KGP2_HUMAN - dbPTM
KGP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KGP2_HUMAN
UniProt AC Q13237
Protein Name cGMP-dependent protein kinase 2
Gene Name PRKG2
Organism Homo sapiens (Human).
Sequence Length 762
Subcellular Localization Apical cell membrane
Lipid-anchor .
Protein Description Crucial regulator of intestinal secretion and bone growth (By similarity). Phosphorylates and activates CFTR on the plasma membrane. Plays a key role in intestinal secretion by regulating cGMP-dependent translocation of CFTR in jejunum (By similarity). Acts downstream of NMDAR to activate the plasma membrane accumulation of GRIA1/GLUR1 in synapse and increase synaptic plasticity. Phosphorylates GRIA1/GLUR1 at Ser-863 (By similarity). Acts as regulator of gene expression and activator of the extracellular signal-regulated kinases MAPK3/ERK1 and MAPK1/ERK2 in mechanically stimulated osteoblasts. Under fluid shear stress, mediates ERK activation and subsequent induction of FOS, FOSL1/FRA1, FOSL2/FRA2 and FOSB that play a key role in the osteoblast anabolic response to mechanical stimulation (By similarity)..
Protein Sequence MGNGSVKPKHSKHPDGHSGNLTTDALRNKVTELERELRRKDAEIQEREYHLKELREQLSKQTVAIAELTEELQNKCIQLNKLQDVVHMQGGSPLQASPDKVPLEVHRKTSGLVSLHSRRGAKAGVSAEPTTRTYDLNKPPEFSFEKARVRKDSSEKKLITDALNKNQFLKRLDPQQIKDMVECMYGRNYQQGSYIIKQGEPGNHIFVLAEGRLEVFQGEKLLSSIPMWTTFGELAILYNCTRTASVKAITNVKTWALDREVFQNIMRRTAQARDEQYRNFLRSVSLLKNLPEDKLTKIIDCLEVEYYDKGDYIIREGEEGSTFFILAKGKVKVTQSTEGHDQPQLIKTLQKGEYFGEKALISDDVRSANIIAEENDVACLVIDRETFNQTVGTFEELQKYLEGYVANLNRDDEKRHAKRSMSNWKLSKALSLEMIQLKEKVARFSSSSPFQNLEIIATLGVGGFGRVELVKVKNENVAFAMKCIRKKHIVDTKQQEHVYSEKRILEELCSPFIVKLYRTFKDNKYVYMLLEACLGGELWSILRDRGSFDEPTSKFCVACVTEAFDYLHRLGIIYRDLKPENLILDAEGYLKLVDFGFAKKIGSGQKTWTFCGTPEYVAPEVILNKGHDFSVDFWSLGILVYELLTGNPPFSGVDQMMTYNLILKGIEKMDFPRKITRRPEDLIRRLCRQNPTERLGNLKNGINDIKKHRWLNGFNWEGLKARSLPSPLQRELKGPIDHSYFDKYPPEKGMPPDELSGWDKDF
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
2N-myristoyl glycine------MGNGSVKPK
------CCCCCCCCC		47.40-
2Myristoylation------MGNGSVKPK
------CCCCCCCCC		47.408636133
11PhosphorylationGSVKPKHSKHPDGHS
CCCCCCCCCCCCCCC		38.49-
92PhosphorylationVVHMQGGSPLQASPD
HHHCCCCCCCCCCCC		29.3023401153
97PhosphorylationGGSPLQASPDKVPLE
CCCCCCCCCCCCCCE		22.2224961811
109PhosphorylationPLEVHRKTSGLVSLH
CCEEEECCCCCEEEE		28.1623401153
110PhosphorylationLEVHRKTSGLVSLHS
CEEEECCCCCEEEEC		32.9123401153
114PhosphorylationRKTSGLVSLHSRRGA
ECCCCCEEEECCCCC		25.9628060719
117PhosphorylationSGLVSLHSRRGAKAG
CCCEEEECCCCCCCC		29.0328060719
131PhosphorylationGVSAEPTTRTYDLNK
CCCCCCCCCCCCCCC		31.56-
157UbiquitinationRKDSSEKKLITDALN
CCCCHHCHHHHHHHC		40.86-
165SumoylationLITDALNKNQFLKRL
HHHHHHCCCHHHHHC		53.64-
165SumoylationLITDALNKNQFLKRL
HHHHHHCCCHHHHHC		53.64-
165UbiquitinationLITDALNKNQFLKRL
HHHHHHCCCHHHHHC		53.64-
193PhosphorylationGRNYQQGSYIIKQGE
CCCCCCCCEEEECCC		14.6024719451
194PhosphorylationRNYQQGSYIIKQGEP
CCCCCCCEEEECCCC		17.3124719451
245PhosphorylationYNCTRTASVKAITNV
HCCCCCCCCCHHHCC		24.4428176443
285PhosphorylationRNFLRSVSLLKNLPE
HHHHHHHHHHHCCCH		29.2724719451
306PhosphorylationIDCLEVEYYDKGDYI
EEEEEEEEECCCCEE		23.34-
307PhosphorylationDCLEVEYYDKGDYII
EEEEEEEECCCCEEE		9.55-
321PhosphorylationIREGEEGSTFFILAK
EEECCCCCEEEEEEE		25.8925627689
354Nitrated tyrosineKTLQKGEYFGEKALI
HHHHCCCCCCCCEEE		26.08-
354NitrationKTLQKGEYFGEKALI
HHHHCCCCCCCCEEE		26.08-
431PhosphorylationWKLSKALSLEMIQLK
HHHHHHHCHHHHHHH		27.4328857561
448PhosphorylationVARFSSSSPFQNLEI
HHHHCCCCCCCCCEE		31.51-
521MethylationVKLYRTFKDNKYVYM
HHHHHHCCCCHHHHH		60.8323644510
521"N6,N6-dimethyllysine"VKLYRTFKDNKYVYM
HHHHHHCCCCHHHHH		60.83-
540PhosphorylationCLGGELWSILRDRGS
HHHHHHHHHHHHCCC		25.1124719451
607PhosphorylationKIGSGQKTWTFCGTP
ECCCCCCEEEECCCC		23.1128857561
609PhosphorylationGSGQKTWTFCGTPEY
CCCCCEEEECCCCCC		17.8028857561
613PhosphorylationKTWTFCGTPEYVAPE
CEEEECCCCCCCCCH		17.7128060719
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 KGP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KGP2_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 KGP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYLK_HUMANMYLKphysical
6547441
PDE9A_HUMANPDE9Aphysical
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 KGP2_HUMAN

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"N-terminal myristoylation is required for membrane localization ofcGMP-dependent protein kinase type II.";
Vaandrager A.B., Ehlert E.M., Jarchau T., Lohmann S.M., de Jonge H.R.;
J. Biol. Chem. 271:7025-7029(1996).
Cited for: MYRISTOYLATION AT GLY-2, AND SUBCELLULAR LOCATION.
Nitration
ReferencePubMed
"The human pituitary nitroproteome: detection of nitrotyrosyl-proteinswith two-dimensional Western blotting, and amino acid sequencedetermination with mass spectrometry.";
Zhan X., Desiderio D.M.;
Biochem. Biophys. Res. Commun. 325:1180-1186(2004).
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASS SPECTROMETRY.

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