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P31689

- DNJA1_HUMAN

UniProt

P31689 - DNJA1_HUMAN

Protein

DnaJ homolog subfamily A member 1

Gene

DNAJA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 158 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    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)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

    1. ATP binding Source: InterPro
    2. chaperone binding Source: UniProtKB
    3. Hsp70 protein binding Source: UniProtKB
    4. low-density lipoprotein particle receptor binding Source: MGI
    5. metal ion binding Source: UniProtKB-KW
    6. protein binding Source: IntAct

    GO - Biological processi

    1. androgen receptor signaling pathway Source: Ensembl
    2. negative regulation of apoptotic process Source: UniProtKB
    3. negative regulation of JUN kinase activity Source: UniProtKB
    4. positive regulation of apoptotic process Source: UniProtKB
    5. protein folding Source: ProtInc
    6. protein localization to mitochondrion Source: UniProtKB
    7. regulation of protein transport Source: UniProtKB
    8. response to heat Source: InterPro
    9. response to unfolded protein Source: ProtInc
    10. spermatogenesis Source: Ensembl
    11. sperm motility Source: Ensembl

    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
    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
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:5229. DNAJA1.

    Subcellular locationi

    Membrane 1 Publication; Lipid-anchor 1 Publication. Cytoplasm 1 Publication. Microsome By similarity. Nucleus 1 Publication. Cytoplasmperinuclear region 1 Publication. Mitochondrion By similarity
    Note: Primarily associated with microsomes. A minor proportion is associated with mitochondria By similarity. Primarily cytoplasmic. A minor proportion is associated with nuclei.By similarity

    GO - Cellular componenti

    1. cytosol Source: UniProt
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi394 – 3941C → S: Loss of farnesylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA31536.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394DnaJ homolog subfamily A member 1PRO_0000071008Add
    BLAST
    Propeptidei395 – 3973Removed in mature formCuratedPRO_0000393941

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei66 – 661N6-acetyllysine1 Publication
    Modified residuei83 – 831Phosphoserine4 Publications
    Modified residuei335 – 3351Phosphoserine5 Publications
    Modified residuei381 – 3811Phosphotyrosine1 Publication
    Modified residuei394 – 3941Cysteine methyl esterCurated
    Lipidationi394 – 3941S-farnesyl cysteine3 Publications

    Keywords - PTMi

    Acetylation, Lipoprotein, Methylation, Phosphoprotein, Prenylation

    Proteomic databases

    MaxQBiP31689.
    PaxDbiP31689.
    PeptideAtlasiP31689.
    PRIDEiP31689.

    PTM databases

    PhosphoSiteiP31689.

    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

    ArrayExpressiP31689.
    BgeeiP31689.
    CleanExiHS_DNAJA1.
    GenevestigatoriP31689.

    Organism-specific databases

    HPAiHPA001306.

    Interactioni

    Subunit structurei

    Identified in a complex with HSPA1B and BAX.1 Publication

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi109534. 88 interactions.
    IntActiP31689. 48 interactions.
    MINTiMINT-5004184.
    STRINGi9606.ENSP00000369127.

    Structurei

    Secondary structure

    1
    397
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi7 – 104
    Helixi19 – 3315
    Helixi35 – 373
    Beta strandi39 – 413
    Helixi42 – 5413
    Helixi58 – 647
    Turni65 – 673

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LO1NMR-A1-70[»]
    2M6YNMR-A1-67[»]
    ProteinModelPortaliP31689.
    SMRiP31689. 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.
    HOGENOMiHOG000226718.
    HOVERGENiHBG066727.
    InParanoidiP31689.
    KOiK09502.
    OMAiGMQVRIQ.
    OrthoDBiEOG7XM2XK.
    PhylomeDBiP31689.
    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]

    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. Align

    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

    MVKETTYYDV LGVKPNATQE ELKKAYRKLA LKYHPDKNPN EGEKFKQISQ    50
    AYEVLSDAKK RELYDKGGEQ AIKEGGAGGG FGSPMDIFDM FFGGGGRMQR 100
    ERRGKNVVHQ LSVTLEDLYN GATRKLALQK NVICDKCEGR GGKKGAVECC 150
    PNCRGTGMQI RIHQIGPGMV QQIQSVCMEC QGHGERISPK DRCKSCNGRK 200
    IVREKKILEV HIDKGMKDGQ KITFHGEGDQ EPGLEPGDII IVLDQKDHAV 250
    FTRRGEDLFM CMDIQLVEAL CGFQKPISTL DNRTIVITSH PGQIVKHGDI 300
    KCVLNEGMPI YRRPYEKGRL IIEFKVNFPE NGFLSPDKLS LLEKLLPERK 350
    EVEETDEMDQ VELVDFDPNQ ERRRHYNGEA YEDDEHHPRG GVQCQTS 397
    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)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti274 – 2741Q → H in BAA02656. (PubMed:8334161)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei327 – 39771NFPEN…QCQTS → SCNVL in isoform 2. 1 PublicationVSP_046566Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_001539.2. [P31689-1]
    UniGeneiHs.445203.

