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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.12
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
PTM	Acetylation
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. Source: HGNC cell proliferation Traceable author statement. Source: ProtInc protein polyubiquitination Traceable author statement. Source: ProtInc regulation of DNA repair Traceable author statement. Source: ProtInc
Cellular component	UBC13-MMS2 complex Inferred from direct assay. Source: HGNC cytoplasm Traceable author statement. Source: HGNC nucleus Inferred from direct assay. Source: HGNC
Molecular function	acid-amino acid ligase activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.14. Source: IntAct
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

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.10

Modified residue

72

1

N6-acetyllysine Ref.11

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

9 – 23

15

Beta strand

27 – 38

12

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 – 127

13

Turn

129 – 133

5

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: 9199207] [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: 9705497] [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: 15489334] [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: 12665801] [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: 10089880] [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: 14562038] [Abstract] Cited for: FUNCTION, INTERACTION WITH UBE2N AND CHFR.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-72, MASS SPECTROMETRY.
[12]	"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: 20061386] [Abstract] Cited for: FUNCTION.
[13]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]	"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: 11473255] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	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	[»]

ProteinModelPortal

Q15819.

SMR

Q15819. Positions 6-145.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29830N.

IntAct

Q15819. 19 interactions.

MINT

MINT-1368221.

STRING

Q15819.

PTM databases

PhosphoSite

Q15819.

Polymorphism databases

DMDM

51701935.

Proteomic databases

PRIDE

Q15819.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324746; ENSP00000326473; ENSG00000169139.

GeneID

7336.

KEGG

hsa:7336.

UCSC

uc003xqm.1. human.

Organism-specific databases

CTD

7336.

GeneCards

GC08P048970.

H-InvDB

HIX0007493.

HGNC

HGNC:12495. UBE2V2.

MIM

603001. gene.

neXtProt

NX_Q15819.

GenAtlas

Search...

Phylogenomic databases

GeneTree

ENSGT00390000009008.

HOGENOM

HBG756483.

HOVERGEN

HBG054552.

InParanoid

Q15819.

OMA

ENRIYSV.

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

InterPro

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

Gene3D

G3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.

KO

K10704.

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

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:	January 25, 2012
This is version 106 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.