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P63037 (DNJA1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Dnaja1
Synonyms:Dnaj2, Hsj2, Hspf4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Co-chaperone of Hsc70. Seems to play a role in protein import into mitochondria By similarity. HAMAP-Rule MF_01152

Subcellular location

Membrane; Lipid-anchor Potential HAMAP-Rule MF_01152.

Sequence similarities

Contains 1 CR-type zinc finger.

Contains 1 J domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 394394DnaJ homolog subfamily A member 1 HAMAP-Rule MF_01152
PRO_0000071009
Propeptide395 – 3973Removed in mature form By similarity
PRO_0000396753

Regions

Domain6 – 6863J
Repeat134 – 1418CXXCXGXG motif HAMAP-Rule MF_01152
Repeat150 – 1578CXXCXGXG motif HAMAP-Rule MF_01152
Repeat177 – 1848CXXCXGXG motif HAMAP-Rule MF_01152
Repeat193 – 2008CXXCXGXG motif HAMAP-Rule MF_01152
Zinc finger121 – 20585CR-type HAMAP-Rule MF_01152
Compositional bias75 – 9622Gly-rich HAMAP-Rule MF_01152

Sites

Metal binding1341Zinc 1 By similarity
Metal binding1371Zinc 1 By similarity
Metal binding1501Zinc 2 By similarity
Metal binding1531Zinc 2 By similarity
Metal binding1771Zinc 2 By similarity
Metal binding1801Zinc 2 By similarity
Metal binding1931Zinc 1 By similarity
Metal binding1961Zinc 1 By similarity

Amino acid modifications

Modified residue661N6-acetyllysine By similarity
Modified residue831Phosphoserine By similarity
Modified residue3351Phosphoserine By similarity
Modified residue3811Phosphotyrosine By similarity
Modified residue3941Cysteine methyl ester By similarity
Lipidation3941S-farnesyl cysteine By similarity

Sequences

Sequence LengthMass (Da)Tools
P63037 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: 1783CE3D5C4CD558

FASTA39744,868
        10         20         30         40         50         60 
MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ AYEVLADSKK 

        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 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF055664 mRNA. Translation: AAC78597.1.
AK083046 mRNA. Translation: BAC38744.1.
BC057876 mRNA. Translation: AAH57876.1.
RefSeqNP_001158143.1. NM_001164671.1.
NP_001158144.1. NM_001164672.1.
NP_032324.1. NM_008298.5.
UniGeneMm.27897.

3D structure databases

ProteinModelPortalP63037.
SMRP63037. Positions 1-347.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid200446. 7 interactions.
DIPDIP-32350N.
IntActP63037. 11 interactions.
MINTMINT-1858917.

Proteomic databases

PaxDbP63037.
PRIDEP63037.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030118; ENSMUSP00000030118; ENSMUSG00000028410.
ENSMUST00000164233; ENSMUSP00000129730; ENSMUSG00000028410.
GeneID15502.
KEGGmmu:15502.
UCSCuc008sht.2. mouse.

Organism-specific databases

CTD3301.
MGIMGI:1270129. Dnaja1.

Phylogenomic databases

eggNOGCOG0484.
HOGENOMHOG000226718.
HOVERGENHBG066727.
InParanoidP63037.
KOK09502.
OMAKIYDEGG.
OrthoDBEOG7XM2XK.
PhylomeDBP63037.
TreeFamTF105141.

Gene expression databases

ArrayExpressP63037.
BgeeP63037.
CleanExMM_DNAJA1.
GenevestigatorP63037.

Family and domain databases

Gene3D1.10.287.110. 1 hit.
2.10.230.10. 1 hit.
HAMAPMF_01152. DnaJ.
InterProIPR012724. DnaJ.
IPR002939. DnaJ_C.
IPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
IPR008971. HSP40/DnaJ_pept-bd.
IPR001305. HSP_DnaJ_Cys-rich_dom.
[Graphical view]
PfamPF01556. CTDII. 1 hit.
PF00226. DnaJ. 1 hit.
PF00684. DnaJ_CXXCXGXG. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. SSF46565. 1 hit.
SSF49493. SSF49493. 3 hits.
SSF57938. SSF57938. 1 hit.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
PS51188. ZF_CR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNAJA1. mouse.
NextBio288400.
PROP63037.
SOURCESearch...

Entry information

Entry nameDNJA1_MOUSE
AccessionPrimary (citable) accession number: P63037
Secondary accession number(s): P54102
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot