NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N;
TISSUE=Colon;
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. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53 (By similarity).
CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
PATHWAY: Protein modification; protein ubiquitination .
SUBUNIT: Component of a E3 ubiquitin ligase complex containing UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X (By similarity).
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

BC019464; AAH19464.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_663395.1; -.

UniGene

Mm.270530

3D structure databases

SMR

P61080; 1-147.

ModBase

P61080.

Organism-specific databases

MGI

MGI:2384911; Ube2d1.

Gene expression databases

ArrayExpress

P61080; -.

GermOnline

ENSMUSG00000019927; Mus musculus.

Ontologies

GO:0031398;	Biological process: positive regulation of protein ubiquitination (inferred from sequence or structural similarity from UniProtKB).
GO:0000209;	Biological process: protein polyubiquitination (inferred from sequence or structural similarity from UniProtKB).
GO:0006511;	Biological process: ubiquitin-dependent protein catabolic process (inferred from sequence or structural similarity from UniProtKB).
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

P61080.

Genome annotation databases

Ensembl

ENSMUSG00000019927; Mus musculus. [Contig view]

GeneID

216080; -.

KEGG

mmu:216080; -.

Phylogenomic databases

HOGENOM

P61080; -.

HOVERGEN

P61080; -.

Other

SOURCE

Ube2d1; Mus musculus.

ProtoNet

P61080.

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`	`1 147`	`147`	`Ubiquitin-conjugating enzyme E2 D1.`	`PRO_0000082461`
`ACT_SITE`	`85 85`		`Glycyl thioester intermediate (By similarity).`

Sequence information

Length: 147 AA [This is the length of the unprocessed precursor]

Molecular weight: 16602 Da [This is the MW of the unprocessed precursor]

CRC64: 2E96FD0179EE119D [This is a checksum on the sequence]

        10         20         30         40         50         60 
MALKRIQKEL SDLQRDPPAH CSAGPVGDDL FHWQATIMGP PDSAYQGGVF FLTVHFPTDY 

        70         80         90        100        110        120 
PFKPPKIAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV 

       130        140 
PDIAQIYKSD KEKYNRHARE WTQKYAM

P61080 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