Q13237 · KGP2_HUMAN
- ProteincGMP-dependent protein kinase 2
- GenePRKG2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids762 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 a 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).
Catalytic activity
- ATP + L-seryl-[protein] = ADP + H+ + O-phospho-L-seryl-[protein]
Activity regulation
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 232-235 | 3',5'-cyclic AMP (UniProtKB | ChEBI) | ||||
Sequence: GELA | ||||||
Binding site | 232-235 | 3',5'-cyclic GMP 1 (UniProtKB | ChEBI) | ||||
Sequence: GELA | ||||||
Binding site | 242-243 | 3',5'-cyclic AMP (UniProtKB | ChEBI) | ||||
Sequence: RT | ||||||
Binding site | 242-243 | 3',5'-cyclic GMP 1 (UniProtKB | ChEBI) | ||||
Sequence: RT | ||||||
Binding site | 347 | 3',5'-cyclic GMP 2 (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 356-359 | 3',5'-cyclic GMP 2 (UniProtKB | ChEBI) | ||||
Sequence: GEKA | ||||||
Binding site | 366-367 | 3',5'-cyclic GMP 2 (UniProtKB | ChEBI) | ||||
Sequence: RS | ||||||
Binding site | 412 | 3',5'-cyclic GMP 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 415 | 3',5'-cyclic GMP 2 (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 459-467 | ATP (UniProtKB | ChEBI) | ||||
Sequence: LGVGGFGRV | ||||||
Binding site | 482 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 576 | Proton acceptor | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apical plasma membrane | |
Cellular Component | cytosol | |
Cellular Component | nuclear membrane | |
Molecular Function | ATP binding | |
Molecular Function | cGMP binding | |
Molecular Function | cGMP-dependent protein kinase activity | |
Molecular Function | identical protein binding | |
Molecular Function | mitogen-activated protein kinase binding | |
Molecular Function | protein kinase activity | |
Molecular Function | protein serine kinase activity | |
Biological Process | negative regulation of chloride transport | |
Biological Process | positive regulation of chondrocyte differentiation | |
Biological Process | positive regulation of protein localization | |
Biological Process | protein kinase A signaling | |
Biological Process | protein localization to plasma membrane | |
Biological Process | protein phosphorylation | |
Biological Process | signal transduction | |
Biological Process | tetrahydrobiopterin metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namecGMP-dependent protein kinase 2
- EC number
- Short namescGK 2; cGK2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ13237
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Spondylometaphyseal dysplasia, Pagnamenta type (SMDP)
- Note
- DescriptionA form of spondylometaphyseal dysplasia, a group of short stature disorders distinguished by abnormalities in the vertebrae and the metaphyses of the tubular bones. SMDP is an autosomal recessive form characterized by short stature and mild platyspondyly with no disproportion between the limbs. Mild metaphyseal changes are present.
- See alsoMIM:619638
Acromesomelic dysplasia 4 (AMD4)
- Note
- DescriptionA form of acromesomelic dysplasia, a skeletal disorder characterized by short stature, very short limbs and hand/foot malformations. The severity of limb abnormalities increases from proximal to distal with profoundly affected hands and feet showing brachydactyly and/or rudimentary fingers (knob-like fingers). AMD4 radiographic hallmarks include mild to moderate platyspondyly, moderate brachydactyly, iliac flaring, and metaphyseal alterations of the long bones that progressively increase with age. AMD4 inheritance is autosomal recessive.
- See alsoMIM:619636
Natural variants in AMD4
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_086537 | 569-762 | missing | in AMD4; decreased protein abundance; unable to phosphorylate RAF1 in response to FGF2 and to inhibit FGF2-induced MAPK signaling; unable to suppress SOX9-induced COL2A1 expression; unable to upregulate COL10A1 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_051633 | 22 | in dbSNP:rs34956759 | |||
Sequence: T → S | ||||||
Natural variant | VAR_040608 | 106 | in dbSNP:rs34616910 | |||
Sequence: H → R | ||||||
Mutagenesis | 412 | Reduces cGMP binding affinity; when associated with A-415. | ||||
Sequence: D → A | ||||||
Mutagenesis | 415 | Reduces cGMP binding affinity; when associated with A-412. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_086537 | 569-762 | in AMD4; decreased protein abundance; unable to phosphorylate RAF1 in response to FGF2 and to inhibit FGF2-induced MAPK signaling; unable to suppress SOX9-induced COL2A1 expression; unable to upregulate COL10A1 | |||
Sequence: Missing | ||||||
Natural variant | VAR_040609 | 716 | in a colorectal adenocarcinoma sample; somatic mutation | |||
Sequence: W → R |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 838 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Lipidation | 2 | UniProt | N-myristoyl glycine | ||||
