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O14933 (UB2L6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin/ISG15-conjugating enzyme E2 L6

EC=6.3.2.19
Alternative name(s):
Retinoic acid-induced gene B protein
Short name=RIG-B
UbcH8
Ubiquitin carrier protein L6
Ubiquitin-protein ligase L6
Gene names
Name:UBE2L6
Synonyms:UBCH8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length153 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin or ISG15 to other proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Promotes ubiquitination and subsequent proteasomal degradation of FLT3. Ref.10 Ref.12 Ref.15

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with RNF19A, RNF19B and RNF144B. Interacts with FLT3 (tyrosine phosphorylated). Ref.11 Ref.13 Ref.14 Ref.15

Tissue specificity

Present in natural killer cells (at protein level). Ref.14

Induction

By IFNB1/IFN-beta. Ref.10

Post-translational modification

ISGylated. Ref.12

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence CAB64566.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

RNF144BQ7Z4194EBI-2129974,EBI-2129982
RNF19BQ6ZMZ03EBI-2129974,EBI-2466594
Rnf40Q8CJB92EBI-2129974,EBI-6110162From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O14933-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O14933-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 153153Ubiquitin/ISG15-conjugating enzyme E2 L6
PRO_0000082478

Sites

Active site861Glycyl thioester intermediate By similarity

Natural variations

Alternative sequence1 – 6666Missing in isoform 2.
VSP_037344

Secondary structure

............................ 153
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 16, 2009. Version 4.
Checksum: D79768775344EFAE

FASTA15317,769
        10         20         30         40         50         60 
MMASMRVVKE LEDLQKKPPP YLRNLSSDDA NVLVWHALLL PDQPPYHLKA FNLRISFPPE 

        70         80         90        100        110        120 
YPFKPPMIKF TTKIYHPNVD ENGQICLPII SSENWKPCTK TCQVLEALNV LVNRPNIREP 

       130        140        150 
LRMDLADLLT QNPELFRKNA EEFTLRFGVD RPS 

« Hide

Isoform 2 [UniParc].

Checksum: CD4DEC38615607B1
Show »

FASTA8710,086

References

« Hide 'large scale' references
[1]"Genomic organization of the human ubiquitin-conjugating enzyme gene, UBE2L6 on chromosome 11q12."
Ardley H.C., Rose S.A., Tan N., Leek J.P., Markham A.F., Robinson P.A.
Cytogenet. Cell Genet. 89:137-140(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
[2]"Human retinoic acid induced gene B (RIG-B) 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.
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Thymus.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[6]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[9]"Physical interaction between specific E2 and Hect E3 enzymes determines functional cooperativity."
Kumar S., Kao W.H., Howley P.M.
J. Biol. Chem. 272:13548-13554(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-153 (ISOFORM 1).
[10]"The UbcH8 ubiquitin E2 enzyme is also the E2 enzyme for ISG15, an IFN-alpha/beta-induced ubiquitin-like protein."
Zhao C., Beaudenon S.L., Kelley M.L., Waddell M.B., Yuan W., Schulman B.A., Huibregtse J.M., Krug R.M.
Proc. Natl. Acad. Sci. U.S.A. 101:7578-7582(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 140-146, FUNCTION IN ISG15 ATTACHMENT, INDUCTION BY IFNB1.
[11]"A novel centrosomal ring-finger protein, dorfin, mediates ubiquitin ligase activity."
Niwa J., Ishigaki S., Doyu M., Suzuki T., Tanaka K., Sobue G.
Biochem. Biophys. Res. Commun. 281:706-713(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF19A.
[12]"Link between the ubiquitin conjugation system and the ISG15 conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2 enzyme."
Takeuchi T., Iwahara S., Saeki Y., Sasajima H., Yokosawa H.
J. Biochem. 138:711-719(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ISGYLATION.
[13]"The p53-inducible E3 ubiquitin ligase p53RFP induces p53-dependent apoptosis."
Huang J., Xu L.-G., Liu T., Zhai Z., Shu H.-B.
FEBS Lett. 580:940-947(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF144B.
[14]"NK lytic-associated molecule, involved in NK cytotoxic function, is an E3 ligase."
Fortier J.M., Kornbluth J.
J. Immunol. 176:6454-6463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RNF19B, TISSUE SPECIFICITY.
[15]"Ubiquitin conjugase UBCH8 targets active FMS-like tyrosine kinase 3 for proteasomal degradation."
Buchwald M., Pietschmann K., Muller J.P., Bohmer F.D., Heinzel T., Kramer O.H.
Leukemia 24:1412-1421(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN UBIQUITINATION OF FLT3, INTERACTION WITH FLT3.
[16]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Crystal structure of Ubch8."
Mizushima T., Suzuki M., Teshima N., Yamane T., Murata S., Tanaka K.
Submitted (MAR-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-153.
[18]"The structure of the UbcH8-ubiquitin complex shows a unique ubiquitin interaction site."
Serniwka S.A., Shaw G.S.
Biochemistry 48:12169-12179(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR IN COMPLEX WITH UBIQUITIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ243268 expand/collapse EMBL AC list , AJ243269, AJ243270, AJ243271 Genomic DNA. Translation: CAB64566.1. Different initiation.
AF061736 mRNA. Translation: AAD17525.1.
AK315755 mRNA. Translation: BAG38109.1.
CR457126 mRNA. Translation: CAG33407.1.
AK226165 mRNA. No translation available.
AP002893 Genomic DNA. No translation available.
CH471076 Genomic DNA. Translation: EAW73757.1.
CH471076 Genomic DNA. Translation: EAW73759.1.
BC032491 mRNA. Translation: AAH32491.1.
AF031141 mRNA. Translation: AAB86433.1.
RefSeqNP_004214.1. NM_004223.4.
NP_937826.1. NM_198183.2.
UniGeneHs.425777.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WZVX-ray2.10A/B2-152[»]
1WZWX-ray2.40A2-152[»]
2KJHNMR-A2-153[»]
ProteinModelPortalO14933.
SMRO14933. Positions 3-152.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114672. 41 interactions.
DIPDIP-41477N.
IntActO14933. 26 interactions.
MINTMINT-240858.
STRING9606.ENSP00000287156.

PTM databases

PhosphoSiteO14933.

Proteomic databases

PaxDbO14933.
PRIDEO14933.

Protocols and materials databases

DNASU9246.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000287156; ENSP00000287156; ENSG00000156587. [O14933-1]
ENST00000340573; ENSP00000341980; ENSG00000156587. [O14933-2]
GeneID9246.
KEGGhsa:9246.
UCSCuc001nkn.2. human. [O14933-1]

Organism-specific databases

CTD9246.
GeneCardsGC11M057319.
HGNCHGNC:12490. UBE2L6.
HPAHPA003328.
MIM603890. gene.
neXtProtNX_O14933.
PharmGKBPA37139.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
HOVERGENHBG063308.
InParanoidO14933.
KOK04553.
OMAPEKPPYN.
OrthoDBEOG7GXPD8.
PhylomeDBO14933.
TreeFamTF313043.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
REACT_98458. Immune System.
SignaLinkO14933.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressO14933.
BgeeO14933.
CleanExHS_UBE2L6.
GenevestigatorO14933.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2L6. human.
EvolutionaryTraceO14933.
GeneWikiUBE2L6.
GenomeRNAi9246.
NextBio34661.
PROO14933.
SOURCESearch...

Entry information

Entry nameUB2L6_HUMAN
AccessionPrimary (citable) accession number: O14933
Secondary accession number(s): A6NDM6 expand/collapse secondary AC list , A8MY53, Q8N5D8, Q9UEZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 140 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM