UB2G2_MOUSE
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 03-AUG-2022, entry version 146.
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}.
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; 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; 13.
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; P60605; -.
DR PeptideAtlas; P60605; -.
DR PRIDE; P60605; -.
DR ProteomicsDB; 298164; -.
DR Antibodypedia; 1148; 422 antibodies from 32 providers.
DR DNASU; 22213; -.
DR Ensembl; ENSMUST00000174510; ENSMUSP00000133515; ENSMUSG00000009293.
DR GeneID; 22213; -.
DR KEGG; mmu:22213; -.
DR UCSC; uc007fwa.1; mouse.
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; KMWRENR; -.
DR OrthoDB; 1317014at2759; -.
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 71 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 256 other tissues.
DR ExpressionAtlas; P60605; baseline and differential.
DR Genevisible; P60605; MM.
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:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IDA:MGI.
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 IDEAL; IID50078; -.
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 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
