Q96B02 (UBE2W_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 W
EC=6.3.2.19

Alternative name(s):
Ubiquitin carrier protein W
Ubiquitin-conjugating enzyme 16
Short name=UBC-16
Ubiquitin-protein ligase W

Gene names

Name:	UBE2W
Synonyms:	UBC16

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	151 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Ref.7 Ref.8 Ref.9
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.10
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.
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	DNA damage DNA repair Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
PTM	Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: UniProtKB-KW cellular response to misfolded protein Inferred from sequence or structural similarity. Source: UniProtKB misfolded or incompletely synthesized protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB proteasomal ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB protein K11-linked ubiquitination Inferred from direct assay Ref.8. Source: UniProtKB protein monoubiquitination Inferred from direct assay Ref.7Ref.8. Source: UniProtKB
Cellular_component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ubiquitin-protein ligase activity Inferred from direct assay Ref.7Ref.8. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 151

151

Ubiquitin-conjugating enzyme E2 W

PRO_0000232689

Sites

Active site

91

1

Glycyl thioester intermediate By similarity

Natural variations

Alternative sequence

1

1

M → MLSPRGVTRARQLLPLRLWP RRSWGDGSIM in isoform 3.

VSP_042974

Alternative sequence

5

1

Q → QTTGRRVEVWFP in isoform 2.

VSP_017943

Experimental info

Mutagenesis

91

1

C → A: Loss of predominant nuclear localization. Ref.1

Sequence conflict

26

1

N → S in BAB13883. Ref.2

Sequence conflict

45

1

P → S in BAA91954. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

151

Helix Strand Turn

Details...

Helix

6 – 17

12

Beta strand

35 – 42

8

Turn

48 – 51

4

Beta strand

53 – 60

8

Turn

62 – 66

5

Beta strand

70 – 76

7

Helix

93 – 95

3

Turn

96 – 98

3

Helix

105 – 115

11

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: 276B585BBC4CEB71	FASTA	151	17,331
	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
	Isoform 2 [UniParc]. Checksum: F41B440840AD0625	FASTA	162	18,660
	10 20 30 40 50 60 MASMQTTGRR VEVWFPKRLQ KELLALQNDP PPGMTLNEKS VQNSITQWIV DMEGAPGTLY 70 80 90 100 110 120 EGEKFQLLFK FSSRYPFDSP QVMFTGENIP VHPHVYSNGH ICLSILTEDW SPALSVQSVC 130 140 150 160 LSIISMLSSC KEKRRPPDNS FYVRTCNKNP KKTKWWYHDD TC
	Isoform 3 [UniParc]. Checksum: 3E0F0920D2F1AD9F	FASTA	180	20,689
	10 20 30 40 50 60 MLSPRGVTRA RQLLPLRLWP RRSWGDGSIM ASMQKRLQKE LLALQNDPPP GMTLNEKSVQ 70 80 90 100 110 120 NSITQWIVDM EGAPGTLYEG EKFQLLFKFS SRYPFDSPQV MFTGENIPVH PHVYSNGHIC 130 140 150 160 170 180 LSILTEDWSP ALSVQSVCLS IISMLSSCKE KRRPPDNSFY VRTCNKNPKK TKWWYHDDTC

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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]	"Structure of the human hypothetical protein LOC55284, a novel homodimeric ubiquitin conjugating enzyme." Structural genomics consortium (SGC) Submitted (SEP-2005) to the PDB data bank 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.

IPI

IPI00029300.
IPI01018247.

RefSeq

NP_001001481.2. NM_001001481.2.
NP_001257944.1. NM_001271015.1.
NP_060769.4. NM_018299.4.

UniGene

Hs.128841.
Hs.718604.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A7L	X-ray	1.82	A/B	1-117	[»]

ProteinModelPortal

Q96B02.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96B02. 63 interactions.

MINT

MINT-1428082.

STRING

9606.ENSP00000397453.

PTM databases

PhosphoSite

Q96B02.

Polymorphism databases

DMDM

74751754.

Proteomic databases

PRIDE

Q96B02.

Protocols and materials databases

DNASU

55284.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000419880; ENSP00000397453; ENSG00000104343.
ENST00000517608; ENSP00000428813; ENSG00000104343.

GeneID

55284.

KEGG

hsa:55284.

UCSC

uc003xzv.3. human.

Organism-specific databases

CTD

55284.

GeneCards

GC08M074692.

HGNC

HGNC:25616. UBE2W.

HPA

HPA045161.

MIM

614277. gene.

neXtProt

NX_Q96B02.

PharmGKB

PA142670657.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5078.

HOGENOM

HOG000233453.

HOVERGEN

HBG063308.

KO

K10688.

OMA

FTGDNIP.

OrthoDB

EOG49CQ8W.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

UniPathway

UPA00143.

Gene expression databases

ArrayExpress

Q96B02.

Bgee

Q96B02.

CleanEx

HS_UBE2W.

Genevestigator

Q96B02.

GermOnline

ENSG00000104343. Homo sapiens.

Family and domain databases

Gene3D

3.10.110.10. 1 hit.

InterPro

IPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]

Pfam

PF00179. UQ_con. 1 hit.
[Graphical view]

SUPFAM

SSF54495. UBQ-conjugat/RWD-like. 1 hit.

PROSITE

PS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

UBE2W. human.

EvolutionaryTrace

Q96B02.

GenomeRNAi

55284.

NextBio

59442.

SOURCE

Search...

Entry information

Entry name

UBE2W_HUMAN

Accession

Primary (citable) accession number: Q96B02
Secondary accession number(s): B4DIV1 , Q1XBE0, Q9H823, Q9HAG6, Q9NV07

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 18, 2006
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.