DNJA2_HUMAN - dbPTM
DNJA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DNJA2_HUMAN
UniProt AC O60884
Protein Name DnaJ homolog subfamily A member 2
Gene Name DNAJA2
Organism Homo sapiens (Human).
Sequence Length 412
Subcellular Localization Membrane
Lipid-anchor .
Protein Description Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro). [PubMed: 24318877]
Protein Sequence MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDGRQIVVKYPPGKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPEVPNIIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ
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
10PhosphorylationNVADTKLYDILGVPP
CCCCCCHHHHHCCCC		11.5127642862
20PhosphorylationLGVPPGASENELKKA
HCCCCCCCHHHHHHH		47.0425693802
25UbiquitinationGASENELKKAYRKLA
CCCHHHHHHHHHHHH		29.2221906983
25AcetylationGASENELKKAYRKLA
CCCHHHHHHHHHHHH		29.2225953088
26UbiquitinationASENELKKAYRKLAK
CCHHHHHHHHHHHHH		64.3721906983
33UbiquitinationKAYRKLAKEYHPDKN
HHHHHHHHHHCCCCC		70.06-
33AcetylationKAYRKLAKEYHPDKN
HHHHHHHHHHCCCCC		70.067683259
35PhosphorylationYRKLAKEYHPDKNPN
HHHHHHHHCCCCCCC		20.2528152594
39AcetylationAKEYHPDKNPNAGDK
HHHHCCCCCCCCCHH		77.93-
39UbiquitinationAKEYHPDKNPNAGDK
HHHHCCCCCCCCCHH		77.9321906983
462-HydroxyisobutyrylationKNPNAGDKFKEISFA
CCCCCCHHHHHCHHH		58.37-
46UbiquitinationKNPNAGDKFKEISFA
CCCCCCHHHHHCHHH		58.3721890473
46AcetylationKNPNAGDKFKEISFA
CCCCCCHHHHHCHHH		58.3725953088
51PhosphorylationGDKFKEISFAYEVLS
CHHHHHCHHHHHHHC		12.6228152594
54PhosphorylationFKEISFAYEVLSNPE
HHHCHHHHHHHCCHH		12.4525839225
54NitrationFKEISFAYEVLSNPE
HHHCHHHHHHHCCHH		12.45-
58PhosphorylationSFAYEVLSNPEKREL
HHHHHHHCCHHHHHH		56.3628152594
62UbiquitinationEVLSNPEKRELYDRY
HHHCCHHHHHHHHHH		53.0521906983
66PhosphorylationNPEKRELYDRYGEQG
CHHHHHHHHHHHHHC		8.1428152594
68MethylationEKRELYDRYGEQGLR
HHHHHHHHHHHHCCC		28.00-
69PhosphorylationKRELYDRYGEQGLRE
HHHHHHHHHHHCCCC		23.3225839225
78PhosphorylationEQGLREGSGGGGGMD
HHCCCCCCCCCCCHH		29.5222617229
121AcetylationEDMMHPLKVSLEDLY
CCCCCCEECCHHHHH		33.9425953088
123PhosphorylationMMHPLKVSLEDLYNG
CCCCEECCHHHHHCC		25.1825849741
128PhosphorylationKVSLEDLYNGKTTKL
ECCHHHHHCCCCCEE		33.9029449344
131UbiquitinationLEDLYNGKTTKLQLS
HHHHHCCCCCEEEEC		49.7521906983
131AcetylationLEDLYNGKTTKLQLS
HHHHHCCCCCEEEEC		49.7530588259
134UbiquitinationLYNGKTTKLQLSKNV
HHCCCCCEEEECCCE		39.1921906983
134AcetylationLYNGKTTKLQLSKNV
HHCCCCCEEEECCCE		39.1923749302
134SumoylationLYNGKTTKLQLSKNV
HHCCCCCEEEECCCE		39.1928112733
1342-HydroxyisobutyrylationLYNGKTTKLQLSKNV
HHCCCCCEEEECCCE		39.19-
139UbiquitinationTTKLQLSKNVLCSAC
CCEEEECCCEEEHHH		60.72-
144PhosphorylationLSKNVLCSACSGQGG
ECCCEEEHHHCCCCC		28.3125159151
147PhosphorylationNVLCSACSGQGGKSG
CEEEHHHCCCCCCCC		33.5925159151
152AcetylationACSGQGGKSGAVQKC
HHCCCCCCCCHHEEC		53.1726051181
152UbiquitinationACSGQGGKSGAVQKC
HHCCCCCCCCHHEEC		53.1721906983
153PhosphorylationCSGQGGKSGAVQKCS
HCCCCCCCCHHEECH		34.95-
158AcetylationGKSGAVQKCSACRGR
CCCCHHEECHHCCCC		24.4525953088
158UbiquitinationGKSGAVQKCSACRGR
CCCCHHEECHHCCCC		24.4521906983
1582-HydroxyisobutyrylationGKSGAVQKCSACRGR
CCCCHHEECHHCCCC		24.45-
184PhosphorylationGMVQQMQSVCSDCNG
HHHHHHHHHHHHCCC		21.5428348404
187PhosphorylationQQMQSVCSDCNGEGE
HHHHHHHHHCCCCCC		42.9424719451
199AcetylationEGEVINEKDRCKKCE
CCCCCCCCHHCCCCC		46.0826051181
199UbiquitinationEGEVINEKDRCKKCE
CCCCCCCCHHCCCCC		46.0821906983
223AcetylationILEVHVDKGMKHGQR
EEEEEECCCCCCCCE		60.8725953088
255UbiquitinationIVLLLQEKEHEVFQR
EEEEEECCCCHHHCC		51.95-
297UbiquitinationDGRQIVVKYPPGKVI
CCCEEEEECCCCCEE		40.94-
302MethylationVVKYPPGKVIEPGCV
EEECCCCCEECCCCE		45.90-
302UbiquitinationVVKYPPGKVIEPGCV
EEECCCCCEECCCCE		45.90-
302"N6,N6-dimethyllysine"VVKYPPGKVIEPGCV
EEECCCCCEECCCCE		45.90-
317SulfoxidationRVVRGEGMPQYRNPF
EEECCCCCCCCCCCC		1.3030846556
326AcetylationQYRNPFEKGDLYIKF
CCCCCCCCCCEEEEE		59.0926051181
326UbiquitinationQYRNPFEKGDLYIKF
CCCCCCCCCCEEEEE		59.0921906983
330PhosphorylationPFEKGDLYIKFDVQF
CCCCCCEEEEEEEEC		13.55-
349PhosphorylationWINPDKLSELEDLLP
EECHHHHHHHHHHCC		45.9720068231
357PhosphorylationELEDLLPSRPEVPNI
HHHHHCCCCCCCCCC		61.5129632367
368PhosphorylationVPNIIGETEEVELQE
CCCCCCCCCEEEEEE		32.0320068231
378PhosphorylationVELQEFDSTRGSGGG
EEEEECCCCCCCCCC		25.8929632367
379PhosphorylationELQEFDSTRGSGGGQ
EEEECCCCCCCCCCC		40.6829632367
382PhosphorylationEFDSTRGSGGGQRRE
ECCCCCCCCCCCCCC		30.8629632367
391PhosphorylationGGQRREAYNDSSDEE
CCCCCCCCCCCCCCC		18.1026846344
394PhosphorylationRREAYNDSSDEESSS
CCCCCCCCCCCCHHC		35.7326503892
395PhosphorylationREAYNDSSDEESSSH
CCCCCCCCCCCHHCC		52.4826503892
399PhosphorylationNDSSDEESSSHHGPG
CCCCCCCHHCCCCCC		34.7823663014
400PhosphorylationDSSDEESSSHHGPGV
CCCCCCHHCCCCCCC		36.6523663014
401PhosphorylationSSDEESSSHHGPGVQ
CCCCCHHCCCCCCCC		28.8728450419
409FarnesylationHHGPGVQCAHQ----
CCCCCCCCCCC----		3.2015308774
409FarnesylationHHGPGVQCAHQ----
CCCCCCCCCCC----		3.2015308774
409MethylationHHGPGVQCAHQ----
CCCCCCCCCCC----		3.20-
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 DNJA2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DNJA2_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 DNJA2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIRA_HUMANHIRAphysical
17242198
RB_HUMANRB1physical
17242198
ERG_HUMANERGphysical
19940115
ABCF2_HUMANABCF2physical
26344197
PYR1_HUMANCADphysical
26344197
TCPD_HUMANCCT4physical
26344197
DCTN1_HUMANDCTN1physical
26344197
HSP7C_HUMANHSPA8physical
26344197
GRP75_HUMANHSPA9physical
26344197
PSA6_HUMANPSMA6physical
26344197
SMC3_HUMANSMC3physical
26344197
TCPA_HUMANTCP1physical
26344197
TBB4B_HUMANTUBB4Bphysical
26344197
XPO1_HUMANXPO1physical
26344197
DNJB1_HUMANDNAJB1physical
28504929
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 DNJA2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND MASSSPECTROMETRY.
Prenylation
ReferencePubMed
"A tagging-via-substrate technology for detection and proteomics offarnesylated proteins.";
Kho Y., Kim S.C., Jiang C., Barma D., Kwon S.W., Cheng J.,Jaunbergs J., Weinbaum C., Tamanoi F., Falck J., Zhao Y.;
Proc. Natl. Acad. Sci. U.S.A. 101:12479-12484(2004).
Cited for: ISOPRENYLATION AT CYS-409.

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