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Q6ZWZ2 (UB2R2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 R2
EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein R2
Ubiquitin-conjugating enzyme E2-CDC34B
Ubiquitin-protein ligase R2
Gene names
Name:Ube2r2
Synonyms:Cdc34b, Ubc3b
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length238 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes monoubiquitination and 'Lys-48'-linked polyubiquitination. May be involved in degradation of katenin By similarity.

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

When phosphorylated, interacts with beta-TrCP (BTRC) By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 238238Ubiquitin-conjugating enzyme E2 R2
PRO_0000280514

Regions

Compositional bias200 – 23839Asp/Glu-rich (acidic)

Sites

Active site931Glycyl thioester intermediate By similarity

Amino acid modifications

Modified residue2331Phosphoserine; by CK2 By similarity

Experimental info

Sequence conflict161E → D in BAC35899. Ref.2
Sequence conflict291R → L in BAC35899. Ref.2
Sequence conflict331V → L in BAC35899. Ref.2
Sequence conflict351E → Y in BAC35899. Ref.2
Sequence conflict371D → Y in BAC35899. Ref.2
Sequence conflict1491R → T in CAC80335. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q6ZWZ2 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: E896CF0116A56308

FASTA23827,166
        10         20         30         40         50         60 
MAQQQMTSSQ KALMLELKSL QEEPVEGFRI TLVDESDLYN WEVAIFGPPN TLYEGGYFKA 

        70         80         90        100        110        120 
HIKFPIDYPY SPPTFRFLTK MWHPNIYENG DVCISILHPP VDDPQSGELP SERWNPTQNV 

       130        140        150        160        170        180 
RTILLSVISL LNEPNTFSPA NVDASVMFRK WRDSKGKDKE YAEIIRKQVS ATKAEAEKDG 

       190        200        210        220        230 
VKVPTTLAEY CIKTKVPSND NSSDLLYDDL YDDDIDDEDE EEEDADCYDD DDSGNEES

« Hide

References

« Hide 'large scale' references
[1]"CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation."
Semplici F., Meggio F., Pinna L.A., Oliviero S.
Oncogene 21:3978-3987(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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].
Strain: C57BL/6J.
Tissue: Liver, Lung and Pancreas.
[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].
Strain: Czech II.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ240086 mRNA. Translation: CAC80335.1.
AK003550 mRNA. Translation: BAB22850.1.
AK007517 mRNA. Translation: BAB25085.1.
AK075703 mRNA. Translation: BAC35899.1.
AK075714 mRNA. Translation: BAC35904.1.
AL807823, AL954379 Genomic DNA. Translation: CAM20979.1.
AL807823, AL954379 Genomic DNA. Translation: CAM27658.1.
BC011112 mRNA. Translation: AAH11112.1.
IPIIPI00420771.
RefSeqNP_080551.1. NM_026275.4.
UniGeneMm.389540.

3D structure databases

ProteinModelPortalQ6ZWZ2.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-4609410.

PTM databases

PhosphoSiteQ6ZWZ2.

Proteomic databases

PaxDbQ6ZWZ2.
PRIDEQ6ZWZ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040008; ENSMUSP00000038813; ENSMUSG00000036241.
GeneID67615.
KEGGmmu:67615.
UCSCuc008sij.1. mouse.

Organism-specific databases

CTD54926.
MGIMGI:1914865. Ube2r2.

Phylogenomic databases

eggNOGCOG5078.
GeneTreeENSGT00530000063512.
HOGENOMHOG000233454.
HOVERGENHBG063308.
InParanoidQ6ZWZ2.
KOK02207.
OMANSEETAM.
OrthoDBEOG4DBTFM.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

BgeeQ6ZWZ2.
CleanExMM_UBE2R2.
GenevestigatorQ6ZWZ2.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBE2R2. mouse.
NextBio325049.
SOURCESearch...

Entry information

Entry nameUB2R2_MOUSE
AccessionPrimary (citable) accession number: Q6ZWZ2
Secondary accession number(s): Q8BW18, Q8VDE5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: July 5, 2004
Last modified: May 29, 2013
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents