Q15819 (UB2V2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 variant 2

Alternative name(s):
DDVit 1
Enterocyte differentiation-associated factor 1
Short name=EDAF-1
Enterocyte differentiation-promoting factor 1
Short name=EDPF-1
MMS2 homolog
Vitamin D3-inducible protein

Gene names

Name:	UBE2V2
Synonyms:	MMS2, UEV2

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	145 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Has no ubiquitin ligase activity on its own. The UBE2V2/UBE2N heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'. This type of poly-ubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Ref.2 Ref.8 Ref.9 Ref.10
Subunit structure	Heterodimer with UBE2N. Binds CHFR.
Tissue specificity	Detected in placenta, colon, liver and skin. Detected at very low levels in most tissues. Ref.1 Ref.2
Induction	Up-regulated in cultured fresh blood cells upon treatment with vitamin D3. Ref.1
Sequence similarities	Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Polymorphism
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA double-strand break processing Inferred from mutant phenotype PubMed 17349954. Source: HGNC cell proliferation Traceable author statement PubMed 9418904. Source: ProtInc negative regulation of neuron apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of DNA repair Inferred from electronic annotation. Source: Compara positive regulation of neuron projection development Inferred from electronic annotation. Source: Compara positive regulation of proteasomal ubiquitin-dependent protein catabolic process Inferred from electronic annotation. Source: Compara positive regulation of synapse assembly Inferred from electronic annotation. Source: Compara protein polyubiquitination Traceable author statement Ref.8. Source: ProtInc regulation of DNA repair Traceable author statement Ref.8. Source: ProtInc
Cellular_component	UBC13-MMS2 complex Inferred from direct assay PubMed 16129784. Source: HGNC cytoplasm Traceable author statement PubMed 16129784. Source: HGNC nucleus Inferred from direct assay PubMed 16129784. Source: HGNC
Molecular_function	acid-amino acid ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
UBC35	Q94A97	3	EBI-714329,EBI-994120	From a different organism.
UBE2N	P61088	3	EBI-714329,EBI-1052908

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 145

144

Ubiquitin-conjugating enzyme E2 variant 2

PRO_0000082602

Natural variations

Natural variant

36

1

E → G.
Corresponds to variant rs11557776 [ dbSNP | Ensembl ].

VAR_052431

Natural variant

40

1

D → H.
Corresponds to variant rs14890 [ dbSNP | Ensembl ].

VAR_052432

Natural variant

78

1

P → Q.
Corresponds to variant rs11557786 [ dbSNP | Ensembl ].

VAR_052433

Secondary structure

1

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145

Helix Strand Turn

Details...

