ID KAP3_HUMAN Reviewed; 418 AA. AC P31323; A4D0R9; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 3. DT 27-MAR-2024, entry version 210. DE RecName: Full=cAMP-dependent protein kinase type II-beta regulatory subunit; GN Name=PRKAR2B; 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]. RC TISSUE=Testis; RX PubMed=2851102; DOI=10.1210/mend-2-12-1364; RA Levy F.O., Oeyen O., Sandberg M., Tasken K., Eskild W., Hansson V., RA Jahnsen T.; RT "Molecular cloning, complementary deoxyribonucleic acid structure and RT predicted full-length amino acid sequence of the hormone-inducible RT regulatory subunit of 3'-5'-cyclic adenosine monophosphate-dependent RT protein kinase from human testis."; RL Mol. Endocrinol. 2:1364-1373(1988). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12690205; DOI=10.1126/science.1083423; RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., RA Adams M.D., Tsui L.-C.; RT "Human chromosome 7: DNA sequence and biology."; RL Science 300:767-772(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, 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 [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY RP 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 [8] 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 [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; SER-85 AND SER-114, 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-69 AND SER-114, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [12] RP INTERACTION WITH GSKIP, AND COMPLEX FORMATION WITH GSK3B AND GSKIP. RX PubMed=25920809; DOI=10.1016/j.bbamcr.2015.04.013; RA Loh J.K., Lin C.C., Yang M.C., Chou C.H., Chen W.S., Hong M.C., Cho C.L., RA Hsu C.M., Cheng J.T., Chou A.K., Chang C.H., Tseng C.N., Wang C.H., RA Lieu A.S., Howng S.L., Hong Y.R.; RT "GSKIP- and GSK3-mediated anchoring strengthens cAMP/PKA/Drp1 axis RT signaling in the regulation of mitochondrial elongation."; RL Biochim. Biophys. Acta 1853:1796-1807(2015). RN [13] RP INTERACTION WITH PRKACA AND PRKACB. RX PubMed=33058759; DOI=10.1016/j.ajhg.2020.09.005; RA Palencia-Campos A., Aoto P.C., Machal E.M.F., Rivera-Barahona A., RA Soto-Bielicka P., Bertinetti D., Baker B., Vu L., Piceci-Sparascio F., RA Torrente I., Boudin E., Peeters S., Van Hul W., Huber C., Bonneau D., RA Hildebrand M.S., Coleman M., Bahlo M., Bennett M.F., Schneider A.L., RA Scheffer I.E., Kibaek M., Kristiansen B.S., Issa M.Y., Mehrez M.I., RA Ismail S., Tenorio J., Li G., Skaalhegg B.S., Otaify G.A., Temtamy S., RA Aglan M., Joench A.E., De Luca A., Mortier G., Cormier-Daire V., RA Ziegler A., Wallis M., Lapunzina P., Herberg F.W., Taylor S.S., RA Ruiz-Perez V.L.; RT "Germline and Mosaic Variants in PRKACA and PRKACB Cause a Multiple RT Congenital Malformation Syndrome."; RL Am. J. Hum. Genet. 107:977-988(2020). 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 PRKACA and PRKACB (PubMed:33058759). CC Interacts with the phosphorylated form of PJA2. Forms a complex CC composed of PRKAR2B, GSK3B and GSKIP through GSKIP interaction; CC facilitates PKA-induced phosphorylation and regulates GSK3B activity CC (PubMed:25920809). {ECO:0000269|PubMed:21423175, CC ECO:0000269|PubMed:25920809, ECO:0000269|PubMed:33058759}. CC -!- INTERACTION: CC P31323; A0A0S2Z4Y8: AKAP10; NbExp=3; IntAct=EBI-2930670, EBI-16428921; CC P31323; A0A0S2Z551: AKAP10; NbExp=3; IntAct=EBI-2930670, EBI-16431716; CC P31323; Q86UN6: AKAP14; NbExp=7; IntAct=EBI-2930670, EBI-2119626; CC P31323; P24588: AKAP5; NbExp=4; IntAct=EBI-2930670, EBI-703640; CC P31323; O43687-2: AKAP7; NbExp=8; IntAct=EBI-2930670, EBI-10185182; CC P31323; Q9BSF0: C2orf88; NbExp=3; IntAct=EBI-2930670, EBI-744298; CC P31323; Q16610: ECM1; NbExp=3; IntAct=EBI-2930670, EBI-947964; CC P31323; P33176: KIF5B; NbExp=3; IntAct=EBI-2930670, EBI-355878; CC P31323; A0A0S2Z5D3: PAK1IP1; NbExp=3; IntAct=EBI-2930670, EBI-16431731; CC P31323; P17612: PRKACA; NbExp=15; IntAct=EBI-2930670, EBI-476586; CC P31323; Q16514: TAF12; NbExp=3; IntAct=EBI-2930670, EBI-1034238; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21423175}. Cell CC membrane {ECO:0000269|PubMed:21423175}. Note=Colocalizes with PJA2 in CC the cytoplasm and at the cell membrane. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M31158; AAA60099.1; -; mRNA. DR EMBL; AK291441; BAF84130.1; -; mRNA. DR EMBL; CH236947; EAL24395.1; -; Genomic_DNA. DR EMBL; CH471070; EAW83390.1; -; Genomic_DNA. DR CCDS; CCDS5740.1; -. DR PIR; A40915; OKHUR2. DR RefSeq; NP_002727.2; NM_002736.2. DR AlphaFoldDB; P31323; -. DR SMR; P31323; -. DR BioGRID; 111563; 146. DR CORUM; P31323; -. DR DIP; DIP-554N; -. DR IntAct; P31323; 75. DR MINT; P31323; -. DR STRING; 9606.ENSP00000265717; -. DR BindingDB; P31323; -. DR ChEMBL; CHEMBL2270; -. DR DrugBank; DB02527; Cyclic adenosine monophosphate. DR GuidetoPHARMACOLOGY; 1475; -. DR iPTMnet; P31323; -. DR MetOSite; P31323; -. DR PhosphoSitePlus; P31323; -. DR BioMuta; PRKAR2B; -. DR DMDM; 206729918; -. DR OGP; P31323; -. DR EPD; P31323; -. DR jPOST; P31323; -. DR MassIVE; P31323; -. DR MaxQB; P31323; -. DR PaxDb; 9606-ENSP00000265717; -. DR PeptideAtlas; P31323; -. DR ProteomicsDB; 54781; -. DR Pumba; P31323; -. DR Antibodypedia; 1082; 423 antibodies from 35 providers. DR DNASU; 5577; -. DR Ensembl; ENST00000265717.5; ENSP00000265717.4; ENSG00000005249.14. DR GeneID; 5577; -. DR KEGG; hsa:5577; -. DR MANE-Select; ENST00000265717.5; ENSP00000265717.4; NM_002736.3; NP_002727.2. DR UCSC; uc003vdx.4; human. DR AGR; HGNC:9392; -. DR CTD; 5577; -. DR DisGeNET; 5577; -. DR GeneCards; PRKAR2B; -. DR HGNC; HGNC:9392; PRKAR2B. DR HPA; ENSG00000005249; Tissue enhanced (adipose). DR MIM; 176912; gene. DR neXtProt; NX_P31323; -. DR OpenTargets; ENSG00000005249; -. DR PharmGKB; PA33758; -. DR VEuPathDB; HostDB:ENSG00000005249; -. DR eggNOG; KOG1113; Eukaryota. DR GeneTree; ENSGT00940000158160; -. DR HOGENOM; CLU_018310_2_0_1; -. DR InParanoid; P31323; -. DR OMA; GEQGDTF; -. DR OrthoDB; 55978at2759; -. DR PhylomeDB; P31323; -. DR TreeFam; TF314920; -. DR PathwayCommons; P31323; -. 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-2565942; Regulation of PLK1 Activity at G2/M Transition. DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes. DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes. DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome. DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes. 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-5620912; Anchoring of the basal body to the plasma membrane. DR Reactome; R-HSA-8854518; AURKA Activation by TPX2. 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; P31323; -. DR SIGNOR; P31323; -. DR BioGRID-ORCS; 5577; 12 hits in 1171 CRISPR screens. DR ChiTaRS; PRKAR2B; human. DR GeneWiki; PRKAR2B; -. DR GenomeRNAi; 5577; -. DR Pharos; P31323; Tchem. DR PRO; PR:P31323; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P31323; Protein. DR Bgee; ENSG00000005249; Expressed in cortical plate and 101 other cell types or tissues. DR ExpressionAtlas; P31323; baseline and differential. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0043198; C:dendritic shaft; ISS:ParkinsonsUK-UCL. DR GO; GO:0043197; C:dendritic spine; ISS:ParkinsonsUK-UCL. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; 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; IEA:Ensembl. DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:BHF-UCL. DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB. DR GO; GO:0006631; P:fatty acid metabolic process; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; TAS:ProtInc. DR GO; GO:0007612; P:learning; IEA:Ensembl. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:Ensembl. DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IDA:BHF-UCL. DR GO; GO:0097332; P:response to antipsychotic drug; IEA:Ensembl. DR CDD; cd00038; CAP_ED; 2. DR CDD; cd12104; DD_RIIbeta_PKA; 1. DR Gene3D; 1.20.890.10; cAMP-dependent protein kinase regulatory subunit, dimerization-anchoring domain; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 2. DR InterPro; IPR012198; cAMP_dep_PK_reg_su. DR InterPro; IPR003117; cAMP_dep_PK_reg_su_I/II_a/b. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. DR InterPro; IPR014710; RmlC-like_jellyroll. DR PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1. DR PANTHER; PTHR11635:SF156; CAMP-DEPENDENT PROTEIN KINASE TYPE II-BETA REGULATORY SUBUNIT; 1. DR Pfam; PF00027; cNMP_binding; 2. DR Pfam; PF02197; RIIa; 1. DR PIRSF; PIRSF000548; PK_regulatory; 1. DR PRINTS; PR00103; CAMPKINASE. DR SMART; SM00100; cNMP; 2. DR SMART; SM00394; RIIa; 1. DR SUPFAM; SSF51206; cAMP-binding domain-like; 2. DR SUPFAM; SSF47391; Dimerization-anchoring domain of cAMP-dependent PK regulatory subunit; 1. DR PROSITE; PS00888; CNMP_BINDING_1; 2. DR PROSITE; PS00889; CNMP_BINDING_2; 2. DR PROSITE; PS50042; CNMP_BINDING_3; 2. DR Genevisible; P31323; HS. PE 1: Evidence at protein level; KW cAMP; cAMP-binding; Cell membrane; Cytoplasm; Membrane; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..418 FT /note="cAMP-dependent protein kinase type II-beta FT regulatory subunit" FT /id="PRO_0000205390" FT REGION 2..153 FT /note="Dimerization and phosphorylation" FT REGION 48..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 154..275 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT BINDING 223 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT BINDING 232 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT BINDING 276..418 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="2" FT BINDING 352 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="2" FT BINDING 361 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="2" FT MOD_RES 69 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 85 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT VARIANT 335 FT /note="E -> D (in dbSNP:rs3729881)" FT /id="VAR_046549" FT CONFLICT 341..342 FT /note="IA -> MP (in Ref. 1; AAA60099)" FT /evidence="ECO:0000305" SQ SEQUENCE 418 AA; 46302 MW; 83F402CCFFEFD186 CRC64; MSIEIPAGLT ELLQGFTVEV LRHQPADLLE FALQHFTRLQ QENERKGTAR FGHEGRTWGD LGAAAGGGTP SKGVNFAEEP MQSDSEDGEE EEAAPADAGA FNAPVINRFT RRASVCAEAY NPDEEEDDAE SRIIHPKTDD QRNRLQEACK DILLFKNLDP EQMSQVLDAM FEKLVKDGEH VIDQGDDGDN FYVIDRGTFD IYVKCDGVGR CVGNYDNRGS FGELALMYNT PRAATITATS PGALWGLDRV TFRRIIVKNN AKKRKMYESF IESLPFLKSL EFSERLKVVD VIGTKVYNDG EQIIAQGDSA DSFFIVESGE VKITMKRKGK SEVEENGAVE IARCSRGQYF GELALVTNKP RAASAHAIGT VKCLAMDVQA FERLLGPCME IMKRNIATYE EQLVALFGTN MDIVEPTA //