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test_full.xml
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test_full.xml
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C:\Users\monar\AppData\Local\Programs\Python\Python39\python.exe C:\Users\monar\PycharmProjects\Haider_Review\test.py
<?xml version="1.0" encoding="UTF-8" standalone="no" ?>
<uniprot xmlns="http://uniprot.org/uniprot" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://uniprot.org/uniprot http://www.uniprot.org/docs/uniprot.xsd">
<entry dataset="Swiss-Prot" created="1987-08-13" modified="2022-12-14" version="255" xmlns="http://uniprot.org/uniprot">
<accession>P05771</accession>
<accession>C5IFJ8</accession>
<accession>D3DWF5</accession>
<accession>O43744</accession>
<accession>P05127</accession>
<accession>Q15138</accession>
<accession>Q93060</accession>
<accession>Q9UE49</accession>
<accession>Q9UE50</accession>
<accession>Q9UEH8</accession>
<accession>Q9UJ30</accession>
<accession>Q9UJ33</accession>
<name>KPCB_HUMAN</name>
<protein>
<recommendedName>
<fullName>Protein kinase C beta type</fullName>
<shortName>PKC-B</shortName>
<shortName>PKC-beta</shortName>
<ecNumber evidence="18 19">2.7.11.13</ecNumber>
</recommendedName>
</protein>
<gene>
<name type="primary">PRKCB</name>
<name type="synonym">PKCB</name>
<name type="synonym">PRKCB1</name>
</gene>
<organism>
<name type="scientific">Homo sapiens</name>
<name type="common">Human</name>
<dbReference type="NCBI Taxonomy" id="9606"/>
<lineage>
<taxon>Eukaryota</taxon>
<taxon>Metazoa</taxon>
<taxon>Chordata</taxon>
<taxon>Craniata</taxon>
<taxon>Vertebrata</taxon>
<taxon>Euteleostomi</taxon>
<taxon>Mammalia</taxon>
<taxon>Eutheria</taxon>
<taxon>Euarchontoglires</taxon>
<taxon>Primates</taxon>
<taxon>Haplorrhini</taxon>
<taxon>Catarrhini</taxon>
<taxon>Hominidae</taxon>
<taxon>Homo</taxon>
</lineage>
</organism>
<reference key="1">
<citation type="journal article" date="1986" name="Science" volume="233" first="859" last="866">
<title>Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways.</title>
<authorList>
<person name="Coussens L."/>
<person name="Parker P.J."/>
<person name="Rhee L."/>
<person name="Yang-Feng T.L."/>
<person name="Chen E."/>
<person name="Waterfield M.D."/>
<person name="Francke U."/>
<person name="Ullrich A."/>
</authorList>
<dbReference type="PubMed" id="3755548"/>
<dbReference type="DOI" id="10.1126/science.3755548"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BETA-II)</scope>
</reference>
<reference key="2">
<citation type="journal article" date="1987" name="FEBS Lett." volume="223" first="138" last="142">
<title>Primary structures of human protein kinase C beta I and beta II differ only in their C-terminal sequences.</title>
<authorList>
<person name="Kubo K."/>
<person name="Ohno S."/>
<person name="Suzuki K."/>
</authorList>
<dbReference type="PubMed" id="3666134"/>
<dbReference type="DOI" id="10.1016/0014-5793(87)80524-0"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II)</scope>
</reference>
<reference key="3">
<citation type="submission" date="2009-04" db="EMBL/GenBank/DDBJ databases">
<authorList>
<consortium name="NIEHS SNPs program"/>
</authorList>
</citation>
<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
</reference>
<reference key="4">
<citation type="journal article" date="1999" name="Genomics" volume="60" first="295" last="308">
<title>Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q.</title>
<authorList>
<person name="Loftus B.J."/>
<person name="Kim U.-J."/>
<person name="Sneddon V.P."/>
<person name="Kalush F."/>
<person name="Brandon R."/>
<person name="Fuhrmann J."/>
<person name="Mason T."/>
<person name="Crosby M.L."/>
<person name="Barnstead M."/>
<person name="Cronin L."/>
<person name="Mays A.D."/>
<person name="Cao Y."/>
<person name="Xu R.X."/>
<person name="Kang H.-L."/>
<person name="Mitchell S."/>
<person name="Eichler E.E."/>
<person name="Harris P.C."/>
<person name="Venter J.C."/>
<person name="Adams M.D."/>
</authorList>
<dbReference type="PubMed" id="10493829"/>
<dbReference type="DOI" id="10.1006/geno.1999.5927"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
</reference>
<reference key="5">
<citation type="submission" date="2005-09" db="EMBL/GenBank/DDBJ databases">
<authorList>
<person name="Mural R.J."/>
<person name="Istrail S."/>
<person name="Sutton G.G."/>
<person name="Florea L."/>
<person name="Halpern A.L."/>
<person name="Mobarry C.M."/>
<person name="Lippert R."/>
<person name="Walenz B."/>
<person name="Shatkay H."/>
<person name="Dew I."/>
<person name="Miller J.R."/>
<person name="Flanigan M.J."/>
<person name="Edwards N.J."/>
<person name="Bolanos R."/>
<person name="Fasulo D."/>
<person name="Halldorsson B.V."/>
<person name="Hannenhalli S."/>
<person name="Turner R."/>
<person name="Yooseph S."/>
<person name="Lu F."/>
<person name="Nusskern D.R."/>
<person name="Shue B.C."/>
<person name="Zheng X.H."/>
<person name="Zhong F."/>
<person name="Delcher A.L."/>
<person name="Huson D.H."/>
<person name="Kravitz S.A."/>
<person name="Mouchard L."/>
<person name="Reinert K."/>
<person name="Remington K.A."/>
<person name="Clark A.G."/>
<person name="Waterman M.S."/>
<person name="Eichler E.E."/>
<person name="Adams M.D."/>
<person name="Hunkapiller M.W."/>
<person name="Myers E.W."/>
<person name="Venter J.C."/>
</authorList>
</citation>
<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
</reference>
<reference key="6">
<citation type="journal article" date="2004" name="Genome Res." volume="14" first="2121" last="2127">
<title>The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).</title>
<authorList>
<consortium name="The MGC Project Team"/>
</authorList>
<dbReference type="PubMed" id="15489334"/>
<dbReference type="DOI" id="10.1101/gr.2596504"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]</scope>
<source>
<tissue>Hippocampus</tissue>
</source>
</reference>
<reference key="7">
<citation type="journal article" date="1995" name="DNA Cell Biol." volume="14" first="213" last="222">
<title>Autoregulation of cloned human protein kinase C beta and gamma gene promoters in U937 cells.</title>
<authorList>
<person name="Mahajna J."/>
<person name="King P."/>
<person name="Parker P."/>
<person name="Haley J."/>
</authorList>
<dbReference type="PubMed" id="7880442"/>
<dbReference type="DOI" id="10.1089/dna.1995.14.213"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69</scope>
</reference>
<reference key="8">
<citation type="journal article" date="1992" name="J. Biol. Chem." volume="267" first="6158" last="6163">
<title>Positive and negative regulation of the transcription of the human protein kinase C beta gene.</title>
<authorList>
<person name="Niino Y.S."/>
<person name="Ohno S."/>
<person name="Suzuki K."/>
</authorList>
<dbReference type="PubMed" id="1556124"/>
<dbReference type="DOI" id="10.1016/s0021-9258(18)42675-0"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58</scope>
</reference>
<reference key="9">
<citation type="journal article" date="1992" name="J. Biol. Chem." volume="267" first="20804" last="20810">
<title>Cloning and characterization of the major promoter of the human protein kinase C beta gene. Regulation by phorbol esters.</title>
<authorList>
<person name="Obeid L.M."/>
<person name="Blobe G.C."/>
<person name="Karolak L.A."/>
<person name="Hannun Y.A."/>
</authorList>
<dbReference type="PubMed" id="1400396"/>
<dbReference type="DOI" id="10.1016/s0021-9258(19)36758-4"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57</scope>
</reference>
<reference key="10">
<citation type="journal article" date="2003" name="Nat. Biotechnol." volume="21" first="566" last="569">
<title>Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.</title>
<authorList>
<person name="Gevaert K."/>
<person name="Goethals M."/>
<person name="Martens L."/>
<person name="Van Damme J."/>
<person name="Staes A."/>
<person name="Thomas G.R."/>
<person name="Vandekerckhove J."/>
</authorList>
<dbReference type="PubMed" id="12665801"/>
<dbReference type="DOI" id="10.1038/nbt810"/>
</citation>
<scope>PROTEIN SEQUENCE OF 2-19</scope>
<scope>ACETYLATION AT ALA-2</scope>
<source>
<tissue>Platelet</tissue>
</source>
</reference>
<reference key="11">
<citation type="submission" date="1997-11" db="EMBL/GenBank/DDBJ databases">
<title>The genomic structure of the human protein kinase C beta gene (PRKCB).</title>
<authorList>
<person name="Greenham J.A."/>
<person name="Adams M.D."/>
<person name="Doggett N.A."/>
<person name="Mole S.E."/>
</authorList>
</citation>
<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-176</scope>
</reference>
<reference key="12">
<citation type="journal article" date="1987" name="DNA" volume="6" first="389" last="394">
<title>Alternative splicing increases the diversity of the human protein kinase C family.</title>
<authorList>
<person name="Coussens L."/>
<person name="Rhee L."/>
<person name="Parker P.J."/>
<person name="Ullrich A."/>
</authorList>
<dbReference type="PubMed" id="3677994"/>
<dbReference type="DOI" id="10.1089/dna.1987.6.389"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-671</scope>
<source>
<tissue>Fetal brain</tissue>
</source>
</reference>
<reference key="13">
<citation type="journal article" date="1987" name="Nucleic Acids Res." volume="15" first="7179" last="7180">
<title>Nucleotide sequence of the 3' portion of a human gene for protein kinase C beta-I/beta-II.</title>
<authorList>
<person name="Kubo K."/>
<person name="Ohno S."/>
<person name="Suzuki K."/>
</authorList>
<dbReference type="PubMed" id="3658678"/>
<dbReference type="DOI" id="10.1093/nar/15.17.7179"/>
</citation>
<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-671</scope>
</reference>
<reference key="14">
<citation type="journal article" date="2001" name="EMBO J." volume="20" first="5692" last="5702">
<title>PKCbeta modulates antigen receptor signaling via regulation of Btk membrane localization.</title>
<authorList>
<person name="Kang S.W."/>
<person name="Wahl M.I."/>
<person name="Chu J."/>
<person name="Kitaura J."/>
<person name="Kawakami Y."/>
<person name="Kato R.M."/>
<person name="Tabuchi R."/>
<person name="Tarakhovsky A."/>
<person name="Kawakami T."/>
<person name="Turck C.W."/>
<person name="Witte O.N."/>
<person name="Rawlings D.J."/>
</authorList>
<dbReference type="PubMed" id="11598012"/>
<dbReference type="DOI" id="10.1093/emboj/20.20.5692"/>
</citation>
<scope>FUNCTION IN PHOSPHORYLATION OF BTK</scope>
</reference>
<reference key="15">
<citation type="journal article" date="2005" name="Cancer Res." volume="65" first="7462" last="7469">
<title>The protein kinase Cbeta-selective inhibitor, enzastaurin (LY317615.HCl), suppresses signaling through the AKT pathway, induces apoptosis, and suppresses growth of human colon cancer and glioblastoma xenografts.</title>
<authorList>
<person name="Graff J.R."/>
<person name="McNulty A.M."/>
<person name="Hanna K.R."/>
<person name="Konicek B.W."/>
<person name="Lynch R.L."/>
<person name="Bailey S.N."/>
<person name="Banks C."/>
<person name="Capen A."/>
<person name="Goode R."/>
<person name="Lewis J.E."/>
<person name="Sams L."/>
<person name="Huss K.L."/>
<person name="Campbell R.M."/>
<person name="Iversen P.W."/>
<person name="Neubauer B.L."/>
<person name="Brown T.J."/>
<person name="Musib L."/>
<person name="Geeganage S."/>
<person name="Thornton D."/>
</authorList>
<dbReference type="PubMed" id="16103100"/>
<dbReference type="DOI" id="10.1158/0008-5472.can-05-0071"/>
</citation>
<scope>ACTIVITY REGULATION</scope>
</reference>
<reference key="16">
<citation type="journal article" date="2008" name="J. Biol. Chem." volume="283" first="6300" last="6311">
<title>The phosphatase PHLPP controls the cellular levels of protein kinase C.</title>
<authorList>
<person name="Gao T."/>
<person name="Brognard J."/>
<person name="Newton A.C."/>
</authorList>
<dbReference type="PubMed" id="18162466"/>
<dbReference type="DOI" id="10.1074/jbc.m707319200"/>
</citation>
<scope>INTERACTION WITH PHLPP1 AND PHLPP2</scope>
</reference>
<reference key="17">
<citation type="journal article" date="2008" name="J. Proteome Res." volume="7" first="526" last="534">
<title>Phosphoproteome of resting human platelets.</title>
<authorList>
<person name="Zahedi R.P."/>
<person name="Lewandrowski U."/>
<person name="Wiesner J."/>
<person name="Wortelkamp S."/>
<person name="Moebius J."/>
<person name="Schuetz C."/>
<person name="Walter U."/>
<person name="Gambaryan S."/>
<person name="Sickmann A."/>
</authorList>
<dbReference type="PubMed" id="18088087"/>
<dbReference type="DOI" id="10.1021/pr0704130"/>
</citation>
<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
<source>
<tissue>Platelet</tissue>
</source>
</reference>
<reference key="18">
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<dbReference type="PubMed" id="19176525"/>
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<scope>FUNCTION</scope>
</reference>
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<dbReference type="PubMed" id="19369195"/>
<dbReference type="DOI" id="10.1074/mcp.m800588-mcp200"/>
</citation>
<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504</scope>
<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641 AND SER-660 (ISOFORM BETA-II)</scope>
<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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<person name="Schule R."/>
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<dbReference type="PubMed" id="20228790"/>
