PKN3_HUMAN - dbPTM
PKN3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKN3_HUMAN
UniProt AC Q6P5Z2
Protein Name Serine/threonine-protein kinase N3
Gene Name PKN3
Organism Homo sapiens (Human).
Sequence Length 889
Subcellular Localization Nucleus . Cytoplasm, perinuclear region . Nuclear and perinuclear Golgi region.
Protein Description Contributes to invasiveness in malignant prostate cancer..
Protein Sequence MEEGAPRQPGPSQWPPEDEKEVIRRAIQKELKIKEGVENLRRVATDRRHLGHVQQLLRSSNRRLEQLHGELRELHARILLPGPGPGPAEPVASGPRPWAEQLRARHLEALRRQLHVELKVKQGAENMTHTCASGTPKERKLLAAAQQMLRDSQLKVALLRMKISSLEASGSPEPGPELLAEELQHRLHVEAAVAEGAKNVVKLLSSRRTQDRKALAEAQAQLQESSQKLDLLRLALEQLLEQLPPAHPLRSRVTRELRAAVPGYPQPSGTPVKPTALTGTLQVRLLGCEQLLTAVPGRSPAAALASSPSEGWLRTKAKHQRGRGELASEVLAVLKVDNRVVGQTGWGQVAEQSWDQTFVIPLERARELEIGVHWRDWRQLCGVAFLRLEDFLDNACHQLSLSLVPQGLLFAQVTFCDPVIERRPRLQRQERIFSKRRGQDFLRASQMNLGMAAWGRLVMNLLPPCSSPSTISPPKGCPRTPTTLREASDPATPSNFLPKKTPLGEEMTPPPKPPRLYLPQEPTSEETPRTKRPHMEPRTRRGPSPPASPTRKPPRLQDFRCLAVLGRGHFGKVLLVQFKGTGKYYAIKALKKQEVLSRDEIESLYCEKRILEAVGCTGHPFLLSLLACFQTSSHACFVTEFVPGGDLMMQIHEDVFPEPQARFYVACVVLGLQFLHEKKIIYRDLKLDNLLLDAQGFLKIADFGLCKEGIGFGDRTSTFCGTPEFLAPEVLTQEAYTRAVDWWGLGVLLYEMLVGECPFPGDTEEEVFDCIVNMDAPYPGFLSVQGLEFIQKLLQKCPEKRLGAGEQDAEEIKVQPFFRTTNWQALLARTIQPPFVPTLCGPADLRYFEGEFTGLPPALTPPAPHSLLTARQQAAFRDFDFVSERFLEP
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
20UbiquitinationQWPPEDEKEVIRRAI
CCCCHHHHHHHHHHH		70.38-
29UbiquitinationVIRRAIQKELKIKEG
HHHHHHHHHCCHHHH		59.92-
58MethylationGHVQQLLRSSNRRLE
HHHHHHHHHCHHHHH		46.78115487711
59PhosphorylationHVQQLLRSSNRRLEQ
HHHHHHHHCHHHHHH		31.7527174698
60PhosphorylationVQQLLRSSNRRLEQL
HHHHHHHCHHHHHHH		28.1127174698
135PhosphorylationTHTCASGTPKERKLL
CEECCCCCHHHHHHH		28.7925159151
140UbiquitinationSGTPKERKLLAAAQQ
CCCHHHHHHHHHHHH		49.28-
155UbiquitinationMLRDSQLKVALLRMK
HHHHHHHHHHHHHHH		20.16-
165PhosphorylationLLRMKISSLEASGSP
HHHHHHHHHHCCCCC		33.4330624053
169PhosphorylationKISSLEASGSPEPGP
HHHHHHCCCCCCCCH		30.3530624053
171PhosphorylationSSLEASGSPEPGPEL
HHHHCCCCCCCCHHH		24.4827050516
198UbiquitinationAAVAEGAKNVVKLLS
HHHHHHHHHHHHHHH		62.22-
202UbiquitinationEGAKNVVKLLSSRRT
HHHHHHHHHHHCCCH		39.15-
205O-linked_GlycosylationKNVVKLLSSRRTQDR
HHHHHHHHCCCHHHH		32.0330379171
205PhosphorylationKNVVKLLSSRRTQDR
HHHHHHHHCCCHHHH		32.0324719451
206PhosphorylationNVVKLLSSRRTQDRK
HHHHHHHCCCHHHHH		26.2524719451
213UbiquitinationSRRTQDRKALAEAQA
CCCHHHHHHHHHHHH		56.92-
254PhosphorylationHPLRSRVTRELRAAV
CCHHHHHHHHHHHHC		19.8129970186
270PhosphorylationGYPQPSGTPVKPTAL
CCCCCCCCCCCCCCC		29.2828555341
273UbiquitinationQPSGTPVKPTALTGT
CCCCCCCCCCCCCCC		37.54-
299PhosphorylationLTAVPGRSPAAALAS
HHCCCCCCHHHHHHC		25.47-
306PhosphorylationSPAAALASSPSEGWL
CHHHHHHCCCCCCHH		43.5629396449
307PhosphorylationPAAALASSPSEGWLR
HHHHHHCCCCCCHHH		27.1721712546
309PhosphorylationAALASSPSEGWLRTK
HHHHCCCCCCHHHHH		51.1718669648
434PhosphorylationQRQERIFSKRRGQDF
HHHHHHHHHHCCHHH		23.9224719451
445PhosphorylationGQDFLRASQMNLGMA
CHHHHHHHHHHHHHH		24.4328348404
466PhosphorylationMNLLPPCSSPSTISP
HHCCCCCCCCCCCCC		51.5721712546
472PhosphorylationCSSPSTISPPKGCPR
CCCCCCCCCCCCCCC		34.9321712546
480PhosphorylationPPKGCPRTPTTLREA
CCCCCCCCCCCHHHC		15.3228985074
482PhosphorylationKGCPRTPTTLREASD
CCCCCCCCCHHHCCC		37.5423312004
483PhosphorylationGCPRTPTTLREASDP
CCCCCCCCHHHCCCC		25.6423312004
488PhosphorylationPTTLREASDPATPSN
CCCHHHCCCCCCCCC		39.1025159151
492PhosphorylationREASDPATPSNFLPK
HHCCCCCCCCCCCCC		32.4121815630
494PhosphorylationASDPATPSNFLPKKT
CCCCCCCCCCCCCCC		35.5427050516
499UbiquitinationTPSNFLPKKTPLGEE
CCCCCCCCCCCCCCC		72.00-
500UbiquitinationPSNFLPKKTPLGEEM
CCCCCCCCCCCCCCC		54.13-
501PhosphorylationSNFLPKKTPLGEEMT
CCCCCCCCCCCCCCC		29.8523186163
508PhosphorylationTPLGEEMTPPPKPPR
CCCCCCCCCCCCCCC		35.6021130716
512UbiquitinationEEMTPPPKPPRLYLP
CCCCCCCCCCCCCCC		73.72-
517PhosphorylationPPKPPRLYLPQEPTS
CCCCCCCCCCCCCCC		20.0229978859
523PhosphorylationLYLPQEPTSEETPRT
CCCCCCCCCCCCCCC		48.2818691976
524PhosphorylationYLPQEPTSEETPRTK
CCCCCCCCCCCCCCC		44.1221815630
527PhosphorylationQEPTSEETPRTKRPH
CCCCCCCCCCCCCCC		17.6421815630
544PhosphorylationPRTRRGPSPPASPTR
CCCCCCCCCCCCCCC		46.4730266825
548PhosphorylationRGPSPPASPTRKPPR
CCCCCCCCCCCCCCC		32.3630266825
550PhosphorylationPSPPASPTRKPPRLQ
CCCCCCCCCCCCCCC		49.1530266825
583AcetylationVQFKGTGKYYAIKAL
EEEECCCCCHHHHHH		34.6212433637
583UbiquitinationVQFKGTGKYYAIKAL
EEEECCCCCHHHHHH		34.62-
588UbiquitinationTGKYYAIKALKKQEV
CCCCHHHHHHHHCCC		39.22-
592UbiquitinationYAIKALKKQEVLSRD
HHHHHHHHCCCCCHH		53.17-
597PhosphorylationLKKQEVLSRDEIESL
HHHCCCCCHHHHHHH		42.7530387612
605PhosphorylationRDEIESLYCEKRILE
HHHHHHHHHHHHHHH		14.0827642862
686UbiquitinationKIIYRDLKLDNLLLD
CEECCCCCHHHHEEC		59.07-
707UbiquitinationIADFGLCKEGIGFGD
HHHCCCCCCCCCCCC		65.11-
716PhosphorylationGIGFGDRTSTFCGTP
CCCCCCCCCCCCCCH		36.5421712546
717PhosphorylationIGFGDRTSTFCGTPE
CCCCCCCCCCCCCHH		22.0021712546
718PhosphorylationGFGDRTSTFCGTPEF
CCCCCCCCCCCCHHH		23.4922322096
722PhosphorylationRTSTFCGTPEFLAPE
CCCCCCCCHHHHCHH		22.3321712546
796UbiquitinationFIQKLLQKCPEKRLG
HHHHHHHHCCHHHCC		52.29-
813UbiquitinationEQDAEEIKVQPFFRT
CCCHHHHCCCCCCCC		37.79-
820PhosphorylationKVQPFFRTTNWQALL
CCCCCCCCCCHHHHH		21.23-
853PhosphorylationRYFEGEFTGLPPALT
HHHCCCCCCCCCCCC		33.2422210691
860PhosphorylationTGLPPALTPPAPHSL
CCCCCCCCCCCCCCH		29.3619369195
866PhosphorylationLTPPAPHSLLTARQQ
CCCCCCCCHHHHHHH		24.8228450419
869PhosphorylationPAPHSLLTARQQAAF
CCCCCHHHHHHHHHH		25.7028450419
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 PKN3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKN3_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 PKN3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RHG10_HUMANARHGAP10physical
11432776
RHG26_HUMANARHGAP26physical
11432776
CAVN1_HUMANPTRFphysical
27173435
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 PKN3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-544; THR-716 ANDTHR-860, AND MASS SPECTROMETRY.
"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-544 AND SER-548, ANDMASS 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-307; THR-508; SER-544;SER-548; THR-722 AND THR-860, AND MASS SPECTROMETRY.
"Proteomics analysis of protein kinases by target class-selectiveprefractionation and tandem mass spectrometry.";
Wissing J., Jaensch L., Nimtz M., Dieterich G., Hornberger R.,Keri G., Wehland J., Daub H.;
Mol. Cell. Proteomics 6:537-547(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-544 AND THR-550, ANDMASS SPECTROMETRY.
"PKN3 is required for malignant prostate cell growth downstream ofactivated PI 3-kinase.";
Leenders F., Moepert K., Schmiedeknecht A., Santel A., Czauderna F.,Aleku M., Penschuck S., Dames S., Sternberger M., Roehl T.,Wellmann A., Arnold W., Giese K., Kaufmann J., Klippel A.;
EMBO J. 23:3303-3313(2004).
Cited for: FUNCTION IN MALIGNANT CELL GROWTH, PHOSPHORYLATION AT THR-718, ANDMUTAGENESIS OF LYS-588 AND THR-718.

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