Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

cGMP-dependent protein kinase 2

Gene

Prkg2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Crucial regulator of intestinal secretion and bone growth (By similarity). Phosphorylates and activates CFTR on the plasma membrane (PubMed:9465038). Plays a key role in intestinal secretion by regulating cGMP-dependent translocation of CFTR in jejunum (Probable). 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 (PubMed:18031684). 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).By similarity1 Publication2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.1 Publication

Enzyme regulationi

Binding of cGMP results in enzyme activation.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei347cAMP or cGMP 2By similarity1
Binding sitei412cAMP or cGMP 2By similarity1
Binding sitei415cAMP or cGMP 2By similarity1
Binding sitei482ATPPROSITE-ProRule annotation1
Active sitei576Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi232 – 235cAMP or cGMP 1By similarity4
Nucleotide bindingi242 – 243cAMP or cGMP 1By similarity2
Nucleotide bindingi357 – 359cAMP or cGMP 2By similarity3
Nucleotide bindingi366 – 367cAMP or cGMP 2By similarity2
Nucleotide bindingi459 – 467ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • cGMP binding Source: UniProtKB-KW
  • cGMP-dependent protein kinase activity Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • negative regulation of chloride transport Source: CAFA
  • peptidyl-serine autophosphorylation Source: RGD
  • protein localization to plasma membrane Source: RGD
  • protein phosphorylation Source: RGD

Keywordsi

Molecular functionKinase, Serine/threonine-protein kinase, Transferase
LigandATP-binding, cGMP, cGMP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.11.12 5301
ReactomeiR-RNO-1474151 Tetrahydrobiopterin (BH4) synthesis, recycling, salvage and regulation
R-RNO-418457 cGMP effects

Names & Taxonomyi

Protein namesi
Recommended name:
cGMP-dependent protein kinase 2 (EC:2.7.11.121 Publication)
Short name:
cGK 2
Short name:
cGK2
Alternative name(s):
cGMP-dependent protein kinase II
Short name:
cGKII
Gene namesi
Name:Prkg2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi3401 Prkg2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi2G → A: Cytosolic localization. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000861252 – 762cGMP-dependent protein kinase 2Add BLAST761

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi2N-myristoyl glycineBy similarity1
Modified residuei110PhosphoserineCombined sources1
Modified residuei117PhosphoserineCombined sources1
Modified residuei431PhosphoserineCombined sources1
Modified residuei609PhosphothreonineBy similarity1

Post-translational modificationi

Myristoylation mediates membrane localization.By similarity

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Proteomic databases

PaxDbiQ64595
PRIDEiQ64595

PTM databases

iPTMnetiQ64595
PhosphoSitePlusiQ64595

Expressioni

Tissue specificityi

Highly expressed in intestinal mucosa and is 20 times less abundant in brain and kidney (PubMed:7937783). Expressed in jejunum, in the apical domain of the villus epithelium (PubMed:15872007).2 Publications

Gene expression databases

BgeeiENSRNOG00000002361
GenevisibleiQ64595 RN

Interactioni

Subunit structurei

Interacts with GRIA1/GLUR1.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003237

Structurei

Secondary structure

1762
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi48 – 80Combined sources33

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4OJKX-ray2.66C/D40-83[»]
ProteinModelPortaliQ64595
SMRiQ64595
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini453 – 711Protein kinasePROSITE-ProRule annotationAdd BLAST259
Domaini712 – 762AGC-kinase C-terminalAdd BLAST51

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni168 – 283cGMP-binding, high affinity; cAMP-binding, moderate affinityBy similarityAdd BLAST116
Regioni286 – 416cGMP-binding, high affinity; cAMP-binding, low affinityBy similarityAdd BLAST131

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0616 Eukaryota
ENOG410XPQQ LUCA
GeneTreeiENSGT00810000125385
HOGENOMiHOG000233033
HOVERGENiHBG006211
InParanoidiQ64595
KOiK19477
OMAiELQSKCI
OrthoDBiEOG091G0S9R
PhylomeDBiQ64595
TreeFamiTF313261

