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Q13976

- KGP1_HUMAN

UniProt

Q13976 - KGP1_HUMAN

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Protein
cGMP-dependent protein kinase 1
Gene
PRKG1, PRKG1B, PRKGR1A, PRKGR1B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Serine/threonine protein kinase that acts as key mediator of the nitric oxide (NO)/cGMP signaling pathway. GMP binding activates PRKG1, which phosphorylates serines and threonines on many cellular proteins. Numerous protein targets for PRKG1 phosphorylation are implicated in modulating cellular calcium, but the contribution of each of these targets may vary substantially among cell types. Proteins that are phosphorylated by PRKG1 regulate platelet activation and adhesion, smooth muscle contraction, cardiac function, gene expression, feedback of the NO-signaling pathway, and other processes involved in several aspects of the CNS like axon guidance, hippocampal and cerebellar learning, circadian rhythm and nociception. Smooth muscle relaxation is mediated through lowering of intracellular free calcium, by desensitization of contractile proteins to calcium, and by decrease in the contractile state of smooth muscle or in platelet activation. Regulates intracellular calcium levels via several pathways: phosphorylates MRVI1/IRAG and inhibits IP3-induced Ca2+ release from intracellular stores, phosphorylation of KCNMA1 (BKCa) channels decreases intracellular Ca2+ levels, which leads to increased opening of this channel. PRKG1 phosphorylates the canonical transient receptor potential channel (TRPC) family which inactivates the associated inward calcium current. Another mode of action of NO/cGMP/PKGI signaling involves PKGI-mediated inactivation of the Ras homolog gene family member A (RhoA). Phosphorylation of RHOA by PRKG1 blocks the action of this protein in myriad processes: regulation of RHOA translocation; decreasing contraction; controlling vesicle trafficking, reduction of myosin light chain phosphorylation resulting in vasorelaxation. Activation of PRKG1 by NO signaling alters also gene expression in a number of tissues. In smooth muscle cells, increased cGMP and PRKG1 activity influence expression of smooth muscle-specific contractile proteins, levels of proteins in the NO/cGMP signaling pathway, down-regulation of the matrix proteins osteopontin and thrombospondin-1 to limit smooth muscle cell migration and phenotype. Regulates vasodilator-stimulated phosphoprotein (VASP) functions in platelets and smooth muscle.9 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

In the absence of cGMP, PRKG1 activity is suppressed by autoinhibitory contacts.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei390 – 3901ATP By similarity
Active sitei484 – 4841Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi167 – 1704cAMP or cGMP
Nucleotide bindingi177 – 1782cAMP or cGMP
Nucleotide bindingi366 – 3749ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. cGMP binding Source: UniProtKB-KW
  3. cGMP-dependent protein kinase activity Source: UniProtKB
  4. calcium channel regulator activity Source: UniProtKB
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton organization Source: ProtInc
  2. blood coagulation Source: Reactome
  3. dendrite development Source: Ensembl
  4. forebrain development Source: Ensembl
  5. negative regulation of platelet aggregation Source: UniProtKB
  6. neuron migration Source: Ensembl
  7. protein phosphorylation Source: ProtInc
  8. regulation of GTPase activity Source: UniProtKB
  9. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Serine/threonine-protein kinase, Transferase

Keywords - Ligandi

ATP-binding, cGMP, cGMP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.12. 2681.
ReactomeiREACT_172761. Ca2+ pathway.
REACT_23767. cGMP effects.
REACT_23898. Rap1 signalling.
SignaLinkiQ13976.

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-dependent protein kinase 1 (EC:2.7.11.12)
Short name:
cGK 1
Short name:
cGK1
Alternative name(s):
cGMP-dependent protein kinase I
Short name:
cGKI
Gene namesi
Name:PRKG1
Synonyms:PRKG1B, PRKGR1A, PRKGR1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9414. PRKG1.

Subcellular locationi

Cytoplasm By similarity
Note: Colocalized with TRPC7 in the plasma membrane By similarity.2 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: Reactome
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Aortic aneurysm, familial thoracic 8 (AAT8) [MIM:615436]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771R → Q in AAT8; impairs cGMP binding; the mutant protein is constitutively active. 1 Publication
VAR_070434

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 121L → A: Loss of binding to PPP1R12A. 1 Publication
Mutagenesisi19 – 191I → A: Loss of binding to PPP1R12A. 1 Publication
Mutagenesisi26 – 261L → P: Loss of binding to PPP1R12A. 1 Publication
Mutagenesisi33 – 331I → A: Loss of binding to PPP1R12A. 1 Publication
Mutagenesisi40 – 401L → A: Loss of binding to PPP1R12A. 1 Publication

Keywords - Diseasei

Aortic aneurysm, Disease mutation

Organism-specific databases

MIMi615436. phenotype.
Orphaneti91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBiPA33777.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 671670cGMP-dependent protein kinase 1
PRO_0000086115Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Disulfide bondi43 – 43Interchain By similarity
Modified residuei59 – 591Phosphothreonine; by autocatalysis By similarity

Post-translational modificationi

Autophosphorylation increases kinase activity.
65 kDa monomer is produced by proteolytic cleavage By similarity.

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ13976.
PaxDbiQ13976.
PRIDEiQ13976.

PTM databases

PhosphoSiteiQ13976.

Expressioni

Tissue specificityi

Primarily expressed in lung and placenta.1 Publication

Gene expression databases

ArrayExpressiQ13976.
BgeeiQ13976.
CleanExiHS_PRKG1.
GenevestigatoriQ13976.

Organism-specific databases

HPAiCAB009629.
HPA007699.

Interactioni

Subunit structurei

Isoform alpha: parallel homodimer or heterodimer and also heterotetramer. Interacts directly with PPP1R12A. Non-covalent dimer of dimer of PRKG1-PRKG1 and PPP1R12A-PPP1R12A. This interaction targets PRKG1 to stress fibers to mediate smooth muscle cell relaxation and vasodilation in responses to rises in cGMP. Isoform beta: antiparallel homodimer. Part of cGMP kinase signaling complex at least composed of ACTA2/alpha-actin, CNN1/calponin H1, PLN/phospholamban, PRKG1 and ITPR1 By similarity. Interacts with MRVI1. Forms a stable complex with ITPR1, MRVI1, and isoform beta of PRKG1. Interacts with TRPC7 (via ankyrin repeat domain). Isoform alpha interacts with RGS2. Interacts with GTF2I.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BMPR2Q138732EBI-3952014,EBI-527196

Protein-protein interaction databases

BioGridi111578. 17 interactions.
DIPiDIP-46288N.
IntActiQ13976. 2 interactions.
MINTiMINT-121708.
STRINGi9606.ENSP00000363092.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 4334
Helixi90 – 10011
Turni102 – 1065
Helixi109 – 11810
Beta strandi120 – 1245
Beta strandi129 – 1313
Beta strandi139 – 1457
Beta strandi148 – 1525
Beta strandi155 – 1606
Beta strandi165 – 1673
Helixi169 – 1735
Beta strandi174 – 1763
Beta strandi178 – 1858
Beta strandi187 – 1937
Helixi194 – 2018
Helixi209 – 2168
Helixi220 – 2234
Helixi227 – 23610
Beta strandi238 – 2425
Beta strandi247 – 2493
Beta strandi257 – 2648
Beta strandi266 – 2705
Beta strandi274 – 2763
Beta strandi279 – 2846
Helixi293 – 2953
Beta strandi296 – 2983
Beta strandi303 – 31715
Helixi318 – 3247
Turni325 – 3273
Helixi329 – 3324

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZXANMR-A/B2-59[»]
3NMDX-ray2.27A/B/C/D/E4-55[»]
3OCPX-ray2.49A/B90-212[»]
3OD0X-ray2.90A/B90-212[»]
3OGJX-ray2.75A/B/C/D90-212[»]
4KU7X-ray1.65A204-354[»]
4KU8X-ray1.99A/B/C204-354[»]
ProteinModelPortaliQ13976.
SMRiQ13976. Positions 9-44, 60-655.

Miscellaneous databases

EvolutionaryTraceiQ13976.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini360 – 619260Protein kinase
Add
BLAST
Domaini620 – 67152AGC-kinase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 102101Required for dimerization
Add
BLAST
Regioni9 – 4436Leucine-zipper
Add
BLAST
Regioni50 – 7526Autoinhibitory domain By similarity
Add
BLAST
Regioni103 – 220118cGMP-binding, high affinity
Add
BLAST
Regioni221 – 341121cGMP-binding, low affinity
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili2 – 5958
Add
BLAST

Domaini

Composed of an N-terminal leucine-zipper domain followed by an autoinhibitory domain, which mediate homodimer formation and inhibit kinase activity, respectively. Next, two cGMP-binding domains are followed by the catalytic domain at the C-terminus. Binding of cGMP to cGMP-binding domains results in a conformational change that activates kinase activity by removing the autoinhibitory domain from the catalytic cleft leaving the catalytic domain free to phosphorylate downstream substrates. Isoforms alpha and beta have identical cGMP-binding and catalytic domains but differ in their leucine zipper and autoinhibitory sequences and therefore differ in their dimerization substrates and kinase enzyme activity.
Heterotetramerization is mediated by the interaction between a coiled-coil of PRKG1 and the leucine/isoleucine zipper of PPP1R12A/MBS, the myosin-binding subunit of the myosin phosphatase.

Sequence similaritiesi

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0515.
HOGENOMiHOG000233033.
HOVERGENiHBG006211.
InParanoidiP14619.
KOiK07376.
OMAiHQDLSRQ.
PhylomeDBiQ13976.
TreeFamiTF313261.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR000961. AGC-kinase_C.
IPR016232. cGMP-dependent_protein_kinase.
IPR002374. cGMP_dep_kinase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014710. RmlC-like_jellyroll.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view]
PIRSFiPIRSF000559. cGMP-dep_kinase. 1 hit.
PRINTSiPR00104. CGMPKINASE.
SMARTiSM00100. cNMP. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS51285. AGC_KINASE_CTER. 1 hit.
PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform Alpha (identifier: Q13976-1) [UniParc]FASTAAdd to Basket

Also known as: CGK1-alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSELEEDFAK ILMLKEERIK ELEKRLSEKE EEIQELKRKL HKCQSVLPVP    50
STHIGPRTTR AQGISAEPQT YRSFHDLRQA FRKFTKSERS KDLIKEAILD 100
NDFMKNLELS QIQEIVDCMY PVEYGKDSCI IKEGDVGSLV YVMEDGKVEV 150
TKEGVKLCTM GPGKVFGELA ILYNCTRTAT VKTLVNVKLW AIDRQCFQTI 200
MMRTGLIKHT EYMEFLKSVP TFQSLPEEIL SKLADVLEET HYENGEYIIR 250
QGARGDTFFI ISKGTVNVTR EDSPSEDPVF LRTLGKGDWF GEKALQGEDV 300
RTANVIAAEA VTCLVIDRDS FKHLIGGLDD VSNKAYEDAE AKAKYEAEAA 350
FFANLKLSDF NIIDTLGVGG FGRVELVQLK SEESKTFAMK ILKKRHIVDT 400
RQQEHIRSEK QIMQGAHSDF IVRLYRTFKD SKYLYMLMEA CLGGELWTIL 450
RDRGSFEDST TRFYTACVVE AFAYLHSKGI IYRDLKPENL ILDHRGYAKL 500
VDFGFAKKIG FGKKTWTFCG TPEYVAPEII LNKGHDISAD YWSLGILMYE 550
LLTGSPPFSG PDPMKTYNII LRGIDMIEFP KKIAKNAANL IKKLCRDNPS 600
ERLGNLKNGV KDIQKHKWFE GFNWEGLRKG TLTPPIIPSV ASPTDTSNFD 650
SFPEDNDEPP PDDNSGWDID F 671
Length:671
Mass (Da):76,364
Last modified:January 23, 2007 - v3
Checksum:i51389502A5E5FBD2
GO
Isoform Beta (identifier: Q13976-2) [UniParc] [UniParc]FASTAAdd to Basket

Also known as: CGK1-beta

The sequence of this isoform differs from the canonical sequence as follows:
     2-89: SELEEDFAKI...AFRKFTKSER → MGTLRDLQYA...TLPFYPKSPQ

Show »
Length:687
Mass (Da):77,935
Checksum:i7A59FA64EE85C0C3
GO
Isoform 3 (identifier: Q13976-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-15: MSELEEDFAKILMLK → MEKQNMFLHGSYILR
     16-297: Missing.

Note: No experimental confirmation available.

Show »
Length:389
Mass (Da):44,185
Checksum:i9792149F93773D55
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti177 – 1771R → Q in AAT8; impairs cGMP binding; the mutant protein is constitutively active. 1 Publication
VAR_070434
Natural varianti249 – 2491I → V.1 Publication
Corresponds to variant rs56082459 [ dbSNP | Ensembl ].
VAR_046773
Natural varianti267 – 2671N → S.1 Publication
Corresponds to variant rs34997494 [ dbSNP | Ensembl ].
VAR_051632
Natural varianti474 – 4741Y → F.1 Publication
VAR_070435
Natural varianti666 – 6661G → A.1 Publication
VAR_070436

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1515MSELE…ILMLK → MEKQNMFLHGSYILR in isoform 3.
VSP_055541Add
BLAST
Alternative sequencei2 – 8988SELEE…TKSER → MGTLRDLQYALQEKIEELRQ RDALIDELELELDQKDELIQ KLQNELDKYRSVIRPATQQA QKQSASTLQGEPRTKRQAIS AEPTAFDIQDLSHVTLPFYP KSPQ in isoform Beta.
VSP_038714Add
BLAST
Alternative sequencei16 – 297282Missing in isoform 3.
VSP_055542Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y07512 mRNA. Translation: CAA68810.1.
D45864 mRNA. Translation: BAA08297.1.
AK093436 mRNA. Translation: BAG52715.1.
EF560730 mRNA. Translation: ABQ59040.1.
Z92867
, Z92869, Z92870, Z92871, Z92872, Z92873, Z92874, Z92875, Z92876, Z92877, Z92878, Z92879, Z92880, Z92881, Z92882, Z92883, Z92884, Z92885 Genomic DNA. Translation: CAB07436.1.
Z92868
, Z92869, Z92870, Z92871, Z92872, Z92873, Z92874, Z92875, Z92876, Z92877, Z92878, Z92879, Z92880, Z92881, Z92882, Z92883, Z92884, Z92885 Genomic DNA. Translation: CAB07437.1.
AL391378
, AC009986, AC022537, AC022025, AC027118, AL731537, AL928686, AL157399, AC026228 Genomic DNA. Translation: CAI39626.1.
AL928686
, AC009986, AC022537, AL731537, AL391378, AL157399, AC027118, AC026228, AC022025 Genomic DNA. Translation: CAI40743.1.
AL157399
, AC022025, AC009986, AL928686, AL731537, AL391378, AC027118, AC026228, AC022537 Genomic DNA. Translation: CAI41305.1.
AL731537
, AL928686, AL391378, AL157399, AC027118, AC026228, AC022537, AC022025, AC009986 Genomic DNA. Translation: CAI17115.1.
AC068062 Genomic DNA. No translation available.
AC069079 Genomic DNA. No translation available.
AC073584 Genomic DNA. No translation available.
AL596105 Genomic DNA. No translation available.
AL607031 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54140.1.
BC062688 mRNA. Translation: AAH62688.1.
BC127090 mRNA. Translation: AAI27091.1.
CCDSiCCDS44399.1. [Q13976-1]
PIRiS05702.
RefSeqiNP_001091982.1. NM_001098512.2. [Q13976-1]
NP_006249.1. NM_006258.3.
UniGeneiHs.407535.

Genome annotation databases

EnsembliENST00000373975; ENSP00000363086; ENSG00000185532.
ENST00000373980; ENSP00000363092; ENSG00000185532. [Q13976-2]
ENST00000401604; ENSP00000384200; ENSG00000185532. [Q13976-1]
GeneIDi5592.
KEGGihsa:5592.
UCSCiuc001jjm.3. human. [Q13976-1]
uc001jjo.3. human. [Q13976-2]

Polymorphism databases

DMDMi6225588.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y07512 mRNA. Translation: CAA68810.1 .
D45864 mRNA. Translation: BAA08297.1 .
AK093436 mRNA. Translation: BAG52715.1 .
EF560730 mRNA. Translation: ABQ59040.1 .
Z92867
, Z92869 , Z92870 , Z92871 , Z92872 , Z92873 , Z92874 , Z92875 , Z92876 , Z92877 , Z92878 , Z92879 , Z92880 , Z92881 , Z92882 , Z92883 , Z92884 , Z92885 Genomic DNA. Translation: CAB07436.1 .
Z92868
, Z92869 , Z92870 , Z92871 , Z92872 , Z92873 , Z92874 , Z92875 , Z92876 , Z92877 , Z92878 , Z92879 , Z92880 , Z92881 , Z92882 , Z92883 , Z92884 , Z92885 Genomic DNA. Translation: CAB07437.1 .
AL391378
, AC009986 , AC022537 , AC022025 , AC027118 , AL731537 , AL928686 , AL157399 , AC026228 Genomic DNA. Translation: CAI39626.1 .
AL928686
, AC009986 , AC022537 , AL731537 , AL391378 , AL157399 , AC027118 , AC026228 , AC022025 Genomic DNA. Translation: CAI40743.1 .
AL157399
, AC022025 , AC009986 , AL928686 , AL731537 , AL391378 , AC027118 , AC026228 , AC022537 Genomic DNA. Translation: CAI41305.1 .
AL731537
, AL928686 , AL391378 , AL157399 , AC027118 , AC026228 , AC022537 , AC022025 , AC009986 Genomic DNA. Translation: CAI17115.1 .
AC068062 Genomic DNA. No translation available.
AC069079 Genomic DNA. No translation available.
AC073584 Genomic DNA. No translation available.
AL596105 Genomic DNA. No translation available.
AL607031 Genomic DNA. No translation available.
CH471083 Genomic DNA. Translation: EAW54140.1 .
BC062688 mRNA. Translation: AAH62688.1 .
BC127090 mRNA. Translation: AAI27091.1 .
CCDSi CCDS44399.1. [Q13976-1 ]
PIRi S05702.
RefSeqi NP_001091982.1. NM_001098512.2. [Q13976-1 ]
NP_006249.1. NM_006258.3.
UniGenei Hs.407535.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZXA NMR - A/B 2-59 [» ]
3NMD X-ray 2.27 A/B/C/D/E 4-55 [» ]
3OCP X-ray 2.49 A/B 90-212 [» ]
3OD0 X-ray 2.90 A/B 90-212 [» ]
3OGJ X-ray 2.75 A/B/C/D 90-212 [» ]
4KU7 X-ray 1.65 A 204-354 [» ]
4KU8 X-ray 1.99 A/B/C 204-354 [» ]
ProteinModelPortali Q13976.
SMRi Q13976. Positions 9-44, 60-655.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111578. 17 interactions.
DIPi DIP-46288N.
IntActi Q13976. 2 interactions.
MINTi MINT-121708.
STRINGi 9606.ENSP00000363092.

Chemistry

BindingDBi Q13976.
ChEMBLi CHEMBL4273.
GuidetoPHARMACOLOGYi 1492.

PTM databases

PhosphoSitei Q13976.

Polymorphism databases

DMDMi 6225588.

Proteomic databases

MaxQBi Q13976.
PaxDbi Q13976.
PRIDEi Q13976.

Protocols and materials databases

DNASUi 5592.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373975 ; ENSP00000363086 ; ENSG00000185532 .
ENST00000373980 ; ENSP00000363092 ; ENSG00000185532 . [Q13976-2 ]
ENST00000401604 ; ENSP00000384200 ; ENSG00000185532 . [Q13976-1 ]
GeneIDi 5592.
KEGGi hsa:5592.
UCSCi uc001jjm.3. human. [Q13976-1 ]
uc001jjo.3. human. [Q13976-2 ]

Organism-specific databases

CTDi 5592.
GeneCardsi GC10P052751.
HGNCi HGNC:9414. PRKG1.
HPAi CAB009629.
HPA007699.
MIMi 176894. gene.
615436. phenotype.
neXtProti NX_Q13976.
Orphaneti 91387. Familial thoracic aortic aneurysm and aortic dissection.
PharmGKBi PA33777.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0515.
HOGENOMi HOG000233033.
HOVERGENi HBG006211.
InParanoidi P14619.
KOi K07376.
OMAi HQDLSRQ.
PhylomeDBi Q13976.
TreeFami TF313261.

Enzyme and pathway databases

BRENDAi 2.7.11.12. 2681.
Reactomei REACT_172761. Ca2+ pathway.
REACT_23767. cGMP effects.
REACT_23898. Rap1 signalling.
SignaLinki Q13976.

Miscellaneous databases

ChiTaRSi PRKG1. human.
EvolutionaryTracei Q13976.
GeneWikii PRKG1.
GenomeRNAii 5592.
NextBioi 21698.
PROi Q13976.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q13976.
Bgeei Q13976.
CleanExi HS_PRKG1.
Genevestigatori Q13976.

Family and domain databases

Gene3Di 2.60.120.10. 2 hits.
InterProi IPR000961. AGC-kinase_C.
IPR016232. cGMP-dependent_protein_kinase.
IPR002374. cGMP_dep_kinase.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR014710. RmlC-like_jellyroll.
IPR002290. Ser/Thr_dual-sp_kinase_dom.
IPR008271. Ser/Thr_kinase_AS.
[Graphical view ]
Pfami PF00027. cNMP_binding. 2 hits.
PF00069. Pkinase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000559. cGMP-dep_kinase. 1 hit.
PRINTSi PR00104. CGMPKINASE.
SMARTi SM00100. cNMP. 2 hits.
SM00133. S_TK_X. 1 hit.
SM00220. S_TKc. 1 hit.
[Graphical view ]
SUPFAMi SSF51206. SSF51206. 2 hits.
SSF56112. SSF56112. 1 hit.
PROSITEi PS51285. AGC_KINASE_CTER. 1 hit.
PS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00108. PROTEIN_KINASE_ST. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and predicted full-length amino acid sequence of the type I beta isozyme of cGMP-dependent protein kinase from human placenta. Tissue distribution and developmental changes in rat."
    Sandberg M., Natarajan V., Ronander I., Kalderon D., Walter U., Lohmann S.M., Jahnsen T.
    FEBS Lett. 255:321-329(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA).
    Tissue: Placenta.
  2. Sandberg M.
    Submitted (OCT-1989) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "cDNA cloning and gene expression of human type Ialpha cGMP-dependent protein kinase."
    Tamura N., Itoh H., Ogawa Y., Nakagawa O., Harada M., Chun T., Suga S., Yoshimasa T., Nakao K.
    Hypertension 27:552-557(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
    Tissue: Lung.
  4. "Characterization of the human gene encoding the type I alpha and type I beta cGMP-dependent protein kinase (PRKG1)."
    Orstavik S., Natarajan V., Tasken K., Jahnsen T., Sandberg M.
    Genomics 42:311-318(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
    Tissue: Cervix.
  7. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM BETA).
  10. "cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets."
    Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U.
    J. Biol. Chem. 269:14509-14517(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF VASP.
  11. "Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Ialpha."
    Surks H.K., Mochizuki N., Kasai Y., Georgescu S.P., Tang K.M., Ito M., Lincoln T.M., Mendelsohn M.E.
    Science 286:1583-1587(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R12A, SUBUNIT, MUTAGENESIS OF LEU-12; ILE-19; LEU-26; ILE-33 AND LEU-40, FUNCTION.
  12. Cited for: FUNCTION IN PHOSPHORYLATION OF RHOA.
  13. "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I."
    Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S., Pilz R.B.
    J. Biol. Chem. 277:32003-32014(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF GTF2I, INTERACTION WITH GTF2I.
  14. "Regulation of cGMP-specific phosphodiesterase (PDE5) phosphorylation in smooth muscle cells."
    Rybalkin S.D., Rybalkina I.G., Feil R., Hofmann F., Beavo J.A.
    J. Biol. Chem. 277:3310-3317(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF PDE5.
  15. "Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure."
    Tang K.M., Wang G.R., Lu P., Karas R.H., Aronovitz M., Heximer S.P., Kaltenbronn K.M., Blumer K.J., Siderovski D.P., Zhu Y., Mendelsohn M.E.
    Nat. Med. 9:1506-1512(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PHOSPHORYLATION OF RGS2, INTERACTION WITH RGS2.
