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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   09-JUL-2014, entry version 91.
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   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; 6.
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   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   ChiTaRS; UBE2G2; mouse.
DR   EvolutionaryTrace; P60605; -.
DR   NextBio; 28670; -.
DR   PRO; PR:P60605; -.
DR   ArrayExpress; P60605; -.
DR   Bgee; P60605; -.
DR   CleanEx; MM_UBE2G2; -.
DR   Genevestigator; P60605; -.
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:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0004842; F:ubiquitin-protein ligase 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 (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
//
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