DNJA1_MOUSE - dbPTM
DNJA1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJA1_MOUSE
UniProt AC P63037
Protein Name DnaJ homolog subfamily A member 1
Gene Name Dnaja1
Organism Mus musculus (Mouse).
Sequence Length 397
Subcellular Localization Membrane
Lipid-anchor. Cytoplasm. Microsome. Mitochondrion. Nucleus. Cytoplasm, perinuclear region. Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity)..
Protein Description Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro). Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV (By similarity). 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..
Protein Sequence MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLADSKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
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
3Ubiquitination-----MVKETTYYDV
-----CCCEEEEEEH
48.3122790023
7Phosphorylation-MVKETTYYDVLGVK
-CCCEEEEEEHHCCC
12.7029514104
14UbiquitinationYYDVLGVKPNATQEE
EEEHHCCCCCCCHHH
30.6522790023
23AcetylationNATQEELKKAYRKLA
CCCHHHHHHHHHHHH
38.3423864654
23UbiquitinationNATQEELKKAYRKLA
CCCHHHHHHHHHHHH
38.3422790023
32UbiquitinationAYRKLALKYHPDKNP
HHHHHHHHHCCCCCC
35.59-
32MalonylationAYRKLALKYHPDKNP
HHHHHHHHHCCCCCC
35.5926320211
37AcetylationALKYHPDKNPNEGEK
HHHHCCCCCCCCCHH
77.9323806337
37UbiquitinationALKYHPDKNPNEGEK
HHHHCCCCCCCCCHH
77.9322790023
44UbiquitinationKNPNEGEKFKQISQA
CCCCCCHHHHHHHHH
69.5822790023
46UbiquitinationPNEGEKFKQISQAYE
CCCCHHHHHHHHHHH
58.7622790023
52PhosphorylationFKQISQAYEVLADSK
HHHHHHHHHHHHHHH
10.0329514104
59UbiquitinationYEVLADSKKRELYDK
HHHHHHHHCHHHHHC
57.2922790023
66UbiquitinationKKRELYDKGGEQAIK
HCHHHHHCHHHHHHH
56.08-
66AcetylationKKRELYDKGGEQAIK
HCHHHHHCHHHHHHH
56.08-
66MalonylationKKRELYDKGGEQAIK
HCHHHHHCHHHHHHH
56.0826320211
83PhosphorylationGAGGGFGSPMDIFDM
CCCCCCCCHHHHHHH
18.1326643407
105UbiquitinationMQRERRGKNVVHQLS
HHHHHCCCCCEEEEE
44.77-
112PhosphorylationKNVVHQLSVTLEDLY
CCCEEEEECCHHHHH
13.3926745281
114PhosphorylationVVHQLSVTLEDLYNG
CEEEEECCHHHHHCC
22.5123984901
119PhosphorylationSVTLEDLYNGATRKL
ECCHHHHHCCHHHHH
24.71-
136UbiquitinationQKNVICDKCEGRGGK
HCCEEEECCCCCCCC
29.76-
136AcetylationQKNVICDKCEGRGGK
HCCEEEECCCCCCCC
29.7623201123
136MalonylationQKNVICDKCEGRGGK
HCCEEEECCCCCCCC
29.7626320211
143UbiquitinationKCEGRGGKKGAVECC
CCCCCCCCCCCEEEC
51.35-
144UbiquitinationCEGRGGKKGAVECCP
CCCCCCCCCCEEECC
56.21-
175PhosphorylationGMVQQIQSVCMECQG
HHHHHHHHHHHHCCC
20.9329899451
252PhosphorylationQKDHAVFTRRGEDLF
CCCCEEEEECCCCEE
16.9221082442
296UbiquitinationSHPGQIVKHGDIKCV
CCCCCEEECCCEEEE
43.4222790023
302S-nitrosylationVKHGDIKCVLNEGMP
EECCCEEEEEECCCC
4.2620925432
302S-nitrosocysteineVKHGDIKCVLNEGMP
EECCCEEEEEECCCC
4.26-
335PhosphorylationFPENGFLSPDKLSLL
CCCCCCCCHHHHHHH
28.8825521595
338UbiquitinationNGFLSPDKLSLLEKL
CCCCCHHHHHHHHHH
43.2722790023
340PhosphorylationFLSPDKLSLLEKLLP
CCCHHHHHHHHHHCC
36.3326824392
344UbiquitinationDKLSLLEKLLPERKE
HHHHHHHHHCCCCCC
56.1222790023
381PhosphorylationRHYNGEAYEDDEHHP
HHCCCCCCCCCCCCC
18.6525159016
394MethylationHPRGGVQCQTS----
CCCCCCCCCCC----
4.41-
394FarnesylationHPRGGVQCQTS----
CCCCCCCCCCC----
4.41-

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 DNJA1_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJA1_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 DNJA1_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DNJA1_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNJA1_MOUSE

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Related Literatures of Post-Translational Modification

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