[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=C57BL/6J; TISSUE=Fetus; DOI=10.1074/jbc.M007640200; PubMed=11278356 [NCBI, ExPASy, EBI, Israel, Japan] Tiwari S., Weissman A.M.; "Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)."; J. Biol. Chem. 276:16193-16200(2001).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

Comments

FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins. Involved in endoplasmic reticulum-associated degradation (ERAD) (By similarity).
CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
PATHWAY: Protein modification; protein ubiquitination .
SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF296657; AAK52608.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010321; AAH10321.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_062777.2; -.

UniGene

Mm.458125

3D structure databases

HSSP

Q02159; 2UCZ. [HSSP ENTRY / PDB]

SMR

P60605; 1-165.

ModBase

P60605.

Protein-protein interaction databases

DIP

DIP:29061N; -.

Organism-specific databases

MGI

MGI:1343188; Ube2g2.

Gene expression databases

ArrayExpress

P60605; -.

CleanEx

MM_UBE2G2; -.

GermOnline

ENSMUSG00000009293; Mus musculus.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from MGI).
GO:0005783;	Cellular component: endoplasmic reticulum (inferred from direct assay from MGI).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0030433;	Biological process: ER-associated protein catabolic process (inferred from direct assay from MGI).
QuickGo view.

Family and domain databases

InterPro

IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.

PANTHER

PTHR11621; UBQ-conjugat_E2; 1.

Pfam

PF00179; UQ_con; 1.
Pfam graphical view of domain structure.

ProDom

PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00212; UBCc; 1.
SMART graphical view of domain structure.

PROSITE

PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P60605.

Genome annotation databases

Ensembl

ENSMUSG00000009293; Mus musculus. [Contig view]

GeneID

22213; -.

KEGG

mmu:22213; -.

Phylogenomic databases

HOVERGEN

P60605; -.

Other

SOURCE

Ube2g2; Mus musculus.

ProtoNet

P60605.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Ligase; Ubl conjugation pathway.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 165`	`165`	`Ubiquitin-conjugating enzyme E2 G2.`	`PRO_0000082484`
`ACT_SITE`	`89 89`		`Glycyl thioester intermediate (By similarity).`

Sequence information

Length: 165 AA [This is the length of the unprocessed precursor]

Molecular weight: 18566 Da [This is the MW of the unprocessed precursor]

CRC64: 74DEC732A79575E3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAGTALKRLM AEYKQLTLNP PEGIVAGPMN EENFFEWEAL IMGPEDTCFE FGVFPAILSF 

        70         80         90        100        110        120 
PLDYPLSPPK MRFTCEMFHP NIYPDGRVCI SILHAPGDDP MGYESSAERW SPVQSVEKIL 

       130        140        150        160 
LSVVSMLAEP NDESGANVDA SKMWRDDREQ FYKIAKQIVQ KSLGL

P60605 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools