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P31689

- DNJA1_HUMAN

UniProt

P31689 - DNJA1_HUMAN

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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

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. G-protein coupled receptor binding Source: ParkinsonsUK-UCL
  4. Hsp70 protein binding Source: UniProtKB
  5. low-density lipoprotein particle receptor binding Source: MGI
  6. metal ion binding Source: UniProtKB-KW
  7. ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. androgen receptor signaling pathway Source: Ensembl
  2. DNA damage response, detection of DNA damage Source: Ensembl
  3. negative regulation of apoptotic process Source: UniProtKB
  4. negative regulation of JUN kinase activity Source: UniProtKB
  5. negative regulation of protein ubiquitination Source: ParkinsonsUK-UCL
  6. positive regulation of apoptotic process Source: UniProtKB
  7. protein folding Source: ProtInc
  8. protein localization to mitochondrion Source: UniProtKB
  9. regulation of protein transport Source: UniProtKB
  10. response to heat Source: InterPro
  11. response to unfolded protein Source: ProtInc
  12. spermatogenesis Source: Ensembl
  13. sperm motility Source: Ensembl
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
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. cytoplasmic side of endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  2. cytosol Source: UniProt
  3. extracellular vesicular exosome Source: UniProt
  4. membrane Source: UniProtKB
  5. mitochondrion Source: UniProtKB-KW
  6. nucleus Source: UniProtKB-KW
Complete GO annotation...

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 cysteine2 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

BgeeiP31689.
CleanExiHS_DNAJA1.
ExpressionAtlasiP31689. baseline and differential.
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. 98 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 – 104Combined sources
Helixi19 – 3315Combined sources
Helixi35 – 373Combined sources
Beta strandi39 – 413Combined sources
Helixi42 – 5413Combined sources
Helixi58 – 647Combined sources
Turni65 – 673Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00490000043321.
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

        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)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:
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_001539.2. [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:
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 .
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:
PDBei
RCSB PDBi
PDBji
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. 98 interactions.
IntActi P31689. 48 interactions.
MINTi MINT-5004184.
STRINGi 9606.ENSP00000369127.

Chemistry

BindingDBi P31689.
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.
GeneTreei ENSGT00490000043321.
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

Bgeei P31689.
CleanExi HS_DNAJA1.
ExpressionAtlasi P31689. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 160 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