PKN2_MOUSE - dbPTM
PKN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKN2_MOUSE
UniProt AC Q8BWW9
Protein Name Serine/threonine-protein kinase N2
Gene Name Pkn2
Organism Mus musculus (Mouse).
Sequence Length 983
Subcellular Localization Cytoplasm . Nucleus . Membrane . Cell projection, lamellipodium . Cytoplasm, cytoskeleton . Cleavage furrow . Midbody . Cell junction . Colocalizes with PTPN13 in lamellipodia-like structures, regions of large actin turnover. Accumulates during telop
Protein Description PKC-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. Plays a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion, tumor cell invasion and transcription activation signaling processes. Phosphorylates CTTN in hyaluronan-induced astrocytes and hence decreases CTTN ability to associate with filamentous actin. Phosphorylates HDAC5, therefore lead to impair HDAC5 import. Direct RhoA target required for the regulation of the maturation of primordial junctions into apical junction formation in bronchial epithelial cells. Required for G2/M phases of the cell cycle progression and abscission during cytokinesis in a ECT2-dependent manner. Stimulates FYN kinase activity that is required for establishment of skin cell-cell adhesion during keratinocytes differentiation. Regulates epithelial bladder cells speed and direction of movement during cell migration and tumor cell invasion. Inhibits Akt pro-survival-induced kinase activity. Mediates Rho protein-induced transcriptional activation via the c-fos serum response factor (SRF). Involved in the negative regulation of ciliogenesis (By similarity)..
Protein Sequence MASNPDRGEILLTELQGDSRTLPFSENVSAVQKLDFSDTMVQQKLDDIKDRIKREIRKELKIKEGAENLRKVTTDKKNLAYVDNILKKSNKKLEELHHKLQELNAHIVVSDPEDSTDCPRTPDTPNSDSRSSTSNNRLMALQKQLDIELKVKQGAENMIQMYSNGSSKDRKLHGTAQQLLQDSKTKIEVIRMQILQAVQTNELAFDNAKPVISPLELRMEELRHHFKIEFAVAEGAKNVMKLLGSGKVTDRKALSEAQARFNESSQKLDLLKYSLEQRLNELPRNHPKSSVVIEELSLVASPTLSPRQSMLSTQNQYSTLSKPAALTGTLEVRLMGCQDILENVPGRSKATSVALPGWSPSDNRSSFMSRTSKSKSGSSRNLLKTDDLSNDVCAVLKLDNTVVGQTSWKPISNQSWDQKFTLELDRSRELEISVYWRDWRSLCAVKFLRLEDFLDNQRHGMCLYLEPQGTLFAEVTFFNPVIERRPKLQRQKKIFSKQQGKTFLRAPQMNINIATWGRLVRRAIPTVNHSGTFSPQTPVPATVPVVDARIPDLAPPASDSTVTKLDFDLEPEPPPAPPRASSLGETDESSELRVLDIPGQGSETVFNIENDRNNLRPKSKSEYELSIPDSGRSCWGVGELDDKRAQQRFQFSLQDFRCCAVLGRGHFGKVLLAEYKHTNEMFAIKALKKGDIVARDEVDSLMCEKRIFETVNSVRHPFLVNLFACFQTKEHVCFVMEYAAGGDLMMHIHTDVFSEPRAVFYAACVVLGLQYLHEHKIVYRDLKLDNLLLDTEGFVKIADFGLCKEGMGYGDRTSTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRRNPERRLGAGEKDAEDVKKHPFFRLTDWSALMDKKVKPPFVPTIRGREDVSNFDDEFTSEAPILTPPREPRILLEEEQEMFHDFDYVADWC
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
3Phosphorylation-----MASNPDRGEI
-----CCCCCCCCCE		47.8226824392
19PhosphorylationLTELQGDSRTLPFSE
EEEECCCCCCCCCCC		33.7129514104
49MalonylationQQKLDDIKDRIKREI
HHHHHHHHHHHHHHH		48.2026073543
76UbiquitinationLRKVTTDKKNLAYVD
HHHCCCCCCHHHHHH		41.28-
77AcetylationRKVTTDKKNLAYVDN
HHCCCCCCHHHHHHH		61.0623806337
87UbiquitinationAYVDNILKKSNKKLE
HHHHHHHHHCCHHHH		50.81-
110PhosphorylationLNAHIVVSDPEDSTD
HCCCEEECCCCCCCC		36.2327087446
115PhosphorylationVVSDPEDSTDCPRTP
EECCCCCCCCCCCCC		25.2025619855
116PhosphorylationVSDPEDSTDCPRTPD
ECCCCCCCCCCCCCC		54.6825619855
121PhosphorylationDSTDCPRTPDTPNSD
CCCCCCCCCCCCCCC		15.6225619855
124PhosphorylationDCPRTPDTPNSDSRS
CCCCCCCCCCCCCCC		26.1025619855
127PhosphorylationRTPDTPNSDSRSSTS
CCCCCCCCCCCCCCC		37.8625619855
129PhosphorylationPDTPNSDSRSSTSNN
CCCCCCCCCCCCCHH		33.6025619855
131PhosphorylationTPNSDSRSSTSNNRL
CCCCCCCCCCCHHHH		41.7525777480
132PhosphorylationPNSDSRSSTSNNRLM
CCCCCCCCCCHHHHH		34.4425777480
133PhosphorylationNSDSRSSTSNNRLMA
CCCCCCCCCHHHHHH		36.4025777480
134PhosphorylationSDSRSSTSNNRLMAL
CCCCCCCCHHHHHHH		33.7725777480
289PhosphorylationLPRNHPKSSVVIEEL
CCCCCCCCCEEEEEE		32.5827087446
290PhosphorylationPRNHPKSSVVIEELS
CCCCCCCCEEEEEEE		26.9126643407
297PhosphorylationSVVIEELSLVASPTL
CEEEEEEECCCCCCC		24.8725293948
301PhosphorylationEELSLVASPTLSPRQ
EEEECCCCCCCCHHH		15.7826239621
303PhosphorylationLSLVASPTLSPRQSM
EECCCCCCCCHHHHH		37.0626745281
305PhosphorylationLVASPTLSPRQSMLS
CCCCCCCCHHHHHCC		22.1027087446
309PhosphorylationPTLSPRQSMLSTQNQ
CCCCHHHHHCCCCCC		23.9928066266
312PhosphorylationSPRQSMLSTQNQYST
CHHHHHCCCCCCHHC		21.2128066266
313PhosphorylationPRQSMLSTQNQYSTL
HHHHHCCCCCCHHCC		27.8128066266
317PhosphorylationMLSTQNQYSTLSKPA
HCCCCCCHHCCCCCH		15.9226643407
318PhosphorylationLSTQNQYSTLSKPAA
CCCCCCHHCCCCCHH		17.0726643407
319PhosphorylationSTQNQYSTLSKPAAL
CCCCCHHCCCCCHHH		30.0726643407
321PhosphorylationQNQYSTLSKPAALTG
CCCHHCCCCCHHHCC		36.3626643407
351PhosphorylationVPGRSKATSVALPGW
CCCCCCCCEEECCCC		27.7225619855
352PhosphorylationPGRSKATSVALPGWS
CCCCCCCEEECCCCC		15.3925619855
359PhosphorylationSVALPGWSPSDNRSS
EEECCCCCCCCCCHH		22.0527087446
361PhosphorylationALPGWSPSDNRSSFM
ECCCCCCCCCCHHHH		41.8425619855
365PhosphorylationWSPSDNRSSFMSRTS
CCCCCCCHHHHHCCC		33.8926239621
366PhosphorylationSPSDNRSSFMSRTSK
CCCCCCHHHHHCCCC		23.0226239621
369PhosphorylationDNRSSFMSRTSKSKS
CCCHHHHHCCCCCCC		30.3226745281
372PhosphorylationSSFMSRTSKSKSGSS
HHHHHCCCCCCCCCC		33.5529514104
376PhosphorylationSRTSKSKSGSSRNLL
HCCCCCCCCCCCCCC		51.5029550500
378PhosphorylationTSKSKSGSSRNLLKT
CCCCCCCCCCCCCCC		32.9629550500
379PhosphorylationSKSKSGSSRNLLKTD
CCCCCCCCCCCCCCC		28.8129550500
496PhosphorylationQRQKKIFSKQQGKTF
HHHHHHHHHHCCCCH		32.7825266776
526PhosphorylationLVRRAIPTVNHSGTF
HHHHHCCCCCCCCCC		28.0326745281
530PhosphorylationAIPTVNHSGTFSPQT
HCCCCCCCCCCCCCC		34.0326745281
532PhosphorylationPTVNHSGTFSPQTPV
CCCCCCCCCCCCCCC		24.7726745281
534PhosphorylationVNHSGTFSPQTPVPA
CCCCCCCCCCCCCCC		18.8821659605
537PhosphorylationSGTFSPQTPVPATVP
CCCCCCCCCCCCCCE		29.6321659605
542PhosphorylationPQTPVPATVPVVDAR
CCCCCCCCCEEECCC		21.1926643407
581PhosphorylationPPAPPRASSLGETDE
CCCCCCHHHCCCCCC		27.6325521595
582PhosphorylationPAPPRASSLGETDES
CCCCCHHHCCCCCCC		39.1327087446
586PhosphorylationRASSLGETDESSELR
CHHHCCCCCCCCCEE		43.1825619855
589PhosphorylationSLGETDESSELRVLD
HCCCCCCCCCEEEEE		31.7425619855
590PhosphorylationLGETDESSELRVLDI
CCCCCCCCCEEEEEC		38.3125619855
619PhosphorylationRNNLRPKSKSEYELS
CCCCCCCCCCCEEEE		44.0625521595
620AcetylationNNLRPKSKSEYELSI
CCCCCCCCCCEEEEC		54.1323806337
621PhosphorylationNLRPKSKSEYELSIP
CCCCCCCCCEEEECC		53.1326824392
623PhosphorylationRPKSKSEYELSIPDS
CCCCCCCEEEECCCC		29.3025619855
626PhosphorylationSKSEYELSIPDSGRS
CCCCEEEECCCCCCC		21.8225619855
630PhosphorylationYELSIPDSGRSCWGV
EEEECCCCCCCCCCC		30.65-
652PhosphorylationAQQRFQFSLQDFRCC
HHHHHCCCHHHHHHH		17.8422006019
728PhosphorylationNLFACFQTKEHVCFV
HHHHHCCCCCEEEEE		20.39-
791PhosphorylationLDNLLLDTEGFVKIA
CCCEEECCCCCEEHH		37.6726643407
809PhosphorylationLCKEGMGYGDRTSTF
CCCCCCCCCCCCCCC		13.6322322096
813PhosphorylationGMGYGDRTSTFCGTP
CCCCCCCCCCCCCCC		36.5422322096
814PhosphorylationMGYGDRTSTFCGTPE
CCCCCCCCCCCCCCC		22.0022322096
815PhosphorylationGYGDRTSTFCGTPEF
CCCCCCCCCCCCCCC		23.4922322096
819PhosphorylationRTSTFCGTPEFLAPE
CCCCCCCCCCCCCHH		22.3322322096
829PhosphorylationFLAPEVLTETSYTRA
CCCHHHHCCCCCCCC		42.2525777480
831PhosphorylationAPEVLTETSYTRAVD
CHHHHCCCCCCCCHH		23.0725777480
929UbiquitinationALMDKKVKPPFVPTI
HHHCCCCCCCCCCCC		56.7222790023
943PhosphorylationIRGREDVSNFDDEFT
CCCCCCCCCCCCCCC		44.0625619855
950PhosphorylationSNFDDEFTSEAPILT
CCCCCCCCCCCCCCC		24.4925619855
951PhosphorylationNFDDEFTSEAPILTP
CCCCCCCCCCCCCCC		36.7625619855
957PhosphorylationTSEAPILTPPREPRI
CCCCCCCCCCCCCCC		31.7825521595
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
815TPhosphorylationKinasePDPK1Q9Z2A0
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKN2_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 PKN2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PKN2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PKN2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-582, AND MASSSPECTROMETRY.

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