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UniProtKB/Swiss-Prot entry P54103


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

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Entry information
Entry name DNJC2_MOUSE
Primary accession number P54103
Secondary accession number Q61866
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on March 6, 2007 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 65)
Name and origin of the protein
Protein name DnaJ homolog subfamily C member 2
Synonyms Zuotin-related factor 1
Mouse Id associate 1
MIDA1
Gene name
Name: Dnajc2
Synonyms: Mida1, Zrf1
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1074/jbc.270.42.24818; PubMed=7559602 [NCBI, ExPASy, EBI, Israel, Japan]
Shoji W., Inoue T., Yamamoto T., Obinata M.;
"MIDA1, a protein associated with Id, regulates cell growth.";
J. Biol. Chem. 270:24818-24825(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
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 MRNA].
STRAIN=C57BL/6;
TISSUE=Brain;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-514, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1006/geno.1995.9969; PubMed=8666407 [NCBI, ExPASy, EBI, Israel, Japan]
Hughes R., Chan F.Y., White R.A., Zon L.I.;
"Cloning and chromosomal localization of a mouse cDNA with homology to the Saccharomyces cerevisiae gene zuotin.";
Genomics 29:546-550(1995).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; THR-48; SER-49; SER-60 AND SER-63, AND MASS SPECTROMETRY.
DOI=10.1021/pr070122r; PubMed=17622165 [NCBI, ExPASy, EBI, Israel, Japan]
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
"A differential phosphoproteomic analysis of retinoic acid-treated P19 cells.";
J. Proteome Res. 6:3174-3186(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
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
D63784; BAA09854.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK131964; BAE20907.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC052027; AAH52027.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U53208; AAC52486.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00126317; -.
PIR A57591; A57591.
RefSeq NP_033610.1; -.
UniGene Mm.266312
3D structure databases
HSSP P25685; 1HDJ. [HSSP ENTRY / PDB]
ModBase P54103.
PTM databases
PhosphoSite P54103; -.
Organism-specific databases
MGI MGI:99470; Dnajc2.
Gene expression databases
ArrayExpress P54103; -.
Bgee P54103; -.
CleanEx MM_DNAJC2; -.
GermOnline ENSMUSG00000029014; Mus musculus.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from InterPro).
GO:0031072; Molecular function: heat shock protein binding (inferred from electronic annotation from InterPro).
GO:0006260; Biological process: DNA replication (inferred from mutant phenotype from MGI).
GO:0000085; Biological process: G2 phase of mitotic cell cycle (inferred from mutant phenotype from MGI).
GO:0045449; Biological process: regulation of transcription (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001623; DnaJ_N.
IPR018253; Heat_shock_DnaJ_CS.
IPR012287; Homeodomain-rel.
IPR015609; Hsp40/DnaJ_Rel.
IPR014778; Myb_DNA-bd.
IPR001005; SANT_DNA-bd.
IPR017884; SANT_eukarya.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
G3DSA:1.10.10.60; Homeodomain-rel; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
PF00249; Myb_DNA-binding; 2.
Pfam graphical view of domain structure.
SMART SM00271; DnaJ; 1.
SM00717; SANT; 2.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; 1.
PS50076; DNAJ_2; 1.
PS51293; SANT; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE P54103; -.
Genome annotation databases
Ensembl ENSMUSG00000029014; Mus musculus. [Contig view]
GeneID 22791; -.
KEGG mmu:22791; -.
Phylogenomic databases
HOVERGEN P54103; -.
OMA P54103; RSKKDCM.
Other
NextBio 303379; -.
SOURCE Dnajc2; Mus musculus.
ProtoNet P54103.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chaperone; Nucleus; Phosphoprotein; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed (By similarity). 
CHAIN   2   621  620     DnaJ homolog subfamily C member 2. PRO_0000071124
DOMAIN   88   161  74     J. 
DOMAIN   449   511  63     SANT 1. 
DOMAIN   549   604  56     SANT 2. 
MOD_RES   47    47        Phosphoserine. 
MOD_RES   48    48        Phosphothreonine. 
MOD_RES   49    49        Phosphoserine. 
MOD_RES   60    60        Phosphoserine. 
MOD_RES   63    63        Phosphoserine. 
CONFLICT   473   473        T -> R (in Ref. 4; AAC52486). 
CONFLICT   478   478        E -> D (in Ref. 4; AAC52486). 
CONFLICT   502   514        KAKSLQKLDPHQK -> EVRGPKSWGSSKR (in Ref. 4; AAC52486). 
Sequence information
Length: 621 AA [This is the length of the unprocessed precursor] Molecular weight: 71722 Da [This is the MW of the unprocessed precursor] CRC64: 0FFC511028EA1C41 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLLLPSAAEG QGTAITHALT SASSVCQVEP VGRWFEAFVK RRNRNASTSF QELEDKKELS 

        70         80         90        100        110        120 
EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY TATQRQIKAA HKAMVLKHHP 

       130        140        150        160        170        180 
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFQ 

       190        200        210        220        230        240 
VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDAFYSFWYN FDSWREFSYL DEEEKEKAEC 

       250        260        270        280        290        300 
RDERKWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE 

       310        320        330        340        350        360 
ARRKEQEAKE KQRQAELEAV RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNSC 

       370        380        390        400        410        420 
KSWNHFSDNE ADRVKMMEEV EKLCDRLELA SLQGLNEILA SSTREVGKAA LEKQIEEVNE 

       430        440        450        460        470        480 
QMRREKEEAD ARMRQASKNA EKSTGGSGSG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI 

       490        500        510        520        530        540 
ANYMNIHSSS GVKRTAKDVI SKAKSLQKLD PHQKDDINKK AFDKFKKEHG VASQADSAAP 

       550        560        570        580        590        600 
SERFEGPCID STPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMRRYKELV 

       610        620 
EMVKAKKAAQ EQVLNASRAR K 

P54103 in FASTA format

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