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P10644

- KAP0_HUMAN

UniProt

P10644 - KAP0_HUMAN

Protein

cAMP-dependent protein kinase type I-alpha regulatory subunit

Gene

PRKAR1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    Functioni

    Regulatory subunit of the cAMP-dependent protein kinases involved in cAMP signaling in cells.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei202 – 2021cAMP 1
    Binding sitei211 – 2111cAMP 1
    Binding sitei326 – 3261cAMP 2
    Binding sitei335 – 3351cAMP 2

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi137 – 254118cAMP 1Add
    BLAST
    Nucleotide bindingi255 – 381127cAMP 2Add
    BLAST

    GO - Molecular functioni

    1. cAMP binding Source: UniProtKB-KW
    2. cAMP-dependent protein kinase inhibitor activity Source: BHF-UCL
    3. cAMP-dependent protein kinase regulator activity Source: BHF-UCL
    4. protein binding Source: IntAct
    5. protein kinase A catalytic subunit binding Source: BHF-UCL
    6. ubiquitin protein ligase binding Source: UniProtKB

    GO - Biological processi

    1. activation of phospholipase C activity Source: Reactome
    2. activation of protein kinase A activity Source: Reactome
    3. blood coagulation Source: Reactome
    4. cardiac muscle cell proliferation Source: Ensembl
    5. cellular response to glucagon stimulus Source: Reactome
    6. energy reserve metabolic process Source: Reactome
    7. epidermal growth factor receptor signaling pathway Source: Reactome
    8. female meiotic division Source: Ensembl
    9. fibroblast growth factor receptor signaling pathway Source: Reactome
    10. innate immune response Source: Reactome
    11. intracellular signal transduction Source: ProtInc
    12. mesoderm formation Source: Ensembl
    13. negative regulation of cAMP-dependent protein kinase activity Source: BHF-UCL
    14. negative regulation of meiosis Source: Ensembl
    15. neurotrophin TRK receptor signaling pathway Source: Reactome
    16. regulation of insulin secretion Source: Reactome
    17. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    18. sarcomere organization Source: Ensembl
    19. signal transduction Source: Reactome
    20. small molecule metabolic process Source: Reactome
    21. transmembrane transport Source: Reactome
    22. water transport Source: Reactome

    Keywords - Ligandi

    cAMP, cAMP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_15334. DARPP-32 events.
    REACT_15530. PKA activation.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_1946. PKA activation in glucagon signalling.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinkiP10644.

    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
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9388. PRKAR1A.

    Subcellular locationi

    Cell membrane 1 Publication

    GO - Cellular componenti

    1. AMP-activated protein kinase complex Source: BHF-UCL
    2. cAMP-dependent protein kinase complex Source: Ensembl
    3. cytosol Source: Reactome
    4. membrane Source: UniProtKB
    5. neuromuscular junction Source: Ensembl
    6. plasma membrane Source: UniProtKB-SubCell
    7. protein complex Source: LIFEdb

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Carney complex 1 (CNC1) [MIM:160980]: CNC is a multiple neoplasia syndrome characterized by spotty skin pigmentation, cardiac and other myxomas, endocrine tumors, and psammomatous melanotic schwannomas.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91S → N in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046894
    Natural varianti74 – 741R → C in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046895
    Natural varianti146 – 1461R → S in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046896
    Natural varianti183 – 1831D → Y in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046897
    Natural varianti213 – 2131A → D in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046898
    Natural varianti289 – 2891G → W in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046899
    Intracardiac myxoma (INTMYX) [MIM:255960]: Inheritance is autosomal recessive.
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Primary pigmented nodular adrenocortical disease 1 (PPNAD1) [MIM:610489]: A 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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Acrodysostosis 1, with or without hormone resistance (ACRDYS1) [MIM:101800]: A 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.6 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti213 – 2131A → T in ACRDYS1. 1 Publication
    VAR_069456
    Natural varianti239 – 2391T → A in ACRDYS1; impairs response of PKA to c-AMP. 1 Publication
    VAR_069458
    Natural varianti285 – 2851Q → R in ACRDYS1. 1 Publication
    VAR_069459
    Natural varianti289 – 2891G → E in ACRDYS1. 1 Publication
    VAR_069460
    Natural varianti327 – 3271I → T in ACRDYS1. 1 Publication
    VAR_069461
    Natural varianti328 – 3281A → V in ACRDYS1. 1 Publication
    VAR_069462
    Natural varianti335 – 3351R → L in ACRDYS1. 1 Publication
    VAR_069464
    Natural varianti335 – 3351R → P in ACRDYS1. 1 Publication
    VAR_069463
    Natural varianti373 – 3731Y → C in ACRDYS1. 1 Publication
    VAR_069465
    Natural varianti373 – 3731Y → H in ACRDYS1. 1 Publication
    VAR_068241

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi373 – 3731Y → A: Impairs response of PKA to c-AMP. 1 Publication

    Keywords - Diseasei

    Cushing syndrome, Disease mutation

    Organism-specific databases

    MIMi101800. phenotype.
    160980. phenotype.
    255960. phenotype.
    610489. phenotype.
    Orphaneti950. Acrodysostosis.
    280651. Acrodysostosis with multiple hormone resistance.
    1359. Carney complex.
    615. Familial atrial myxoma.
    189439. Primary pigmented nodular adrenocortical disease.
    PharmGKBiPA33754.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 381381cAMP-dependent protein kinase type I-alpha regulatory subunitPRO_0000205377Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 381380cAMP-dependent protein kinase type I-alpha regulatory subunit, N-terminally processedPRO_0000421785Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine4 Publications
    Disulfide bondi18 – 18Interchain (with C-39)By similarity
    Disulfide bondi39 – 39Interchain (with C-18)By similarity
    Modified residuei83 – 831Phosphoserine8 Publications
    Modified residuei101 – 1011PhosphoserineBy similarity

    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

    MaxQBiP10644.
    PaxDbiP10644.
    PeptideAtlasiP10644.
    PRIDEiP10644.

    2D gel databases

    OGPiP10644.
    REPRODUCTION-2DPAGEIPI00021831.

    PTM databases

    PhosphoSiteiP10644.

    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

    ArrayExpressiP10644.
    BgeeiP10644.
    CleanExiHS_PRKAR1A.
    GenevestigatoriP10644.

    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.
    GABARAPL1Q9H0R82EBI-476431,EBI-746969
    PLEKHF2Q9H8W43EBI-476431,EBI-742388
    PRKACAP176122EBI-476431,EBI-476586
    PRKXP518172EBI-476431,EBI-4302903
    RFC2P352507EBI-476431,EBI-476409
    SETQ011052EBI-476431,EBI-1053182

    Protein-protein interaction databases

    BioGridi111559. 68 interactions.
    DIPiDIP-34368N.
    IntActiP10644. 55 interactions.
    MINTiMINT-1194164.
    STRINGi9606.ENSP00000351410.

    Structurei

    3D structure databases

    ProteinModelPortaliP10644.
    SMRiP10644. Positions 14-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 136136Dimerization and phosphorylationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi96 – 1005Pseudophosphorylation motif

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0664.
    HOGENOMiHOG000196669.
    HOVERGENiHBG002025.
    InParanoidiP10644.
    KOiK04739.
    OMAiFSAEVYT.
    PhylomeDBiP10644.
    TreeFamiTF314920.

