Reviewed, UniProtKB/Swiss-Prot P31689 (DNJA1_HUMAN)

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Complete proteome]

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.
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 Phosphoprotein Prenylation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	protein folding Ref.2 Traceable author statement. Source: ProtInc response to unfolded protein Ref.2 Traceable author statement. Source: ProtInc
Cellular component	anchored to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	heat shock protein binding Inferred from electronic annotation. Source: InterPro low-density lipoprotein receptor binding Inferred from direct assay. Source: MGI unfolded protein binding Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
LSM2	Q9Y333	2	EBI-347834,EBI-347416
OSGEP	Q9NPF4	1	EBI-347834,EBI-1056510
UQCRC1	P31930	1	EBI-347834,EBI-1052596

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 397	397	DnaJ homolog subfamily A member 1		PRO_0000071008
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.15
	Modified residue	66	1	N6-acetyllysine Ref.15
	Modified residue	83	1	Phosphoserine Ref.9 Ref.10 Ref.13 Ref.14
	Modified residue	335	1	Phosphoserine Ref.9 Ref.10 Ref.13 Ref.14 Ref.11
	Modified residue	340	1	Phosphoserine Ref.11
	Modified residue	381	1	Phosphotyrosine Ref.7 Ref.8
	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)
	P31689-1 [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.
[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.
IPI	IPI00012535.
PIR	S34630.
RefSeq	NP_001530.1.
UniGene	Hs.445203 Hs.707338
3D structure databases
SMR	P31689. Positions 3-68, 4-95, 102-330.
ModBase	Search...
Protein-protein interaction databases
IntAct	P31689. 35 interactions.
STRING	P31689.
PTM databases
PhosphoSite	P31689.
Proteomic databases
PeptideAtlas	P31689.
PRIDE	P31689.
Genome annotation databases
Ensembl	ENST00000330899; ENSP00000369127; ENSG00000086061; Homo sapiens. [Genome view]
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.
PharmGKB	PA27408.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG08536.
HOGENOM	HBG635315.
HOVERGEN	P31689.
InParanoid	P31689.
OMA	HSVFTRR.
OrthoDB	EOG951H9B.
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	IPR002939. 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]
Gene3D	G3DSA:1.10.287.110. DnaJ_N. 1 hit.
PANTHER	PTHR11821. Hsp40/DnaJ_Rel. 1 hit.
Pfam	PF00226. DnaJ. 1 hit. PF01556. DnaJ_C. 1 hit. PF00684. DnaJ_CXXCXGXG. 1 hit. [Graphical view]
PRINTS	PR00625. DNAJPROTEIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
PROSITE	PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. PS51188. ZF_CR. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
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:	January 19, 2010
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.