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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: DnaJ homolog subfamily C member 7

UniprotKB/SwissProt ID: Q99615 (Q99615)

Gene Name: DNAJC7

Organism: Homo sapiens (Human)

Function: Acts as a co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR001623 DnaJ_domain
IPR036869 J_dom_sf
IPR011990 TPR-like_helical_dom_sf
IPR019734 TPR_rpt

The S-nitrosylation sites of Q99615

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 105 FVRGHLREGK C HLSLGNAMAA  CCCHHCCCEE E EECCHHHCCH  6%
2 116 HLSLGNAMAA C RSFQRALELD  CCCHHCCCEE E EECCHHHCCH  2.45%
3 164 EKRDFRKVVF C MDRALEFAPA  CCCHHCCCEE E EECCHHHCCH  1.55%
4 175 MDRALEFAPA C HRFKILKAEC  CCCHHCCCEE E EECCHHHCCH  2% 19483679
5 185 CHRFKILKAE C LAMLGRYPEA  CCCHHCCCEE E EECCHHHCCH  3.33%
6 219 NADALYVRGL C LYYEDCIEKA  CCCHHCCCEE E EECCHHHCCH  2.27%
7 225 VRGLCLYYED C IEKAVQFFVQ  CCCHHCCCEE E EECCHHHCCH  2.64%
8 247 LRMAPDHEKA C IACRNAKALK  CCCHHCCCEE E EECCHHHCCH  2.76%
9 317 LRKLDDAIED C TNAVKLDDTY  CCCHHCCCEE E EECCHHHCCH  1.73%
10 337 YIKAYLRRAQ C YMDTEQYEEA  CCCHHCCCEE E EECCHHHCCH  2.72%