    Family and domain databases

    Gene3Di2.60.120.10. 2 hits.
    InterProiIPR002373. cAMP/cGMP_kin.
    IPR012198. 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.
    PRINTSiPR00103. CAMPKINASE.
    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. Align

    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

    MESGSTAASE EARSLRECEL YVQKHNIQAL LKDSIVQLCT ARPERPMAFL    50
    REYFERLEKE EAKQIQNLQK AGTRTDSRED EISPPPPNPV VKGRRRRGAI 100
    SAEVYTEEDA ASYVRKVIPK DYKTMAALAK AIEKNVLFSH LDDNERSDIF 150
    DAMFSVSFIA GETVIQQGDE GDNFYVIDQG ETDVYVNNEW ATSVGEGGSF 200
    GELALIYGTP RAATVKAKTN VKLWGIDRDS YRRILMGSTL RKRKMYEEFL 250
    SKVSILESLD KWERLTVADA LEPVQFEDGQ KIVVQGEPGD EFFIILEGSA 300
    AVLQRRSENE EFVEVGRLGP SDYFGEIALL MNRPRAATVV ARGPLKCVKL 350
    DRPRFERVLG PCSDILKRNI QQYNSFVSLS V 381
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91S → N in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046894
    Natural varianti74 – 741R → C in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046895
    Natural varianti146 – 1461R → S in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046896
    Natural varianti183 – 1831D → Y in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046897
    Natural varianti213 – 2131A → D in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046898
    Natural varianti213 – 2131A → T in ACRDYS1. 1 Publication
    VAR_069456
    Natural varianti227 – 2271D → N.1 Publication
    VAR_069457
    Natural varianti239 – 2391T → A in ACRDYS1; impairs response of PKA to c-AMP. 1 Publication
    VAR_069458
    Natural varianti285 – 2851Q → R in ACRDYS1. 1 Publication
    VAR_069459
    Natural varianti289 – 2891G → E in ACRDYS1. 1 Publication
    VAR_069460
    Natural varianti289 – 2891G → W in CNC1; exhibits increased PKA activity which is attributed to decreased binding to cAMP and/or the catalytic subunit. 1 Publication
    VAR_046899
    Natural varianti327 – 3271I → T in ACRDYS1. 1 Publication
    VAR_069461
    Natural varianti328 – 3281A → V in ACRDYS1. 1 Publication
    VAR_069462
    Natural varianti335 – 3351R → L in ACRDYS1. 1 Publication
    VAR_069464
    Natural varianti335 – 3351R → P in ACRDYS1. 1 Publication
    VAR_069463
    Natural varianti373 – 3731Y → C in ACRDYS1. 1 Publication
    VAR_069465
    Natural varianti373 – 3731Y → H in ACRDYS1. 1 Publication
    VAR_068241

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei326 – 33712EIALL…RPRAA → HLIISRRSIPLG in isoform 2. CuratedVSP_054833Add
    BLAST
    Alternative sequencei338 – 38144Missing in isoform 2. CuratedVSP_054834Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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]
    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.4. human. [P10644-1]

    Polymorphism databases

    DMDMi125193.

    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS11678.1. [P10644-1 ]
    CCDS62307.1. [P10644-2 ]
    PIRi A34627. OKHU1R.
    RefSeqi NP_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 ]
    UniGenei Hs.280342.
    Hs.745160.

    3D structure databases

    ProteinModelPortali P10644.
    SMRi P10644. Positions 14-380.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111559. 68 interactions.
    DIPi DIP-34368N.
    IntActi P10644. 55 interactions.
    MINTi MINT-1194164.
    STRINGi 9606.ENSP00000351410.

    Chemistry

    BindingDBi P10644.

    PTM databases

    PhosphoSitei P10644.

    Polymorphism databases

    DMDMi 125193.

    2D gel databases

    OGPi P10644.
    REPRODUCTION-2DPAGE IPI00021831.

    Proteomic databases

    MaxQBi P10644.
    PaxDbi P10644.
    PeptideAtlasi P10644.
    PRIDEi P10644.

