KAP3_HUMAN
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 03-AUG-2022, entry version 201.
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}.
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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; 139.
DR CORUM; P31323; -.
DR DIP; DIP-554N; -.
DR IntAct; P31323; 73.
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; P31323; -.
DR PeptideAtlas; P31323; -.
DR PRIDE; P31323; -.
DR ProteomicsDB; 54781; -.
DR Antibodypedia; 1082; 391 antibodies from 35 providers.
DR DNASU; 5577; -.
DR Ensembl; ENST00000265717.5; ENSP00000265717.4; ENSG00000005249.13.
DR Ensembl; ENST00000639737.2; ENSP00000491687.1; ENSG00000284096.2.
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 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; YDNWSPP; -.
DR OrthoDB; 1047290at2759; -.
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; 11 hits in 1091 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 99 other tissues.
DR ExpressionAtlas; P31323; baseline and differential.
DR Genevisible; P31323; HS.
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; TAS:Reactome.
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:0045121; C:membrane raft; 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 GO; GO:0097338; P:response to clozapine; IEA:Ensembl.
DR CDD; cd00038; CAP_ED; 2.
DR Gene3D; 2.60.120.10; -; 2.
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 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