  16. "Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides."
    Wooldridge A.A., MacDonald J.A., Erdodi F., Ma C., Borman M.A., Hartshorne D.J., Haystead T.A.J.
    J. Biol. Chem. 279:34496-34504(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "IRAG mediates NO/cGMP-dependent inhibition of platelet aggregation and thrombus formation."
    Antl M., von Bruehl M.-L., Eiglsperger C., Werner M., Konrad I., Kocher T., Wilm M., Hofmann F., Massberg S., Schlossmann J.
    Blood 109:552-559(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN THE INHIBITION OF PLATELET AGGREGATION, FUNCTION IN PHOSPHORYLATION OF MRVI1, SUBCELLULAR LOCATION, INTERACTION WITH MRVI1 AND ITPR1.
  18. "Interactions between the leucine-zipper motif of cGMP-dependent protein kinase and the C-terminal region of the targeting subunit of myosin light chain phosphatase."
    Lee E., Hayes D.B., Langsetmo K., Sundberg E.J., Tao T.C.
    J. Mol. Biol. 373:1198-1212(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R12A.
  19. "Probing the interaction between the coiled coil leucine zipper of cGMP-dependent protein kinase Ialpha and the C terminus of the myosin binding subunit of the myosin light chain phosphatase."
    Sharma A.K., Zhou G.-P., Kupferman J., Surks H.K., Christensen E.N., Chou J.J., Mendelsohn M.E., Rigby A.C.
    J. Biol. Chem. 283:32860-32869(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PPP1R12A, SUBUNIT.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action."
    Francis S.H., Busch J.L., Corbin J.D., Sibley D.
    Pharmacol. Rev. 62:525-563(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "Functional regulation of transient receptor potential canonical 7 by cGMP-dependent protein kinase Ialpha."
    Yuasa K., Matsuda T., Tsuji A.
    Cell. Signal. 23:1179-1187(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM ALPHA) IN PHOSPHORYLATION OF TRPC7, INTERACTION WITH TRPC7, SUBCELLULAR LOCATION.
  24. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  25. "Rapid and accurate structure determination of coiled-coil domains using NMR dipolar couplings: application to cGMP-dependent protein kinase Ialpha."
    Schnell J.R., Zhou G.-P., Zweckstetter M., Rigby A.C., Chou J.J.
    Protein Sci. 14:2421-2428(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2-58, INTERACTION WITH PPP1R12A, SUBUNIT, COILED-COIL.
  26. "A crystal structure of the cyclic GMP-dependent protein kinase I{beta} dimerization/docking domain reveals molecular details of isoform-specific anchoring."
    Casteel D.E., Smith-Nguyen E.V., Sankaran B., Roh S.H., Pilz R.B., Kim C.
    J. Biol. Chem. 285:32684-32688(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.27 ANGSTROMS) OF 4-55 (ISOFORM BETA), SUBUNIT.
  27. "Co-crystal structures of PKG Ibeta (92-227) with cGMP and cAMP reveal the molecular details of cyclic-nucleotide binding."
    Kim J.J., Casteel D.E., Huang G., Kwon T.H., Ren R.K., Zwart P., Headd J.J., Brown N.G., Chow D.C., Palzkill T., Kim C.
    PLoS ONE 6:E18413-E18413(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 92-227 (ISOFORM BETA) IN COMPLEX WITH CGMP AND CAMP.
  28. "Patterns of somatic mutation in human cancer genomes."
    Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.
    , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
    Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS [LARGE SCALE ANALYSIS] VAL-249 AND SER-267.
  29. Cited for: VARIANT AAT8 GLN-177, VARIANTS PHE-474 AND ALA-666, CHARACTERIZATION OF VARIANT AAT8 GLN-177.

Entry informationi

Entry nameiKGP1_HUMAN
AccessioniPrimary (citable) accession number: Q13976
Secondary accession number(s): A5YM56
, B3KSF3, E2PU10, P14619, Q5JP05, Q5JSJ6, Q6P5T7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 145 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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