Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  DnaJ homolog subfamily C member 7  

UniProtKB / Swiss-Prot ID :  DNJC7_HUMAN

Gene Name (Synonyms) : 
DNAJC7, TPR2, TTC2  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. Cytoplasm, cytoskeleton. Note=Colocalizes with NR1I3 to microtubules (By similarity). 

Protein Function :  Acts as 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). 

Protein Sequence MAAAAECDVVMAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAA...
Predicted Secondary Structure CCCHHHHHHHHHHHHHHHCCHHHHHHHHHHHHHHHHHHHHHCCHHHHHHHHHHHHHCCCCCHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAE
---CCCHHH
13.05UniProtKB
Link-
8Caspase cleavage aspartic acidAAECDVVMA
HHHHHHHHH
27.79Phosphositeplus
Link-
39PhosphotyrosineGNAYYAKKD
HHHHHHHCC
14.99PhosphoELM
Link-
41Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AYYAKKDYN
HHHHHCCHH
30.01Phosphositeplus
Link-
50PhosphotyrosineEAYNYYTKA
HHHHHHHHH
10.39HPRD
Link-
50PhosphotyrosineEAYNYYTKA
HHHHHHHHH
10.39Phosphositeplus
Link-
50Phosphotyrosine.EAYNYYTKA
HHHHHHHHH
10.39UniProtKB
Link-
128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ELDHKNAQA
HHCCCCHHH
54.36Phosphositeplus
Link-
137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QQEFKNANA
HHHHHHHHH
55.16Phosphositeplus
Link-
155Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TDFEKRDFR
HHHHHHHHH
58.21Phosphositeplus
Link-
175S-nitrosocysteineFAPACHRFK
HCCCCHHHH
2.00dbSNO
Link-
182Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FKILKAECL
HHHHHHHHH
45.68Phosphositeplus
Link-
273Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EGNYKLAYE
HCCHHHHHH
30.55Phosphositeplus
Link-
327PhosphotyrosineLDDTYIKAY
HCCCCHHHH
13.86Phosphositeplus
Link-
329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DTYIKAYLR
CCCHHHHHH
22.14Phosphositeplus
Link-
368Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KQLLKNAQL
HHHHHHHHH
59.85Phosphositeplus
Link-
384Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KDYYKILGV
HHHHHHHHC
25.81Phosphositeplus
Link-
390Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LGVDKNASE
HHCHHHCCH
52.59Phosphositeplus
Link-
442Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LSDPKKKTR
HCCHHHHHH
72.41Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
SMAD9_HUMANphysical interactionMINT-62135MINT15231748
M3K3_HUMANphysical interactionMINT-48516MINT14743216
DISC1_HUMANphysical interaction
physical interaction
EBI-1105658
EBI-1105663
intact17043677
17043677
NF1_HUMANin vivoHPRD:07046HPRD8836031
HUS1_HUMANin vitro
in vivo
HPRD:07046HPRD11573955
RAD9A_HUMANin vitro
in vivo
HPRD:07046HPRD11573955
RAD1_HUMANin vitro
in vivo
HPRD:07046HPRD11573955
SMUF1_HUMANin vivoHPRD:07046HPRD15761153
DNJC7_HUMANin vitroHPRD:07046HPRD11573955
SMAD9_HUMANyeast 2-hybridHPRD:07046HPRD15231748
HUS1_HUMANENSP00000313311STRING
RAD9A_HUMANENSP00000313311STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-50, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures