[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. DOI=10.1186/1471-2164-6-166; PubMed=16305752 [NCBI, ExPASy, EBI, Israel, Japan] Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; "Characterization of 954 bovine full-CDS cDNA sequences."; BMC Genomics 6:166-166(2005).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Fetal pons; NIH - Mammalian Gene Collection (MGC) project; Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.

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

BT026143; ABG66982.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC118376; AAI18377.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_001069796.1; -.

UniGene

Bt.64954

3D structure databases

SMR

Q17QG5; 1-165.

ModBase

Q17QG5.

Ontologies

GO:0004842;	Molecular function: ubiquitin-protein ligase activity (inferred from electronic annotation from EC).
GO:0043687;	Biological process: post-translational protein modification (inferred from electronic annotation from InterPro).
GO:0051246;	Biological process: regulation of protein metabolic process (inferred from electronic annotation from InterPro).
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).

Genome annotation databases

Ensembl

ENSBTAG00000013911; Bos taurus. [Contig view]

GeneID

614471; -.

KEGG

bta:614471; -.

Phylogenomic databases

HOVERGEN

Q17QG5; -.

Other

ProtoNet

Q17QG5.

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_0000259961`
`ACT_SITE`	`89 89`		`Glycyl thioester intermediate (By similarity).`

Sequence information

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

Molecular weight: 18552 Da [This is the MW of the unprocessed precursor]

CRC64: 74DEC72A049575E3 [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 FYKVAKQIVQ KSLGL

Q17QG5 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