KPCD3_HUMAN - dbPTM
KPCD3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KPCD3_HUMAN
UniProt AC O94806
Protein Name Serine/threonine-protein kinase D3
Gene Name PRKD3
Organism Homo sapiens (Human).
Sequence Length 890
Subcellular Localization Cytoplasm . Membrane . Translocation to the cell membrane is required for kinase activation.
Protein Description Converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. Involved in resistance to oxidative stress (By similarity)..
Protein Sequence MSANNSPPSAQKSVLPTAIPAVLPAASPCSSPKTGLSARLSNGSFSAPSLTNSRGSVHTVSFLLQIGLTRESVTIEAQELSLSAVKDLVCSIVYQKFPECGFFGMYDKILLFRHDMNSENILQLITSADEIHEGDLVEVVLSALATVEDFQIRPHTLYVHSYKAPTFCDYCGEMLWGLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRRLSNVSLPGPGLSVPRPLQPEYVALPSEESHVHQEPSKRIPSWSGRPIWMEKMVMCRVKVPHTFAVHSYTRPTICQYCKRLLKGLFRQGMQCKDCKFNCHKRCASKVPRDCLGEVTFNGEPSSLGTDTDIPMDIDNNDINSDSSRGLDDTEEPSPPEDKMFFLDPSDLDVERDEEAVKTISPSTSNNIPLMRVVQSIKHTKRKSSTMVKEGWMVHYTSRDNLRKRHYWRLDSKCLTLFQNESGSKYYKEIPLSEILRISSPRDFTNISQGSNPHCFEIITDTMVYFVGENNGDSSHNPVLAATGVGLDVAQSWEKAIRQALMPVTPQASVCTSPGQGKDHKDLSTSISVSNCQIQENVDISTVYQIFADEVLGSGQFGIVYGGKHRKTGRDVAIKVIDKMRFPTKQESQLRNEVAILQNLHHPGIVNLECMFETPERVFVVMEKLHGDMLEMILSSEKSRLPERITKFMVTQILVALRNLHFKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRSKGYNRSLDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAFMYPPNPWREISGEAIDLINNLLQVKMRKRYSVDKSLSHPWLQDYQTWLDLREFETRIGERYITHESDDARWEIHAYTHNLVYPKHFIMAPNPDDMEEDP
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
2Phosphorylation------MSANNSPPS
------CCCCCCCCH		39.4429255136
6Phosphorylation--MSANNSPPSAQKS
--CCCCCCCCHHHHC		37.6929255136
9PhosphorylationSANNSPPSAQKSVLP
CCCCCCCHHHHCCCC		46.8730177828
13PhosphorylationSPPSAQKSVLPTAIP
CCCHHHHCCCCCCHH		19.4623403867
17PhosphorylationAQKSVLPTAIPAVLP
HHHCCCCCCHHHHCC		32.8120068231
27PhosphorylationPAVLPAASPCSSPKT
HHHCCCCCCCCCCCC		28.6620201521
30PhosphorylationLPAASPCSSPKTGLS
CCCCCCCCCCCCCCC		53.7320201521
31PhosphorylationPAASPCSSPKTGLSA
CCCCCCCCCCCCCCE		36.8125159151
34UbiquitinationSPCSSPKTGLSARLS
CCCCCCCCCCCEECC		46.9021890473
34PhosphorylationSPCSSPKTGLSARLS
CCCCCCCCCCCEECC		46.9028450419
37PhosphorylationSSPKTGLSARLSNGS
CCCCCCCCEECCCCC		16.8222617229
41PhosphorylationTGLSARLSNGSFSAP
CCCCEECCCCCCCCC		33.3222167270
44PhosphorylationSARLSNGSFSAPSLT
CEECCCCCCCCCCCC		21.9322167270
46PhosphorylationRLSNGSFSAPSLTNS
ECCCCCCCCCCCCCC		40.7530266825
49PhosphorylationNGSFSAPSLTNSRGS
CCCCCCCCCCCCCCC		47.7623403867
51PhosphorylationSFSAPSLTNSRGSVH
CCCCCCCCCCCCCEE		35.1722167270
53PhosphorylationSAPSLTNSRGSVHTV
CCCCCCCCCCCEEHH		32.5522167270
120UbiquitinationRHDMNSENILQLITS
ECCCCCHHHHHHHHC		39.8421890473
166PhosphorylationVHSYKAPTFCDYCGE
EEECCCCCHHHHHHH		41.5830387612
170PhosphorylationKAPTFCDYCGEMLWG
CCCCHHHHHHHHHHH		11.9730387612
189UbiquitinationGLKCEGCGLNYHKRC
CCCCCCCCCCCCCCC		28.0221890473
213PhosphorylationGVRKRRLSNVSLPGP
CCCCCCCCCCCCCCC		33.1230266825
216PhosphorylationKRRLSNVSLPGPGLS
CCCCCCCCCCCCCCC		32.8529255136
223PhosphorylationSLPGPGLSVPRPLQP
CCCCCCCCCCCCCCC		35.6718691976
232PhosphorylationPRPLQPEYVALPSEE
CCCCCCCEEECCCCC		9.5628796482
237PhosphorylationPEYVALPSEESHVHQ
CCEEECCCCCCCCCC		55.6418691976
240PhosphorylationVALPSEESHVHQEPS
EECCCCCCCCCCCCC		27.1027642862
247PhosphorylationSHVHQEPSKRIPSWS
CCCCCCCCCCCCCCC		33.5418691976
252PhosphorylationEPSKRIPSWSGRPIW
CCCCCCCCCCCCCEE		31.3522617229
254PhosphorylationSKRIPSWSGRPIWME
CCCCCCCCCCCEECE		29.3023403867
293UbiquitinationQYCKRLLKGLFRQGM
HHHHHHHHHHHHCCC		59.1521890473
315PhosphorylationNCHKRCASKVPRDCL
CCCHHHHCCCCHHHC		37.5024719451
332PhosphorylationVTFNGEPSSLGTDTD
EEECCCCCCCCCCCC		33.6122210691
336PhosphorylationGEPSSLGTDTDIPMD
CCCCCCCCCCCCCCC		40.8130576142
351PhosphorylationIDNNDINSDSSRGLD
CCCCCCCCCCCCCCC		38.9222210691
360PhosphorylationSSRGLDDTEEPSPPE
CCCCCCCCCCCCCCC		41.7521815630
364PhosphorylationLDDTEEPSPPEDKMF
CCCCCCCCCCCCCCE		57.2623401153
389PhosphorylationRDEEAVKTISPSTSN
CCHHHHHHCCCCCCC		21.7930266825
391PhosphorylationEEAVKTISPSTSNNI
HHHHHHCCCCCCCCC		20.3029255136
393PhosphorylationAVKTISPSTSNNIPL
HHHHCCCCCCCCCCH		37.3630266825
394PhosphorylationVKTISPSTSNNIPLM
HHHCCCCCCCCCCHH		38.5730266825
395PhosphorylationKTISPSTSNNIPLMR
HHCCCCCCCCCCHHH		32.0130266825
406PhosphorylationPLMRVVQSIKHTKRK
CHHHHHHHHHHCCCC		23.2230576142
408UbiquitinationMRVVQSIKHTKRKSS
HHHHHHHHHCCCCCC		50.9329967540
414PhosphorylationIKHTKRKSSTMVKEG
HHHCCCCCCCCEECC		34.7719369195
415PhosphorylationKHTKRKSSTMVKEGW
HHCCCCCCCCEECCE		24.4522817900
426PhosphorylationKEGWMVHYTSRDNLR
ECCEEEEEECCCCCH		8.59-
442PhosphorylationRHYWRLDSKCLTLFQ
HEEEEECHHHEEEEE		29.8423312004
446PhosphorylationRLDSKCLTLFQNESG
EECHHHEEEEECCCC		34.6923312004
452PhosphorylationLTLFQNESGSKYYKE
EEEEECCCCCCEEEE		56.7828348404
455AcetylationFQNESGSKYYKEIPL
EECCCCCCEEEECCH		57.0026051181
456PhosphorylationQNESGSKYYKEIPLS
ECCCCCCEEEECCHH		22.8224719451
457PhosphorylationNESGSKYYKEIPLSE
CCCCCCEEEECCHHH		13.0929341593
463PhosphorylationYYKEIPLSEILRISS
EEEECCHHHHHCCCC		19.7524719451
469PhosphorylationLSEILRISSPRDFTN
HHHHHCCCCCCCCCC		28.0523532336
470PhosphorylationSEILRISSPRDFTNI
HHHHCCCCCCCCCCC		22.9124719451
471UbiquitinationEILRISSPRDFTNIS
