ID   UB2G2_MOUSE             Reviewed;         165 AA.
AC   P60605; P56554;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 1.
DT   27-MAR-2024, entry version 155.
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:0000312|MGI:MGI:1343188};
GN   Synonyms=Ubc7 {ECO:0000250|UniProtKB:P60604};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC   STRAIN=C57BL/6J; TISSUE=Fetus;
RX   PubMed=11278356; DOI=10.1074/jbc.m007640200;
RA   Tiwari S., Weissman A.M.;
RT   "Endoplasmic reticulum (ER)-associated degradation of T cell receptor
RT   subunits. Involvement of ER-associated ubiquitin-conjugating enzymes
RT   (E2s).";
RL   J. Biol. Chem. 276:16193-16200(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Liver, Pancreas, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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   -!- INTERACTION:
CC       P60605; P60605: Ube2g2; NbExp=13; IntAct=EBI-9108745, EBI-9108745;
CC       P60605; Q9UKV5: AMFR; Xeno; NbExp=10; IntAct=EBI-9108745, EBI-1046367;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:11278356}. Lipid droplet
CC       {ECO:0000250|UniProtKB:P60604}.
CC   -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
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DR   EMBL; AF296657; AAK52608.1; -; mRNA.
DR   EMBL; BC010321; AAH10321.1; -; mRNA.
DR   CCDS; CCDS56722.1; -.
DR   RefSeq; NP_062777.2; NM_019803.3.
DR   PDB; 3FSH; X-ray; 2.76 A; A/B=1-165.
DR   PDBsum; 3FSH; -.
DR   AlphaFoldDB; P60605; -.
DR   BMRB; P60605; -.
DR   SMR; P60605; -.
DR   BioGRID; 204416; 14.
DR   DIP; DIP-29061N; -.
DR   IntAct; P60605; 1.
DR   MINT; P60605; -.
DR   STRING; 10090.ENSMUSP00000133515; -.
DR   iPTMnet; P60605; -.
DR   PhosphoSitePlus; P60605; -.
DR   SwissPalm; P60605; -.
DR   EPD; P60605; -.
DR   PaxDb; 10090-ENSMUSP00000133515; -.
DR   PeptideAtlas; P60605; -.
DR   ProteomicsDB; 298164; -.
DR   Pumba; P60605; -.
DR   Antibodypedia; 1148; 469 antibodies from 32 providers.
DR   DNASU; 22213; -.
DR   Ensembl; ENSMUST00000174510.8; ENSMUSP00000133515.2; ENSMUSG00000009293.18.
DR   GeneID; 22213; -.
DR   KEGG; mmu:22213; -.
DR   UCSC; uc007fwa.1; mouse.
DR   AGR; MGI:1343188; -.
DR   CTD; 7327; -.
DR   MGI; MGI:1343188; Ube2g2.
DR   VEuPathDB; HostDB:ENSMUSG00000009293; -.
DR   eggNOG; KOG0426; Eukaryota.
DR   GeneTree; ENSGT00940000158193; -.
DR   HOGENOM; CLU_030988_10_1_1; -.
DR   InParanoid; P60605; -.
DR   OMA; NIDACKM; -.
DR   OrthoDB; 149628at2759; -.
DR   PhylomeDB; P60605; -.
DR   TreeFam; TF101118; -.
DR   Reactome; R-MMU-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 22213; 20 hits in 76 CRISPR screens.
DR   ChiTaRS; Ube2g2; mouse.
DR   EvolutionaryTrace; P60605; -.
DR   PRO; PR:P60605; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P60605; Protein.
DR   Bgee; ENSMUSG00000009293; Expressed in otic placode and 259 other cell types or tissues.
DR   ExpressionAtlas; P60605; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
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; IPI:IntAct.
DR   GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:MGI.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0035458; P:cellular response to interferon-beta; ISO:MGI.
DR   GO; GO:1904153; P:negative regulation of retrograde protein transport, ER to cytosol; ISO:MGI.
DR   GO; GO:0030163; P:protein catabolic process; ISO:MGI.
DR   GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:MGI.
DR   CDD; cd00195; UBCc; 1.
DR   Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR   IDEAL; IID50078; -.
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.
DR   Genevisible; P60605; MM.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; ATP-binding; Endoplasmic reticulum;
KW   Lipid droplet; 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_0000082484"
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"
FT   HELIX           2..18
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   STRAND          24..30
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   STRAND          36..42
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   TURN            48..51
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   STRAND          53..59
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   TURN            62..65
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   STRAND          86..88
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   HELIX           116..128
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   HELIX           132..134
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   HELIX           138..145
FT                   /evidence="ECO:0007829|PDB:3FSH"
FT   HELIX           148..162
FT                   /evidence="ECO:0007829|PDB:3FSH"
SQ   SEQUENCE   165 AA;  18566 MW;  74DEC732A79575E3 CRC64;
     MAGTALKRLM AEYKQLTLNP PEGIVAGPMN EENFFEWEAL IMGPEDTCFE FGVFPAILSF
     PLDYPLSPPK MRFTCEMFHP NIYPDGRVCI SILHAPGDDP MGYESSAERW SPVQSVEKIL
     LSVVSMLAEP NDESGANVDA SKMWRDDREQ FYKIAKQIVQ KSLGL
//