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Protein

cAMP-dependent protein kinase type I-alpha regulatory subunit

Gene

PRKAR1A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei202cAMP 11
Binding sitei211cAMP 11
Binding sitei326cAMP 21
Binding sitei335cAMP 21

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi137 – 254cAMP 1Add BLAST118
Nucleotide bindingi255 – 381cAMP 2Add BLAST127

GO - Molecular functioni

  • cAMP binding Source: UniProtKB-KW
  • cAMP-dependent protein kinase inhibitor activity Source: BHF-UCL
  • cAMP-dependent protein kinase regulator activity Source: BHF-UCL
  • protein kinase A catalytic subunit binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

cAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000108946-MONOMER.
ReactomeiR-HSA-163615. PKA activation.
R-HSA-164378. PKA activation in glucagon signalling.
R-HSA-180024. DARPP-32 events.
R-HSA-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-HSA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-HSA-5610787. Hedgehog 'off' state.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP10644.
SIGNORiP10644.

Names & Taxonomyi

Protein namesi
Recommended name:
cAMP-dependent protein kinase type I-alpha regulatory subunit
Alternative name(s):
Tissue-specific extinguisher 1
Short name:
TSE1
Cleaved into the following chain:
Gene namesi
Name:PRKAR1A
Synonyms:PKR1, PRKAR1, TSE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9388. PRKAR1A.

Subcellular locationi

GO - Cellular componenti

  • cAMP-dependent protein kinase complex Source: Ensembl
  • ciliary base Source: Reactome
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • membrane Source: UniProtKB
  • neuromuscular junction Source: Ensembl
  • nucleotide-activated protein kinase complex Source: BHF-UCL
  • plasma membrane raft Source: UniProtKB
  • protein complex Source: LIFEdb
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Involvement in diseasei

Carney complex 1 (CNC1)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCNC is a multiple neoplasia syndrome characterized by spotty skin pigmentation, cardiac and other myxomas, endocrine tumors, and psammomatous melanotic schwannomas.
See also OMIM:160980
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0468949S → N in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication1
Natural variantiVAR_04689574R → C in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 2 PublicationsCorresponds to variant rs137853303dbSNPEnsembl.1
Natural variantiVAR_046896146R → S in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication1
Natural variantiVAR_046897183D → Y in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication1
Natural variantiVAR_046898213A → D in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; reduces protein degradation. 2 PublicationsCorresponds to variant rs281864786dbSNPEnsembl.1
Natural variantiVAR_046899289G → W in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; accelerates protein degradation. 2 Publications1
Intracardiac myxoma (INTMYX)
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionInheritance is autosomal recessive.
See also OMIM:255960
Primary pigmented nodular adrenocortical disease 1 (PPNAD1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare bilateral adrenal defect causing ACTH-independent Cushing syndrome. Macroscopic appearance of the adrenals is characteristic with small pigmented micronodules observed in the cortex. Clinical manifestations of Cushing syndrome include facial and truncal obesity, abdominal striae, muscular weakness, osteoporosis, arterial hypertension, diabetes. PPNAD1 is most often diagnosed in patients with Carney complex, a multiple neoplasia syndrome. However it can also be observed in patients without other manifestations.
See also OMIM:610489
Acrodysostosis 1, with or without hormone resistance (ACRDYS1)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of skeletal dysplasia characterized by short stature, severe brachydactyly, facial dysostosis, and nasal hypoplasia. Affected individuals often have advanced bone age and obesity. Laboratory studies show resistance to multiple hormones, including parathyroid, thyrotropin, calcitonin, growth hormone-releasing hormone, and gonadotropin. However, not all patients show endocrine abnormalities.
See also OMIM:101800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075533175Y → C in ACRDYS1; reduces PKA activity; decreases cAMP binding. 1 Publication1
Natural variantiVAR_069456213A → T in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation. 2 Publications1
Natural variantiVAR_069458239T → A in ACRDYS1; impairs response of PKA to c-AMP. 1 Publication1
Natural variantiVAR_069459285Q → R in ACRDYS1; reduces PKA activity; decreases cAMP binding. 2 Publications1
Natural variantiVAR_069460289G → E in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation. 2 Publications1
Natural variantiVAR_069461327I → T in ACRDYS1. 1 PublicationCorresponds to variant rs387906695dbSNPEnsembl.1
Natural variantiVAR_069462328A → V in ACRDYS1; disrupts cAMP binding. 2 Publications1
Natural variantiVAR_069464335R → L in ACRDYS1; disrupts cAMP binding. 2 Publications1
Natural variantiVAR_069463335R → P in ACRDYS1. 1 PublicationCorresponds to variant rs387906694dbSNPEnsembl.1
Natural variantiVAR_069465373Y → C in ACRDYS1. 1 Publication1
Natural variantiVAR_068241373Y → H in ACRDYS1. 1 PublicationCorresponds to variant rs387906693dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi373Y → A: Impairs response of PKA to c-AMP. 1 Publication1

