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P31689 (DNJA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 156. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria. HAMAP-Rule MF_01152

Subcellular location

Membrane; Lipid-anchor Potential HAMAP-Rule MF_01152.

Sequence similarities

Contains 1 CR-type zinc finger.

Contains 1 J domain.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainRepeat
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionChaperone
   PTMAcetylation
Lipoprotein
Methylation
Phosphoprotein
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processandrogen receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein folding

Traceable author statement Ref.2. Source: ProtInc

response to heat

Inferred from electronic annotation. Source: InterPro

response to unfolded protein

Traceable author statement Ref.2. Source: ProtInc

sperm motility

Inferred from electronic annotation. Source: Ensembl

spermatogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from direct assay PubMed 21231916. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

membrane

Inferred from direct assay PubMed 21231916. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: InterPro

chaperone binding

Inferred from physical interaction PubMed 21231916. Source: UniProt

low-density lipoprotein particle receptor binding

Inferred from direct assay PubMed 15082773. Source: MGI

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 22085931. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AICDAQ9GZX76EBI-347834,EBI-3834328

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P31689-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P31689-2)

Also known as: nDnaJA1;

The sequence of this isoform differs from the canonical sequence as follows:
     327-397: NFPENGFLSP...PRGGVQCQTS → SCNVL
Note: High expression in testis and lung but low in thymus, prostate, colon and liver.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394DnaJ homolog subfamily A member 1 HAMAP-Rule MF_01152
PRO_0000071008
Propeptide395 – 3973Removed in mature form Probable
PRO_0000393941

Regions

Domain6 – 6863J
Repeat134 – 1418CXXCXGXG motif HAMAP-Rule MF_01152
Repeat150 – 1578CXXCXGXG motif HAMAP-Rule MF_01152
Repeat177 – 1848CXXCXGXG motif HAMAP-Rule MF_01152
Repeat193 – 2008CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger121 – 20585CR-type HAMAP-Rule MF_01152
Compositional bias75 – 9622Gly-rich HAMAP-Rule MF_01152

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 residue661N6-acetyllysine Ref.16
Modified residue831Phosphoserine Ref.11 Ref.12 Ref.15 Ref.17
Modified residue3351Phosphoserine Ref.11 Ref.12 Ref.15 Ref.17 Ref.19
Modified residue3811Phosphotyrosine Ref.10
Modified residue3941Cysteine methyl ester Probable
Lipidation3941S-farnesyl cysteine Ref.8

Natural variations

Alternative sequence327 – 39771NFPEN…QCQTS → SCNVL in isoform 2.
VSP_046566

Experimental info

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

Secondary structure

............. 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 (nDnaJA1) [UniParc].

Checksum: E3FFC159AA4BE7C7
Show »

FASTA33137,045

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Expression of a novel DnaJA1 alternative splicing in human testis and sperm."
Hu Y., Zhou Z., Huang X., Xu M., Lu L., Xu Z., Li J., Sha J.
Int. J. Androl. 27:343-349(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
Tissue: Testis.
[4]"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] (ISOFORM 1).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Amygdala.
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[8]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, ISOPRENYLATION AT CYS-394.
[9]"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] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[16]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83 AND SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D13388 mRNA. Translation: BAA02656.1.
L08069 mRNA. Translation: AAC37517.1.
AY186741 mRNA. Translation: AAO31694.1.
BT007292 mRNA. Translation: AAP35956.1.
AK289623 mRNA. Translation: BAF82312.1.
CH471071 Genomic DNA. Translation: EAW58525.1.
CH471071 Genomic DNA. Translation: EAW58526.1.
BC008182 mRNA. Translation: AAH08182.1.
CCDSCCDS6533.1. [P31689-1]
PIRS34630.
RefSeqNP_001530.1. NM_001539.2. [P31689-1]
UniGeneHs.445203.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LO1NMR-A1-70[»]
2M6YNMR-A1-67[»]
ProteinModelPortalP31689.
SMRP31689. Positions 1-346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109534. 102 interactions.
IntActP31689. 44 interactions.
MINTMINT-5004184.
STRING9606.ENSP00000369127.

Chemistry

ChEMBLCHEMBL2189122.

PTM databases

PhosphoSiteP31689.

Polymorphism databases

DMDM1706474.

Proteomic databases

MaxQBP31689.
PaxDbP31689.
PeptideAtlasP31689.
PRIDEP31689.

Protocols and materials databases

DNASU3301.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330899; ENSP00000369127; ENSG00000086061. [P31689-1]
GeneID3301.
KEGGhsa:3301.
UCSCuc003zsd.1. human. [P31689-1]

Organism-specific databases

CTD3301.
GeneCardsGC09P033025.
H-InvDBHIX0007975.
HGNCHGNC:5229. DNAJA1.
HPAHPA001306.
MIM602837. gene.
neXtProtNX_P31689.
PharmGKBPA31536.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0484.
HOGENOMHOG000226718.
HOVERGENHBG066727.
InParanoidP31689.
KOK09502.
OMAGMQVRIQ.
OrthoDBEOG7XM2XK.
PhylomeDBP31689.
TreeFamTF105141.

Gene expression databases

ArrayExpressP31689.
BgeeP31689.
CleanExHS_DNAJA1.
GenevestigatorP31689.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPMF_01152. DnaJ.
InterProIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDNAJA1.
GenomeRNAi3301.
NextBio13099.
PROP31689.
SOURCESearch...

Entry information

Entry nameDNJA1_HUMAN
AccessionPrimary (citable) accession number: P31689
Secondary accession number(s): Q5T7Q0, Q86TL9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 156 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 9

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