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Protein

DnaJ homolog subfamily A member 1

Gene

Dnaja1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). 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.By similarity1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi134 – 1341Zinc 1By similarity
Metal bindingi137 – 1371Zinc 1By similarity
Metal bindingi150 – 1501Zinc 2By similarity
Metal bindingi153 – 1531Zinc 2By similarity
Metal bindingi177 – 1771Zinc 2By similarity
Metal bindingi180 – 1801Zinc 2By similarity
Metal bindingi193 – 1931Zinc 1By similarity
Metal bindingi196 – 1961Zinc 1By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri121 – 20585CR-typeAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • androgen receptor signaling pathway Source: MGI
  • DNA damage response, detection of DNA damage Source: Ensembl
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of JUN kinase activity Source: UniProtKB
  • negative regulation of protein ubiquitination Source: MGI
  • positive regulation of apoptotic process Source: UniProtKB
  • protein localization to mitochondrion Source: UniProtKB
  • protein refolding Source: GO_Central
  • regulation of protein transport Source: UniProtKB
  • response to heat Source: InterPro
  • spermatogenesis Source: MGI
  • sperm motility Source: MGI
  • toxin transport Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
DnaJ homolog subfamily A member 1
Alternative name(s):
DnaJ protein homolog 2
Heat shock 40 kDa protein 4
Heat shock protein J2
Short name:
HSJ-2
Gene namesi
Name:Dnaja1
Synonyms:Dnaj2, Hsj2, Hspf4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1270129. Dnaja1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 394394DnaJ homolog subfamily A member 1PRO_0000071009Add
BLAST
Propeptidei395 – 3973Removed in mature formBy similarityPRO_0000396753

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N6-acetyllysineBy similarity
Modified residuei83 – 831PhosphoserineBy similarity
Modified residuei335 – 3351PhosphoserineBy similarity
Modified residuei381 – 3811PhosphotyrosineBy similarity
Modified residuei394 – 3941Cysteine methyl esterBy similarity
Lipidationi394 – 3941S-farnesyl cysteineBy similarity

Keywords - PTMi

Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

Proteomic databases

MaxQBiP63037.
PaxDbiP63037.
PRIDEiP63037.

Expressioni

Gene expression databases

BgeeiP63037.
CleanExiMM_DNAJA1.
ExpressionAtlasiP63037. baseline and differential.
GenevisibleiP63037. MM.

Interactioni

Subunit structurei

Identified in a complex with HSPA1B and BAX.1 Publication

Protein-protein interaction databases

BioGridi200446. 7 interactions.
DIPiDIP-32350N.
IntActiP63037. 12 interactions.
MINTiMINT-1858917.
STRINGi10090.ENSMUSP00000030118.

Structurei

3D structure databases

ProteinModelPortaliP63037.
SMRiP63037. Positions 1-346.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 6863JAdd
BLAST
Repeati134 – 1418CXXCXGXG motif
Repeati150 – 1578CXXCXGXG motif
Repeati177 – 1848CXXCXGXG motif
Repeati193 – 2008CXXCXGXG motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi75 – 9622Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 CR-type zinc finger.Curated
Contains 1 J domain.Curated

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri121 – 20585CR-typeAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00490000043321.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiP63037.
KOiK09502.
OMAiFQKPITT.
OrthoDBiEOG7XM2XK.
PhylomeDBiP63037.
TreeFamiTF105141.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P63037-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ
60 70 80 90 100
AYEVLADSKK 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:August 31, 2004 - v1
Checksum:i1783CE3D5C4CD558
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055664 mRNA. Translation: AAC78597.1.
AK083046 mRNA. Translation: BAC38744.1.
BC057876 mRNA. Translation: AAH57876.1.
CCDSiCCDS18049.1.
RefSeqiNP_001158143.1. NM_001164671.1.
NP_001158144.1. NM_001164672.1.
NP_032324.1. NM_008298.5.
UniGeneiMm.27897.

Genome annotation databases

EnsembliENSMUST00000030118; ENSMUSP00000030118; ENSMUSG00000028410.
ENSMUST00000164233; ENSMUSP00000129730; ENSMUSG00000028410.
GeneIDi15502.
KEGGimmu:15502.
UCSCiuc008sht.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF055664 mRNA. Translation: AAC78597.1.
AK083046 mRNA. Translation: BAC38744.1.
BC057876 mRNA. Translation: AAH57876.1.
CCDSiCCDS18049.1.
RefSeqiNP_001158143.1. NM_001164671.1.
NP_001158144.1. NM_001164672.1.
NP_032324.1. NM_008298.5.
UniGeneiMm.27897.

3D structure databases

ProteinModelPortaliP63037.
SMRiP63037. Positions 1-346.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200446. 7 interactions.
DIPiDIP-32350N.
IntActiP63037. 12 interactions.
MINTiMINT-1858917.
STRINGi10090.ENSMUSP00000030118.

Proteomic databases

MaxQBiP63037.
PaxDbiP63037.
PRIDEiP63037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000030118; ENSMUSP00000030118; ENSMUSG00000028410.
ENSMUST00000164233; ENSMUSP00000129730; ENSMUSG00000028410.
GeneIDi15502.
KEGGimmu:15502.
UCSCiuc008sht.2. mouse.

Organism-specific databases

CTDi3301.
MGIiMGI:1270129. Dnaja1.

Phylogenomic databases

eggNOGiCOG0484.
GeneTreeiENSGT00490000043321.
HOGENOMiHOG000226718.
HOVERGENiHBG066727.
InParanoidiP63037.
KOiK09502.
OMAiFQKPITT.
OrthoDBiEOG7XM2XK.
PhylomeDBiP63037.
TreeFamiTF105141.

Miscellaneous databases

ChiTaRSiDnaja1. mouse.
NextBioi288400.
PROiP63037.
SOURCEiSearch...

Gene expression databases

BgeeiP63037.
CleanExiMM_DNAJA1.
ExpressionAtlasiP63037. baseline and differential.
GenevisibleiP63037. MM.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPiMF_01152. DnaJ.
InterProiIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamiPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A DnaJ-like gene, Hsj2, maps to mouse chromosome 5, at approximately 24 cM from the centromere."
    Royaux I., Minner F., Goffinet A.M., de Rouvroit C.L.
    Genomics 53:415-415(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Spinal cord.
  3. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 106-124 AND 375-389, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  5. "hsp70-DnaJ chaperone pair prevents nitric oxide- and CHOP-induced apoptosis by inhibiting translocation of Bax to mitochondria."
    Gotoh T., Terada K., Oyadomari S., Mori M.
    Cell Death Differ. 11:390-402(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH HSPA1B AND BAX.

Entry informationi

Entry nameiDNJA1_MOUSE
AccessioniPrimary (citable) accession number: P63037
Secondary accession number(s): P54102
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 22, 2015
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.