ID KAP1_HUMAN Reviewed; 381 AA. AC P31321; Q8N422; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 4. DT 24-JAN-2024, entry version 209. DE RecName: Full=cAMP-dependent protein kinase type I-beta regulatory subunit; GN Name=PRKAR1B; 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], AND CLEAVAGE OF INITIATOR METHIONINE. RX PubMed=1708242; DOI=10.1016/0006-291x(91)90904-l; RA Solberg R., Tasken K., Keiserud A., Jahnsen T.; RT "Molecular cloning, cDNA structure and tissue-specific expression of the RT human regulatory subunit RI beta of cAMP-dependent protein kinases."; RL Biochem. Biophys. Res. Commun. 176:166-172(1991). RN [2] RP SEQUENCE REVISION TO 98-100. RC TISSUE=Testis; RX PubMed=7925653; DOI=10.1006/excr.1994.1297; RA Solberg R., Tasken K., Wen W., Coghlan V.M., Meinkoth J.L., Scott J.D., RA Jahnsen T., Taylor S.S.; RT "Human regulatory subunit RI beta of cAMP-dependent protein kinases: RT expression, holoenzyme formation and microinjection into living cells."; RL Exp. Cell Res. 214:595-605(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Amygdala, and 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain, and Cervix; 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 [5] RP NITRATION [LARGE SCALE ANALYSIS] AT TYR-21, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Pituitary adenoma; RX PubMed=16777052; DOI=10.1016/j.ab.2006.05.024; RA Zhan X., Desiderio D.M.; RT "Nitroproteins from a human pituitary adenoma tissue discovered with a RT nitrotyrosine affinity column and tandem mass spectrometry."; RL Anal. Biochem. 354:279-289(2006). RN [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77 AND SER-83, AND RP 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, 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 [9] RP FUNCTION, AND INTERACTION WITH PRKX. RX PubMed=20819953; DOI=10.1074/jbc.m110.155150; RA Diskar M., Zenn H.M., Kaupisch A., Kaufholz M., Brockmeyer S., Sohmen D., RA Berrera M., Zaccolo M., Boshart M., Herberg F.W., Prinz A.; RT "Regulation of cAMP-dependent protein kinases: the human protein kinase X RT (PrKX) reveals the role of the catalytic subunit alphaH-alphaI loop."; RL J. Biol. Chem. 285:35910-35918(2010). RN [10] RP INTERACTION WITH C2ORF88/SMAKAP, AND SUBCELLULAR LOCATION. RX PubMed=23115245; DOI=10.1074/jbc.m112.395970; RA Burgers P.P., Ma Y., Margarucci L., Mackey M., van der Heyden M.A., RA Ellisman M., Scholten A., Taylor S.S., Heck A.J.; RT "A small novel A-kinase anchoring protein (AKAP) that localizes RT specifically protein kinase A-regulatory subunit I (PKA-RI) to the plasma RT membrane."; RL J. Biol. Chem. 287:43789-43797(2012). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-83, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE 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 [13] RP INVOLVEMENT IN MASNS, DEVELOPMENTAL STAGE, VARIANTS MASNS LEU-167; LYS-196 RP AND TRP-335, AND CHARACTERIZATION OF VARIANTS MASNS LEU-167; LYS-196 AND RP TRP-335. RX PubMed=33833410; DOI=10.1038/s41436-021-01152-7; RA Marbach F., Stoyanov G., Erger F., Stratakis C.A., Settas N., London E., RA Rosenfeld J.A., Torti E., Haldeman-Englert C., Sklirou E., Kessler E., RA Ceulemans S., Nelson S.F., Martinez-Agosto J.A., Palmer C.G.S., RA Signer R.H., Andrews M.V., Grange D.K., Willaert R., Person R., RA Telegrafi A., Sievers A., Laugsch M., Theiss S., Cheng Y., Lichtarge O., RA Katsonis P., Stocco A., Schaaf C.P.; RT "Variants in PRKAR1B cause a neurodevelopmental disorder with autism RT spectrum disorder, apraxia, and insensitivity to pain."; RL Genet. Med. 23:1465-1473(2021). CC -!- FUNCTION: Regulatory subunit of the cAMP-dependent protein kinases CC involved in cAMP signaling in cells. {ECO:0000269|PubMed:20819953}. CC -!- SUBUNIT: The inactive holoenzyme is composed of two regulatory chains CC and two catalytic chains. Activation by cAMP releases the two active CC catalytic monomers and the regulatory dimer. Interacts with PRKX; CC regulates this cAMP-dependent protein kinase. Interacts with CC C2orf88/smAKAP; this interaction may target PRKAR1B to the plasma CC membrane. {ECO:0000269|PubMed:20819953, ECO:0000269|PubMed:23115245}. CC -!- INTERACTION: CC P31321; Q86UN6: AKAP14; NbExp=3; IntAct=EBI-2805516, EBI-2119626; CC P31321; O43687-2: AKAP7; NbExp=5; IntAct=EBI-2805516, EBI-10185182; CC P31321; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-2805516, EBI-11954519; CC P31321; O95817: BAG3; NbExp=3; IntAct=EBI-2805516, EBI-747185; CC P31321; P46379-2: BAG6; NbExp=3; IntAct=EBI-2805516, EBI-10988864; CC P31321; Q8IYS8: BOD1L2; NbExp=3; IntAct=EBI-2805516, EBI-12118438; CC P31321; Q5T5Y3-3: CAMSAP1; NbExp=6; IntAct=EBI-2805516, EBI-12036363; CC P31321; Q9HC52: CBX8; NbExp=3; IntAct=EBI-2805516, EBI-712912; CC P31321; Q8IW40: CCDC103; NbExp=5; IntAct=EBI-2805516, EBI-10261970; CC P31321; Q16543: CDC37; NbExp=3; IntAct=EBI-2805516, EBI-295634; CC P31321; P38936: CDKN1A; NbExp=3; IntAct=EBI-2805516, EBI-375077; CC P31321; Q96LK0: CEP19; NbExp=5; IntAct=EBI-2805516, EBI-741885; CC P31321; P10606: COX5B; NbExp=5; IntAct=EBI-2805516, EBI-1053725; CC P31321; Q9UI36-2: DACH1; NbExp=3; IntAct=EBI-2805516, EBI-10186082; CC P31321; O60941-5: DTNB; NbExp=3; IntAct=EBI-2805516, EBI-11984733; CC P31321; Q96G04: EEF2KMT; NbExp=3; IntAct=EBI-2805516, EBI-747840; CC P31321; Q3B820: FAM161A; NbExp=3; IntAct=EBI-2805516, EBI-719941; CC P31321; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-2805516, EBI-6658203; CC P31321; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-2805516, EBI-11958845; CC P31321; Q8NHY3: GAS2L2; NbExp=3; IntAct=EBI-2805516, EBI-7960826; CC P31321; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-2805516, EBI-7251368; CC P31321; Q9NVN8: GNL3L; NbExp=3; IntAct=EBI-2805516, EBI-746682; CC P31321; Q92805: GOLGA1; NbExp=3; IntAct=EBI-2805516, EBI-6164177; CC P31321; Q92917: GPKOW; NbExp=3; IntAct=EBI-2805516, EBI-746309; CC P31321; P43080: GUCA1A; NbExp=3; IntAct=EBI-2805516, EBI-6873005; CC P31321; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-2805516, EBI-14103818; CC P31321; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-2805516, EBI-11955401; CC P31321; Q15735: INPP5J; NbExp=3; IntAct=EBI-2805516, EBI-10236940; CC P31321; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-2805516, EBI-2556193; CC P31321; P33176: KIF5B; NbExp=3; IntAct=EBI-2805516, EBI-355878; CC P31321; Q969R5: L3MBTL2; NbExp=3; IntAct=EBI-2805516, EBI-739909; CC P31321; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-2805516, EBI-726510; CC P31321; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-2805516, EBI-739832; CC P31321; O95983-2: MBD3; NbExp=3; IntAct=EBI-2805516, EBI-11978579; CC P31321; Q96G25-2: MED8; NbExp=3; IntAct=EBI-2805516, EBI-10286267; CC P31321; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-2805516, EBI-14086479; CC P31321; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-2805516, EBI-741158; CC P31321; Q9UBU9: NXF1; NbExp=3; IntAct=EBI-2805516, EBI-398874; CC P31321; Q92569: PIK3R3; NbExp=3; IntAct=EBI-2805516, EBI-79893; CC P31321; Q9NR33: POLE4; NbExp=3; IntAct=EBI-2805516, EBI-867034; CC P31321; P54646: PRKAA2; NbExp=3; IntAct=EBI-2805516, EBI-1383852; CC P31321; P17612: PRKACA; NbExp=8; IntAct=EBI-2805516, EBI-476586; CC P31321; P10644: PRKAR1A; NbExp=6; IntAct=EBI-2805516, EBI-476431; CC P31321; Q99633: PRPF18; NbExp=3; IntAct=EBI-2805516, EBI-2798416; CC P31321; O95456: PSMG1; NbExp=3; IntAct=EBI-2805516, EBI-6286129; CC P31321; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-2805516, EBI-2798044; CC P31321; P13631: RARG; NbExp=5; IntAct=EBI-2805516, EBI-2568901; CC P31321; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-2805516, EBI-11984663; CC P31321; Q9UHR5: SAP30BP; NbExp=3; IntAct=EBI-2805516, EBI-751683; CC P31321; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-2805516, EBI-747035; CC P31321; Q92529: SHC3; NbExp=3; IntAct=EBI-2805516, EBI-79084; CC P31321; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-2805516, EBI-2872322; CC P31321; Q13573: SNW1; NbExp=3; IntAct=EBI-2805516, EBI-632715; CC P31321; O75716: STK16; NbExp=3; IntAct=EBI-2805516, EBI-749295; CC P31321; Q96C24: SYTL4; NbExp=3; IntAct=EBI-2805516, EBI-747142; CC P31321; Q5VWN6: TASOR2; NbExp=3; IntAct=EBI-2805516, EBI-745958; CC P31321; Q15561: TEAD4; NbExp=3; IntAct=EBI-2805516, EBI-747736; CC P31321; P10827: THRA; NbExp=5; IntAct=EBI-2805516, EBI-286285; CC P31321; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-2805516, EBI-10241197; CC P31321; Q9BZF9: UACA; NbExp=3; IntAct=EBI-2805516, EBI-350510; CC P31321; Q14119: VEZF1; NbExp=3; IntAct=EBI-2805516, EBI-11980193; CC P31321; Q05516: ZBTB16; NbExp=3; IntAct=EBI-2805516, EBI-711925; CC P31321; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-2805516, EBI-746595; CC P31321; Q13360-2: ZNF177; NbExp=3; IntAct=EBI-2805516, EBI-12272076; CC P31321; Q86UD4: ZNF329; NbExp=3; IntAct=EBI-2805516, EBI-7233259; CC P31321; P13682: ZNF35; NbExp=3; IntAct=EBI-2805516, EBI-11041653; CC P31321; Q86VK4-3: ZNF410; NbExp=3; IntAct=EBI-2805516, EBI-11741890; CC P31321; P36508: ZNF76; NbExp=3; IntAct=EBI-2805516, EBI-7254550; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23115245}. 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 -!- DEVELOPMENTAL STAGE: Expressed at high levels in the pituitary, CC diencephalon, mesencephalon, and hypothalamus in embryos at Carnegie CC stage 22. {ECO:0000269|PubMed:33833410}. CC -!- PTM: The pseudophosphorylation site binds to the substrate-binding CC region of the catalytic chain, resulting in the inhibition of its CC activity. CC -!- DISEASE: Marbach-Schaaf neurodevelopmental syndrome (MASNS) CC [MIM:619680]: An autosomal dominant neurodevelopmental disorder CC characterized by global developmental delay, speech delay, behavioral CC abnormalities, hypotonia, and movement disorders including dyspraxia, CC apraxia, and clumsiness. More variable features include high pain CC tolerance, sleep disturbances, and variable non-specific dysmorphic CC features. {ECO:0000269|PubMed:33833410}. Note=The disease is caused by CC variants affecting the gene represented in this entry. 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; M65066; AAC37564.1; -; mRNA. DR EMBL; AK315951; BAH14322.1; -; mRNA. DR EMBL; AK315990; BAH14361.1; -; mRNA. DR EMBL; BC026734; AAH26734.1; -; mRNA. DR EMBL; BC036828; AAH36828.2; -; mRNA. DR CCDS; CCDS34579.1; -. DR PIR; JH0392; OKHUR1. DR RefSeq; NP_001158230.1; NM_001164758.1. DR RefSeq; NP_001158231.1; NM_001164759.1. DR RefSeq; NP_001158232.1; NM_001164760.1. DR RefSeq; NP_001158233.1; NM_001164761.1. DR RefSeq; NP_001158234.1; NM_001164762.1. DR RefSeq; NP_002726.1; NM_002735.2. DR PDB; 4DIN; X-ray; 3.70 A; B=1-381. DR PDB; 4F9K; X-ray; 2.80 A; A/B/C/D=11-73. DR PDBsum; 4DIN; -. DR PDBsum; 4F9K; -. DR AlphaFoldDB; P31321; -. DR SMR; P31321; -. DR BioGRID; 111561; 170. DR IntAct; P31321; 101. DR MINT; P31321; -. DR STRING; 9606.ENSP00000385749; -. DR ChEMBL; CHEMBL2320; -. DR GuidetoPHARMACOLOGY; 1473; -. DR GlyGen; P31321; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P31321; -. DR PhosphoSitePlus; P31321; -. DR BioMuta; PRKAR1B; -. DR DMDM; 229463042; -. DR EPD; P31321; -. DR jPOST; P31321; -. DR MassIVE; P31321; -. DR MaxQB; P31321; -. DR PaxDb; 9606-ENSP00000385749; -. DR PeptideAtlas; P31321; -. DR ProteomicsDB; 54780; -. DR Pumba; P31321; -. DR Antibodypedia; 10769; 400 antibodies from 32 providers. DR DNASU; 5575; -. DR Ensembl; ENST00000360274.8; ENSP00000353415.4; ENSG00000188191.16. DR Ensembl; ENST00000403562.5; ENSP00000385349.1; ENSG00000188191.16. DR Ensembl; ENST00000406797.5; ENSP00000385749.1; ENSG00000188191.16. DR Ensembl; ENST00000537384.6; ENSP00000440449.1; ENSG00000188191.16. DR Ensembl; ENST00000544935.5; ENSP00000444487.1; ENSG00000188191.16. DR GeneID; 5575; -. DR KEGG; hsa:5575; -. DR MANE-Select; ENST00000537384.6; ENSP00000440449.1; NM_001164760.2; NP_001158232.1. DR UCSC; uc003siu.3; human. DR AGR; HGNC:9390; -. DR CTD; 5575; -. DR DisGeNET; 5575; -. DR GeneCards; PRKAR1B; -. DR HGNC; HGNC:9390; PRKAR1B. DR HPA; ENSG00000188191; Tissue enriched (brain). DR MalaCards; PRKAR1B; -. DR MIM; 176911; gene. DR MIM; 619680; phenotype. DR neXtProt; NX_P31321; -. DR OpenTargets; ENSG00000188191; -. DR Orphanet; 412066; PRKAR1B-related neurodegenerative dementia with intermediate filaments. DR PharmGKB; PA33756; -. DR VEuPathDB; HostDB:ENSG00000188191; -. DR eggNOG; KOG1113; Eukaryota. DR GeneTree; ENSGT00940000157513; -. DR HOGENOM; CLU_018310_1_1_1; -. DR InParanoid; P31321; -. DR OMA; QILAWQK; -. DR OrthoDB; 55978at2759; -. DR PhylomeDB; P31321; -. DR TreeFam; TF314920; -. DR PathwayCommons; P31321; -. 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-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; P31321; -. DR SIGNOR; P31321; -. DR BioGRID-ORCS; 5575; 21 hits in 1158 CRISPR screens. DR ChiTaRS; PRKAR1B; human. DR GeneWiki; PRKAR1B; -. DR GenomeRNAi; 5575; -. DR Pharos; P31321; Tbio. DR PRO; PR:P31321; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; P31321; Protein. DR Bgee; ENSG00000188191; Expressed in Brodmann (1909) area 10 and 164 other cell types or tissues. DR ExpressionAtlas; P31321; baseline and differential. DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; NAS:UniProtKB. DR GO; GO:0097546; C:ciliary base; TAS:Reactome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IEA:Ensembl. DR GO; GO:0005771; C:multivesicular body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098794; C:postsynapse; IEA:Ensembl. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW. 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:0034236; F:protein kinase A catalytic subunit binding; IPI:BHF-UCL. DR GO; GO:0007611; P:learning or memory; IEA:Ensembl. DR GO; GO:2000480; P:negative regulation of cAMP-dependent protein kinase activity; IDA:BHF-UCL. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IEA:Ensembl. DR GO; GO:1903367; P:positive regulation of fear response; IEA:Ensembl. DR GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; NAS:UniProtKB. DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IEA:Ensembl. DR CDD; cd00038; CAP_ED; 2. DR CDD; cd12102; DD_RIbeta_PKA; 1. DR DisProt; DP02632; -. 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; IPR042818; RIbeta_DD. DR InterPro; IPR014710; RmlC-like_jellyroll. DR PANTHER; PTHR11635; CAMP-DEPENDENT PROTEIN KINASE REGULATORY CHAIN; 1. DR PANTHER; PTHR11635:SF126; CAMP-DEPENDENT PROTEIN KINASE TYPE I-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; P31321; HS. PE 1: Evidence at protein level; KW 3D-structure; cAMP; cAMP-binding; Cell membrane; Disease variant; KW Disulfide bond; Intellectual disability; Membrane; Methylation; Nitration; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:1708242" FT CHAIN 2..381 FT /note="cAMP-dependent protein kinase type I-beta regulatory FT subunit" FT /id="PRO_0000205381" FT REGION 2..136 FT /note="Dimerization and phosphorylation" FT REGION 67..98 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 96..100 FT /note="Pseudophosphorylation motif" FT COMPBIAS 67..82 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 137..254 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT BINDING 202 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT BINDING 211 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT BINDING 255..381 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="2" FT BINDING 326 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="2" FT BINDING 335 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="2" FT MOD_RES 3 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 21 FT /note="3'-nitrotyrosine" FT /evidence="ECO:0007744|PubMed:16777052" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 83 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 85 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:P12849" FT MOD_RES 97 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:P12849" FT DISULFID 18 FT /note="Interchain (with C-39)" FT /evidence="ECO:0000250" FT DISULFID 39 FT /note="Interchain (with C-18)" FT /evidence="ECO:0000250" FT VARIANT 167 FT /note="Q -> L (in MASNS; uncertain significance; decreased FT basal PKA enzymatic activity in lysates from transfected FT cells; requires 2 nucleotide substitutions)" FT /evidence="ECO:0000269|PubMed:33833410" FT /id="VAR_086687" FT VARIANT 196 FT /note="E -> K (in MASNS; decreased basal PKA enzymatic FT activity in lysates from transfected cells)" FT /evidence="ECO:0000269|PubMed:33833410" FT /id="VAR_086688" FT VARIANT 335 FT /note="R -> W (in MASNS; decreased basal PKA enzymatic FT activity in lysates from transfected cells)" FT /evidence="ECO:0000269|PubMed:33833410" FT /id="VAR_086689" FT CONFLICT 270 FT /note="A -> R (in Ref. 1; AAC37564)" FT /evidence="ECO:0000305" FT HELIX 19..24 FT /evidence="ECO:0007829|PDB:4F9K" FT TURN 27..31 FT /evidence="ECO:0007829|PDB:4F9K" FT HELIX 32..41 FT /evidence="ECO:0007829|PDB:4F9K" FT HELIX 46..68 FT /evidence="ECO:0007829|PDB:4F9K" SQ SEQUENCE 381 AA; 43073 MW; 1ED7BFEC30897191 CRC64; MASPPACPSE EDESLKGCEL YVQLHGIQQV LKDCIVHLCI SKPERPMKFL REHFEKLEKE ENRQILARQK SNSQSDSHDE EVSPTPPNPV VKARRRRGGV SAEVYTEEDA VSYVRKVIPK DYKTMTALAK AISKNVLFAH LDDNERSDIF DAMFPVTHIA GETVIQQGNE GDNFYVVDQG EVDVYVNGEW VTNISEGGSF GELALIYGTP RAATVKAKTD LKLWGIDRDS YRRILMGSTL RKRKMYEEFL SKVSILESLE KWERLTVADA LEPVQFEDGE KIVVQGEPGD DFYIITEGTA SVLQRRSPNE EYVEVGRLGP SDYFGEIALL LNRPRAATVV ARGPLKCVKL DRPRFERVLG PCSEILKRNI QRYNSFISLT V //