Helix

11 – 24

14

Beta strand

29 – 37

9

Beta strand

45 – 51

7

Turn

57 – 60

4

Beta strand

62 – 68

7

Turn

71 – 75

5

Beta strand

79 – 84

6

Turn

93 – 95

3

Helix

100 – 102

3

Helix

104 – 107

4

Helix

115 – 126

12

Helix

129 – 132

4

Sequences

	Sequence		Length	Mass (Da)
	Q15819 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 98D632A1AEC0AADE	FASTA	145	16,363
	10 20 30 40 50 60 MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN 70 80 90 100 110 120 RIYSLKVECG PKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVVLQ 130 140 ELRRLMMSKE NMKLPQPPEG QTYNN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular Cloning of a 1alpha,25-dihydroxyvitamin D3 inducible transcript (DDVit 1) in human blood monocytes." Fritsche J., Rehli M., Krause S.W., Andreesen R., Kreutz M. Biochem. Biophys. Res. Commun. 235:407-412(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY. Tissue: Blood.
[2]	"The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family." Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F. Nucleic Acids Res. 26:3908-3914(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Tissue: Colon carcinoma.
[3]	"Isolation and characterization of a putative human enterocyte differentiation promoting factor (EDPF-1)." Faria J., Wild G.E. Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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 (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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]. Tissue: Bone marrow, Urinary bladder and Uterus.
[7]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11. Tissue: Platelet.
[8]	"Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair." Hofmann R.M., Pickart C.M. Cell 96:645-653(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBE2N.
[9]	"The Chfr mitotic checkpoint protein functions with Ubc13-Mms2 to form Lys63-linked polyubiquitin chains." Bothos J., Summers M.K., Venere M., Scolnick D.M., Halazonetis T.D. Oncogene 22:7101-7107(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBE2N AND CHFR.
[10]	"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.
[11]	"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].
[12]	"Crystal structure of the human ubiquitin conjugating enzyme complex, hMms2-hUbc13." Moraes T.F., Edwards R.A., McKenna S., Pastushok L., Xiao W., Glover J.N.M., Ellison M.J. Nat. Struct. Biol. 8:669-673(2001) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
[13]	"Molecular insights into the function of RING Finger (RNF)-containing proteins hRNF8 and hRNF168 in Ubc13/Mms2-dependent ubiquitylation." Campbell S.J., Edwards R.A., Leung C.C., Neculai D., Hodge C.D., Dhe-Paganon S., Glover J.N. J. Biol. Chem. 287:23900-23910(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.8 ANGSTROMS) OF 1-144 IN COMPLEX WITH RNF8 AND UBE2N.
[14]	"OTUB1 co-opts Lys48-linked ubiquitin recognition to suppress E2 enzyme function." Juang Y.C., Landry M.C., Sanches M., Vittal V., Leung C.C., Ceccarelli D.F., Mateo A.R., Pruneda J.N., Mao D.Y., Szilard R.K., Orlicky S., Munro M., Brzovic P.S., Klevit R.E., Sicheri F., Durocher D. Mol. Cell 45:384-397(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 25-271 IN COMPLEX WITH UBE2N AND OTUB1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X98091 mRNA. Translation: CAA66717.1.
AF049140 mRNA. Translation: AAC05381.1.
U62136 mRNA. Translation: AAB04758.2.
BT006744 mRNA. Translation: AAP35390.1.
CR407628 mRNA. Translation: CAG28556.1.
BC007051 mRNA. Translation: AAH07051.1.
BC016332 mRNA. Translation: AAH16332.1.
BC016710 mRNA. Translation: AAH16710.1.
BC028673 mRNA. Translation: AAH28673.1.
BC062418 mRNA. Translation: AAH62418.1.

IPI

IPI00019600.

PIR

JC5525.

RefSeq

NP_003341.1. NM_003350.2.

UniGene

Hs.491695.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J74	X-ray	1.90	A	1-145	[»]
1J7D	X-ray	1.85	A	1-145	[»]
1ZGU	NMR	-	A	7-145	[»]
3VON	X-ray	3.15	B/D/F/I/K/M/P/R/T/W/Y/a/d/f/h/k/m/o	6-143	[»]
4EPO	X-ray	4.80	A/E/I	1-144	[»]

ProteinModelPortal

Q15819.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29830N.

IntAct

Q15819. 19 interactions.

MINT

MINT-1368221.

STRING

9606.ENSP00000326473.

PTM databases

PhosphoSite

Q15819.

Polymorphism databases

DMDM

51701935.

Proteomic databases

PaxDb

Q15819.

PRIDE

Q15819.

Protocols and materials databases

DNASU

7336.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000523111; ENSP00000428209; ENSG00000169139.

GeneID

7336.

KEGG

hsa:7336.

UCSC

uc003xqm.3. human.

Organism-specific databases

CTD

7336.

GeneCards

GC08P048970.

HGNC

HGNC:12495. UBE2V2.

MIM

603001. gene.

neXtProt

NX_Q15819.

PharmGKB

PA37143.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG239185.

HOVERGEN

HBG054552.

InParanoid

Q15819.

KO

K10704.

OMA

IPILAKW.

OrthoDB

EOG4VHK75.

PhylomeDB

Q15819.

Enzyme and pathway databases

Reactome

REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q15819.

Bgee

Q15819.

CleanEx

HS_UBE2V2.

Genevestigator

Q15819.

GermOnline

ENSG00000169139. 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

ChEMBL

CHEMBL5235.

ChiTaRS

UBE2V2. human.

EvolutionaryTrace

Q15819.

GenomeRNAi

7336.

NextBio

28718.

SOURCE

Search...

Entry information

Entry name

UB2V2_HUMAN

Accession

Primary (citable) accession number: Q15819

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 120 of the entry and version 4 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.