HHHCCCCCCCCCCCC		32.8227667366
535PhosphorylationRQALMPVTPQASVCT
HHHHCCCCCCCCEEC		12.1025159151
539PhosphorylationMPVTPQASVCTSPGQ
CCCCCCCCEECCCCC		16.6925159151
542PhosphorylationTPQASVCTSPGQGKD
CCCCCEECCCCCCCC		35.4825159151
543PhosphorylationPQASVCTSPGQGKDH
CCCCEECCCCCCCCC		23.1625159151
557UbiquitinationHKDLSTSISVSNCQI
CCCCCEEEEEECCEE		4.8327667366
605UbiquitinationTGRDVAIKVIDKMRF
CCCCEEHHHHHHCCC		24.33-
615UbiquitinationDKMRFPTKQESQLRN
HHCCCCCHHHHHHHH		52.9129967540
626UbiquitinationQLRNEVAILQNLHHP
HHHHHHHHHHHCCCC		4.9927667366
730UbiquitinationFARIIGEKSFRRSVV
CCEECCCCCHHCCCC		50.0832142685
731PhosphorylationARIIGEKSFRRSVVG
CEECCCCCHHCCCCC		21.4923401153
735PhosphorylationGEKSFRRSVVGTPAY
CCCCHHCCCCCCHHH		19.5229255136
739PhosphorylationFRRSVVGTPAYLAPE
HHCCCCCCHHHHCHH		7.9821945579
742PhosphorylationSVVGTPAYLAPEVLR
CCCCCHHHHCHHHHH		12.4721945579
802PhosphorylationPNPWREISGEAIDLI
CCCHHHCCHHHHHHH		26.3121082442
816UbiquitinationINNLLQVKMRKRYSV
HHHHHHHHHHHCCCC		21.74-
822PhosphorylationVKMRKRYSVDKSLSH
HHHHHCCCCCCCCCC		28.0719369195
852PhosphorylationETRIGERYITHESDD
HHHHCEEEEECCCCC		13.0822817900
867PhosphorylationARWEIHAYTHNLVYP
CCEEEEEEECCCCCC		8.3822817900
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
731SPhosphorylationKinasePRKCAP17252
GPS
731SPhosphorylationKinasePKC-FAMILY-GPS
731SPhosphorylationKinasePKC-Uniprot
735SPhosphorylationKinasePRKD3O94806
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KPCD3_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 KPCD3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SKA2_HUMANSKA2physical
21988832
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 KPCD3_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-41 AND SER-44, AND MASSSPECTROMETRY.
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-6; SER-27;SER-30; SER-31; THR-34; SER-41; SER-44; SER-213; SER-216; SER-237;SER-247; SER-252; SER-364; SER-414; SER-415; THR-535; SER-539; THR-542AND SER-543, AND MASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-31, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-30; SER-41;SER-44 AND SER-364, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6; SER-27; SER-31;SER-37; SER-41; SER-44; SER-213; SER-216; SER-252; SER-364; SER-391;SER-395; THR-535; SER-543; SER-731 AND SER-735, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-391 AND SER-735, ANDMASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, 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-41 AND SER-44, AND MASSSPECTROMETRY.

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