    Genome annotation databases

    EnsembliENST00000330899; ENSP00000369127; ENSG00000086061. [P31689-1]
    GeneIDi3301.
    KEGGihsa:3301.
    UCSCiuc003zsd.1. human. [P31689-1]
    uc003zse.1. human.

    Polymorphism databases

    DMDMi1706474.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS6533.1. [P31689-1 ]
    PIRi S34630.
    RefSeqi NP_001530.1. NM_001539.2. [P31689-1 ]
    UniGenei Hs.445203.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LO1 NMR - A 1-70 [» ]
    2M6Y NMR - A 1-67 [» ]
    ProteinModelPortali P31689.
    SMRi P31689. Positions 1-346.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109534. 88 interactions.
    IntActi P31689. 48 interactions.
    MINTi MINT-5004184.
    STRINGi 9606.ENSP00000369127.

    Chemistry

    ChEMBLi CHEMBL2189122.

    PTM databases

    PhosphoSitei P31689.

    Polymorphism databases

    DMDMi 1706474.

    Proteomic databases

    MaxQBi P31689.
    PaxDbi P31689.
    PeptideAtlasi P31689.
    PRIDEi P31689.

    Protocols and materials databases

    DNASUi 3301.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330899 ; ENSP00000369127 ; ENSG00000086061 . [P31689-1 ]
    GeneIDi 3301.
    KEGGi hsa:3301.
    UCSCi uc003zsd.1. human. [P31689-1 ]
    uc003zse.1. human.

    Organism-specific databases

    CTDi 3301.
    GeneCardsi GC09P033025.
    H-InvDB HIX0007975.
    HGNCi HGNC:5229. DNAJA1.
    HPAi HPA001306.
    MIMi 602837. gene.
    neXtProti NX_P31689.
    PharmGKBi PA31536.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0484.
    HOGENOMi HOG000226718.
    HOVERGENi HBG066727.
    InParanoidi P31689.
    KOi K09502.
    OMAi GMQVRIQ.
    OrthoDBi EOG7XM2XK.
    PhylomeDBi P31689.
    TreeFami TF105141.

    Miscellaneous databases

    GeneWikii DNAJA1.
    GenomeRNAii 3301.
    NextBioi 13099.
    PROi P31689.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P31689.
    Bgeei P31689.
    CleanExi HS_DNAJA1.
    Genevestigatori P31689.

    Family and domain databases

    Gene3Di 1.10.287.110. 1 hit.
    2.10.230.10. 1 hit.
    HAMAPi MF_01152. DnaJ.
    InterProi 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 ]
    Pfami PF01556. CTDII. 1 hit.
    PF00226. DnaJ. 1 hit.
    PF00684. DnaJ_CXXCXGXG. 1 hit.
    [Graphical view ]
    PRINTSi PR00625. JDOMAIN.
    SMARTi SM00271. DnaJ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46565. SSF46565. 1 hit.
    SSF49493. SSF49493. 3 hits.
    SSF57938. SSF57938. 1 hit.
    PROSITEi PS00636. DNAJ_1. 1 hit.
    PS50076. DNAJ_2. 1 hit.
    PS51188. ZF_CR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (ISOFORM 1).
    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] (ISOFORM 1).
    3. "Expression of a novel DnaJA1 alternative splicing in human testis and sperm."
      Hu Y., Zhou Z., Huang X., Xu M., Lu L., Xu Z., Li J., Sha J.
      Int. J. Androl. 27:343-349(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Testis.
    4. "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] (ISOFORM 1).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Amygdala.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Placenta.
    8. "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: FUNCTION, INDUCTION BY HEAT, ISOPRENYLATION AT CYS-394.
    9. "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: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ISOPRENYLATION.
    10. "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, ISOPRENYLATION AT CYS-394, MUTAGENESIS OF CYS-394.
    11. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    17. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro."
      Rauch J.N., Gestwicki J.E.
      J. Biol. Chem. 289:1402-1414(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    23. "Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer."
      Stark J.L., Mehla K., Chaika N., Acton T.B., Xiao R., Singh P.K., Montelione G.T., Powers R.
      Biochemistry 53:1360-1372(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-67, FUNCTION.

    Entry informationi

    Entry nameiDNJA1_HUMAN
    AccessioniPrimary (citable) accession number: P31689
    Secondary accession number(s): Q5T7Q0, Q86TL9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 158 of the entry and version 2 of the sequence. [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
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3