQUENCE   170 AA;  19509 MW;  36B61766D995B332 CRC64;
     MTELQSALLL RRQLAELNKN PVEGFSAGLI DDNDLYRWEV LIIGPPDTLY EGGVFKAHLT
     FPKDYPLRPP KMKFITEIWH PNVDKNGDVC ISILHEPGED KYGYEKPEER WLPIHTVETI
     MISVISMLAD PNGDSPANVD AAKEWREDRN GEFKRKVARC VRKSQETAFE
 
 
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