RBCC

Full text data of PRKACB

PRKACB [Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
cAMP-dependent protein kinase catalytic subunit beta; PKA C-beta; 2.7.11.11

UniProt P22694
ID KAPCB_HUMAN Reviewed; 351 AA.
AC P22694; B1APG4; B4DKB0; B4E2Q1; Q14VH1; Q59GC0; Q5BNE9; Q5BNF0;
read moreAC Q5BNF1; Q5BNF2; Q5BNF3; Q5CZ92; Q5T1K3; Q7Z3M1; Q8IYR5; Q8IZQ0;
AC Q96B09;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 153.
DE RecName: Full=cAMP-dependent protein kinase catalytic subunit beta;
DE Short=PKA C-beta;
DE EC=2.7.11.11;
GN Name=PRKACB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=2342480;
RA Beebe S.J., Oyen O., Sandberg M., Froysa A., Hansson V., Jahnsen T.;
RT "Molecular cloning of a tissue-specific protein kinase (C gamma) from
RT human testis -- representing a third isoform for the catalytic subunit
RT of cAMP-dependent protein kinase.";
RL Mol. Endocrinol. 4:465-475(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 7).
RC TISSUE=Retina, and Salivary gland;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 9 AND 10).
RC TISSUE=Brain, Thalamus, and Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 8).
RC TISSUE=Brain;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-30 (ISOFORMS 2; 5 AND 6), NUCLEOTIDE
RP SEQUENCE [MRNA] OF 1-16 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-13 (ISOFORM 4), AND TISSUE SPECIFICITY.
RX PubMed=11589697; DOI=10.1046/j.0014-2956.2001.02429.x;
RA Orstavik S., Reinton N., Frengen E., Langeland B.T., Jahnsen T.,
RA Skalhegg B.S.;
RT "Identification of novel splice variants of the human catalytic
RT subunit Cbeta of cAMP-dependent protein kinase.";
RL Eur. J. Biochem. 268:5066-5073(2001).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-15 (ISOFORM 1), AND FUNCTION.
RX PubMed=12420224; DOI=10.1038/sj.onc.1205986;
RA Wu K.-J., Mattioli M., Morse H.C., Dalla-Favera R.;
RT "c-MYC activates protein kinase A (PKA) by direct transcriptional
RT activation of the PKA catalytic subunit beta (PKA-CB) gene.";
RL Oncogene 21:7872-7882(2002).
RN [11]
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 [12]
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.,
RA Buerckstuemmer T., 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 [13]
RP FUNCTION, 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 [14]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-106.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Mediates cAMP-dependent signaling triggered by receptor
CC binding to GPCRs. PKA activation regulates diverse cellular
CC processes such as cell proliferation, the cell cycle,
CC differentiation and regulation of microtubule dynamics, chromatin
CC condensation and decondensation, nuclear envelope disassembly and
CC reassembly, as well as regulation of intracellular transport
CC mechanisms and ion flux. Regulates the abundance of
CC compartmentalized pools of its regulatory subunits through
CC phosphorylation of PJA2 which binds and ubiquitinates these
CC subunits, leading to their subsequent proteolysis.
CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC -!- COFACTOR: Magnesium.
CC -!- ENZYME REGULATION: Activated by cAMP.
CC -!- SUBUNIT: A number of inactive tetrameric holoenzymes are produced
CC by the combination of homo- or heterodimers of the different
CC regulatory subunits associated with two catalytic subunits. cAMP
CC causes the dissociation of the inactive holoenzyme into a dimer of
CC regulatory subunits bound to four cAMP and two free monomeric
CC catalytic subunits. The cAMP-dependent protein kinase catalytic
CC subunit binds PJA2 (By similarity).
CC -!- INTERACTION:
CC Q92917:GPKOW; NbExp=4; IntAct=EBI-5258763, EBI-746309;
CC P08238:HSP90AB1; NbExp=2; IntAct=EBI-2679622, EBI-352572;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Nucleus (By
CC similarity). Note=Translocates into the nucleus (monomeric
CC catalytic subunit) (By similarity). The inactive holoenzyme is
CC found in the cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=Beta1;
CC IsoId=P22694-1; Sequence=Displayed;
CC Name=2; Synonyms=Beta2;
CC IsoId=P22694-2; Sequence=VSP_017364;
CC Name=3; Synonyms=Beta3;
CC IsoId=P22694-3; Sequence=VSP_017369, VSP_017370;
CC Note=Incomplete sequence;
CC Name=4; Synonyms=Beta4;
CC IsoId=P22694-4; Sequence=VSP_017368, VSP_017371;
CC Note=Incomplete sequence;
CC Name=5; Synonyms=Beta4ab;
CC IsoId=P22694-5; Sequence=VSP_017366;
CC Note=Incomplete sequence;
CC Name=6; Synonyms=Beta4abc;
CC IsoId=P22694-6; Sequence=VSP_017365;
CC Name=7;
CC IsoId=P22694-7; Sequence=VSP_017367;
CC Note=No experimental confirmation available;
CC Name=8;
CC IsoId=P22694-8; Sequence=VSP_036556, VSP_036557;
CC Name=9;
CC IsoId=P22694-9; Sequence=VSP_043372;
CC Note=No experimental confirmation available;
CC Name=10;
CC IsoId=P22694-10; Sequence=VSP_017366, VSP_046238;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Isoform 1 is most abundant in the brain, with
CC low level expression in kidney. Isoform 2 is predominantly
CC expressed in thymus, spleen and kidney. Isoform 3 and isoform 4
CC are only expressed in the brain.
CC -!- PTM: Asn-3 is partially deaminated to Asp giving rise to 2 major
CC isoelectric variants, called CB and CA respectively (By
CC similarity).
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cAMP subfamily.
CC -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC -!- SIMILARITY: Contains 1 protein kinase domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92426.1; Type=Frameshift; Positions=322;
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/prkacb/";
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DR EMBL; M34181; AAA60170.1; -; mRNA.
DR EMBL; BX537705; CAD97818.1; -; mRNA.
DR EMBL; BX641026; CAE46017.1; -; mRNA.
DR EMBL; AB209189; BAD92426.1; ALT_SEQ; mRNA.
DR EMBL; CR936631; CAI56774.1; -; mRNA.
DR EMBL; AK091420; BAG52356.1; -; mRNA.
DR EMBL; AK296482; BAG59122.1; -; mRNA.
DR EMBL; AK304375; BAG65213.1; -; mRNA.
DR EMBL; DQ667174; ABG25919.1; -; Genomic_DNA.
DR EMBL; AL359504; CAI14540.1; -; Genomic_DNA.
DR EMBL; AL450063; CAI14540.1; JOINED; Genomic_DNA.
DR EMBL; AL359504; CAI14541.1; -; Genomic_DNA.
DR EMBL; AL450063; CAI14541.1; JOINED; Genomic_DNA.
DR EMBL; AL450063; CAI16844.1; -; Genomic_DNA.
DR EMBL; AL359504; CAI16844.1; JOINED; Genomic_DNA.
DR EMBL; AL450063; CAI16845.1; -; Genomic_DNA.
DR EMBL; AL359504; CAI16845.1; JOINED; Genomic_DNA.
DR EMBL; AL450063; CAI16846.1; -; Genomic_DNA.
DR EMBL; CH471097; EAW73248.1; -; Genomic_DNA.
DR EMBL; BC016285; AAH16285.1; -; mRNA.
DR EMBL; BC035058; AAH35058.1; -; mRNA.
DR EMBL; AY927364; AAX19487.1; -; mRNA.
DR EMBL; AY927365; AAX19488.1; -; mRNA.
DR EMBL; AY927366; AAX19489.1; -; mRNA.
DR EMBL; AY927367; AAX19490.1; -; mRNA.
DR EMBL; AY927368; AAX19491.1; -; mRNA.
DR EMBL; AF538872; AAN16454.1; -; Genomic_DNA.
DR PIR; A34724; OKHUCB.
DR RefSeq; NP_001229786.1; NM_001242857.1.
DR RefSeq; NP_001229787.1; NM_001242858.1.
DR RefSeq; NP_001229788.1; NM_001242859.1.
DR RefSeq; NP_001229789.1; NM_001242860.1.
DR RefSeq; NP_001229790.1; NM_001242861.1.
DR RefSeq; NP_001229791.1; NM_001242862.1.
DR RefSeq; NP_002722.1; NM_002731.2.
DR RefSeq; NP_891993.1; NM_182948.2.
DR RefSeq; NP_997461.1; NM_207578.1.
DR RefSeq; XP_005271076.1; XM_005271019.1.
DR UniGene; Hs.487325; -.
DR ProteinModelPortal; P22694; -.
DR SMR; P22694; 15-351.
DR IntAct; P22694; 31.
DR MINT; MINT-1178341; -.
DR BindingDB; P22694; -.
DR ChEMBL; CHEMBL2918; -.
DR GuidetoPHARMACOLOGY; 1477; -.
DR PhosphoSite; P22694; -.
DR DMDM; 125210; -.
DR PaxDb; P22694; -.
DR PRIDE; P22694; -.
DR DNASU; 5567; -.
DR Ensembl; ENST00000370682; ENSP00000359716; ENSG00000142875.
DR Ensembl; ENST00000370685; ENSP00000359719; ENSG00000142875.
DR Ensembl; ENST00000370688; ENSP00000359722; ENSG00000142875.
DR Ensembl; ENST00000370689; ENSP00000359723; ENSG00000142875.
DR Ensembl; ENST00000394838; ENSP00000378314; ENSG00000142875.
DR Ensembl; ENST00000394839; ENSP00000378315; ENSG00000142875.
DR GeneID; 5567; -.
DR KEGG; hsa:5567; -.
DR UCSC; uc001djq.3; human.
DR CTD; 5567; -.
DR GeneCards; GC01P084543; -.
DR HGNC; HGNC:9381; PRKACB.
DR HPA; CAB010363; -.
DR HPA; HPA029754; -.
DR MIM; 176892; gene.
DR neXtProt; NX_P22694; -.
DR PharmGKB; PA33749; -.
DR eggNOG; COG0515; -.
DR HOGENOM; HOG000233033; -.
DR HOVERGEN; HBG108317; -.
DR KO; K04345; -.
DR OMA; GKEFCEF; -.
DR OrthoDB; EOG7VX8WD; -.
DR BRENDA; 2.7.11.11; 2681.
DR Reactome; REACT_111102; Signal Transduction.
DR Reactome; REACT_111217; Metabolism.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_13685; Neuronal System.
DR Reactome; REACT_15518; Transmembrane transport of small molecules.
DR Reactome; REACT_604; Hemostasis.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P22694; -.
DR ChiTaRS; PRKACB; human.
DR GeneWiki; PRKACB; -.
DR GenomeRNAi; 5567; -.
DR NextBio; 21570; -.
DR PRO; PR:P22694; -.
DR ArrayExpress; P22694; -.
DR Bgee; P22694; -.
DR Genevestigator; P22694; -.
DR GO; GO:0005952; C:cAMP-dependent protein kinase complex; TAS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0004691; F:cAMP-dependent protein kinase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IDA:UniProtKB.
DR GO; GO:0007202; P:activation of phospholipase C activity; TAS:Reactome.
DR GO; GO:0034199; P:activation of protein kinase A activity; TAS:Reactome.
DR GO; GO:0007188; P:adenylate cyclase-modulating G-protein coupled receptor signaling pathway; TAS:UniProtKB.
DR GO; GO:0007596; P:blood coagulation; TAS:Reactome.
DR GO; GO:0071377; P:cellular response to glucagon stimulus; TAS:Reactome.
DR GO; GO:0006112; P:energy reserve metabolic process; TAS:Reactome.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
DR GO; GO:0006094; P:gluconeogenesis; TAS:Reactome.
DR GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR GO; GO:0007243; P:intracellular protein kinase cascade; TAS:Reactome.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
