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Reviewed, UniProtKB/Swiss-Prot P31689 (DNJA1_HUMAN)

Last modified January 19, 2010. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DnaJ homolog subfamily A member 1
Alternative name(s):
    Heat shock 40 kDa protein 4
    DnaJ protein homolog 2
    HDJ-2
    Heat shock protein J2
      Short name=HSJ-2
    HSDJ
Gene names
Name: DNAJA1
Synonyms: DNAJ2, HDJ2, HSJ2, HSPF4
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria.

Subcellular location

Membrane; Lipid-anchor Potential.

Sequence similarities

Contains 1 CR-type zinc finger.

Contains 1 J domain.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397DnaJ homolog subfamily A member 1
PRO_0000071008

Regions

Domain6 – 6863J
Repeat134 – 1418CXXCXGXG motif
Repeat150 – 1578CXXCXGXG motif
Repeat177 – 1848CXXCXGXG motif
Repeat193 – 2008CXXCXGXG motif
Zinc finger121 – 20585CR-type
Compositional bias75 – 9622Gly-rich

Sites

Metal binding1341Zinc 1 By similarity
Metal binding1371Zinc 1 By similarity
Metal binding1501Zinc 2 By similarity
Metal binding1531Zinc 2 By similarity
Metal binding1771Zinc 2 By similarity
Metal binding1801Zinc 2 By similarity
Metal binding1931Zinc 1 By similarity
Metal binding1961Zinc 1 By similarity

Amino acid modifications

Modified residue441N6-acetyllysine Ref.15
Modified residue661N6-acetyllysine Ref.15
Modified residue831Phosphoserine Ref.9 Ref.10 Ref.13 Ref.14
Modified residue3351Phosphoserine Ref.9 Ref.10 Ref.13 Ref.14 Ref.11
Modified residue3401Phosphoserine Ref.11
Modified residue3811Phosphotyrosine Ref.7 Ref.8
Lipidation3941S-farnesyl cysteine Ref.5

Experimental info

Mutagenesis3941C → S: Loss of farnesylation.
Sequence conflict2741Q → H in BAA02656. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P31689-1 [UniParc].

Last modified October 1, 1996. Version 2.
Checksum: A899C06F6BB32780

FASTA39744,868
        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 

« Hide

References

« Hide 'large scale' references
[1]"Human cDNA encoding DnaJ protein homologue."
Oh S., Iwahori A., Kato S.
Biochim. Biophys. Acta 1174:114-116(1993) [PubMed: 8334161] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of a unique human homologue of the Escherichia coli DNAJ heat shock protein."
Chellaiah A., Davis A., Mohanakumar T.
Biochim. Biophys. Acta 1174:111-113(1993) [PubMed: 8334160] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta.
[5]"HSDJ, a human homolog of DnaJ, is farnesylated and is involved in protein import into mitochondria."
Kanazawa M., Terada K., Kato S., Mori M.
J. Biochem. 121:890-895(1997) [PubMed: 9192730] [Abstract]
Cited for: CHARACTERIZATION, ISOPRENYLATION AT CYS-394.
[6]"Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70."
Terada K., Mori M.
J. Biol. Chem. 275:24728-24734(2000) [PubMed: 10816573] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
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.
Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, MASS SPECTROMETRY.
[8]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
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. expand/collapse author list , 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.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, MASS SPECTROMETRY.
[9]"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."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, MASS SPECTROMETRY.
Tissue: Epithelium.
[10]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, MASS SPECTROMETRY.
[11]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-340, MASS SPECTROMETRY.
[12]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, MASS SPECTROMETRY.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, MASS SPECTROMETRY.
Tissue: T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-44 AND LYS-66, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13388 mRNA. Translation: BAA02656.1.
L08069 mRNA. Translation: AAC37517.1.
BT007292 mRNA. Translation: AAP35956.1.
BC008182 mRNA. Translation: AAH08182.1.
IPIIPI00012535.
PIRS34630.
RefSeqNP_001530.1.
UniGeneHs.445203
Hs.707338

3D structure databases

SMRP31689. Positions 3-68, 4-95, 102-330.
ModBaseSearch...

Protein-protein interaction databases

IntActP31689. 35 interactions.
STRINGP31689.

PTM databases

PhosphoSiteP31689.

Proteomic databases

PeptideAtlasP31689.
PRIDEP31689.

Genome annotation databases

EnsemblENST00000330899; ENSP00000369127; ENSG00000086061; Homo sapiens. [Genome view]
GeneID3301.
KEGGhsa:3301.
UCSCuc003zsd.1. human.

Organism-specific databases

CTD3301.
GeneCardsGC09P033015.
HGNCHGNC:5229. DNAJA1.
HPAHPA001306.
MIM602837. gene.
PharmGKBPA27408.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08536.
HOGENOMHBG635315.
HOVERGENP31689.
InParanoidP31689.
OMAHSVFTRR.
OrthoDBEOG951H9B.
PhylomeDBP31689.

Enzyme and pathway databases

Pathway_Interaction_DBar_tf_pathway. Regulation of Androgen receptor activity.

Gene expression databases

ArrayExpressP31689.
BgeeP31689.
CleanExHS_DNAJA1.
GenevestigatorP31689.
GermOnlineENSG00000086061. Homo sapiens.

Family and domain databases

InterProIPR002939. DnaJ_C.
IPR001623. DnaJ_N.
IPR018253. Heat_shock_DnaJ_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR015609. Hsp40/DnaJ_Rel.
IPR003095. Hsp_DnaJ.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
Gene3DG3DSA:1.10.287.110. DnaJ_N. 1 hit.
PANTHERPTHR11821. Hsp40/DnaJ_Rel. 1 hit.
PfamPF00226. DnaJ. 1 hit.
PF01556. DnaJ_C. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSPR00625. DNAJPROTEIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio13099.
SOURCESearch...

Entry information

Entry nameDNJA1_HUMAN
AccessionPrimary (citable) accession number: P31689
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: January 19, 2010
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents