PKN_DROME - dbPTM
PKN_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PKN_DROME
UniProt AC A1Z7T0
Protein Name Serine/threonine-protein kinase N
Gene Name Pkn
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1190
Subcellular Localization Cytoplasm . Nucleus. Membrane. Cell projection, lamellipodium. Cytoplasm, cytoskeleton. Cleavage furrow. Midbody. Cell junction.
Protein Description Pkc-related serine/threonine-protein kinase and Rho/Rac effector protein that participates in specific signal transduction responses in the cell. May play a role in the regulation of cell cycle progression, actin cytoskeleton assembly, cell migration, cell adhesion and transcription activation signaling processes (By similarity). Plays a role in regulating Rho-mediated dorsal closure during embryogenesis..
Protein Sequence MSDSYYQGEYIKHPVLYELSHKYGFTENLPESCMSIRLEEIKEAIRREIRKELKIKEGAEKLREVAKDRRSLSDVAVLVKKSKSKLAELKSELQELESQILLTSANTAVNSNGQESITACIDPNGGFLVSGAVGGLGGGNTALEGGAPATANDKVLASLEKQLQIEMKVKTGAENMIQSLGIGCDKKLLAEAHQMLADSKAKIEFLRLRIIKVKQNREQADRLKASRQMIDEHGQTIGGNNSSQPQSLETTLEERIEELRHRLRIEAAVVDGAKNVIRTLQTANRAPDKKALQEAHGRLSESSRKLDLLRYSLDLRRQELPADSPAAQQLKTELQIVQLSTSPAPVTYTSLQSGQAGILGGKPYQSVSSLGRCASVTGKLEVRLLGCQDLLEDVPGRSRRDKDNNSSPGDLRSFVKGVTSRSSSKSYSVKDETSIEIMAVIKLDNITVGQTSWKQCSQQAWDQRFSIDLDRSRELEIGVYWRDWRSLCAVKVLRLEEFIDDVRHGMALQLEPQGLLFAEVKFLNPMISQKPKLRRQRMIFNRQQAKNISRAKQMNINVATWGRLLKRNAPNHVHMGSAGSGSSLTGSSPMVVGGSRDSESPISRTPSSDALVEPEPYTPGEQAQNLEFDPDAGINEHVETPGEYPDPAASGLSGMRPLSMHMQGISVLPPESPPVATGAAGRPNTLSLQMPGASKGQVIQGGRTAAPTTAPPPPPVLKATSTTPILDQEVIPQLGKLYVGSSQQQYAQQSSPIIQEPATPTIYGNSAAAGAPQFPQPAQRQEKQPPQQQPIYANQYELNVAKAAAAASVYSPSSSTTSNSNQQQQQQRRNVARGLQYRESGGLETGRAGKQPPNAGMLSMDNFRLLSVLGRGHFGKVILSQLRSNNQYYAIKALKKGDIIARDEVESLLSEKRIFEVANAMRHPFLVNLYSCFQTEQHVCFVMEYAAGGDLMMHIHTDVFLEPRAVFYAACVVLGLQYLHENKIIYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTGTFCGTPEFLAPEVLTETSYTRAVDWWGLGVLIFEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSLEAIAVMRRLLRKNPERRLGSSERDAEDVKKQAFFRSIVWDDLLLRKVKPPFVPTINHLEDVSNFDEEFTSEKAQLTPPKEPRHLTEEEQLLFQDFSYTAEWC
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
17PhosphorylationYIKHPVLYELSHKYG
CCCCHHHHHHHHHCC		18.3019429919
20PhosphorylationHPVLYELSHKYGFTE
CHHHHHHHHHCCCCC		13.1419429919
71PhosphorylationEVAKDRRSLSDVAVL
HHHHHCCCHHHHHHH		32.8719429919
73PhosphorylationAKDRRSLSDVAVLVK
HHHCCCHHHHHHHHH		31.1419429919
580PhosphorylationVHMGSAGSGSSLTGS
EECCCCCCCCCCCCC		34.9121082442
595PhosphorylationSPMVVGGSRDSESPI
CCEEECCCCCCCCCC		27.3022817900
598PhosphorylationVVGGSRDSESPISRT
EECCCCCCCCCCCCC		38.5729892262
600PhosphorylationGGSRDSESPISRTPS
CCCCCCCCCCCCCCC		31.3319429919
603PhosphorylationRDSESPISRTPSSDA
CCCCCCCCCCCCCCC		33.2219429919
709PhosphorylationGRTAAPTTAPPPPPV
CCCCCCCCCCCCCCC		35.7921082442
721PhosphorylationPPVLKATSTTPILDQ
CCCCEECCCCCCCCH		34.8319060867
722PhosphorylationPVLKATSTTPILDQE
CCCEECCCCCCCCHH		32.0322668510
723PhosphorylationVLKATSTTPILDQEV
CCEECCCCCCCCHHH		14.2219060867
750PhosphorylationQQQYAQQSSPIIQEP
HHHHHHHCCCCCCCC		26.4621082442
759PhosphorylationPIIQEPATPTIYGNS
CCCCCCCCCCCCCCC		31.5121082442
792PhosphorylationPPQQQPIYANQYELN
CCCCCCCCCCHHHHH		13.2419429919
796PhosphorylationQPIYANQYELNVAKA
CCCCCCHHHHHHHHH		23.3819429919
810PhosphorylationAAAAASVYSPSSSTT
HHHHHHCCCCCCCCC		16.6218281928
811PhosphorylationAAAASVYSPSSSTTS
HHHHHCCCCCCCCCC		19.0230478224
837PhosphorylationNVARGLQYRESGGLE
HHHHHHHHHHCCCCC		22.7618281928
840PhosphorylationRGLQYRESGGLETGR
HHHHHHHCCCCCCCC		29.2118511481
1020PhosphorylationGMGFGDRTGTFCGTP
CCCCCCCCCCCCCCH		45.3621082442
1022PhosphorylationGFGDRTGTFCGTPEF
CCCCCCCCCCCCHHH		18.3521082442
1026PhosphorylationRTGTFCGTPEFLAPE
CCCCCCCCHHHCCHH		22.3321082442
1164PhosphorylationTSEKAQLTPPKEPRH
HHHCCCCCCCCCCCC		26.0119429919
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 PKN_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PKN_DROME !!
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 PKN_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SQH_DROMEsqhgenetic
25131196
CAPZB_DROMEcpbgenetic
25131196
RHO1_DROMERho1genetic
10323867
PP1B_DROMEflwgenetic
25131196
JNK_DROMEbskgenetic
10323867
JNK_DROMEbskgenetic
24531729
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PKN_DROME

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory