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Q96B02 (UBE2W_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 W

EC=6.3.2.19
Alternative name(s):
N-terminus-conjugating E2
Ubiquitin carrier protein W
Ubiquitin-conjugating enzyme 16
Short name=UBC-16
Ubiquitin-protein ligase W
Gene names
Name:UBE2W
Synonyms:UBC16
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length151 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Catalyzes monoubiquitination. Involved in degradation of misfolded chaperone substrates by mediating monoubiquitination of STUB1/CHIP, leading to recruitment of ATXN3 to monoubiquitinated STUB1/CHIP, and restriction of the length of ubiquitin chain attached to STUB1/CHIP substrates by ATXN3. After UV irradiation, but not after mitomycin-C (MMC) treatment, acts as a specific E2 ubiquitin-conjugating enzyme for the Fanconi anemia complex by associating with E3 ubiquitin-protein ligase FANCL and catalyzing monoubiquitination of FANCD2, a key step in the DNA damage pathway. In vitro catalyzes 'Lys-11'-linked polyubiquitination. Transfers ubiquitin in complex with RING/U-box type E3s that do not have active site cysteine residues to form thioester bonds with ubiquitin, and preferentially ubiquitinates the N-terminus of substrates, such as ATXN3, STUB1 and SUMO2. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Homodimer. Interacts with FANCL. Interacts with STUB1/CHIP By similarity. Ref.7 Ref.12

Subcellular location

Nucleus. Note: In the nucleus, colocalizes with FANCL. Ref.1

Tissue specificity

Widely expressed, with highest expression in brain, liver, pancreas and heart. Ref.1

Post-translational modification

Ubiquitinated in vitro in the presence of FANCL By similarity. Autoubiquitinated at Met-1. Ref.10

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q96B02-1)

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: Q96B02-2)

The sequence of this isoform differs from the canonical sequence as follows:
     5-5: Q → QTTGRRVEVWFP
Isoform 3 (identifier: Q96B02-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLSPRGVTRARQLLPLRLWPRRSWGDGSIM
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 151151Ubiquitin-conjugating enzyme E2 W
PRO_0000232689

Sites

Active site911Glycyl thioester intermediate By similarity

Amino acid modifications

Cross-link1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)

Natural variations

Alternative sequence11M → MLSPRGVTRARQLLPLRLWP RRSWGDGSIM in isoform 3.
VSP_042974
Alternative sequence51Q → QTTGRRVEVWFP in isoform 2.
VSP_017943

Experimental info

Mutagenesis831H → N: Impaired substrate ubiquitination of both Tau and ATXN3. Ref.11
Mutagenesis911C → A: Loss of predominant nuclear localization. Ref.1
Sequence conflict261N → S in BAB13883. Ref.2
Sequence conflict451P → S in BAA91954. Ref.2

Secondary structure

.................. 151
Helix Strand Turn

Details...

Sequences

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

Last modified December 1, 2001. Version 1.
Checksum: 276B585BBC4CEB71

FASTA15117,331
        10         20         30         40         50         60 
MASMQKRLQK ELLALQNDPP PGMTLNEKSV QNSITQWIVD MEGAPGTLYE GEKFQLLFKF 

        70         80         90        100        110        120 
SSRYPFDSPQ VMFTGENIPV HPHVYSNGHI CLSILTEDWS PALSVQSVCL SIISMLSSCK 

       130        140        150 
EKRRPPDNSF YVRTCNKNPK KTKWWYHDDT C 

« Hide

Isoform 2 [UniParc].

Checksum: F41B440840AD0625
Show »

FASTA16218,660
Isoform 3 [UniParc].

Checksum: 3E0F0920D2F1AD9F
Show »

FASTA18020,689

References

« Hide 'large scale' references
[1]"Cloning, characterization and subcellular localization of a gene encoding a human Ubiquitin-conjugating enzyme (E2) homologous to the Arabidopsis thaliana UBC-16 gene product."
Yin G., Ji C., Wu T., Shen Z., Xu X., Xie Y., Mao Y.
Front. Biosci. 11:1500-1507(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-91.
[2]"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] (ISOFORMS 1; 2 AND 3).
Tissue: Embryo, Hippocampus and Placenta.
[3]"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).
[4]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]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].
[6]"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: Urinary bladder.
[7]"Mechanistic insight into site-restricted monoubiquitination of FANCD2 by Ube2t, FANCL, and FANCI."
Alpi A.F., Pace P.E., Babu M.M., Patel K.J.
Mol. Cell 32:767-777(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH FANCL.
[8]"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to preferred lysines."
David Y., Ziv T., Admon A., Navon A.
J. Biol. Chem. 285:8595-8604(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"UBE2W interacts with FANCL and regulates the monoubiquitination of Fanconi anemia protein FANCD2."
Zhang Y., Zhou X., Zhao L., Li C., Zhu H., Xu L., Shan L., Liao X., Guo Z., Huang P.
Mol. Cells 31:113-122(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Ube2W conjugates ubiquitin to alpha-amino groups of protein N-termini."
Tatham M.H., Plechanovova A., Jaffray E.G., Salmen H., Hay R.T.
Biochem. J. 453:137-145(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION AT MET-1, SUBSTRATE SPECIFICITY.
[11]"The ubiquitin-conjugating enzyme (E2) Ube2w ubiquitinates the N terminus of substrates."
Scaglione K.M., Basrur V., Ashraf N.S., Konen J.R., Elenitoba-Johnson K.S., Todi S.V., Paulson H.L.
J. Biol. Chem. 288:18784-18788(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBSTRATE SPECIFICITY, MUTAGENESIS OF HIS-83.
[12]"A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-function screen."
Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J., Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K., Arrowsmith C.H., Raught B., Dhe-Paganon S.
Mol. Cell. Proteomics 11:329-341(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 1-117, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY948289 mRNA. Translation: AAY24555.1.
AK001873 mRNA. Translation: BAA91954.1.
AK021735 mRNA. Translation: BAB13883.1.
AK024050 mRNA. Translation: BAB14800.1.
AK295792 mRNA. Translation: BAG58613.1.
CR457275 mRNA. Translation: CAG33556.1.
CH471068 Genomic DNA. Translation: EAW87009.1.
CH471068 Genomic DNA. Translation: EAW87011.1.
AC022826 Genomic DNA. No translation available.
BC016326 mRNA. Translation: AAH16326.1.
CCDSCCDS47874.2. [Q96B02-3]
RefSeqNP_001001481.2. NM_001001481.2.
NP_001257944.1. NM_001271015.1.
NP_060769.4. NM_018299.4. [Q96B02-3]
UniGeneHs.128841.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A7LX-ray1.82A/B1-117[»]
ProteinModelPortalQ96B02.
SMRQ96B02. Positions 1-117.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120572. 67 interactions.
IntActQ96B02. 67 interactions.
MINTMINT-1428082.
STRING9606.ENSP00000397453.

PTM databases

PhosphoSiteQ96B02.

Polymorphism databases

DMDM74751754.

Proteomic databases

MaxQBQ96B02.
PRIDEQ96B02.

Protocols and materials databases

DNASU55284.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000517608; ENSP00000428813; ENSG00000104343. [Q96B02-3]
ENST00000602593; ENSP00000473561; ENSG00000104343. [Q96B02-1]
ENST00000602969; ENSP00000473516; ENSG00000104343. [Q96B02-2]
GeneID55284.
KEGGhsa:55284.
UCSCuc003xzt.3. human. [Q96B02-3]
uc003xzu.4. human. [Q96B02-2]

Organism-specific databases

CTD55284.
GeneCardsGC08M074692.
HGNCHGNC:25616. UBE2W.
HPAHPA045161.
MIM614277. gene.
neXtProtNX_Q96B02.
PharmGKBPA142670657.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233453.
HOVERGENHBG063308.
KOK10688.
PhylomeDBQ96B02.
TreeFamTF314582.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ96B02.
UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ96B02.
BgeeQ96B02.
CleanExHS_UBE2W.
GenevestigatorQ96B02.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2W. human.
EvolutionaryTraceQ96B02.
GenomeRNAi55284.
NextBio59442.
PROQ96B02.
SOURCESearch...

Entry information

Entry nameUBE2W_HUMAN
AccessionPrimary (citable) accession number: Q96B02
Secondary accession number(s): B4DIV1 expand/collapse secondary AC list , Q1XBE0, Q9H823, Q9HAG6, Q9NV07
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 119 of the entry and version 1 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 8

Human chromosome 8: entries, gene names and cross-references to MIM