KAP1_HUMAN
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 03-AUG-2022, entry version 201.
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).
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 -!- PTM: The pseudophosphorylation site binds to the substrate-binding
CC region of the catalytic chain, resulting in the inhibition of its
CC activity.
CC -!- SIMILARITY: Belongs to the cAMP-dependent kinase regulatory chain
CC family. {ECO:0000305}.
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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; 167.
DR IntAct; P31321; 101.
DR MINT; P31321; -.
DR STRING; 9606.ENSP00000385749; -.
DR ChEMBL; CHEMBL2320; -.
DR GuidetoPHARMACOLOGY; 1473; -.
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; P31321; -.
DR PeptideAtlas; P31321; -.
DR PRIDE; P31321; -.
DR ProteomicsDB; 54780; -.
DR Antibodypedia; 10769; 367 antibodies from 32 providers.
DR DNASU; 5575; -.
DR Ensembl; ENST00000360274.8; ENSP00000353415.4; ENSG00000188191.15.
DR Ensembl; ENST00000403562.5; ENSP00000385349.1; ENSG00000188191.15.
DR Ensembl; ENST00000406797.5; ENSP00000385749.1; ENSG00000188191.15.
DR Ensembl; ENST00000537384.6; ENSP00000440449.1; ENSG00000188191.15.
DR Ensembl; ENST00000544935.5; ENSP00000444487.1; ENSG00000188191.15.
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 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 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; LYVQKHC; -.
DR OrthoDB; 1047290at2759; -.
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 1080 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 162 other tissues.
DR ExpressionAtlas; P31321; baseline and differential.
DR Genevisible; P31321; HS.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; IBA:GO_Central.
DR GO; GO:0097546; C:ciliary base; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
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: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:1904058; P:positive regulation of sensory perception of pain; 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; 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; IPR042818; RIbeta_DD.
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; cAMP; cAMP-binding; Cell membrane; Disulfide bond; Membrane;
KW Methylation; Nitration; Nucleotide-binding; Phosphoprotein;
KW 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 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
