P31689 (DNJA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	397 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Membrane
Domain	Repeat Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chaperone
PTM	Acetylation Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein folding Traceable author statement. Source: ProtInc response to heat Inferred from electronic annotation. Source: InterPro response to unfolded protein Traceable author statement. Source: ProtInc
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro heat shock protein binding Inferred from electronic annotation. Source: InterPro low-density lipoprotein particle receptor binding Inferred from direct assay. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 394	394	DnaJ homolog subfamily A member 1		PRO_0000071008
	Propeptide	395 – 397	3	Removed in mature form Probable		PRO_0000393941
Regions
	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
	Zinc finger	121 – 205	85	CR-type
	Compositional bias	75 – 96	22	Gly-rich
Sites
	Metal binding	134	1	Zinc 1 By similarity
	Metal binding	137	1	Zinc 1 By similarity
	Metal binding	150	1	Zinc 2 By similarity
	Metal binding	153	1	Zinc 2 By similarity
	Metal binding	177	1	Zinc 2 By similarity
	Metal binding	180	1	Zinc 2 By similarity
	Metal binding	193	1	Zinc 1 By similarity
	Metal binding	196	1	Zinc 1 By similarity
Amino acid modifications
	Modified residue	44	1	N6-acetyllysine Ref.14
	Modified residue	66	1	N6-acetyllysine Ref.14
	Modified residue	83	1	Phosphoserine Ref.9 Ref.10 Ref.12 Ref.13
	Modified residue	335	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.12 Ref.13
	Modified residue	340	1	Phosphoserine Ref.11
	Modified residue	381	1	Phosphotyrosine Ref.7 Ref.8
	Modified residue	394	1	Cysteine methyl ester Probable
	Lipidation	394	1	S-farnesyl cysteine Ref.5
Experimental info
	Mutagenesis	394	1	C → S: Loss of farnesylation.
	Sequence conflict	274	1	Q → H in BAA02656. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P31689 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: A899C06F6BB32780	FASTA	397	44,868
	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

References

	« Hide 'large scale' referencesShow '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. , 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. Tissue: Lung carcinoma.
[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: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[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. Tissue: Cervix carcinoma.
[12]	"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. Tissue: Embryonic kidney.
[13]	"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: Leukemic T-cell.
[14]	"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.
[15]	"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: 21269460] [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. BT007292 mRNA. Translation: AAP35956.1. BC008182 mRNA. Translation: AAH08182.1.
IPI	IPI00012535.
PIR	S34630.
RefSeq	NP_001530.1. NM_001539.2.
UniGene	Hs.445203. Hs.707338.
3D structure databases
ProteinModelPortal	P31689.
SMR	P31689. Positions 3-68, 101-369.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31689. 24 interactions.
MINT	MINT-5004184.
STRING	P31689.
PTM databases
PhosphoSite	P31689.
Polymorphism databases
DMDM	1706474.
Proteomic databases
PeptideAtlas	P31689.
PRIDE	P31689.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000330899; ENSP00000369127; ENSG00000086061.
GeneID	3301.
KEGG	hsa:3301.
UCSC	uc003zsd.1. human.
Organism-specific databases
CTD	3301.
GeneCards	GC09P033015.
HGNC	HGNC:5229. DNAJA1.
HPA	HPA001306.
MIM	602837. gene.
neXtProt	NX_P31689.
PharmGKB	PA27408.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08536.
HOGENOM	HBG635315.
HOVERGEN	HBG066727.
InParanoid	P31689.
OMA	HSVFTRR.
OrthoDB	EOG4RJG1R.
PhylomeDB	P31689.
Enzyme and pathway databases
Pathway_Interaction_DB	ar_tf_pathway. Regulation of Androgen receptor activity.
Gene expression databases
ArrayExpress	P31689.
Bgee	P31689.
CleanEx	HS_DNAJA1.
Genevestigator	P31689.
GermOnline	ENSG00000086061. Homo sapiens.
Family and domain databases
InterPro	IPR012724. DnaJ. IPR002939. DnaJ_C. IPR001623. DnaJ_N. IPR018253. Heat_shock_DnaJ_CS. IPR008971. HSP40/DnaJ_pept-bd. IPR003095. Hsp_DnaJ. IPR001305. HSP_DnaJ_Cys-rich_dom. [Graphical view]
Gene3D	G3DSA:1.10.287.110. DnaJ_N. 1 hit. G3DSA:2.10.230.10. HSP_DnaJ_cys-rich. 1 hit.
KO	K09502.
Pfam	PF00226. DnaJ. 1 hit. PF01556. DnaJ_C. 1 hit. PF00684. DnaJ_CXXCXGXG. 1 hit. [Graphical view]
PRINTS	PR00625. JDOMAIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
SUPFAM	SSF46565. DnaJ_N. 1 hit. SSF49493. HSP40_DnaJ_pep. 2 hits. SSF57938. HSP_DnaJ_cys-rich. 1 hit.
PROSITE	PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. PS51188. ZF_CR. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	13099.
SOURCE	Search...

Entry information

Entry name

DNJA1_HUMAN

Accession

Primary (citable) accession number: P31689

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	December 14, 2011
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.