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 01-MAY-2013, entry version 83.
DE RecName: Full=Ubiquitin-conjugating enzyme E2 G2;
DE EC=6.3.2.19;
DE AltName: Full=Ubiquitin carrier protein G2;
DE AltName: Full=Ubiquitin-protein ligase G2;
GN Name=Ube2g2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
CC covalent attachment to other proteins. In vitro catalyzes 'Lys-
CC 48'-linked polyubiquitination. Involved in endoplasmic reticulum-
CC associated degradation (ERAD) (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC diphosphate + protein N-ubiquityllysine.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
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DR EMBL; AF296657; AAK52608.1; -; mRNA.
DR EMBL; BC010321; AAH10321.1; -; mRNA.
DR IPI; IPI01026711; -.
DR RefSeq; NP_062777.2; NM_019803.3.
DR UniGene; Mm.458125; -.
DR PDB; 3FSH; X-ray; 2.76 A; A/B=1-165.
DR PDBsum; 3FSH; -.
DR ProteinModelPortal; P60605; -.
DR DIP; DIP-29061N; -.
DR PhosphoSite; P60605; -.
DR PaxDb; P60605; -.
DR PRIDE; P60605; -.
DR Ensembl; ENSMUST00000174510; ENSMUSP00000133515; ENSMUSG00000009293.
DR GeneID; 22213; -.
DR KEGG; mmu:22213; -.
DR CTD; 7327; -.
DR MGI; MGI:1343188; Ube2g2.
DR eggNOG; COG5078; -.
DR HOVERGEN; HBG063308; -.
DR InParanoid; P60605; -.
DR KO; K04555; -.
DR OMA; RRLMAEY; -.
DR OrthoDB; EOG4GB77C; -.
DR UniPathway; UPA00143; -.
DR ChiTaRS; UBE2G2; mouse.
DR EvolutionaryTrace; P60605; -.
DR NextBio; 28670; -.
DR ArrayExpress; P60605; -.
DR Bgee; P60605; -.
DR CleanEx; MM_UBE2G2; -.
DR Genevestigator; P60605; -.
DR GermOnline; ENSMUSG00000009293; Mus musculus.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein ligase activity; ISS:UniProtKB.
DR GO; GO:0030433; P:ER-associated protein catabolic process; IDA:MGI.
DR GO; GO:0070936; P:protein K48-linked ubiquitination; ISS:UniProtKB.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
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; UBQ-conjugat/RWD-like; 1.
DR PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
DR PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Complete proteome; Ligase;
KW Nucleotide-binding; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1 165 Ubiquitin-conjugating enzyme E2 G2.
FT /FTId=PRO_0000082484.
FT ACT_SITE 89 89 Glycyl thioester intermediate (By
FT similarity).
FT HELIX 1 18
FT STRAND 24 30
FT STRAND 36 42
FT TURN 48 51
FT STRAND 53 59
FT TURN 62 65
FT STRAND 70 75
FT STRAND 86 88
FT HELIX 91 93
FT HELIX 116 128
FT HELIX 132 134
FT HELIX 138 145
FT HELIX 148 162
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
//
