DNJA3_HUMAN - dbPTM
DNJA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJA3_HUMAN
UniProt AC Q96EY1
Protein Name DnaJ homolog subfamily A member 3, mitochondrial
Gene Name DNAJA3
Organism Homo sapiens (Human).
Sequence Length 480
Subcellular Localization Mitochondrion matrix. Cytoplasm, cytosol. Cell junction, synapse, postsynaptic cell membrane
Peripheral membrane protein. Recruited to the postsynaptic cell membrane of the neuromuscular junction through interaction with MUSK..
Protein Description Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway..
Protein Sequence MAARCSTRWLLVVVGTPRLPAISGRGARPPREGVVGAWLSRKLSVPAFASSLTSCGPRALLTLRPGVSLTGTKHNPFICTASFHTSAPLAKEDYYQILGVPRNASQKEIKKAYYQLAKKYHPDTNKDDPKAKEKFSQLAEAYEVLSDEVKRKQYDAYGSAGFDPGASGSQHSYWKGGPTVDPEELFRKIFGEFSSSSFGDFQTVFDQPQEYFMELTFNQAAKGVNKEFTVNIMDTCERCNGKGNEPGTKVQHCHYCGGSGMETINTGPFVMRSTCRRCGGRGSIIISPCVVCRGAGQAKQKKRVMIPVPAGVEDGQTVRMPVGKREIFITFRVQKSPVFRRDGADIHSDLFISIAQALLGGTARAQGLYETINVTIPPGTQTDQKIRMGGKGIPRINSYGYGDHYIHIKIRVPKRLTSRQQSLILSYAEDETDVEGTVNGVTLTSSGGSTMDSSAGSKARREAGEDEEGFLSKLKKMFTS
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
23PhosphorylationTPRLPAISGRGARPP
CCCCCCCCCCCCCCC		25.2526425664
40PhosphorylationGVVGAWLSRKLSVPA
CCHHHHHHHHCCHHH		19.37-
51PhosphorylationSVPAFASSLTSCGPR
CHHHHHHHHHHCCCC		32.0323879269
54PhosphorylationAFASSLTSCGPRALL
HHHHHHHHCCCCCEE		23.5223879269
58MethylationSLTSCGPRALLTLRP
HHHHCCCCCEEEECC		24.1323455924
62PhosphorylationCGPRALLTLRPGVSL
CCCCCEEEECCCCCC		22.9023879269
72PhosphorylationPGVSLTGTKHNPFIC
CCCCCCCCCCCCEEE		24.7220860994
91AcetylationHTSAPLAKEDYYQIL
ECCCCCCCCCHHHHH		59.8230592965
111MalonylationASQKEIKKAYYQLAK
CCHHHHHHHHHHHHH		47.4826320211
111SuccinylationASQKEIKKAYYQLAK
CCHHHHHHHHHHHHH		47.4827452117
113PhosphorylationQKEIKKAYYQLAKKY
HHHHHHHHHHHHHHH		10.71-
114PhosphorylationKEIKKAYYQLAKKYH
HHHHHHHHHHHHHHC		11.25-
118AcetylationKAYYQLAKKYHPDTN
HHHHHHHHHHCCCCC		63.5625953088
130SuccinylationDTNKDDPKAKEKFSQ
CCCCCCHHHHHHHHH		78.1823954790
134AcetylationDDPKAKEKFSQLAEA
CCHHHHHHHHHHHHH		50.0023954790
136PhosphorylationPKAKEKFSQLAEAYE
HHHHHHHHHHHHHHH		35.0426699800
142PhosphorylationFSQLAEAYEVLSDEV
HHHHHHHHHHCCHHH		9.7026699800
146PhosphorylationAEAYEVLSDEVKRKQ
HHHHHHCCHHHHHHH		36.5826699800
150UbiquitinationEVLSDEVKRKQYDAY
HHCCHHHHHHHHCCC		52.40-
152 (in isoform 2)Ubiquitination-47.7121890473
152AcetylationLSDEVKRKQYDAYGS
CCHHHHHHHHCCCCC		47.7126051181
152 (in isoform 1)Ubiquitination-47.7121890473
152UbiquitinationLSDEVKRKQYDAYGS
CCHHHHHHHHCCCCC		47.7121890473
