[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=BALB/c; TISSUE=Brain; DOI=10.1074/jbc.271.5.2789; PubMed=8576256 [NCBI, ExPASy, EBI, Israel, Japan] Matuschewski K., Hauser H.P., Treier M., Jentsch S.; "Identification of a novel family of ubiquitin-conjugating enzymes with distinct amino-terminal extensions."; J. Biol. Chem. 271:2789-2794(1996).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Mammary tumor; 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. Mediates the selective degradation of short-lived and abnormal proteins.
CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
PATHWAY: Protein modification; protein ubiquitination .
SUBUNIT: Interacts with RNF14.
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

X92665; CAA63353.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC003781; AAH03781.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_033481.1; -.

UniGene

Mm.4429

3D structure databases

HSSP

P15731; 1QCQ. [HSSP ENTRY / PDB]

SMR

P52482; 46-193.

ModBase

P52482.

Organism-specific databases

MGI

MGI:107411; Ube2e1.

Gene expression databases

GermOnline

ENSMUSG00000021774; Mus musculus.

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

P52482.

Genome annotation databases

Ensembl

ENSMUSG00000021774; Mus musculus. [Contig view]

GeneID

22194; -.

KEGG

mmu:22194; -.

Phylogenomic databases

HOGENOM

P52482; -.

HOVERGEN

P52482; -.

Other

SOURCE

Ube2e1; Mus musculus.

ProtoNet

P52482.

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`	`1 193`	`193`	`Ubiquitin-conjugating enzyme E2 E1.`	`PRO_0000082471`
`COMPBIAS`	`9 18`	`10`	`Poly-Ser.`
`ACT_SITE`	`131 131`		`Glycyl thioester intermediate (By similarity).`

Sequence information

Length: 193 AA [This is the length of the unprocessed precursor]

Molecular weight: 21333 Da [This is the MW of the unprocessed precursor]

CRC64: B535B3095EF6C445 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSDDDSRAST SSSSSSSSNQ QTEKEGSTPK KKESKVSMSK NSKLLSTSAK RIQKELADIT 

        70         80         90        100        110        120 
LDPPPNCSAG PKGDNIYEWR STILGPPGSV YEGGVFFLDI TFTPEYPFKP PKVTFRTRIY 

       130        140        150        160        170        180 
HCNINSQGVI CLDILKDNWS PALTISKVLL SICSLLTDCN PADPLVGSIA TQYMTNRAEH 

       190 
DRMARQWTKR YAT

P52482 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