    Protocols and materials databases

    DNASUi 5573.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358598 ; 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 ]
    GeneIDi 5573.
    KEGGi hsa:5573.
    UCSCi uc002jhg.4. human. [P10644-1 ]

    Organism-specific databases

    CTDi 5573.
    GeneCardsi GC17P066508.
    GeneReviewsi PRKAR1A.
    HGNCi HGNC:9388. PRKAR1A.
    HPAi CAB019378.
    HPA049847.
    HPA049979.
    MIMi 101800. phenotype.
    160980. phenotype.
    188830. gene.
    255960. phenotype.
    610489. phenotype.
    neXtProti NX_P10644.
    Orphaneti 950. Acrodysostosis.
    280651. Acrodysostosis with multiple hormone resistance.
    1359. Carney complex.
    615. Familial atrial myxoma.
    189439. Primary pigmented nodular adrenocortical disease.
    PharmGKBi PA33754.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0664.
    HOGENOMi HOG000196669.
    HOVERGENi HBG002025.
    InParanoidi P10644.
    KOi K04739.
    OMAi FSAEVYT.
    PhylomeDBi P10644.
    TreeFami TF314920.

    Enzyme and pathway databases

    Reactomei REACT_15334. DARPP-32 events.
    REACT_15530. PKA activation.
    REACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
    REACT_1946. PKA activation in glucagon signalling.
    REACT_24023. Regulation of water balance by renal Aquaporins.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinki P10644.

    Miscellaneous databases

    ChiTaRSi PRKAR1A. human.
    GenomeRNAii 5573.
    NextBioi 21602.
    PROi P10644.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P10644.
    Bgeei P10644.
    CleanExi HS_PRKAR1A.
    Genevestigatori P10644.

