UB2G1_MACFA
ID UB2G1_MACFA Reviewed; 170 AA.
AC Q4R5Y8;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=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; ORFNames=QtsA-19729;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-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'-, 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 -!- 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; AB169404; BAE01487.1; -; mRNA.
DR RefSeq; NP_001270329.1; NM_001283400.1.
DR AlphaFoldDB; Q4R5Y8; -.
DR SMR; Q4R5Y8; -.
DR STRING; 9541.XP_005582616.1; -.
DR GeneID; 101867309; -.
DR CTD; 7326; -.
DR eggNOG; KOG0425; Eukaryota.
DR OrthoDB; 1317014at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB.
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_0000424515"
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_0000281858"
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; 19437 MW; 35D57766D997B132 CRC64;
MTELQSALLL RRQLAELNKN PVEGFSAGLI DDNDLYRWEV LIIGPPDTLY EGGVFKAHLT
FPKDYPLRPP KMKFITEIWH PNVDKNGDVC ISILHEPGED KYGYEKPEGR WLPIHTVETI
MISVISMLAD PNGDSPANVD AAKEWREDRN GEFKRKVARC VRKSQETAFE
