P31689 (DNJA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 143.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames 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 |
| ||||
| Organism | Homo sapiens (Human) [Reference 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. |
| 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
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 | |||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||
| 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
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References
| « Hide '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 |
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| 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 |
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| 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. | ||||||||
Relevant documents
| Human chromosome 9 Human chromosome 9: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
