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UniProtKB/Swiss-Prot entry P31689


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

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Entry information
Entry name DNJA1_HUMAN
Primary accession number P31689
Secondary accession numbers None
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on October 1, 1996 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 93)
Name and origin of the protein
Protein name DnaJ homolog subfamily A member 1
Synonyms Heat shock 40 kDa protein 4
DnaJ protein homolog 2
HDJ-2
HSJ-2
HSDJ
Gene name
Name: DNAJA1
Synonyms: DNAJ2, HDJ2, HSJ2, HSPF4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0167-4781(93)90104-L; PubMed=8334161 [NCBI, ExPASy, EBI, Israel, Japan]
Oh S., Iwahori A., Kato S.;
"Human cDNA encoding DnaJ protein homologue.";
Biochim. Biophys. Acta 1174:114-116(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0167-4781(93)90103-K; PubMed=8334160 [NCBI, ExPASy, EBI, Israel, Japan]
Chellaiah A., Davis A., Mohanakumar T.;
"Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein.";
Biochim. Biophys. Acta 1174:111-113(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
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).
[5]
CHARACTERIZATION, AND ISOPRENYLATION AT CYS-394.
PubMed=9192730 [NCBI, ExPASy, EBI, Israel, Japan]
Kanazawa M., Terada K., Kato S., Mori M.;
"HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria.";
J. Biochem. 121:890-895(1997).
[6]
CHARACTERIZATION.
DOI=10.1074/jbc.M002021200; PubMed=10816573 [NCBI, ExPASy, EBI, Israel, Japan]
Terada K., Mori M.;
"Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70.";
J. Biol. Chem. 275:24728-24734(2000).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, AND MASS SPECTROMETRY.
DOI=10.1038/nbt1046; PubMed=15592455 [NCBI, ExPASy, EBI, Israel, Japan]
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
Nat. Biotechnol. 23:94-101(2005).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-340, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
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
D13388; BAA02656.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L08069; AAC37517.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT007292; AAP35956.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008182; AAH08182.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S34630; S34630.
RefSeq NP_001530.1; -.
UniGene Hs.445203
3D structure databases
HSSP P25685; 1HDJ. [HSSP ENTRY / PDB]
SMR P31689; 3-68.
ModBase P31689.
Protein-protein interaction databases
IntAct P31689; -.
PTM databases
PhosphoSite P31689; -.
Organism-specific databases
HGNC HGNC:5229; DNAJA1.
GenAtlas DNAJA1.
HPA HPA001306; -.
MIM 602837; gene. [NCBI / EBI]
PharmGKB PA27408; -.
GeneCards P31689.
Gene expression databases
ArrayExpress P31689; -.
CleanEx HS_DNAJA1; -.
GermOnline ENSG00000086061; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from HPA).
GO:0005856; Cellular component: cytoskeleton (inferred from direct assay from HPA).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0031072; Molecular function: heat shock protein binding (inferred from electronic annotation from InterPro).
GO:0050750; Molecular function: low-density lipoprotein receptor binding (inferred from direct assay from MGI).
GO:0051082; Molecular function: unfolded protein binding (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006457; Biological process: protein folding (traceable author statement from ProtInc).
GO:0006986; Biological process: response to unfolded protein (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002939; DnaJ_C.
IPR001623; DnaJ_N.
IPR015609; Hsp40/DnaJ_Rel.
IPR003095; Hsp_DnaJ.
IPR001305; HSP_DnaJ_cys-rich.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
PF01556; DnaJ_C; 1.
PF00684; DnaJ_CXXCXGXG; 1.
Pfam graphical view of domain structure.
PRINTS PR00625; DNAJPROTEIN.
SMART SM00271; DnaJ; 1.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; 1.
PS50076; DNAJ_2; 1.
PS51188; ZF_CR; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P31689.
ProtoNet P31689.
Proteomic databases
PeptideAtlas P31689; -.
Genome annotation databases
Ensembl ENSG00000086061; Homo sapiens. [Contig view]
GeneID 3301; -.
KEGG hsa:3301; -.
Phylogenomic databases
HOGENOM P31689; -.
HOVERGEN P31689; -.
Other
LinkHub P31689; -.
NextBio 13099; -.
SOURCE DNAJA1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Chaperone; Lipoprotein; Membrane; Metal-binding; Phosphoprotein; Prenylation; Repeat; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   397  397     DnaJ homolog subfamily A member 1. PRO_0000071008
DOMAIN   6    68  63     J. 
REPEAT   134   141  8     CXXCXGXG motif. 
REPEAT   150   157  8     CXXCXGXG motif. 
REPEAT   177   184  8     CXXCXGXG motif. 
REPEAT   193   200  8     CXXCXGXG motif. 
ZN_FING   121   205  85     CR-type. 
COMPBIAS   75    96  22     Gly-rich. 
METAL   134   134        Zinc 1 (By similarity). 
METAL   137   137        Zinc 1 (By similarity). 
METAL   150   150        Zinc 2 (By similarity). 
METAL   153   153        Zinc 2 (By similarity). 
METAL   177   177        Zinc 2 (By similarity). 
METAL   180   180        Zinc 2 (By similarity). 
METAL   193   193        Zinc 1 (By similarity). 
METAL   196   196        Zinc 1 (By similarity). 
MOD_RES   83    83        Phosphoserine. 
MOD_RES   335   335        Phosphoserine. 
MOD_RES   340   340        Phosphoserine. 
MOD_RES   381   381        Phosphotyrosine. 
LIPID   394   394        S-farnesyl cysteine. 
MUTAGEN   394   394        C->S: Loss of farnesylation. 
CONFLICT   274   274        Q -> H (in Ref. 1; BAA02656). 
Sequence information
Length: 397 AA [This is the length of the unprocessed precursor] Molecular weight: 44868 Da [This is the MW of the unprocessed precursor] CRC64: A899C06F6BB32780 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLSDAKK 

        70         80         90        100        110        120 
RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR ERRGKNVVHQ LSVTLEDLYN 

       130        140        150        160        170        180 
GATRKLALQK NVICDKCEGR GGKKGAVECC PNCRGTGMQI RIHQIGPGMV QQIQSVCMEC 

       190        200        210        220        230        240 
QGHGERISPK DRCKSCNGRK IVREKKILEV HIDKGMKDGQ KITFHGEGDQ EPGLEPGDII 

       250        260        270        280        290        300 
IVLDQKDHAV FTRRGEDLFM CMDIQLVEAL CGFQKPISTL DNRTIVITSH PGQIVKHGDI 

       310        320        330        340        350        360 
KCVLNEGMPI YRRPYEKGRL IIEFKVNFPE NGFLSPDKLS LLEKLLPERK EVEETDEMDQ 

       370        380        390 
VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS 

P31689 in FASTA format

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