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UniProtKB/Swiss-Prot entry Q6ZWZ2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name UB2R2_MOUSE
Primary accession number Q6ZWZ2
Secondary accession numbers Q8BW18 Q8VDE5
Integrated into Swiss-Prot on April 3, 2007
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 47)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 R2
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase R2
Ubiquitin carrier protein R2
E2-CDC34B
Gene name
Name: Ube2r2
Synonyms: Cdc34b, Ubc3b
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1038/sj.onc.1205574; PubMed=12037680 [NCBI, ExPASy, EBI, Israel, Japan]
Semplici F., Meggio F., Pinna L.A., Oliviero S.;
"CK2-dependent phosphorylation of the E2 ubiquitin conjugating enzyme UBC3B induces its interaction with beta-TrCP and enhances beta-catenin degradation.";
Oncogene 21:3978-3987(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Liver, Lung, and Pancreas;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
The mouse genome sequencing consortium;
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II;
TISSUE=Mammary tumor;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ240086; CAC80335.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK003550; BAB22850.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK007517; BAB25085.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075703; BAC35899.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK075714; BAC35904.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL807823; CAM20979.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL954379; CAM20979.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL807823; CAM27658.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL954379; CAM27658.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011112; AAH11112.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_080551.1; -.
UniGene Mm.389540
3D structure databases
HSSP P50550; 1A3S. [HSSP ENTRY / PDB]
SMR Q6ZWZ2; 9-181.
ModBase Q6ZWZ2.
PTM databases
PhosphoSite Q6ZWZ2; -.
Organism-specific databases
MGI MGI:1914865; Ube2r2.
Gene expression databases
ArrayExpress Q6ZWZ2; -.
CleanEx MM_UBE2R2; -.
Ontologies
GO
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from electronic annotation from EC).
GO:0043687; Biological process: post-translational protein modification (inferred from electronic annotation from InterPro).
GO:0051246; Biological process: regulation of protein metabolic process (inferred from electronic annotation from InterPro).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.
Gene3D G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
PANTHER PTHR11621; UBQ-conjugat_E2; 1.
Pfam PF00179; UQ_con; 1.
Pfam graphical view of domain structure.
ProDom PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00212; UBCc; 1.
SMART graphical view of domain structure.
PROSITE PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q6ZWZ2.
Genome annotation databases
Ensembl ENSMUSG00000036241; Mus musculus. [Contig view]
GeneID 67615; -.
KEGG mmu:67615; -.
Phylogenomic databases
HOVERGEN Q6ZWZ2; -.
Other
NextBio 325049; -.
SOURCE Ube2r2; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Ligase; Phosphoprotein; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   238  238     Ubiquitin-conjugating enzyme E2 R2. PRO_0000280514
COMPBIAS   200   238  39     Asp/Glu-rich (acidic). 
ACT_SITE   93    93        Glycyl thioester intermediate (By similarity). 
MOD_RES   233   233        Phosphoserine; by CK2 (By similarity). 
CONFLICT   16    16        E -> D (in Ref. 2; BAC35899). 
CONFLICT   29    29        R -> L (in Ref. 2; BAC35899). 
CONFLICT   33    33        V -> L (in Ref. 2; BAC35899). 
CONFLICT   35    35        E -> Y (in Ref. 2; BAC35899). 
CONFLICT   37    37        D -> Y (in Ref. 2; BAC35899). 
CONFLICT   149   149        R -> T (in Ref. 1; CAC80335). 
Sequence information
Length: 238 AA [This is the length of the unprocessed precursor] Molecular weight: 27166 Da [This is the MW of the unprocessed precursor] CRC64: E896CF0116A56308 [This is a checksum on the sequence]
        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 

Q6ZWZ2 in FASTA format

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