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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen receptor signaling pathway Inferred from electronic annotation. Source: Compara 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: Compara spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro low-density lipoprotein particle receptor binding Inferred from direct assay PubMed 15082773. Source: MGI metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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

66

1

N6-acetyllysine Ref.12

Modified residue

83

1

Phosphoserine Ref.8 Ref.9 Ref.11 Ref.13

Modified residue

335

1

Phosphoserine Ref.8 Ref.9 Ref.11 Ref.13 Ref.15

Modified residue

381

1

Phosphotyrosine Ref.7

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

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

397

Helix Strand Turn

Details...

Helix

7 – 10

4

Helix

19 – 33

15

Helix

35 – 37

3

Beta strand

39 – 41

3

Helix

42 – 54

13

Helix

58 – 64

7

Turn

65 – 67

3

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-381, MASS SPECTROMETRY.
[8]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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.
[11]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"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, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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, 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. NM_001539.2.

UniGene

Hs.445203.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LO1	NMR	-	A	1-70	[»]

ProteinModelPortal

P31689.

ModBase

Search...

Protein-protein interaction databases

IntAct

P31689. 27 interactions.

MINT

MINT-5004184.

STRING

9606.ENSP00000369127.

PTM databases

PhosphoSite

P31689.

Polymorphism databases

DMDM

1706474.

Proteomic databases

PaxDb

P31689.

PeptideAtlas

P31689.

PRIDE

P31689.

Protocols and materials databases

DNASU

3301.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000330899; ENSP00000369127; ENSG00000086061.

GeneID

3301.

KEGG

hsa:3301.

UCSC

uc003zsd.1. human.

Organism-specific databases

CTD

3301.

GeneCards

GC09P033025.

H-InvDB

HIX0007975.

HGNC

HGNC:5229. DNAJA1.

HPA

HPA001306.

MIM

602837. gene.

neXtProt

NX_P31689.

PharmGKB

PA31536.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0484.

HOGENOM

HOG000226718.

HOVERGEN

HBG066727.

InParanoid

P31689.

KO

K09502.

OMA

ETTYYDI.

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

Gene3D

1.10.287.110. 1 hit.
2.10.230.10. 1 hit.

InterPro

IPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]

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

GenomeRNAi

3301.

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:	May 1, 2013
This is version 143 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.