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Database: UniProt
Entry: P60605
LinkDB: P60605
Original site: P60605 
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   26-NOV-2014, entry version 95.
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP +
CC       diphosphate + protein N-ubiquityllysine. {ECO:0000255|PROSITE-
CC       ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000255|PROSITE-ProRule:PRU00388}.
CC   -!- INTERACTION:
CC       Self; NbExp=11; IntAct=EBI-9108745, EBI-9108745;
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   UniGene; Mm.458125; -.
DR   PDB; 3FSH; X-ray; 2.76 A; A/B=1-165.
DR   PDBsum; 3FSH; -.
DR   ProteinModelPortal; P60605; -.
DR   SMR; P60605; 2-165.
DR   BioGrid; 204416; 7.
DR   DIP; DIP-29061N; -.
DR   PhosphoSite; P60605; -.
DR   MaxQB; P60605; -.
DR   PaxDb; P60605; -.
DR   PRIDE; P60605; -.
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   eggNOG; COG5078; -.
DR   HOVERGEN; HBG063308; -.
DR   InParanoid; P60605; -.
DR   KO; K04555; -.
DR   OMA; DMFHPNI; -.
DR   OrthoDB; EOG7VB2HT; -.
DR   TreeFam; TF101118; -.
DR   UniPathway; UPA00143; -.
DR   EvolutionaryTrace; P60605; -.
DR   NextBio; 28670; -.
DR   PRO; PR:P60605; -.
DR   Bgee; P60605; -.
DR   CleanEx; MM_UBE2G2; -.
DR   ExpressionAtlas; P60605; baseline and differential.
DR   Genevestigator; P60605; -.
DR   GO; GO:0005829; C:cytosol; IDA:MGI.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0016881; F:acid-amino acid ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB.
DR   GO; GO:0030433; P:ER-associated ubiquitin-dependent 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; SSF54495; 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.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00388,
FT                                ECO:0000255|PROSITE-ProRule:PRU10133}.
FT   HELIX         1     18       {ECO:0000244|PDB:3FSH}.
FT   STRAND       24     30       {ECO:0000244|PDB:3FSH}.
FT   STRAND       36     42       {ECO:0000244|PDB:3FSH}.
FT   TURN         48     51       {ECO:0000244|PDB:3FSH}.
FT   STRAND       53     59       {ECO:0000244|PDB:3FSH}.
FT   TURN         62     65       {ECO:0000244|PDB:3FSH}.
FT   STRAND       70     75       {ECO:0000244|PDB:3FSH}.
FT   STRAND       86     88       {ECO:0000244|PDB:3FSH}.
FT   HELIX        91     93       {ECO:0000244|PDB:3FSH}.
FT   HELIX       116    128       {ECO:0000244|PDB:3FSH}.
FT   HELIX       132    134       {ECO:0000244|PDB:3FSH}.
FT   HELIX       138    145       {ECO:0000244|PDB:3FSH}.
FT   HELIX       148    162       {ECO:0000244|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
//
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