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Protein

DnaJ homolog subfamily A member 1

Gene

DNAJA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Co-chaperone for HSPA8/Hsc70 (PubMed:10816573). Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (PubMed:24318877). Plays a role in protein transport into mitochondria via its role as co-chaperone. Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis (PubMed:14752510). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (PubMed:24512202).5 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi134Zinc 1By similarity1
Metal bindingi137Zinc 1By similarity1
Metal bindingi150Zinc 2By similarity1
Metal bindingi153Zinc 2By similarity1
Metal bindingi177Zinc 2By similarity1
Metal bindingi180Zinc 2By similarity1
Metal bindingi193Zinc 1By similarity1
Metal bindingi196Zinc 1By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri121 – 205CR-typeAdd BLAST85

GO - Molecular functioni

  • ATPase activator activity Source: UniProtKB
  • ATP binding Source: InterPro
  • C3HC4-type RING finger domain binding Source: BHF-UCL
  • chaperone binding Source: UniProtKB
  • G-protein coupled receptor binding Source: ParkinsonsUK-UCL
  • Hsp70 protein binding Source: UniProtKB
  • low-density lipoprotein particle receptor binding Source: MGI
  • metal ion binding Source: UniProtKB-KW
  • Tat protein binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • unfolded protein binding Source: InterPro

GO - Biological processi

  • androgen receptor signaling pathway Source: Ensembl
  • DNA damage response, detection of DNA damage Source: Ensembl
  • flagellated sperm motility Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of establishment of protein localization to mitochondrion Source: ParkinsonsUK-UCL
  • negative regulation of JUN kinase activity Source: UniProtKB
  • negative regulation of nitrosative stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  • positive regulation of apoptotic process Source: UniProtKB
  • protein folding Source: ProtInc
  • protein localization to mitochondrion Source: UniProtKB
  • regulation of protein transport Source: UniProtKB
  • response to heat Source: InterPro
  • response to unfolded protein Source: ProtInc
  • spermatogenesis Source: Ensembl
  • toxin transport Source: Ensembl

Keywordsi

Molecular functionChaperone
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-3371497 HSP90 chaperone cycle for steroid hormone receptors (SHR)

Names & Taxonomyi

Protein namesi
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 namesi
Name:DNAJA1
Synonyms:DNAJ2, HDJ2, HSJ2, HSPF4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000086061.15
HGNCiHGNC:5229 DNAJA1
MIMi602837 gene
neXtProtiNX_P31689

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Microsome, Mitochondrion, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi394C → S: Loss of farnesylation. 1 Publication1

Organism-specific databases

DisGeNETi3301
OpenTargetsiENSG00000086061
PharmGKBiPA31536

Chemistry databases

ChEMBLiCHEMBL2189122

Polymorphism and mutation databases

BioMutaiDNAJA1
DMDMi1706474

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000710081 – 394DnaJ homolog subfamily A member 1Add BLAST394
PropeptideiPRO_0000393941395 – 397Removed in mature formCurated3

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N6-acetyllysineCombined sources1
Modified residuei83PhosphoserineCombined sources1
Modified residuei335PhosphoserineCombined sources1
Modified residuei381PhosphotyrosineCombined sources1
Modified residuei394Cysteine methyl esterCurated1
Lipidationi394S-farnesyl cysteine2 Publications1

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

EPDiP31689
PaxDbiP31689
PeptideAtlasiP31689
PRIDEiP31689
ProteomicsDBi54799

PTM databases

iPTMnetiP31689
PhosphoSitePlusiP31689
SwissPalmiP31689

Expressioni

Tissue specificityi

Ubiquitous. Isoform 2 is highly expressed in testis and lung, but detected at low levels in thymus, prostate, colon and liver.2 Publications

Inductioni

Up-regulated by heat shock.1 Publication

Gene expression databases

BgeeiENSG00000086061
CleanExiHS_DNAJA1
GenevisibleiP31689 HS

Organism-specific databases

HPAiHPA001306

Interactioni

Subunit structurei

Identified in a complex with HSPA1B and BAX (PubMed:14752510). Interacts with RNF207 (PubMed:25281747).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AICDAQ9GZX76EBI-347834,EBI-3834328

GO - Molecular functioni

  • C3HC4-type RING finger domain binding Source: BHF-UCL
  • chaperone binding Source: UniProtKB
  • G-protein coupled receptor binding Source: ParkinsonsUK-UCL
  • Hsp70 protein binding Source: UniProtKB
  • low-density lipoprotein particle receptor binding Source: MGI
  • Tat protein binding Source: ParkinsonsUK-UCL
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL
  • unfolded protein binding Source: InterPro

Protein-protein interaction databases

BioGridi109534, 172 interactors
IntActiP31689, 117 interactors
MINTiP31689
STRINGi9606.ENSP00000369127

Chemistry databases

BindingDBiP31689

Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 10Combined sources4
Helixi19 – 33Combined sources15
Helixi35 – 37Combined sources3
Beta strandi39 – 41Combined sources3
Helixi42 – 54Combined sources13
Helixi58 – 64Combined sources7
Turni65 – 67Combined sources3

3D structure databases

ProteinModelPortaliP31689
SMRiP31689
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 68JAdd BLAST63
Repeati134 – 141CXXCXGXG motif8
Repeati150 – 157CXXCXGXG motif8
Repeati177 – 184CXXCXGXG motif8
Repeati193 – 200CXXCXGXG motif8

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi75 – 96Gly-richAdd BLAST22

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri121 – 205CR-typeAdd BLAST85

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG0712 Eukaryota
COG0484 LUCA
GeneTreeiENSGT00860000133716
HOGENOMiHOG000226718
HOVERGENiHBG066727
InParanoidiP31689
KOiK09502
OMAiCDGHGMK
OrthoDBiEOG091G0CAC
PhylomeDBiP31689
TreeFamiTF105141

Family and domain databases

CDDicd06257 DnaJ, 1 hit
cd10719 DnaJ_zf, 1 hit
Gene3Di1.10.287.110, 1 hit
HAMAPiMF_01152 DnaJ, 1 hit
InterProiView protein in InterPro
IPR012724 DnaJ
IPR002939 DnaJ_C
IPR001623 DnaJ_domain
IPR018253 DnaJ_domain_CS
IPR008971 HSP40/DnaJ_pept-bd
IPR001305 HSP_DnaJ_Cys-rich_dom
IPR036410 HSP_DnaJ_Cys-rich_dom_sf
IPR036869 J_dom_sf
PfamiView protein in Pfam
PF00226 DnaJ, 1 hit
PF01556 DnaJ_C, 1 hit
PF00684 DnaJ_CXXCXGXG, 1 hit
PRINTSiPR00625 JDOMAIN
SMARTiView protein in SMART
SM00271 DnaJ, 1 hit
SUPFAMiSSF46565 SSF46565, 1 hit
SSF49493 SSF49493, 3 hits
SSF57938 SSF57938, 1 hit
PROSITEiView protein in PROSITE
PS00636 DNAJ_1, 1 hit
PS50076 DNAJ_2, 1 hit
PS51188 ZF_CR, 1 hit

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P31689-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ
60 70 80 90 100
AYEVLSDAKK RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR
110 120 130 140 150
ERRGKNVVHQ LSVTLEDLYN GATRKLALQK NVICDKCEGR GGKKGAVECC
160 170 180 190 200
PNCRGTGMQI RIHQIGPGMV QQIQSVCMEC QGHGERISPK DRCKSCNGRK
210 220 230 240 250
IVREKKILEV HIDKGMKDGQ KITFHGEGDQ EPGLEPGDII IVLDQKDHAV
260 270 280 290 300
FTRRGEDLFM CMDIQLVEAL CGFQKPISTL DNRTIVITSH PGQIVKHGDI
310 320 330 340 350
KCVLNEGMPI YRRPYEKGRL IIEFKVNFPE NGFLSPDKLS LLEKLLPERK
360 370 380 390
EVEETDEMDQ VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS
Length:397
Mass (Da):44,868
Last modified:October 1, 1996 - v2
Checksum:iA899C06F6BB32780
GO
Isoform 2 (identifier: P31689-2) [UniParc]FASTAAdd to basket
Also known as: nDnaJA1

The sequence of this isoform differs from the canonical sequence as follows:
     327-397: NFPENGFLSP...PRGGVQCQTS → SCNVL

Show »
Length:331
Mass (Da):37,045
Checksum:iE3FFC159AA4BE7C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti274Q → H in BAA02656 (PubMed:8334161).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_046566327 – 397NFPEN…QCQTS → SCNVL in isoform 2. 1 PublicationAdd BLAST71

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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
CCDSiCCDS6533.1 [P31689-1]
PIRiS34630
RefSeqiNP_001530.1, NM_001539.3 [P31689-1]
UniGeneiHs.445203
Hs.707338

Genome annotation databases

EnsembliENST00000330899; ENSP00000369127; ENSG00000086061 [P31689-1]
GeneIDi3301
KEGGihsa:3301
UCSCiuc003zsd.2 human [P31689-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiDNJA1_HUMAN
AccessioniPrimary (citable) accession number: P31689
Secondary accession number(s): Q5T7Q0, Q86TL9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 1, 1996
Last modified: July 18, 2018
This is version 198 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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