159PhosphorylationKQYDAYGSAGFDPGA
HHHCCCCCCCCCCCC		16.73-
167PhosphorylationAGFDPGASGSQHSYW
CCCCCCCCCCCCCCC		44.9127080861
169PhosphorylationFDPGASGSQHSYWKG
CCCCCCCCCCCCCCC		23.4017525332
175UbiquitinationGSQHSYWKGGPTVDP
CCCCCCCCCCCCCCH		45.84-
226AcetylationQAAKGVNKEFTVNIM
HHCCCCCCEEEEEEE		52.3725038526
233SulfoxidationKEFTVNIMDTCERCN
CEEEEEEEHHHHHCC		2.7021406390
238MethylationNIMDTCERCNGKGNE
EEEHHHHHCCCCCCC		22.7323455924
287PhosphorylationGRGSIIISPCVVCRG
CCCCEEEECCEEECC		11.2224670416
293MethylationISPCVVCRGAGQAKQ
EECCEEECCCCCCCC		26.7923455924
317PhosphorylationAGVEDGQTVRMPVGK
CCCCCCCEEEEECCC		18.6620068231
335MalonylationFITFRVQKSPVFRRD
EEEEEEECCCCCCCC		54.6026320211
335SuccinylationFITFRVQKSPVFRRD
EEEEEEECCCCCCCC		54.6027452117
398PhosphorylationKGIPRINSYGYGDHY
CCCCCCCCCCCCCCE		19.9825159151
399PhosphorylationGIPRINSYGYGDHYI
CCCCCCCCCCCCCEE		15.1830108239
401PhosphorylationPRINSYGYGDHYIHI
CCCCCCCCCCCEEEE		15.9030108239
405PhosphorylationSYGYGDHYIHIKIRV
CCCCCCCEEEEEEEC		10.0329083192
417PhosphorylationIRVPKRLTSRQQSLI
EECCCCCCHHHHEEE		26.37-
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 DNJA3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJA3_HUMAN !!
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 DNJA3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RNF34_HUMANRNF34physical
12118383
F131C_HUMANFAM131Cphysical
16189514
ZBT22_HUMANZBTB22physical
16189514
JAK2_HUMANJAK2physical
11679576
INGR2_HUMANIFNGR2physical
11679576
HSP7C_HUMANHSPA8physical
11679576
RASA1_HUMANRASA1physical
11116152
CHIP_HUMANSTUB1physical
21710689
GRP75_HUMANHSPA9physical
22544056
IKBB_HUMANNFKBIBphysical
15601829
RS18_HUMANRPS18physical
22939629
NDUS7_HUMANNDUFS7physical
22939629
MYO1C_HUMANMYO1Cphysical
22939629
SCFD1_HUMANSCFD1physical
22939629
QCR8_HUMANUQCRQphysical
22939629
KDM1A_HUMANKDM1Aphysical
23455924
CARM1_HUMANCARM1physical
23455924
ANM6_HUMANPRMT6physical
23455924
EGFR_HUMANEGFRphysical
23698466
HS90A_HUMANHSP90AA1physical
23698466
PI5PA_HUMANINPP5Jphysical
25416956
OSGI1_HUMANOSGIN1physical
25416956
NOC4L_HUMANNOC4Lphysical
25416956
GCC1_HUMANGCC1physical
25416956
F214B_HUMANFAM214Bphysical
25416956
FRMD6_HUMANFRMD6physical
25416956
C2CD6_HUMANALS2CR11physical
25416956
PYR1_HUMANCADphysical
26344197
GRP75_HUMANHSPA9physical
26344197
KAPCA_HUMANPRKACAphysical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DNJA3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-169, AND MASSSPECTROMETRY.

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