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   24-JAN-2024, entry version 79.
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.ENSMFAP00000005086; -.
DR   eggNOG; KOG0425; Eukaryota.
DR   OrthoDB; 149628at2759; -.
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; Ubiquitin Conjugating Enzyme; 1.
DR   InterPro; IPR000608; UBQ-conjugat_E2.
DR   InterPro; IPR023313; UBQ-conjugating_AS.
DR   InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR   PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR   PANTHER; PTHR24067:SF3; UBIQUITIN-CONJUGATING ENZYME E2 G1; 1.
DR   Pfam; PF00179; UQ_con; 1.
DR   SMART; SM00212; UBCc; 1.
DR   SUPFAM; SSF54495; UBC-like; 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
//