ID   UB2G2_BOVIN             Reviewed;         165 AA.
AC   Q17QG5;
DT   14-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Ubiquitin-conjugating enzyme E2 G2;
DE            EC=2.3.2.23;
DE   AltName: Full=E2 ubiquitin-conjugating enzyme G2;
DE   AltName: Full=Ubiquitin carrier protein G2;
DE   AltName: Full=Ubiquitin-protein ligase G2;
GN   Name=UBE2G2 {ECO:0000250|UniProtKB:P60604};
GN   Synonyms=UBC7 {ECO:0000250|UniProtKB:P60604};
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].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Fetal pons;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) 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. Involved in endoplasmic reticulum-associated
CC       degradation (ERAD). Required for sterol-induced ubiquitination of 3-
CC       hydroxy-3-methylglutaryl coenzyme A reductase and its subsequent
CC       proteasomal degradation. {ECO:0000250|UniProtKB:P60604}.
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:P60604, ECO:0000255|PROSITE-
CC         ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- SUBUNIT: Interacts with AUP1 (via C-terminus); the interaction recruits
CC       UBE2G2 to lipid droplets. Interacts with ubiquitin ligases AMFR/gp78
CC       and RNF139/TRC8; recruitment to lipid droplets by AUP1 facilitates
CC       interaction of UBE2G2 with AMFR and RNF139, leading to sterol-induced
CC       ubiquitination of 3-hydroxy-3-methylglutaryl coenzyme A reductase and
CC       its subsequent proteasomal degradation. {ECO:0000250|UniProtKB:P60604}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P60605}. Lipid droplet
CC       {ECO:0000250|UniProtKB:P60604}.
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; BT026143; ABG66982.1; -; mRNA.
DR   EMBL; BC118376; AAI18377.1; -; mRNA.
DR   RefSeq; NP_001069796.1; NM_001076328.1.
DR   AlphaFoldDB; Q17QG5; -.
DR   BMRB; Q17QG5; -.
DR   SMR; Q17QG5; -.
DR   STRING; 9913.ENSBTAP00000055782; -.
DR   PaxDb; 9913-ENSBTAP00000055782; -.
DR   Ensembl; ENSBTAT00000063929.2; ENSBTAP00000055782.2; ENSBTAG00000048090.2.
DR   GeneID; 614471; -.
DR   KEGG; bta:614471; -.
DR   CTD; 7327; -.
DR   VEuPathDB; HostDB:ENSBTAG00000048090; -.
DR   VGNC; VGNC:36582; UBE2G2.
DR   eggNOG; KOG0426; Eukaryota.
DR   GeneTree; ENSGT00940000158193; -.
DR   HOGENOM; CLU_030988_10_1_1; -.
DR   InParanoid; Q17QG5; -.
DR   OMA; NIDACKM; -.
DR   Reactome; R-BTA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-BTA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000009136; Chromosome 1.
DR   Bgee; ENSBTAG00000048090; Expressed in vas deferens and 107 other cell types or tissues.
DR   ExpressionAtlas; Q17QG5; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
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:0035458; P:cellular response to interferon-beta; IEA:Ensembl.
DR   GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; IEA:Ensembl.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; 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:SF154; UBIQUITIN-CONJUGATING ENZYME E2 G2; 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; Endoplasmic reticulum; Lipid droplet;
KW   Nucleotide-binding; Reference proteome; Transferase;
KW   Ubl conjugation pathway.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P60604"
FT   CHAIN           2..165
FT                   /note="Ubiquitin-conjugating enzyme E2 G2"
FT                   /id="PRO_0000259961"
FT   DOMAIN          4..164
FT                   /note="UBC core"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388"
FT   ACT_SITE        89
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00388,
FT                   ECO:0000255|PROSITE-ProRule:PRU10133"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P60604"
SQ   SEQUENCE   165 AA;  18552 MW;  74DEC72A049575E3 CRC64;
     MAGTALKRLM AEYKQLTLNP PEGIVAGPMN EENFFEWEAL IMGPEDTCFE FGVFPAILSF
     PLDYPLSPPK MRFTCEMFHP NIYPDGRVCI SILHAPGDDP MGYESSAERW SPVQSVEKIL
     LSVVSMLAEP NDESGANVDA SKMWRDDREQ FYKVAKQIVQ KSLGL
//