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UniProtKB/Swiss-Prot entry Q7TSS2


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

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Entry information
Entry name UB2Q1_MOUSE
Primary accession number Q7TSS2
Secondary accession numbers Q3UIY3 Q6P913 Q80UT5 Q8K2T0 Q9D7E1
Integrated into Swiss-Prot on February 21, 2006
Sequence was last modified on February 21, 2006 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 41)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 Q1
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase Q1
Ubiquitin carrier protein Q1
Gene name
Name: Ube2q1
Synonyms: Ube2q
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] (ISOFORM 1).
STRAIN=129/Sv;
Altmann M.E., Schulze E., Adham I.M., Koehler M., Engel W.;
"Isolation and characterization of the human UBE2Q gene and its murine ortholog.";
Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-422 (ISOFORM 1).
TISSUE=Brain, Mammary gland, and Thymus;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-422 (ISOFORM 1).
STRAIN=C57BL/6J;
TISSUE=Fetal heart, and Tongue;
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).
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
AY112699; AAM60815.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK009324; BAB26217.2; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK146707; BAE27373.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030044; AAH30044.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC051487; AAH51487.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC060966; AAH60966.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC082275; AAH82275.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_081591.3; -.
UniGene Mm.41438
3D structure databases
SMR Q7TSS2; 248-409.
ModBase Q7TSS2.
PTM databases
PhosphoSite Q7TSS2; -.
Organism-specific databases
MGI MGI:1917343; Ube2q1.
Gene expression databases
ArrayExpress Q7TSS2; -.
CleanEx MM_UBE2Q1; -.
GermOnline ENSMUSG00000042572; Mus musculus.
Ontologies
GO
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from electronic annotation from EC).
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; FALSE_NEG.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q7TSS2.
ProtoNet Q7TSS2.
Genome annotation databases
Ensembl ENSMUSG00000042572; Mus musculus. [Contig view]
GeneID 70093; -.
KEGG mmu:70093; -.
Phylogenomic databases
HOGENOM Q7TSS2; -.
HOVERGEN Q7TSS2; -.
Other
NextBio 330988; -.
SOURCE Ube2q1; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; ATP-binding; Ligase; Nucleotide-binding; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   422  422     Ubiquitin-conjugating enzyme E2 Q1. PRO_0000223877
ACT_SITE   351   351        Glycyl thioester intermediate (By similarity). 
VAR_SEQ   1   169        Missing (in isoform 2). VSP_017297
CONFLICT   121   121        V -> G (in Ref. 1; AAM60815). 
CONFLICT   125   126        DP -> AL (in Ref. 1; AAM60815). 
CONFLICT   139   139        K -> R (in Ref. 1; AAM60815). 
Sequence information
Length: 422 AA [This is the length of the unprocessed precursor] Molecular weight: 46173 Da [This is the MW of the unprocessed precursor] CRC64: 845897861B36971F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MQQPQPQGQQ QPGPGQQLGV QGAAPGAGGG PGGGPGPGPC LRRELKLLES IFHRGHERFR 

        70         80         90        100        110        120 
IASACLDELS CEFLLAGAGG AGAGAAPGPH LPSRGSVPGD PVRIHCNITE SYPAVPPIWS 

       130        140        150        160        170        180 
VESDDPNLAA VLERLVDIKK GNTLLLQHLK RIISDLCKLY NLPQHPDVEM LDQPLPAEQC 

       190        200        210        220        230        240 
TQEEVSSEDE DEEMPEDTED LDHYEMKEEE PAEGKKSEDD GIGKENLAIL EKIKKNQRQD 

       250        260        270        280        290        300 
YLNGAVSGSV QATDRLMKEL RDIYRSQSFK GGNYAVELVN DSLYDWNVKL LKVDQDSALH 

       310        320        330        340        350        360 
NDLQILKEKE GADFILLNFS FKDNFPFDPP FVRVVSPVLS GGYVLGGGAI CMELLTKQGW 

       370        380        390        400        410        420 
SSAYSIESVI MQISATLVKG KARVQFGANK SQYSLTRAQQ SYKSLVQIHE KNGWYTPPKE 


DG 

Q7TSS2 in FASTA format

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