ID B1APG2_HUMAN Unreviewed; 209 AA. AC B1APG2; DT 08-APR-2008, integrated into UniProtKB/TrEMBL. DT 08-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 111. DE SubName: Full=Protein kinase cAMP-activated catalytic subunit beta {ECO:0000313|Ensembl:ENSP00000397175.1}; DE Flags: Fragment; GN Name=PRKACB {ECO:0000313|Ensembl:ENSP00000397175.1}; 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 {ECO:0000313|Ensembl:ENSP00000397175.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000397175.1, ECO:0000313|Proteomes:UP000005640} 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., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., RA Bethel G., 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., Clee C., RA Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., RA Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., RA Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R., RA Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., RA Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S., RA Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., RA Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., RA Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., RA Knights A.J., 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., McLaren S., Milne S., RA Mistry S., Moore M.J., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., RA Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., RA Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., RA Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., RA Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., RA Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., RA Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., RA Coulson A., Vaudin M., Sulston J.E., Durbin R., 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., Banerjee R., Bryant S.P., Burford D.C., RA Burrill W.D., Clegg S.M., Dhami P., Dovey O., Faulkner L.M., Gribble S.M., RA Langford C.F., Pandian R.D., Porter K.M., Prigmore E.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [2] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [3] {ECO:0000313|Ensembl:ENSP00000397175.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CC {ECO:0000256|RuleBase:RU000304}. 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; AL359504; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL450063; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; B1APG2; -. DR SMR; B1APG2; -. DR MassIVE; B1APG2; -. DR MaxQB; B1APG2; -. DR PeptideAtlas; B1APG2; -. DR ProteomicsDB; 3294; -. DR Antibodypedia; 4160; 485 antibodies from 36 providers. DR Ensembl; ENST00000413538.5; ENSP00000397175.1; ENSG00000142875.21. DR UCSC; uc057hys.1; human. DR HGNC; HGNC:9381; PRKACB. DR VEuPathDB; HostDB:ENSG00000142875; -. DR GeneTree; ENSGT00940000161169; -. DR ChiTaRS; PRKACB; human. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000142875; Expressed in endothelial cell and 213 other cell types or tissues. DR ExpressionAtlas; B1APG2; baseline and differential. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR PANTHER; PTHR24353:SF116; CAMP-DEPENDENT PROTEIN KINASE CATALYTIC SUBUNIT BETA; 1. DR PANTHER; PTHR24353; CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASE; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Kinase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE- KW ProRule:PRU10141}; KW Proteomics identification {ECO:0007829|EPD:B1APG2, KW ECO:0007829|MaxQB:B1APG2}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527, KW ECO:0000256|RuleBase:RU000304}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 39..209 FT /note="Protein kinase" FT /evidence="ECO:0000259|PROSITE:PS50011" FT BINDING 68 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141" FT NON_TER 209 FT /evidence="ECO:0000313|Ensembl:ENSP00000397175.1" SQ SEQUENCE 209 AA; 24324 MW; BF05CD20C002D0C7 CRC64; MSACSSSEIS VKEFLAKAKE DFLKKWENPT QNNAGLEDFE RKKTLGTGSF GRVMLVKHKA TEQYYAMKIL DKQKVVKLKQ IEHTLNEKRI LQAVNFPFLV RLEYAFKDNS NLYMVMEYVP GGEMFSHLRR IGRFSEPHAR FYAAQIVLTF EYLHSLDLIY RDLKPENLLI DHQGYIQVTD FGFAKRVKGR TWTLCGTPEY LAPEIILSK //