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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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