Sequence: G | |||||||
Chain | PRO_0000086123 | 2-762 | UniProt | cGMP-dependent protein kinase 2 | |||
Sequence: GNGSVKPKHSKHPDGHSGNLTTDALRNKVTELERELRRKDAEIQEREYHLKELREQLSKQTVAIAELTEELQNKCIQLNKLQDVVHMQGGSPLQASPDKVPLEVHRKTSGLVSLHSRRGAKAGVSAEPTTRTYDLNKPPEFSFEKARVRKDSSEKKLITDALNKNQFLKRLDPQQIKDMVECMYGRNYQQGSYIIKQGEPGNHIFVLAEGRLEVFQGEKLLSSIPMWTTFGELAILYNCTRTASVKAITNVKTWALDREVFQNIMRRTAQARDEQYRNFLRSVSLLKNLPEDKLTKIIDCLEVEYYDKGDYIIREGEEGSTFFILAKGKVKVTQSTEGHDQPQLIKTLQKGEYFGEKALISDDVRSANIIAEENDVACLVIDRETFNQTVGTFEELQKYLEGYVANLNRDDEKRHAKRSMSNWKLSKALSLEMIQLKEKVARFSSSSPFQNLEIIATLGVGGFGRVELVKVKNENVAFAMKCIRKKHIVDTKQQEHVYSEKRILEELCSPFIVKLYRTFKDNKYVYMLLEACLGGELWSILRDRGSFDEPTSKFCVACVTEAFDYLHRLGIIYRDLKPENLILDAEGYLKLVDFGFAKKIGSGQKTWTFCGTPEYVAPEVILNKGHDFSVDFWSLGILVYELLTGNPPFSGVDQMMTYNLILKGIEKMDFPRKITRRPEDLIRRLCRQNPTERLGNLKNGINDIKKHRWLNGFNWEGLKARSLPSPLQRELKGPIDHSYFDKYPPEKGMPPDELSGWDKDF | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 110 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 117 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 431 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 431 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 609 | UniProt | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for region, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-25 | Disordered | ||||
Sequence: MGNGSVKPKHSKHPDGHSGNLTTDA | ||||||
Coiled coil | 23-85 | |||||
Sequence: TDALRNKVTELERELRRKDAEIQEREYHLKELREQLSKQTVAIAELTEELQNKCIQLNKLQDV | ||||||
Region | 117-138 | Disordered | ||||
Sequence: SRRGAKAGVSAEPTTRTYDLNK | ||||||
Region | 168-283 | cGMP-binding, high affinity; cAMP-binding, moderate affinity | ||||
Sequence: FLKRLDPQQIKDMVECMYGRNYQQGSYIIKQGEPGNHIFVLAEGRLEVFQGEKLLSSIPMWTTFGELAILYNCTRTASVKAITNVKTWALDREVFQNIMRRTAQARDEQYRNFLRS | ||||||
Region | 286-416 | cGMP-binding, high affinity; cAMP-binding, low affinity | ||||
Sequence: LLKNLPEDKLTKIIDCLEVEYYDKGDYIIREGEEGSTFFILAKGKVKVTQSTEGHDQPQLIKTLQKGEYFGEKALISDDVRSANIIAEENDVACLVIDRETFNQTVGTFEELQKYLEGYVANLNRDDEKRH | ||||||
Domain | 453-711 | Protein kinase | ||||
Sequence: LEIIATLGVGGFGRVELVKVKNENVAFAMKCIRKKHIVDTKQQEHVYSEKRILEELCSPFIVKLYRTFKDNKYVYMLLEACLGGELWSILRDRGSFDEPTSKFCVACVTEAFDYLHRLGIIYRDLKPENLILDAEGYLKLVDFGFAKKIGSGQKTWTFCGTPEYVAPEVILNKGHDFSVDFWSLGILVYELLTGNPPFSGVDQMMTYNLILKGIEKMDFPRKITRRPEDLIRRLCRQNPTERLGNLKNGINDIKKHRWL | ||||||
Domain | 712-762 | AGC-kinase C-terminal | ||||
Sequence: NGFNWEGLKARSLPSPLQRELKGPIDHSYFDKYPPEKGMPPDELSGWDKDF | ||||||
Region | 740-762 | Disordered | ||||
Sequence: YFDKYPPEKGMPPDELSGWDKDF |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q13237-1
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.
- Name1
- Length762
- Mass (Da)87,432
- Last updated1996-11-01 v1
- ChecksumFA7BA149906B5996
Q13237-2
- Name2
- Differences from canonical
- 441-469: Missing
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B7ZA25 | B7ZA25_HUMAN | PRKG2 | 342 |
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 57-58 | in Ref. 2; BAA18934 | ||||
Sequence: QL → HG | ||||||
Sequence conflict | 154 | in Ref. 5; CAA76073 | ||||
Sequence: S → I | ||||||
Sequence conflict | 388 | in Ref. 3; BAG60035 | ||||
Sequence: N → D | ||||||
Alternative sequence | VSP_055121 | 441-469 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 460 | in Ref. 2; BAA18934 | ||||
Sequence: G → A |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X94612 EMBL· GenBank· DDBJ | CAA64318.1 EMBL· GenBank· DDBJ | mRNA | ||
D70899 EMBL· GenBank· DDBJ | BAA18934.1 EMBL· GenBank· DDBJ | mRNA | ||
AK297673 EMBL· GenBank· DDBJ | BAG60035.1 EMBL· GenBank· DDBJ | mRNA | ||
AC098819 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC139722 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
Y16106 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16107 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16108 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16109 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16110 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16111 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16112 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16113 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16114 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16115 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16116 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16117 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16118 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16119 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16120 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16121 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16122 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Y16123 EMBL· GenBank· DDBJ | CAA76073.1 EMBL· GenBank· DDBJ | Genomic DNA |