[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). TISSUE=Melanoma; The German cDNA consortium; Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 116-375 (ISOFORM 2). TISSUE=Ovary, Placenta, and Uterus; 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).
[3]	SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. DOI=10.1016/j.bbrc.2005.11.026; PubMed=16300736 [NCBI, ExPASy, EBI, Israel, Japan] Seghatoleslam A., Zambrano A., Millon R., Ganguli G., Argentini M., Cromer A., Abecassis J., Wasylyk B.; "Analysis of a novel human gene, LOC92912, over-expressed in hypopharyngeal tumours."; Biochem. Biophys. Res. Commun. 339:422-429(2006).
[4]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 197-363. Structural genomics consortium (SGC); "Structure of human ubiquitin-conjugating enzyme (UBCI) involved in embryo attachment and implantation."; Submitted (JAN-2006) to the PDB data bank.

Comments

FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity).
CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
PATHWAY: Protein modification; protein ubiquitination .
SUBCELLULAR LOCATION: Cytoplasm.
ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name 1

Isoform ID Q8WVN8-1

This is the isoform sequence displayed in this entry.

Name 2

Isoform ID Q8WVN8-2

Features which should be applied to build the isoform sequence: VSP_017298, VSP_017299.
TISSUE SPECIFICITY: Detected in hypopharyngeal head and neck squamous cell carcinoma, in tumor masses and invasive epithelium.
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

AL832429; CAH10654.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC006827; AAH06827.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC017708; AAH17708.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034342; AAH34342.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_775740.1; -.

UniGene

Hs.23033

3D structure databases

PDB

1ZUO; X-ray; 1.80 A; A/B=197-363.

[ExPASy / RCSB / EBI]

PDBsum

1ZUO; -.

ModBase

Q8WVN8.

Organism-specific databases

H-InvDB

HIX0012448; -.
HIX0038395; -.

HGNC:19248; UBE2Q2.

PA142670652; -.

Gene expression databases

ArrayExpress

Q8WVN8; -.

CleanEx

HS_UBE2Q2; -.

GermOnline

ENSG00000140367; Homo sapiens.

Family and domain databases

InterPro

IPR006575; RWD.
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

SM00591; RWD; 1.
SM00212; UBCc; 1.
SMART graphical view of domain structure.

PROSITE

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

BLOCKS

Q8WVN8.

Genome annotation databases

Ensembl

ENSG00000140367; Homo sapiens. [Contig view]

GeneID

92912; -.

KEGG

hsa:92912; -.

Phylogenomic databases

HOGENOM

Q8WVN8; -.

HOVERGEN

Q8WVN8; -.

Other

Q8WVN8; -.

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

Keywords

3D-structure; Alternative splicing; ATP-binding; Cytoplasm; Ligase; Nucleotide-binding; Ubl conjugation pathway.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 375`	`375`	`Ubiquitin-conjugating enzyme E2 Q2.`	`PRO_0000223879`
`COMPBIAS`	`134 178`	`45`	`Glu-rich.`
`ACT_SITE`	`304 304`		`Glycyl thioester intermediate (By similarity).`
`VAR_SEQ`	`296 314`		`YVLGGGALCMELLTKQGWS -> LVHPSKGRWLNMLTVVCLD (in isoform 2).`	`VSP_017298`
`VAR_SEQ`	`315 375`		`Missing (in isoform 2).`	`VSP_017299`
`HELIX`	`203 217`	`15`
`HELIX`	`220 223`	`4`
`STRAND`	`226 232`	`7`
`STRAND`	`235 243`	`9`
`HELIX`	`251 263`	`13`
`STRAND`	`267 273`	`7`
`TURN`	`276 279`	`4`
`STRAND`	`284 290`	`7`
`STRAND`	`292 294`	`3`
`HELIX`	`299 301`	`3`
`HELIX`	`306 308`	`3`
`TURN`	`310 312`	`3`
`HELIX`	`319 332`	`14`
`HELIX`	`348 361`	`14`

Sequence information

Length: 375 AA [This is the length of the unprocessed precursor]

Molecular weight: 42818 Da [This is the MW of the unprocessed precursor]

CRC64: 7DE07315E89178A3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVSGLKAEL KFLASIFDKN HERFRIVSWK LDELHCQFLV PQQGSPHSLP PPLTLHCNIT 

        70         80         90        100        110        120 
ESYPSSSPIW FVDSEDPNLT SVLERLEDTK NNNLLRQQLK WLICELCSLY NLPKHLDVEM 

       130        140        150        160        170        180 
LDQPLPTGQN GTTEEVTSEE EEEEEEMAED IEDLDHYEMK EEEPISGKKS EDEGIEKENL 

       190        200        210        220        230        240 
AILEKIRKTQ RQDHLNGAVS GSVQASDRLM KELRDIYRSQ SYKTGIYSVE LINDSLYDWH 

       250        260        270        280        290        300 
VKLQKVDPDS PLHSDLQILK EKEGIEYILL NFSFKDNFPF DPPFVRVVLP VLSGGYVLGG 

       310        320        330        340        350        360 
GALCMELLTK QGWSSAYSIE SVIMQINATL VKGKARVQFG ANKNQYNLAR AQQSYNSIVQ 

       370 
IHEKNGWYTP PKEDG

Q8WVN8 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