Q9D2M8 (UB2V2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ubiquitin-conjugating enzyme E2 variant 2

Alternative name(s):
Ubc-like protein MMS2

Gene names

Name:	Ube2v2
Synonyms:	Mms2, Uev2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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 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.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Coding sequence diversity	Alternative splicing
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular function	acid-amino acid ligase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 145	144	Ubiquitin-conjugating enzyme E2 variant 2		PRO_0000082603
Amino acid modifications
	Modified residue	2	1	N-acetylalanine By similarity
	Modified residue	72	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	56 – 97	42	Missing in isoform 2.		VSP_011529
Experimental info
	Sequence conflict	16	1	L → W in BAC26094. Ref.2
	Sequence conflict	38	1	D → N in BAC25968. Ref.2
	Sequence conflict	38	1	D → N in BAC27311. Ref.2
	Sequence conflict	38	1	D → N in BAC28128. Ref.2
	Sequence conflict	38	1	D → N in BAB31753. Ref.3
	Sequence conflict	76	1	A → D in AAG22084. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 98D63173902C6611	FASTA	145	16,367
	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
	Isoform 2 [UniParc]. Checksum: 8EF809082980A3DE	FASTA	103	11,674
	10 20 30 40 50 60 MAVSTGVKVP RNFRLLEELE EGQKGVGDGT VSWGLEDDED MTLTRWTGMI IGPPRVDARS 70 80 90 100 IPVLAKWQNS YSIKVILQEL RRLMMSKENM KLPQPPEGQT YNN

References

	« Hide 'large scale' referencesShow '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: 11406273] [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. , 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: 16141072] [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. , 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: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[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: 15489334] [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.
IPI	IPI00402913. IPI00670546.
RefSeq	NP_001152823.1. NM_001159351.1. NP_076074.2. NM_023585.4. XP_003084687.1. XM_003084639.1.
UniGene	Mm.235407. Mm.390775. Mm.482264.
3D structure databases
ProteinModelPortal	Q9D2M8.
SMR	Q9D2M8. Positions 6-145.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9D2M8. 3 interactions.
STRING	Q9D2M8.
PTM databases
PhosphoSite	Q9D2M8.
Proteomic databases
PRIDE	Q9D2M8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000115776; ENSMUSP00000111442; ENSMUSG00000022674. ENSMUST00000115777; ENSMUSP00000111443; ENSMUSG00000022674.
GeneID	100503412. 70620.
KEGG	mmu:100503412. mmu:70620.
UCSC	uc008oab.1. mouse.
Organism-specific databases
CTD	7336.
MGI	MGI:1917870. Ube2v2.
Phylogenomic databases
GeneTree	ENSGT00390000009008.
HOGENOM	HBG756483.
HOVERGEN	HBG054552.
InParanoid	Q9D2M8.
OMA	ENRIYSV.
PhylomeDB	Q9D2M8.
Gene expression databases
Bgee	Q9D2M8.
CleanEx	MM_UBE2V2.
Genevestigator	Q9D2M8.
GermOnline	ENSMUSG00000068964. Mus musculus.
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	331994.
SOURCE	Search...

Entry information

Entry name

UB2V2_MOUSE

Accession

Primary (citable) accession number: Q9D2M8
Secondary accession number(s): A6X924 , Q8BGH6, Q8CE99, Q8K2V7, Q9CYD7, Q9ERI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 91 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program