Family and domain databases

CDDicd00038 CAP_ED, 2 hits
cd05572 STKc_cGK, 1 hit
Gene3Di2.60.120.10, 2 hits
InterProiView protein in InterPro
IPR000961 AGC-kinase_C
IPR002374 cGMP_dep_kinase
IPR018490 cNMP-bd-like
IPR018488 cNMP-bd_CS
IPR000595 cNMP-bd_dom
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR014710 RmlC-like_jellyroll
IPR008271 Ser/Thr_kinase_AS
IPR035014 STKc_cGK
PfamiView protein in Pfam
PF00027 cNMP_binding, 2 hits
PF00069 Pkinase, 1 hit
PIRSFiPIRSF000559 cGMP-dep_kinase, 1 hit
PRINTSiPR00104 CGMPKINASE
SMARTiView protein in SMART
SM00100 cNMP, 2 hits
SM00133 S_TK_X, 1 hit
SM00220 S_TKc, 1 hit
SUPFAMiSSF51206 SSF51206, 2 hits
SSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

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

Q64595-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGNGSVKPKH SKHPDGQSGN LSNEALRSKV AELEREVKRK DAELQEREYH
60 70 80 90 100
LKELREQLAK QTVAIAELTE ELQSKCIQLN KLQDVIHVQG GSPLQASPDK
110 120 130 140 150
VPLDVHRKTS GLVSLHSRRG AKAGVSAEPT SRTYDLNKPP EFSFEKARVR
160 170 180 190 200
KDSSEKKLIT DALNKNQFLK RLDPQQIKDM VECMYGRNYQ QGSYIVKQGE
210 220 230 240 250
PGNHIFVLAE GRLEVFQGEK LLSSIPMWTT FGELAILYNC TRTASVKAIT
260 270 280 290 300
NVKTWALDRE VFQNIMRRTA QARDEEYRNF LRSVSLLKNL PEDKLTKIID
310 320 330 340 350
CLEVEYYDKG DYIIREGEEG STFFILAKGK VKVTQSTEGH DQPQLIKTLQ
360 370 380 390 400
KGEYFGEKAL ISDDVRSANI IAEENDVACL VIDRETFNQT VGTFDELQKY
410 420 430 440 450
LEGYVATLNR DDEKRHAKRS MSSWKLSKAL SLEMIQLKEK VARFSSTSPF
460 470 480 490 500
QNLEIIATLG VGGFGRVELV KVKNENIAFA MKCIRKKHIV DTKQQEHVYS
510 520 530 540 550
EKRILEELCS PFIVKLYRTF KDNKYVYMLL EACLGGELWS ILRDRGSFDE
560 570 580 590 600
PTSKFCVACV TEAFDYLHRL GIIYRDLKPE NLILDADGYL KLVDFGFAKK
610 620 630 640 650
IGSGQKTWTF CGTPEYVAPE VILNKGHDFS VDFWSLGILV YELLTGNPPF
660 670 680 690 700
SGIDQMMTYN LILKGIEKMD FPRKITRRPE DLIRRLCRQN PTERLGNLKN
710 720 730 740 750
GINDIKKHRW LNGFNWEGLK ARSLPSPLRR ELSGPIDHSY FDKYPPEKGV
760
PPDEMSGWDK DF
Length:762
Mass (Da):87,182
Last modified:November 1, 1996 - v1
Checksum:iF0DF4F7684675B38
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z36276 mRNA Translation: CAA85284.1
PIRiI59329
RefSeqiNP_037144.1, NM_013012.1
UniGeneiRn.87721

Genome annotation databases

EnsembliENSRNOT00000003237; ENSRNOP00000003237; ENSRNOG00000002361
GeneIDi25523
KEGGirno:25523
UCSCiRGD:3401 rat

Similar proteinsi

Entry informationi

Entry nameiKGP2_RAT
AccessioniPrimary (citable) accession number: Q64595
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health