Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
PKG1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
PKG1 an AGC kinase of the PKG family. Type I cGMP-dependent protein kinase; relaxes vascular smooth muscle and inhibits platelet aggregation. Binding of cGMP results in enzyme activation. Two splice variant isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: EC 2.7.11.12; Kinase, protein; Protein kinase, AGC; Protein kinase, Ser/Thr (non-receptor); AGC group; PKG family
Cellular Component: Golgi apparatus; cytoplasm; plasma membrane; cytosol
Molecular Function: protein binding; calcium channel regulator activity; cGMP-dependent protein kinase activity; cGMP binding; ATP binding
Biological Process: regulation of GTPase activity; forebrain development; neuron migration; dendrite development; signal transduction; blood coagulation; actin cytoskeleton organization and biogenesis; protein amino acid phosphorylation
Reference #:  Q13976 (UniProtKB)
Alt. Names/Synonyms: cGK 1; cGK1; cGKI; cGKI-alpha; cGKI-BETA; cGMP-dependent protein kinase 1; cGMP-dependent protein kinase I; DKFZp686K042; FLJ36117; KGP1; MGC71944; PGK; PKG; PRKG1; PRKG1B; PRKGR1A; PRKGR1B; protein kinase, cGMP-dependent, regulatory, type I, beta; protein kinase, cGMP-dependent, type I
Gene Symbols: PRKG1
Molecular weight: 76,364 Da
Basal Isoelectric point: 5.74  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

PKG1
Protein Structure Not Found.

Substrate Sequence Logo
Sequence Logo

STRING  |  Scansite  |  KinBase  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  DISEASE  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Sites Implicated In
transcription, altered: T517‑p
enzymatic activity, induced: T59‑p, S65‑p, T517‑p
phosphorylation: T517‑p
ubiquitination: S65‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

► Hide Isoforms 		 
0 1 - gap
0 1 S27-p KELEKRLsEKEEEIQ
1 0 S45 RKLHKCQSVLPVPsT
2 0 V49 KCQSVLPVPsTHIGP
2 0 S51-p QSVLPVPsTHIGPRT
3 0 T59-p THIGPRTtRAQGIsA
4 0 S65-p TtRAQGIsAEPQTYR
1 0 S73 AEPQTYRSFHDLRQA
2 0 T85-p RQAFRKFtKSERSKD
0 1 Y212-p GLIKHTEyMEFLKsV
0 1 S218-p EyMEFLKsVPTFQSL
0 1 S231-p SLPEEILsKLADVLE
0 1 Y247-p THYENGEyIIRQGAR
0 2 S273-p VNVTREDsPSEDPVF
0 1 Y433-p RTFKDSKyLyMLMEA
0 1 Y435-p FKDSKyLyMLMEACL
0 2 R483 HSKGIIYRDLKPENL
0 1 Y497-p LILDHRGyAKLVDFG
0 1 K513 AKKIGFGKKtWtFCG
0 7 T515-p KIGFGKKtWtFCGTP
1 19 T517-p GFGKKtWtFCGTPEY
0 1 T521 KtWtFCGTPEYVAPE
0 1 K582 DMIEFPKKIAKNAAN
0 3 K607-a SERLGNLkNGVKDIQ
0 3 K615-a NGVKDIQkHkWFEGF
0 3 K617-a VKDIQkHkWFEGFNW
0 1 S647 VASPTDTSNFDSFPE
  PKG1 iso2  
Y9-p GTLRDLQyALQEKIE
- gap
S51 NELDKYRSVIRPATQ
S64-p TQQAQKQsASTLQGE
S66 QAQKQsASTLQGEPR
T74 TLQGEPRTKRQAIsA
S80-p RTKRQAIsAEPTAFD
I88 AEPTAFDIQDLSHVT
P100 HVTLPFYPKSPQSKD
Y227 GLIKHTEYMEFLKSV
S233 EYMEFLKSVPTFQSL
S246 SLPEEILSKLADVLE
Y262 THYENGEYIIRQGAR
S288 VNVTREDSPSEDPVF
Y448 RTFKDSKYLYMLMEA
Y450 FKDSKYLYMLMEACL
R498 HSKGIIYRDLKPENL
Y512 LILDHRGYAKLVDFG
K528 AKKIGFGKKTWtFCG
T530 KIGFGKKTWtFCGTP
T532-p GFGKKTWtFCGTPEY
T536 KTWtFCGTPEYVAPE
K597 DMIEFPKKIAKNAAN
K622 SERLGNLKNGVKDIQ
K630 NGVKDIQKHKWFEGF
K632 VKDIQKHKWFEGFNW
S662 VASPTDTSNFDSFPE
  mouse

► Hide Isoforms 		 
- gap
S27 KELEKRLSEKEEEIQ
S45 RKLHKCQSVLPVPST
V49 KCQSVLPVPSTHIGP
S51 QSVLPVPSTHIGPRT
T59 THIGPRTTRAQGISA
S65 TTRAQGISAEPQTYR
S73 AEPQTYRSFHDLRQA
T85 RQAFRKFTKSERSKD
Y212 GLIKHTEYMEFLKSV
S218 EYMEFLKSVPTFQSL
S231 SLPDEILSKLADVLE
Y247 THYENGEYIIRQGAR
S273-p VNVTREDsPSEDPVF
Y433 RTFKDSKYLYMLMEA
Y435 FKDSKYLYMLMEACL
R483-m1 HSKGIIYrDLKPENL
Y497 LILDHRGYAKLVDFG
K513-a AKKIGFGkKtWtFCG
T515-p KIGFGkKtWtFCGtP
T517-p GFGkKtWtFCGtPEY
T521-p KtWtFCGtPEYVAPE
K582-a DMIEFPKkIAKNAAN
K607 SERLGNLKNGVKDIQ
K615 NGVKDIQKHKWFEGF
K617 VKDIQKHKWFEGFNW
S647-p VASPTDTsNFDSFPE
  PKG1 iso2  
Y9 GTLRDLQYALQEKIE
- gap
S51 NELDKYRSVIRPATQ
S64 TQQAQKQSASTLQGE
S66 QAQKQSASTLQGEPR
T74 TLQGEPRTKRQAISA
S80 RTKRQAISAEPTAFD
I88 AEPTAFDIQDLSHVT
P100 HVTLPFYPKSPQSKD
Y227 GLIKHTEYMEFLKSV
S233 EYMEFLKSVPTFQSL
S246 SLPDEILSKLADVLE
Y262 THYENGEYIIRQGAR
S288 VNVTREDSPSEDPVF
Y448 RTFKDSKYLYMLMEA
Y450 FKDSKYLYMLMEACL
R498 HSKGIIYRDLKPENL
Y512 LILDHRGYAKLVDFG
K528 AKKIGFGKKtWtFCG
T530-p KIGFGKKtWtFCGtP
T532-p GFGKKtWtFCGtPEY
T536-p KtWtFCGtPEYVAPE
K597 DMIEFPKKIAKNAAN
K622 SERLGNLKNGVKDIQ
K630 NGVKDIQKHKWFEGF
K632 VKDIQKHKWFEGFNW
S662 VASPTDTSNFDSFPE
  cow

 
- gap
S27-p KELEKRLsEKEEEIQ
S45-p RKLHKCQsVLPVPsT
V49 KCQsVLPVPsTHIGP
S51-p QsVLPVPsTHIGPRT
T59-p THIGPRTtRAQGIsA
S65-p TtRAQGIsAEPQTYR
S73-p AEPQTYRsFHDLRQA
T85-p RQAFRKFtKSERSKD
Y212 GLIKHTEYMEFLKSV
S218 EYMEFLKSVPTFQSL
S231 SLPEEILSKLADVLE
Y247 THYENGEYIIRQGAR
S273 VNVTREDSPNEDPVF
Y433 RTFKDSKYLYMLMEA
Y435 FKDSKYLYMLMEACL
R483 HSKGIIYRDLKPENL
Y497 LILDHRGYAKLVDFG
K513 AKKIGFGKKTWtFCG
T515 KIGFGKKTWtFCGTP
T517-p GFGKKTWtFCGTPEY
T521 KTWtFCGTPEYVAPE
K582 DMIEFPKKIAKNAAN
K607 SERLGNLKNGVKDIQ
K615 NGVKDIQKHKWFEGF
K617 VKDIQKHKWFEGFNW
S647 VASPTDTSNFDSFPE
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.