KAP2_HUMAN
ID KAP2_HUMAN Reviewed; 404 AA.
AC P13861; Q16823; Q9BUB1;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=cAMP-dependent protein kinase type II-alpha regulatory subunit;
GN Name=PRKAR2A; Synonyms=PKR2, PRKAR2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=2540040; DOI=10.1016/0014-5793(89)80253-4;
RA Oyen O., Myklebust F., Scott J.D., Hansson V., Jahnsen T.;
RT "Human testis cDNA for the regulatory subunit RII alpha of cAMP-dependent
RT protein kinase encodes an alternate amino-terminal region.";
RL FEBS Lett. 246:57-64(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-87.
RX PubMed=9003463; DOI=10.1016/s0167-4781(96)00152-2;
RA Foss K.B., Solberg R., Simard J., Myklebust F., Hansson V., Jahnsen T.,
RA Tasken K.;
RT "Molecular cloning, upstream sequence and promoter studies of the human
RT gene for the regulatory subunit RII alpha of cAMP-dependent protein
RT kinase.";
RL Biochim. Biophys. Acta 1350:98-108(1997).
RN [7]
RP INTERACTION WITH CBFA2T3.
RX PubMed=11823486; DOI=10.4049/jimmunol.168.4.1590;
RA Schillace R.V., Andrews S.F., Liberty G.A., Davey M.P., Carr D.W.;
RT "Identification and characterization of myeloid translocation gene 16b as a
RT novel a kinase anchoring protein in T lymphocytes.";
RL J. Immunol. 168:1590-1599(2002).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Prostate cancer;
RX PubMed=17487921; DOI=10.1002/elps.200600782;
RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.;
RT "Toward a global characterization of the phosphoproteome in prostate cancer
RT cells: identification of phosphoproteins in the LNCaP cell line.";
RL Electrophoresis 28:2027-2034(2007).
RN [12]
RP INTERACTION WITH MYRIP.
RX PubMed=17827149; DOI=10.1074/jbc.m705167200;
RA Goehring A.S., Pedroja B.S., Hinke S.A., Langeberg L.K., Scott J.D.;
RT "MyRIP anchors protein kinase A to the exocyst complex.";
RL J. Biol. Chem. 282:33155-33167(2007).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-58; SER-78; SER-80
RP AND SER-99, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-99, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78; SER-80 AND SER-99, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48; THR-54; SER-58; SER-78
RP AND SER-80, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [22]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PJA2.
RX PubMed=21423175; DOI=10.1038/ncb2209;
RA Lignitto L., Carlucci A., Sepe M., Stefan E., Cuomo O., Nistico R.,
RA Scorziello A., Savoia C., Garbi C., Annunziato L., Feliciello A.;
RT "Control of PKA stability and signalling by the RING ligase praja2.";
RL Nat. Cell Biol. 13:412-422(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78 AND SER-80, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP INTERACTION WITH ADCY8.
RX PubMed=22976297; DOI=10.1242/jcs.111427;
RA Willoughby D., Halls M.L., Everett K.L., Ciruela A., Skroblin P.,
RA Klussmann E., Cooper D.M.;
RT "A key phosphorylation site in AC8 mediates regulation of Ca(2+)-dependent
RT cAMP dynamics by an AC8-AKAP79-PKA signalling complex.";
RL J. Cell Sci. 125:5850-5859(2012).
RN [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-58; SER-78; SER-80;
RP SER-99 AND SER-395, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-54; SER-58; SER-78; SER-80
RP AND SER-350, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [29]
RP INTERACTION WITH GSKIP, AND COMPLEX FORMATION WITH GSKIP AND GSK3B.
RX PubMed=27484798; DOI=10.1074/jbc.m116.738047;
RA Dema A., Schroeter M.F., Perets E., Skroblin P., Moutty M.C., Deak V.A.,
RA Birchmeier W., Klussmann E.;
RT "The A-Kinase Anchoring Protein (AKAP) Glycogen Synthase Kinase 3beta
RT Interaction Protein (GSKIP) Regulates beta-Catenin through Its Interactions
RT with Both Protein Kinase A (PKA) and GSK3beta.";
RL J. Biol. Chem. 291:19618-19630(2016).
CC -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases
CC involved in cAMP signaling in cells. Type II regulatory chains mediate
CC membrane association by binding to anchoring proteins, including the
CC MAP2 kinase.
CC -!- SUBUNIT: The inactive form of the enzyme is composed of two regulatory
CC chains and two catalytic chains. Activation by cAMP produces two active
CC catalytic monomers and a regulatory dimer that binds four cAMP
CC molecules. Interacts with AKAP4 and CBFA2T3. Interacts with the
CC phosphorylated form of PJA2. Interacts with MYRIP. This interaction may
CC link PKA to components of the exocytosis machinery, thus facilitating
CC exocytosis, including insulin release (By similarity). Forms a complex
CC composed of PRKAR2A, GSK3B and GSKIP through GSKIP interaction;
CC facilitates PKA-induced phosphorylation and regulates GSK3B activity
CC (PubMed:27484798). Interacts with ADCY8; inhibits adenylate cyclase
CC activity through PKA phosphorylation (PubMed:22976297). {ECO:0000250,
CC ECO:0000269|PubMed:22976297, ECO:0000269|PubMed:27484798}.
CC -!- INTERACTION:
CC P13861; Q92667: AKAP1; NbExp=5; IntAct=EBI-2556122, EBI-2119593;
CC P13861; O75969: AKAP3; NbExp=2; IntAct=EBI-2556122, EBI-9033101;
CC P13861; P24588: AKAP5; NbExp=5; IntAct=EBI-2556122, EBI-703640;
CC P13861; O43823: AKAP8; NbExp=3; IntAct=EBI-2556122, EBI-1237481;
CC P13861; P03259-2; Xeno; NbExp=5; IntAct=EBI-2556122, EBI-7225021;
CC P13861-2; Q86UN6: AKAP14; NbExp=3; IntAct=EBI-11752137, EBI-2119626;
CC P13861-2; O43687-2: AKAP7; NbExp=5; IntAct=EBI-11752137, EBI-10185182;
CC P13861-2; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-11752137, EBI-473196;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell
CC membrane {ECO:0000269|PubMed:21423175}. Note=Colocalizes with PJA2 in
CC the cytoplasm and the cell membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P13861-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P13861-2; Sequence=VSP_056821;
CC -!- TISSUE SPECIFICITY: Four types of regulatory chains are found: I-alpha,
CC I-beta, II-alpha, and II-beta. Their expression varies among tissues
CC and is in some cases constitutive and in others inducible.
CC -!- PTM: Phosphorylated by the activated catalytic chain.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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DR EMBL; X14968; CAA33094.1; -; mRNA.
DR EMBL; BT007225; AAP35889.1; -; mRNA.
DR EMBL; AC141002; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC144546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471055; EAW64926.1; -; Genomic_DNA.
DR EMBL; CH471055; EAW64927.1; -; Genomic_DNA.
DR EMBL; BC002763; AAH02763.1; -; mRNA.
DR EMBL; X99455; CAA67817.1; -; Genomic_DNA.
DR CCDS; CCDS2778.1; -. [P13861-1]
DR CCDS; CCDS82771.1; -. [P13861-2]
DR PIR; S03885; OKHU2R.
DR RefSeq; NP_001308911.1; NM_001321982.1. [P13861-1]
DR RefSeq; NP_001308912.1; NM_001321983.1. [P13861-2]
DR RefSeq; NP_004148.1; NM_004157.3. [P13861-1]
DR RefSeq; XP_011532244.1; XM_011533942.2. [P13861-1]
DR RefSeq; XP_016862304.1; XM_017006815.1.
DR PDB; 2IZX; X-ray; 1.30 A; A/B=4-44.
DR PDB; 2KYG; NMR; -; A/B=1-45.
DR PDB; 4ZP3; X-ray; 2.63 A; A/B/C/D/E/F/G/H/I/J/K/L=2-44.
DR PDB; 5H78; X-ray; 2.00 A; A/B=5-49.
DR PDB; 5XBY; X-ray; 3.25 A; A/B/C/D=5-44.
DR PDBsum; 2IZX; -.
DR PDBsum; 2KYG; -.
DR PDBsum; 4ZP3; -.
DR PDBsum; 5H78; -.
DR PDBsum; 5XBY; -.
DR AlphaFoldDB; P13861; -.
DR BMRB; P13861; -.
DR SMR; P13861; -.
DR BioGRID; 111562; 146.
DR CORUM; P13861; -.
DR DIP; DIP-552N; -.
DR IntAct; P13861; 97.
DR MINT; P13861; -.
DR STRING; 9606.ENSP00000265563; -.
DR BindingDB; P13861; -.
DR ChEMBL; CHEMBL2221; -.
DR DrugBank; DB05798; GEM-231.
DR GuidetoPHARMACOLOGY; 1474; -.
DR GlyGen; P13861; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P13861; -.
DR PhosphoSitePlus; P13861; -.
DR SwissPalm; P13861; -.
DR BioMuta; PRKAR2A; -.
DR DMDM; 125198; -.
DR OGP; P13861; -.
DR EPD; P13861; -.
DR jPOST; P13861; -.
DR MassIVE; P13861; -.
DR MaxQB; P13861; -.
DR PaxDb; P13861; -.
DR PeptideAtlas; P13861; -.
DR PRIDE; P13861; -.
DR ProteomicsDB; 52996; -. [P13861-1]
DR ProteomicsDB; 79069; -.
DR Antibodypedia; 3555; 484 antibodies from 35 providers.
DR DNASU; 5576; -.
DR Ensembl; ENST00000265563.13; ENSP00000265563.8; ENSG00000114302.16. [P13861-1]
DR Ensembl; ENST00000296446.12; ENSP00000296446.8; ENSG00000114302.16. [P13861-2]
DR Ensembl; ENST00000454963.5; ENSP00000394041.1; ENSG00000114302.16. [P13861-1]
DR GeneID; 5576; -.
DR KEGG; hsa:5576; -.
DR MANE-Select; ENST00000265563.13; ENSP00000265563.8; NM_004157.4; NP_004148.1.
DR UCSC; uc003cux.2; human. [P13861-1]
DR CTD; 5576; -.
DR DisGeNET; 5576; -.
DR GeneCards; PRKAR2A; -.
DR HGNC; HGNC:9391; PRKAR2A.
DR HPA; ENSG00000114302; Tissue enhanced (skeletal muscle, testis).
DR MIM; 176910; gene.
DR neXtProt; NX_P13861; -.
DR OpenTargets; ENSG00000114302; -.
DR PharmGKB; PA33757; -.
DR VEuPathDB; HostDB:ENSG00000114302; -.
DR eggNOG; KOG1113; Eukaryota.
DR GeneTree; ENSGT00940000154836; -.
DR HOGENOM; CLU_018310_2_0_1; -.
DR InParanoid; P13861; -.
DR OMA; REAVSHN; -.
DR PhylomeDB; P13861; -.
DR TreeFam; TF314920; -.
DR PathwayCommons; P13861; -.
DR Reactome; R-HSA-163615; PKA activation.
DR Reactome; R-HSA-164378; PKA activation in glucagon signalling.
DR Reactome; R-HSA-180024; DARPP-32 events.
DR Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR Reactome; R-HSA-432040; Vasopressin regulates renal water homeostasis via Aquaporins.
DR Reactome; R-HSA-442720; CREB1 phosphorylation through the activation of Adenylate Cyclase.
DR Reactome; R-HSA-5610787; Hedgehog 'off' state.