Keywords - Diseasei

Cushing syndrome, Disease mutation

Organism-specific databases

DisGeNETi5573.
MalaCardsiPRKAR1A.
MIMi101800. phenotype.
160980. phenotype.
255960. phenotype.
610489. phenotype.
OpenTargetsiENSG00000108946.
Orphaneti950. Acrodysostosis.
280651. Acrodysostosis with multiple hormone resistance.
520. Acute promyelocytic leukemia.
1359. Carney complex.
615. Familial atrial myxoma.
189439. Primary pigmented nodular adrenocortical disease.
PharmGKBiPA33754.

Polymorphism and mutation databases

DMDMi125193.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002053771 – 381cAMP-dependent protein kinase type I-alpha regulatory subunitAdd BLAST381
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00004343542 – 381cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedAdd BLAST380

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei3PhosphoserineBy similarity1
Disulfide bondi18Interchain (with C-39)By similarity
Disulfide bondi39Interchain (with C-18)By similarity
Modified residuei75PhosphothreonineCombined sources1
Modified residuei77PhosphoserineCombined sources1
Modified residuei83PhosphoserineCombined sources1
Modified residuei101PhosphoserineBy similarity1
Modified residuei258PhosphoserineBy similarity1

Post-translational modificationi

The pseudophosphorylation site binds to the substrate-binding region of the catalytic chain, resulting in the inhibition of its activity.

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

EPDiP10644.
MaxQBiP10644.
PaxDbiP10644.
PeptideAtlasiP10644.
PRIDEiP10644.

2D gel databases

OGPiP10644.
REPRODUCTION-2DPAGEIPI00021831.

PTM databases

iPTMnetiP10644.
PhosphoSitePlusiP10644.
SwissPalmiP10644.

Expressioni

Tissue specificityi

Four types of regulatory chains are found: I-alpha, I-beta, II-alpha, and II-beta. Their expression varies among tissues and is in some cases constitutive and in others inducible.

Gene expression databases

BgeeiENSG00000108946.
CleanExiHS_PRKAR1A.
ExpressionAtlasiP10644. baseline and differential.
GenevisibleiP10644. HS.

Organism-specific databases

HPAiCAB019378.
HPA049847.
HPA049979.

Interactioni

Subunit structurei

The inactive holoenzyme is composed of two regulatory chains and two catalytic chains. Activation by cAMP releases the two active catalytic monomers and the regulatory dimer. PRKAR1A also interacts with RFC2; the complex may be involved in cell survival. Interacts with AKAP4. Interacts with RARA; the interaction occurs in the presence of cAMP or FSH and regulates RARA transcriptional activity. Interacts with the phosphorylated form of PJA2. Interacts with CBFA2T3 (By similarity). Interacts with PRKX; regulates this cAMP-dependent protein kinase. Interacts with C2orf88/smAKAP; this interaction may target PRKAR1A to the plasma membrane. Interacts with AICDA.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P03259-25EBI-476431,EBI-7225021From a different organism.
C2orf88Q9BSF03EBI-476431,EBI-744298
GABARAPL1Q9H0R82EBI-476431,EBI-746969
PLEKHF2Q9H8W43EBI-476431,EBI-742388
PRKACAP176125EBI-476431,EBI-476586
PRKXP518172EBI-476431,EBI-4302903
RFC2P352507EBI-476431,EBI-476409
SETQ011052EBI-476431,EBI-1053182

GO - Molecular functioni

  • protein kinase A catalytic subunit binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111559. 87 interactors.
DIPiDIP-34368N.
IntActiP10644. 68 interactors.
MINTiMINT-1194164.
STRINGi9606.ENSP00000351410.

Structurei

3D structure databases

ProteinModelPortaliP10644.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 136Dimerization and phosphorylationAdd BLAST136

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi96 – 100Pseudophosphorylation motif5

Sequence similaritiesi

Contains 2 cyclic nucleotide-binding domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP10644.
KOiK04739.
OMAiFDAMFPC.
OrthoDBiEOG091G0F1K.
PhylomeDBiP10644.
TreeFamiTF314920.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P10644-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL
60 70 80 90 100
REYFERLEKE EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI
110 120 130 140 150
SAEVYTEEDA ASYVRKVIPK DYKTMAALAK AIEKNVLFSH LDDNERSDIF
160 170 180 190 200
DAMFSVSFIA GETVIQQGDE GDNFYVIDQG ETDVYVNNEW ATSVGEGGSF
210 220 230 240 250
GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL RKRKMYEEFL
260 270 280 290 300
SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA
310 320 330 340 350
AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL
360 370 380
DRPRFERVLG PCSDILKRNI QQYNSFVSLS V
Length:381
Mass (Da):42,982
Last modified:July 1, 1989 - v1
Checksum:i2D04F08CE8857A6D
GO
Isoform 2 (identifier: P10644-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     326-337: EIALLMNRPRAA → HLIISRRSIPLG
     338-381: Missing.

Note: No experimental confirmation available. Gene prediction based on EST data.
Show »
Length:337
Mass (Da):38,003
Checksum:i8C14AF540F3150CF
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0468949S → N in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication1
Natural variantiVAR_04689574R → C in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 2 PublicationsCorresponds to variant rs137853303dbSNPEnsembl.1
Natural variantiVAR_046896146R → S in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication1
Natural variantiVAR_075533175Y → C in ACRDYS1; reduces PKA activity; decreases cAMP binding. 1 Publication1
Natural variantiVAR_046897183D → Y in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication1
Natural variantiVAR_046898213A → D in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; reduces protein degradation. 2 PublicationsCorresponds to variant rs281864786dbSNPEnsembl.1
Natural variantiVAR_069456213A → T in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation. 2 Publications1
Natural variantiVAR_069457227D → N.1 Publication1
Natural variantiVAR_069458239T → A in ACRDYS1; impairs response of PKA to c-AMP. 1 Publication1
Natural variantiVAR_069459285Q → R in ACRDYS1; reduces PKA activity; decreases cAMP binding. 2 Publications1
Natural variantiVAR_069460289G → E in ACRDYS1; reduces PKA activity; decreases cAMP binding; reduces protein degradation. 2 Publications1
Natural variantiVAR_046899289G → W in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit; accelerates protein degradation. 2 Publications1
Natural variantiVAR_069461327I → T in ACRDYS1. 1 PublicationCorresponds to variant rs387906695dbSNPEnsembl.1
Natural variantiVAR_069462328A → V in ACRDYS1; disrupts cAMP binding. 2 Publications1
Natural variantiVAR_069464335R → L in ACRDYS1; disrupts cAMP binding. 2 Publications1
Natural variantiVAR_069463335R → P in ACRDYS1. 1 PublicationCorresponds to variant rs387906694dbSNPEnsembl.1
Natural variantiVAR_069465373Y → C in ACRDYS1. 1 Publication1
Natural variantiVAR_068241373Y → H in ACRDYS1. 1 PublicationCorresponds to variant rs387906693dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_054833326 – 337EIALL…RPRAA → HLIISRRSIPLG in isoform 2. CuratedAdd BLAST12
Alternative sequenceiVSP_054834338 – 381Missing in isoform 2. CuratedAdd BLAST44

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18468 mRNA. Translation: AAB50922.1.
M33336 mRNA. Translation: AAB50921.1.
S54705 mRNA. No translation available.
S54707 mRNA. No translation available.
S54709 mRNA. No translation available.
S54711 mRNA. No translation available.
Y07642 mRNA. Translation: CAA68925.1.
AC079210 Genomic DNA. No translation available.
BC036285 mRNA. Translation: AAH36285.1.
BC093042 mRNA. Translation: AAH93042.1.
CCDSiCCDS11678.1. [P10644-1]
CCDS62307.1. [P10644-2]
PIRiA34627. OKHU1R.
RefSeqiNP_001263218.1. NM_001276289.1. [P10644-1]
NP_001263219.1. NM_001276290.1. [P10644-2]
NP_001265362.1. NM_001278433.1. [P10644-1]
NP_002725.1. NM_002734.4. [P10644-1]
NP_997636.1. NM_212471.2. [P10644-1]
NP_997637.1. NM_212472.2. [P10644-1]
XP_011523285.1. XM_011524983.2. [P10644-1]
XP_011523286.1. XM_011524984.2. [P10644-1]
XP_011523287.1. XM_011524985.2. [P10644-1]
UniGeneiHs.280342.
Hs.745160.

Genome annotation databases

EnsembliENST00000358598; ENSP00000351410; ENSG00000108946. [P10644-1]
ENST00000392711; ENSP00000376475; ENSG00000108946. [P10644-1]
ENST00000536854; ENSP00000445625; ENSG00000108946. [P10644-1]
ENST00000586397; ENSP00000466459; ENSG00000108946. [P10644-1]
ENST00000588188; ENSP00000468106; ENSG00000108946. [P10644-2]
ENST00000589228; ENSP00000464977; ENSG00000108946. [P10644-1]
GeneIDi5573.
KEGGihsa:5573.
UCSCiuc002jhg.5. human. [P10644-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M18468 mRNA. Translation: AAB50922.1.
M33336 mRNA. Translation: AAB50921.1.
S54705 mRNA. No translation available.
S54707 mRNA. No translation available.
S54709 mRNA. No translation available.
S54711 mRNA. No translation available.
Y07642 mRNA. Translation: CAA68925.1.
AC079210 Genomic DNA. No translation available.
BC036285 mRNA. Translation: AAH36285.1.
BC093042 mRNA. Translation: AAH93042.1.
CCDSiCCDS11678.1. [P10644-1]
CCDS62307.1. [P10644-2]
PIRiA34627. OKHU1R.
RefSeqiNP_001263218.1. NM_001276289.1. [P10644-1]
NP_001263219.1. NM_001276290.1. [P10644-2]
NP_001265362.1. NM_001278433.1. [P10644-1]
NP_002725.1. NM_002734.4. [P10644-1]
NP_997636.1. NM_212471.2. [P10644-1]
NP_997637.1. NM_212472.2. [P10644-1]
XP_011523285.1. XM_011524983.2. [P10644-1]
XP_011523286.1. XM_011524984.2. [P10644-1]
XP_011523287.1. XM_011524985.2. [P10644-1]
UniGeneiHs.280342.
Hs.745160.

3D structure databases

ProteinModelPortaliP10644.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111559. 87 interactors.
DIPiDIP-34368N.
IntActiP10644. 68 interactors.
MINTiMINT-1194164.
STRINGi9606.ENSP00000351410.

PTM databases

iPTMnetiP10644.
PhosphoSitePlusiP10644.
SwissPalmiP10644.

Polymorphism and mutation databases

DMDMi125193.

2D gel databases

OGPiP10644.
REPRODUCTION-2DPAGEIPI00021831.

Proteomic databases

EPDiP10644.
MaxQBiP10644.
PaxDbiP10644.
PeptideAtlasiP10644.
PRIDEiP10644.

Protocols and materials databases

DNASUi5573.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358598; ENSP00000351410; ENSG00000108946. [P10644-1]
ENST00000392711; ENSP00000376475; ENSG00000108946. [P10644-1]
ENST00000536854; ENSP00000445625; ENSG00000108946. [P10644-1]
ENST00000586397; ENSP00000466459; ENSG00000108946. [P10644-1]
ENST00000588188; ENSP00000468106; ENSG00000108946. [P10644-2]
ENST00000589228; ENSP00000464977; ENSG00000108946. [P10644-1]
GeneIDi5573.
KEGGihsa:5573.
UCSCiuc002jhg.5. human. [P10644-1]

Organism-specific databases

CTDi5573.
DisGeNETi5573.
GeneCardsiPRKAR1A.
GeneReviewsiPRKAR1A.
HGNCiHGNC:9388. PRKAR1A.
HPAiCAB019378.
HPA049847.
HPA049979.
MalaCardsiPRKAR1A.
MIMi101800. phenotype.
160980. phenotype.
188830. gene.
255960. phenotype.
610489. phenotype.
neXtProtiNX_P10644.
OpenTargetsiENSG00000108946.
Orphaneti950. Acrodysostosis.
280651. Acrodysostosis with multiple hormone resistance.
520. Acute promyelocytic leukemia.
1359. Carney complex.
615. Familial atrial myxoma.
189439. Primary pigmented nodular adrenocortical disease.
PharmGKBiPA33754.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1113. Eukaryota.
COG0664. LUCA.
GeneTreeiENSGT00530000062947.
HOGENOMiHOG000196669.
HOVERGENiHBG002025.
InParanoidiP10644.
KOiK04739.
OMAiFDAMFPC.
OrthoDBiEOG091G0F1K.
PhylomeDBiP10644.
TreeFamiTF314920.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000108946-MONOMER.
ReactomeiR-HSA-163615. PKA activation.
R-HSA-164378. PKA activation in glucagon signalling.
R-HSA-180024. DARPP-32 events.
R-HSA-381676. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
R-HSA-432040. Vasopressin regulates renal water homeostasis via Aquaporins.
R-HSA-5610787. Hedgehog 'off' state.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP10644.
SIGNORiP10644.

Miscellaneous databases

ChiTaRSiPRKAR1A. human.
GenomeRNAii5573.
PROiP10644.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000108946.
CleanExiHS_PRKAR1A.
ExpressionAtlasiP10644. baseline and differential.
GenevisibleiP10644. HS.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR012198. cAMP_dep_PK_reg_su.
IPR003117. cAMP_dep_PK_reg_su_I/II_a/b.
IPR018490. cNMP-bd-like.
IPR018488. cNMP-bd_CS.
IPR000595. cNMP-bd_dom.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00027. cNMP_binding. 2 hits.
PF02197. RIIa. 1 hit.
[Graphical view]
PIRSFiPIRSF000548. PK_regulatory. 1 hit.
SMARTiSM00100. cNMP. 2 hits.
SM00394. RIIa. 1 hit.
[Graphical view]
SUPFAMiSSF47391. SSF47391. 1 hit.
SSF51206. SSF51206. 2 hits.
PROSITEiPS00888. CNMP_BINDING_1. 2 hits.
PS00889. CNMP_BINDING_2. 2 hits.
PS50042. CNMP_BINDING_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKAP0_HUMAN
AccessioniPrimary (citable) accession number: P10644
Secondary accession number(s): K7ER48, Q567S7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: November 30, 2016
This is version 197 of the entry and version 1 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.