DNAJA2 | ENSG00000069345 | NCBI 10294

Details for: DNAJA2

Gene ID: 10294

Symbol: DNAJA2

Ensembl ID: ENSG00000069345

Description: DnaJ heat shock protein family (Hsp40) member A2

Associated with

Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Hsp90 chaperone cycle for steroid hormone receptors (shr) in the presence of ligand
(R-HSA-3371497)
Atpase activator activity
(GO:0001671)
Atp binding
(GO:0005524)
Cytoplasm
(GO:0005737)
Cytosol
(GO:0005829)
Extracellular exosome
(GO:0070062)
Hsp70 protein binding
(GO:0030544)
Membrane
(GO:0016020)
Metal ion binding
(GO:0046872)
Positive regulation of cell population proliferation
(GO:0008284)
Protein-folding chaperone binding
(GO:0051087)
Protein binding
(GO:0005515)
Protein refolding
(GO:0042026)
Response to heat
(GO:0009408)
Unfolded protein binding
(GO:0051082)

Other Information

Proteins

DnaJ homolog subfamily A member 2

Genular Protein ID: 124872915

Symbol: DNJA2_HUMAN

Name: DnaJ homolog subfamily A member 2

UniProtKB Accession Codes:

O60884 B2R7L7 O14711

Database IDs:

Citations:

PubMed ID: 9383053

Title: Human CPR (cell cycle progression restoration) genes impart a Far-phenotype on yeast cells.

PubMed ID: 9383053

DOI: 10.1093/genetics/147.3.1063

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 10508479

Title: Antigens recognized by autologous antibody in patients with renal-cell carcinoma.

PubMed ID: 10508479

DOI: 10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5

PubMed ID: 10816573

Title: Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70.

PubMed ID: 10816573

DOI: 10.1074/jbc.m002021200

PubMed ID: 15308774

Title: A tagging-via-substrate technology for detection and proteomics of farnesylated proteins.

PubMed ID: 15308774

DOI: 10.1073/pnas.0403413101

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 24318877

Title: Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro.

PubMed ID: 24318877

DOI: 10.1074/jbc.m113.521997

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

Sequence Information:

Length: 412
Mass: 45746
Checksum: 8F1BC367425CB428
Sequence:

MANVADTKLY DILGVPPGAS ENELKKAYRK LAKEYHPDKN PNAGDKFKEI SFAYEVLSNP 
EKRELYDRYG EQGLREGSGG GGGMDDIFSH IFGGGLFGFM GNQSRSRNGR RRGEDMMHPL 
KVSLEDLYNG KTTKLQLSKN VLCSACSGQG GKSGAVQKCS ACRGRGVRIM IRQLAPGMVQ 
QMQSVCSDCN GEGEVINEKD RCKKCEGKKV IKEVKILEVH VDKGMKHGQR ITFTGEADQA 
PGVEPGDIVL LLQEKEHEVF QRDGNDLHMT YKIGLVEALC GFQFTFKHLD GRQIVVKYPP 
GKVIEPGCVR VVRGEGMPQY RNPFEKGDLY IKFDVQFPEN NWINPDKLSE LEDLLPSRPE 
VPNIIGETEE VELQEFDSTR GSGGGQRREA YNDSSDEESS SHHGPGVQCA HQ

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: DNAJA2

Associated with

Other Information

Human CPR (cell cycle progression restoration) genes impart a Far-phenotype on yeast cells. PubMed ID: 9383053

Complete sequencing and characterization of 21,243 full-length human cDNAs. PubMed ID: 14702039

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Antigens recognized by autologous antibody in patients with renal-cell carcinoma. PubMed ID: 10508479

Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. PubMed ID: 10816573

A tagging-via-substrate technology for detection and proteomics of farnesylated proteins. PubMed ID: 15308774

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro. PubMed ID: 24318877

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

N-terminome analysis of the human mitochondrial proteome. PubMed ID: 25944712

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733