[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1074/jbc.272.21.13548; PubMed=9153201 [NCBI, ExPASy, EBI, Israel, Japan] Kumar S., Kao W.H., Howley P.M.; "Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity."; J. Biol. Chem. 272:13548-13554(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. Liu T., Mao M., Zhang J., Wu J., Zhang Q., Fu G., Shen Y., Zhou J., Yu Y., Wang Z., Chen S., Chen Z.; "Human retinoic acid induced gene B (RIG-B) mRNA."; Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. PubMed=10894956 [NCBI, ExPASy, EBI, Israel, Japan] Ardley H.C., Rose S.A., Tan N., Leek J.P., Markham A.F., Robinson P.A.; "Genomic organization of the human ubiquitin-conjugating enzyme gene, UBE2L6 on chromosome 11q12."; Cytogenet. Cell Genet. 89:137-140(2000).
[4]	PROTEIN SEQUENCE OF 139-145, FUNCTION IN ISG15 ATTACHMENT, AND INDUCTION BY INTERFERON BETA. DOI=10.1073/pnas.0402528101; PubMed=15131269 [NCBI, ExPASy, EBI, Israel, Japan] Zhao C., Beaudenon S.L., Kelley M.L., Waddell M.B., Yuan W., Schulman B.A., Huibregtse J.M., Krug R.M.; "The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein."; Proc. Natl. Acad. Sci. U.S.A. 101:7578-7582(2004).
[5]	INTERACTION WITH RNF19A. DOI=10.1006/bbrc.2001.4414; PubMed=11237715 [NCBI, ExPASy, EBI, Israel, Japan] Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.; "A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity."; Biochem. Biophys. Res. Commun. 281:706-713(2001).
[6]	INTERACTION WITH RNF144B. DOI=10.1016/j.febslet.2005.09.105; PubMed=16427630 [NCBI, ExPASy, EBI, Israel, Japan] Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.; "The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis."; FEBS Lett. 580:940-947(2006).
[7]	INTERACTION WITH RNF19B, AND TISSUE SPECIFICITY. PubMed=16709802 [NCBI, ExPASy, EBI, Israel, Japan] Fortier J.M., Kornbluth J.; "NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase."; J. Immunol. 176:6454-6463(2006).
[8]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-152. Mizushima T., Suzuki M., Teshima N., Yamane T., Murata S., Tanaka K.; "Crystal structure of Ubch8."; Submitted (MAR-2005) to the PDB data bank.

Comments

FUNCTION: Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53.
CATALYTIC ACTIVITY: ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.
PATHWAY: Protein modification; protein ubiquitination .
SUBUNIT: Interacts with RNF19A, RNF19B and RNF144B.
TISSUE SPECIFICITY: Present in natural killer cells (at protein level).
INDUCTION: By interferon beta.
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

AF031141; AAB86433.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF061736; AAD17525.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ243268; CAB64566.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ243269; CAB64566.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ243270; CAB64566.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ243271; CAB64566.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_004214.1; -.

UniGene

Hs.425777

3D structure databases

PDB

1WZV; X-ray; 2.10 A; A/B=1-152.	[ExPASy / RCSB / EBI]
1WZW; X-ray; 2.40 A; A=1-152.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1WZV; -.
1WZW; -.

ModBase

O14933.

Organism-specific databases

HGNC:12490; UBE2L6.

HPA003328; -.

603890; gene. [NCBI / EBI]

PharmGKB

PA37139; -.

GeneCards

O14933.

Gene expression databases

ArrayExpress

O14933; -.

CleanEx

HS_UBE2L6; -.

GermOnline

ENSG00000156587; Homo sapiens.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0004842;	Molecular function: ubiquitin-protein ligase activity (traceable author statement from ProtInc).
GO:0006464;	Biological process: protein modification process (traceable author statement from ProtInc).
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

O14933.

Genome annotation databases

Ensembl

ENSG00000156587; Homo sapiens. [Contig view]

GeneID

9246; -.

KEGG

hsa:9246; -.

Phylogenomic databases

HOVERGEN

O14933; -.

Other

SOURCE

UBE2L6; Homo sapiens.

ProtoNet

O14933.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; Ligase; Ubl conjugation pathway.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 152`	`152`	`Ubiquitin/ISG15-conjugating enzyme E2 L6.`	`PRO_0000082478`
`ACT_SITE`	`85 85`		`Glycyl thioester intermediate (By similarity).`
`HELIX`	`3 15`	`13`
`STRAND`	`21 26`	`6`
`STRAND`	`33 38`	`6`
`HELIX`	`45 47`	`3`
`STRAND`	`48 55`	`8`
`TURN`	`58 61`	`4`
`STRAND`	`66 71`	`6`
`HELIX`	`87 89`	`3`
`TURN`	`91 93`	`3`
`HELIX`	`100 112`	`13`
`STRAND`	`116 118`	`3`
`HELIX`	`122 130`	`9`
`HELIX`	`132 146`	`15`

Sequence information

Length: 152 AA [This is the length of the unprocessed precursor]

Molecular weight: 17638 Da [This is the MW of the unprocessed precursor]

CRC64: 372AB553CE44A67A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MASMRVVKEL EDLQKKPPPY LRNLSSDDAN VLVWHALLLP DQPPYHLKAF NLRISFPPEY 

        70         80         90        100        110        120 
PFKPPMIKFT TKIYHPNVDE NGQICLPIIS SENWKPCTKT CQVLEALNVL VNRPNIREPL 

       130        140        150 
RMDLADLLTQ NPELFRKNAE EFTLRFGVDR PS

O14933 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