DR GO; GO:0097338; P:response to clozapine; IEA:Ensembl.
DR GO; GO:0044281; P:small molecule metabolic process; TAS:Reactome.
DR GO; GO:0007268; P:synaptic transmission; TAS:Reactome.
DR GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
DR GO; GO:0019433; P:triglyceride catabolic process; TAS:Reactome.
DR GO; GO:0006833; P:water transport; TAS:Reactome.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR002290; Ser/Thr_dual-sp_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; cAMP; Cell membrane;
KW Complete proteome; Cytoplasm; Kinase; Lipoprotein; Membrane;
KW Myristate; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 351 cAMP-dependent protein kinase catalytic
FT subunit beta.
FT /FTId=PRO_0000086060.
FT DOMAIN 44 298 Protein kinase.
FT DOMAIN 299 351 AGC-kinase C-terminal.
FT NP_BIND 50 58 ATP (By similarity).
FT ACT_SITE 167 167 Proton acceptor (By similarity).
FT BINDING 73 73 ATP (By similarity).
FT MOD_RES 3 3 Deamidated asparagine (By similarity).
FT MOD_RES 11 11 Phosphoserine (By similarity).
FT MOD_RES 49 49 Phosphothreonine (By similarity).
FT MOD_RES 69 69 Phosphotyrosine (By similarity).
FT MOD_RES 140 140 Phosphoserine (By similarity).
FT MOD_RES 196 196 Phosphothreonine (By similarity).
FT MOD_RES 198 198 Phosphothreonine (By similarity).
FT MOD_RES 202 202 Phosphothreonine (By similarity).
FT MOD_RES 331 331 Phosphotyrosine (By similarity).
FT MOD_RES 339 339 Phosphoserine (By similarity).
FT LIPID 2 2 N-myristoyl glycine (By similarity).
FT VAR_SEQ 1 16 MGNAATAKKGSEVESV -> MAAYREPPCNQYTGTTTALQK
FT LEGFASRLFHRHSKGTAHDQKTALENDSLHFSEHTALWDRS
FT M (in isoform 2).
FT /FTId=VSP_017364.
FT VAR_SEQ 1 15 MGNAATAKKGSEVES -> MSARKSSDASACSSSEISDSF
FT (in isoform 6).
FT /FTId=VSP_017365.
FT VAR_SEQ 1 15 MGNAATAKKGSEVES -> MGLSRKSSDASACSSSEISDSF
FT (in isoform 9).
FT /FTId=VSP_043372.
FT VAR_SEQ 1 14 MGNAATAKKGSEVE -> MSARKSSDASACSSSEI (in
FT isoform 5 and isoform 10).
FT /FTId=VSP_017366.
FT VAR_SEQ 1 14 MGNAATAKKGSEVE -> MGLSRKSSDASACSSSEI (in
FT isoform 7).
FT /FTId=VSP_017367.
FT VAR_SEQ 1 13 Missing (in isoform 4).
FT /FTId=VSP_017368.
FT VAR_SEQ 1 12 Missing (in isoform 3).
FT /FTId=VSP_017369.
FT VAR_SEQ 13 16 VESV -> MGLL (in isoform 3).
FT /FTId=VSP_017370.
FT VAR_SEQ 14 14 E -> M (in isoform 4).
FT /FTId=VSP_017371.
FT VAR_SEQ 79 111 Missing (in isoform 10).
FT /FTId=VSP_046238.
FT VAR_SEQ 256 257 VR -> NF (in isoform 8).
FT /FTId=VSP_036556.
FT VAR_SEQ 258 351 Missing (in isoform 8).
FT /FTId=VSP_036557.
FT VARIANT 106 106 R -> Q (in dbSNP:rs36117118).
FT /FTId=VAR_040594.
FT CONFLICT 80 80 V -> G (in Ref. 3; CAI56774).
FT CONFLICT 159 159 H -> N (in Ref. 8; AAH35058).
FT CONFLICT 163 163 L -> I (in Ref. 8; AAH35058).
FT CONFLICT 233 233 A -> V (in Ref. 3; CAI56774).
FT CONFLICT 261 261 H -> N (in Ref. 8; AAH35058).
SQ SEQUENCE 351 AA; 40623 MW; 5C7443FBBA1C9BEC CRC64;
MGNAATAKKG SEVESVKEFL AKAKEDFLKK WENPTQNNAG LEDFERKKTL GTGSFGRVML
VKHKATEQYY AMKILDKQKV VKLKQIEHTL NEKRILQAVN FPFLVRLEYA FKDNSNLYMV
MEYVPGGEMF SHLRRIGRFS EPHARFYAAQ IVLTFEYLHS LDLIYRDLKP ENLLIDHQGY
IQVTDFGFAK RVKGRTWTLC GTPEYLAPEI ILSKGYNKAV DWWALGVLIY EMAAGYPPFF
ADQPIQIYEK IVSGKVRFPS HFSSDLKDLL RNLLQVDLTK RFGNLKNGVS DIKTHKWFAT
TDWIAIYQRK VEAPFIPKFR GSGDTSNFDD YEEEDIRVSI TEKCAKEFGE F
//

MIM 176892
*RECORD*
*FIELD* NO
176892
*FIELD* TI
*176892 PROTEIN KINASE, cAMP-DEPENDENT, CATALYTIC, BETA; PRKACB
*FIELD* TX
One of the best characterized classes of kinases is the cAMP-dependent
read moreprotein kinases (PKA). Two PKA isoforms exist, designated types I and
II, which differ in their dimeric R subunits, designated RI and RII,
respectively. Furthermore, there are at least 2 products for each of the
RI and RII subunits: RI-alpha (188830), RI-beta (176911), RII-alpha
(176910), and RII-beta (176912). The C subunit has also been shown to
consist of more than one gene product. Mammalian C-alpha, C-beta, and
C-gamma cDNAs have been cloned. Berube et al. (1991) assigned the
catalytic subunit C-beta of PKA to human chromosome 1 by Southern blot
analysis of somatic cell hybrids. By in situ hybridization, the gene was
localized to 1p36.1. (Also see Simard et al. (1992).)

*FIELD* RF
1. Berube, D.; Simard, J.; Sandberg, M.; Grzeschik, K.-H.; Gagne,
R.; Hansson, V.; Jahnsen, T.: Assignment of the gene encoding the
catalytic subunit C(beta) of cAMP-dependent protein kinase to the
p36 band on chromosome 1. (Abstract) Cytogenet. Cell Genet. 58:
1850 only, 1991.

2. Simard, J.; Berube, D.; Sandberg, M.; Grzeschik, K.-H.; Gagne,
R.; Hansson, V.; Jahnsen, T.: Assignment of the gene encoding the
catalytic subunit C-beta of cAMP-dependent protein kinase to the p36
band on chromosome 1. Hum. Genet. 88: 653-657, 1992.

*FIELD* CD
Victor A. McKusick: 8/21/1991

*FIELD* ED
terry: 09/05/1996
carol: 3/18/1993
carol: 5/11/1992
supermim: 3/16/1992
carol: 2/23/1992
carol: 11/6/1991
carol: 9/4/1991

RBCC Red Blood Cell Collection

Full text data of PRKACB