    Family and domain databases

    Gene3Di 2.60.120.10. 2 hits.
    InterProi IPR002373. cAMP/cGMP_kin.
    IPR012198. 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 ]
    Pfami PF00027. cNMP_binding. 2 hits.
    PF02197. RIIa. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000548. PK_regulatory. 1 hit.
    PRINTSi PR00103. CAMPKINASE.
    SMARTi SM00100. cNMP. 2 hits.
    SM00394. RIIa. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47391. SSF47391. 1 hit.
    SSF51206. SSF51206. 2 hits.
    PROSITEi PS00888. CNMP_BINDING_1. 2 hits.
    PS00889. CNMP_BINDING_2. 2 hits.
    PS50042. CNMP_BINDING_3. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, cDNA structure and deduced amino acid sequence for a type I regulatory subunit of cAMP-dependent protein kinase from human testis."
      Sandberg M., Tasken K., Oeyen O., Hansson V., Jahnsen T.
      Biochem. Biophys. Res. Commun. 149:939-945(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    2. "The two mRNA forms for the type I alpha regulatory subunit of cAMP-dependent protein kinase from human testis are due to the use of different polyadenylation site signals."
      Sandberg M., Skalhegg B., Jahnsen T.
      Biochem. Biophys. Res. Commun. 167:323-330(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    3. "Subtractive hybridization cloning of a tissue-specific extinguisher: TSE1 encodes a regulatory subunit of protein kinase A."
      Jones K.W., Shapero M.H., Chevrette M., Fournier R.E.
      Cell 66:861-872(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "The human gene for the regulatory subunit RI alpha of cyclic adenosine 3', 5'-monophosphate-dependent protein kinase: two distinct promoters provide differential regulation of alternately spliced messenger ribonucleic acids."
      Solberg R., Sandberg M., Natarajan V., Torjesen P.A., Hansson V., Jahnsen T., Tasken K.
      Endocrinology 138:169-181(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Testis.
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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 1).
      Tissue: Lymph and Uterus.
    7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-13, ACETYLATION AT MET-1.
      Tissue: Platelet.
    8. "Mutations of the PRKAR1A gene in Cushing's syndrome due to sporadic primary pigmented nodular adrenocortical disease."
      Groussin L., Jullian E., Perlemoine K., Louvel A., Leheup B., Luton J.P., Bertagna X., Bertherat J.
      J. Clin. Endocrinol. Metab. 87:4324-4329(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN PPNAD1.
    9. "The second subunit of the replication factor C complex (RFC40) and the regulatory subunit (RIalpha) of protein kinase A form a protein complex promoting cell survival."
      Gupte R.S., Weng Y., Liu L., Lee M.Y.
      Cell Cycle 4:323-329(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RFC2.
    10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Smad6 is a protein kinase X phosphorylation substrate and is required for HL-60 cell differentiation."
      Glesne D., Huberman E.
      Oncogene 25:4086-4098(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKX.
    12. "PKA-mediated phosphorylation regulates the function of activation-induced deaminase (AID) in B cells."
      Pasqualucci L., Kitaura Y., Gu H., Dalla-Favera R.
      Proc. Natl. Acad. Sci. U.S.A. 103:395-400(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AICDA.
    13. "Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
      Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
      J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
      Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
      Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    21. "Activity of retinoic acid receptor-alpha is directly regulated at its protein kinase A sites in response to follicle-stimulating hormone signaling."
      Santos N.C., Kim K.H.
      Endocrinology 151:2361-2372(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RARA, FUNCTION.
    22. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    24. Cited for: INVOLVEMENT IN ACRDYS1, MUTAGENESIS OF TYR-373.
    25. Cited for: INTERACTION WITH PJA2.
    26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "An unusual presentation of Carney complex with diffuse primary pigmented nodular adrenocortical disease on one adrenal gland and a nonpigmented adrenocortical adenoma and focal primary pigmented nodular adrenocortical disease on the other."
      Tung S.C., Hwang D.Y., Yang J.W., Chen W.J., Lee C.T.
      Endocr. J. 59:823-830(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN CNC1.
    28. "A small novel A-kinase anchoring protein (AKAP) that localizes specifically protein kinase A-regulatory subunit I (PKA-RI) to the plasma membrane."
      Burgers P.P., Ma Y., Margarucci L., Mackey M., van der Heyden M.A., Ellisman M., Scholten A., Taylor S.S., Heck A.J.
      J. Biol. Chem. 287:43789-43797(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C2ORF88/SMAKAP, SUBCELLULAR LOCATION.
    29. Cited for: INVOLVEMENT IN CNC1.
    30. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. Cited for: VARIANT CNC1 CYS-74.
    33. "In vitro functional studies of naturally occurring pathogenic PRKAR1A mutations that are not subject to nonsense mRNA decay."
      Greene E.L., Horvath A.D., Nesterova M., Giatzakis C., Bossis I., Stratakis C.A.
      Hum. Mutat. 29:633-639(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS CNC1 ASN-9; SER-146; TYR-183; ASP-213 AND TRP-289, CHARACTERIZATION OF VARIANTS CNC1 ASN-9; CYS-74; SER-146; TYR-183; ASP-213 AND TRP-289.
    34. Cited for: VARIANT ACRDYS1 HIS-373.
    35. Cited for: VARIANTS ACRDYS1 THR-327 AND PRO-335.
    36. Cited for: VARIANTS ACRDYS1 ARG-285; GLU-289; VAL-328 AND LEU-335.
    37. "PRKAR1A mutation affecting cAMP-mediated G protein-coupled receptor signaling in a patient with acrodysostosis and hormone resistance."
      Nagasaki K., Iida T., Sato H., Ogawa Y., Kikuchi T., Saitoh A., Ogata T., Fukami M.
      J. Clin. Endocrinol. Metab. 97:E1808-E1813(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ACRDYS1 ALA-239, CHARACTERIZATION OF VARIANT ACRDYS1 ALA-239.
    38. Cited for: VARIANTS ACRDYS1 THR-213 AND CYS-373, VARIANT ASN-227.

    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: October 1, 2014
    This is version 173 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

    External Data

    Dasty 3