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Q9D2M8 (UB2V2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 variant 2
Alternative name(s):
Ubc-like protein MMS2
Gene names
Name:Ube2v2
Synonyms:Mms2, Uev2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length145 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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.1

Subunit structure

Heterodimer with UBE2N. Binds CHFR By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence caution

The sequence AAH29742.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9D2M8-1)

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: Q9D2M8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     56-97: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 145144Ubiquitin-conjugating enzyme E2 variant 2
PRO_0000082603

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Natural variations

Alternative sequence56 – 9742Missing in isoform 2.
VSP_011529

Experimental info

Sequence conflict161L → W in BAC26094. Ref.2
Sequence conflict381D → N in BAC25968. Ref.2
Sequence conflict381D → N in BAC27311. Ref.2
Sequence conflict381D → N in BAC28128. Ref.2
Sequence conflict381D → N in BAB31753. Ref.3
Sequence conflict761A → D in AAG22084. Ref.1

Sequences

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

Last modified January 23, 2007. Version 4.
Checksum: 98D63173902C6611

FASTA14516,367
        10         20         30         40         50         60 
MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRTNYEN 

        70         80         90        100        110        120 
RIYSLKVECG SKYPEAPPSV RFVTKINMNG INNSSGMVDA RSIPVLAKWQ NSYSIKVILQ 

       130        140 
ELRRLMMSKE NMKLPQPPEG QTYNN 

« Hide

Isoform 2 [UniParc].

Checksum: 8EF809082980A3DE
Show »

FASTA10311,674

References

« Hide 'large scale' references
[1]"Molecular cloning and functional characterization of two murine cDNAs which encode Ubc variants involved in DNA repair and mutagenesis."
Franko J., Ashley C., Xiao W.
Biochim. Biophys. Acta 1519:70-77(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Embryo, Fetus and Skin.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"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).
Strain: C57BL/6.
Tissue: Embryonic germ cell, Fetal brain and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF303828 mRNA. Translation: AAG22084.1.
AK017786 mRNA. Translation: BAB30932.1.
AK019486 mRNA. Translation: BAB31753.1.
AK028472 mRNA. Translation: BAC25968.1.
AK028742 mRNA. Translation: BAC26094.1.
AK031233 mRNA. Translation: BAC27311.1.
AK033016 mRNA. Translation: BAC28128.1.
CT010522 Genomic DNA. Translation: CAO77942.1.
BC029742 mRNA. Translation: AAH29742.1. Different initiation.
BC058374 mRNA. Translation: AAH58374.1.
BC083098 mRNA. Translation: AAH83098.1.
CCDSCCDS37265.1. [Q9D2M8-1]
CCDS49771.1. [Q9D2M8-2]
RefSeqNP_001152823.1. NM_001159351.1. [Q9D2M8-2]
NP_076074.2. NM_023585.4. [Q9D2M8-1]
UniGeneMm.235407.
Mm.390775.

3D structure databases

ProteinModelPortalQ9D2M8.
SMRQ9D2M8. Positions 6-145.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid214171. 4 interactions.
IntActQ9D2M8. 3 interactions.

PTM databases

PhosphoSiteQ9D2M8.

Proteomic databases

MaxQBQ9D2M8.
PaxDbQ9D2M8.
PRIDEQ9D2M8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000115776; ENSMUSP00000111442; ENSMUSG00000022674. [Q9D2M8-2]
ENSMUST00000115777; ENSMUSP00000111443; ENSMUSG00000022674. [Q9D2M8-1]
GeneID70620.
KEGGmmu:70620.
UCSCuc007yhp.2. mouse. [Q9D2M8-1]
uc007yhq.2. mouse. [Q9D2M8-2]

Organism-specific databases

CTD7336.
MGIMGI:1917870. Ube2v2.

Phylogenomic databases

eggNOGNOG239185.
GeneTreeENSGT00740000115534.
HOVERGENHBG054552.
InParanoidQ9D2M8.
KOK10704.
OMAIPILAKW.
OrthoDBEOG77M8R5.
PhylomeDBQ9D2M8.
TreeFamTF316971.

Gene expression databases

ArrayExpressQ9D2M8.
BgeeQ9D2M8.
CleanExMM_UBE2V2.
GenevestigatorQ9D2M8.

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

NextBio331994.
PROQ9D2M8.
SOURCESearch...

Entry information

Entry nameUB2V2_MOUSE
AccessionPrimary (citable) accession number: Q9D2M8
Secondary accession number(s): A6X924 expand/collapse secondary AC list , Q8BGH6, Q8CE99, Q8K2V7, Q9CYD7, Q9ERI8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 112 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot