DNJC7_MOUSE - dbPTM
DNJC7_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJC7_MOUSE
UniProt AC Q9QYI3
Protein Name DnaJ homolog subfamily C member 7
Gene Name Dnajc7
Organism Mus musculus (Mouse).
Sequence Length 494
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton . Colocalizes with NR1I3 at microtubules.
Protein Description 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 (By similarity). Recruits NR1I3 to the cytoplasm..
Protein Sequence MAATAECDVVMAATEPELLEDEDAKREAESFKEQGNAYYAKKDYNEAYNYYTKAIDMCPNNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAEVDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQFVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACVACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRQLEDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQFEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDANNIFKAFFGGPGGFSFEASGPGNFYFQFG
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAATAECDV
------CCCCCCCCE		17.33-
25UbiquitinationLLEDEDAKREAESFK
HHCCHHHHHHHHHHH		64.1927667366
41UbiquitinationQGNAYYAKKDYNEAY
HHCCEEECCCHHHHH		30.0127667366
48PhosphorylationKKDYNEAYNYYTKAI
CCCHHHHHHHHHHHH		9.49-
50PhosphorylationDYNEAYNYYTKAIDM
CHHHHHHHHHHHHHH		10.39-
58GlutathionylationYTKAIDMCPNNASYY
HHHHHHHCCCCCHHC		2.6424333276
58S-nitrosocysteineYTKAIDMCPNNASYY
HHHHHHHCCCCCHHC		2.64-
58S-nitrosylationYTKAIDMCPNNASYY
HHHHHHHCCCCCHHC		2.6421278135
128UbiquitinationRALELDHKNAQAQQE
HHHHHCCCCHHHHHH		54.36-
147UbiquitinationNAVMEYEKIAEVDFE
HHHHEEHHHEECCCC		46.44-
155UbiquitinationIAEVDFEKRDFRKVV
HEECCCCCCCHHHHH		58.21-
182AcetylationCHRFKILKAECLAML
HHHHHHHHHHHHHHH		45.6822826441
182UbiquitinationCHRFKILKAECLAML
HHHHHHHHHHHHHHH		45.68-
207PhosphorylationSDILRMDSTNADALY
HHHHCCCCCCCCHHH		17.7629176673
208PhosphorylationDILRMDSTNADALYV
HHHCCCCCCCCHHHH		30.1129176673
250GlutathionylationHEKACVACRNAKALK
HHHHHHHHHCHHHHH		1.3924333276
259AcetylationNAKALKAKKEDGNKA
CHHHHHCCHHHCCHH		55.927628135
260AcetylationAKALKAKKEDGNKAF
HHHHHCCHHHCCHHH		66.937628145
268AcetylationEDGNKAFKEGNYKLA
HHCCHHHHHCCHHHH		70.357628155
273UbiquitinationAFKEGNYKLAYELYT
HHHHCCHHHHHHHHH		30.55-
290UbiquitinationLGIDPNNIKTNAKLY
HCCCCCCCCCCCEEE		8.0727667366
295UbiquitinationNNIKTNAKLYCNRGT
CCCCCCCEEEECCCH		41.90-
306UbiquitinationNRGTVNSKLRQLEDA
CCCHHHHHHHHHHHH		42.3527667366
306MalonylationNRGTVNSKLRQLEDA
CCCHHHHHHHHHHHH		42.3526320211
329UbiquitinationKLDDTYIKAYLRRAQ
CCCHHHHHHHHHHHH		22.14-
352UbiquitinationEEAVRDYEKVYQTEK
HHHHHHHHHHHHHHC		40.0927667366
360PhosphorylationKVYQTEKTKEHKQLL
HHHHHHCCHHHHHHH		35.1225159016
368UbiquitinationKEHKQLLKNAQLELK
HHHHHHHHHHCHHHH		59.8527667366
382UbiquitinationKKSKRKDYYKILGVD
HHHHCCCHHHHHCCC		15.0827667366
384UbiquitinationSKRKDYYKILGVDKN
HHCCCHHHHHCCCCC		25.81-
390UbiquitinationYKILGVDKNASEDEI
HHHHCCCCCCCHHHH		52.59-
393PhosphorylationLGVDKNASEDEIKKA
HCCCCCCCHHHHHHH		55.7826824392
398UbiquitinationNASEDEIKKAYRKRA
CCCHHHHHHHHHHHH		29.3327667366
417PhosphorylationPDRHSGASAEVQKEE
CCCCCCCCHHHHHHH		28.6129514104
442UbiquitinationFTILSDPKKKTRYDS
HHHCCCCCCCCCCCC		72.41-
445PhosphorylationLSDPKKKTRYDSGQD
CCCCCCCCCCCCCCC		43.2626643407
447PhosphorylationDPKKKTRYDSGQDLD
CCCCCCCCCCCCCCC		21.4926643407
449PhosphorylationKKKTRYDSGQDLDEE
CCCCCCCCCCCCCCC		29.4426643407
480PhosphorylationFGGPGGFSFEASGPG
HCCCCCEEEEECCCC		26.0026643407
484PhosphorylationGGFSFEASGPGNFYF
CCEEEEECCCCCEEE		38.0226643407
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of DNJC7_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJC7_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of DNJC7_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBE4A_MOUSEUbe4aphysical
15189447
HS90A_HUMANHSP90AA1physical
15189447
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNJC7_MOUSE

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Related Literatures of Post-Translational Modification

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