DR Reactome; R-HSA-9010642; ROBO receptors bind AKAP5.
DR Reactome; R-HSA-9634597; GPER1 signaling.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR Reactome; R-HSA-983231; Factors involved in megakaryocyte development and platelet production.
DR SignaLink; P13861; -.
DR SIGNOR; P13861; -.
DR BioGRID-ORCS; 5576; 42 hits in 1088 CRISPR screens.
DR ChiTaRS; PRKAR2A; human.
DR EvolutionaryTrace; P13861; -.
DR GeneWiki; PRKAR2A; -.
DR GenomeRNAi; 5576; -.
DR Pharos; P13861; Tchem.
DR PRO; PR:P13861; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P13861; protein.
DR Bgee; ENSG00000114302; Expressed in buccal mucosa cell and 205 other tissues.
DR ExpressionAtlas; P13861; baseline and differential.
DR Genevisible; P13861; HS.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0097546; C:ciliary base; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0031588; C:nucleotide-activated protein kinase complex; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0030552; F:cAMP binding; IBA:GO_Central.
DR GO; GO:0004862; F:cAMP-dependent protein kinase inhibitor activity; IDA:BHF-UCL.
DR GO; GO:0008603; F:cAMP-dependent protein kinase regulator activity; IDA:BHF-UCL.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc.
DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IDA:BHF-UCL.
DR CDD; cd00038; CAP_ED; 2.
DR DisProt; DP02333; -.
DR Gene3D; 2.60.120.10; -; 2.
DR IDEAL; IID00411; -.
DR InterPro; IPR012198; cAMP_dep_PK_reg_su.
DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR Pfam; PF00027; cNMP_binding; 2.
DR Pfam; PF02197; RIIa; 1.
DR PIRSF; PIRSF000548; PK_regulatory; 1.
DR SMART; SM00100; cNMP; 2.
DR SMART; SM00394; RIIa; 1.
DR SUPFAM; SSF51206; SSF51206; 2.
DR PROSITE; PS00888; CNMP_BINDING_1; 2.
DR PROSITE; PS00889; CNMP_BINDING_2; 2.
DR PROSITE; PS50042; CNMP_BINDING_3; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; cAMP; cAMP-binding;
KW Cell membrane; Cytoplasm; Membrane; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..404
FT /note="cAMP-dependent protein kinase type II-alpha
FT regulatory subunit"
FT /id="PRO_0000205385"
FT REGION 2..138
FT /note="Dimerization and phosphorylation"
FT REGION 47..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139..260
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 208
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 217
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT BINDING 261..404
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 338
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT BINDING 347
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 54
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 99
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 215
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P00515"
FT MOD_RES 350
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 292..313
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_056821"
FT HELIX 10..24
FT /evidence="ECO:0007829|PDB:2IZX"
FT HELIX 29..43
FT /evidence="ECO:0007829|PDB:2IZX"
SQ SEQUENCE 404 AA; 45518 MW; C7D6E8E476E1DB65 CRC64;
MSHIQIPPGL TELLQGYTVE VLRQQPPDLV EFAVEYFTRL REARAPASVL PAATPRQSLG
HPPPEPGPDR VADAKGDSES EEDEDLEVPV PSRFNRRVSV CAETYNPDEE EEDTDPRVIH
PKTDEQRCRL QEACKDILLF KNLDQEQLSQ VLDAMFERIV KADEHVIDQG DDGDNFYVIE
RGTYDILVTK DNQTRSVGQY DNRGSFGELA LMYNTPRAAT IVATSEGSLW GLDRVTFRRI
IVKNNAKKRK MFESFIESVP LLKSLEVSER MKIVDVIGEK IYKDGERIIT QGEKADSFYI
IESGEVSILI RSRTKSNKDG GNQEVEIARC HKGQYFGELA LVTNKPRAAS AYAVGDVKCL
VMDVQAFERL LGPCMDIMKR NISHYEEQLV KMFGSSVDLG NLGQ