<dbReference type="DOI" id="10.1038/nature08839"/>
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<scope>FUNCTION IN HISTONE H3 PHOSPHORYLATION</scope>
<scope>CATALYTIC ACTIVITY</scope>
<scope>SUBCELLULAR LOCATION</scope>
<scope>INTERACTION WITH KDM1A; PKN1 AND AR</scope>
</reference>
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<dbReference type="PubMed" id="12417015"/>
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<scope>REVIEW ON FUNCTION</scope>
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<dbReference type="PubMed" id="20186491"/>
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<scope>REVIEW ON FUNCTION</scope>
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<dbReference type="PubMed" id="21269460"/>
<dbReference type="DOI" id="10.1186/1752-0509-5-17"/>
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<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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<dbReference type="PubMed" id="23186163"/>
<dbReference type="DOI" id="10.1021/pr300630k"/>
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<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-17; SER-206; SER-311; THR-314 AND THR-642</scope>
<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
<source>
<tissue>Erythroleukemia</tissue>
</source>
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<dbReference type="PubMed" id="24275569"/>
<dbReference type="DOI" id="10.1016/j.jprot.2013.11.014"/>
</citation>
<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641 AND SER-660 (ISOFORM BETA-II)</scope>
<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
<source>
<tissue>Liver</tissue>
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<reference key="26">
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<authorList>
<person name="Lee E.E."/>
<person name="Ma J."/>
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</authorList>
<dbReference type="PubMed" id="25982116"/>
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</citation>
<scope>FUNCTION</scope>
<scope>CATALYTIC ACTIVITY</scope>
</reference>
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<person name="Grodsky N."/>
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<dbReference type="PubMed" id="17115692"/>
<dbReference type="DOI" id="10.1021/bi061128h"/>
</citation>
<scope>X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 321-660 IN COMPLEX WITH INHIBITOR</scope>
<scope>PHOSPHORYLATION AT THR-500; THR-642 AND SER-661</scope>
</reference>
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<title>Patterns of somatic mutation in human cancer genomes.</title>
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<dbReference type="PubMed" id="17344846"/>
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<scope>VARIANTS [LARGE SCALE ANALYSIS] MET-144; MET-496 AND HIS-588</scope>
</reference>
<comment type="function">
<text evidence="3 11 17 18 19">Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a direct role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via direct phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity (PubMed:11598012). Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (AR)-dependent transcription, by being recruited to AR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A (PubMed:20228790). In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. Participates in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1 (PubMed:25982116). Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity). Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription (PubMed:19176525).</text>
</comment>
<comment type="catalytic activity">
<reaction evidence="18 19">
<text>ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]</text>
<dbReference type="Rhea" id="RHEA:17989"/>
<dbReference type="Rhea" id="RHEA-COMP:9863"/>
<dbReference type="Rhea" id="RHEA-COMP:11604"/>
<dbReference type="ChEBI" id="CHEBI:15378"/>
<dbReference type="ChEBI" id="CHEBI:29999"/>
<dbReference type="ChEBI" id="CHEBI:30616"/>
<dbReference type="ChEBI" id="CHEBI:83421"/>
<dbReference type="ChEBI" id="CHEBI:456216"/>
<dbReference type="EC" id="2.7.11.13"/>
</reaction>
<physiologicalReaction direction="left-to-right" evidence="18 19">
<dbReference type="Rhea" id="RHEA:17990"/>
</physiologicalReaction>
</comment>
<comment type="catalytic activity">
<reaction evidence="18">
<text>ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]</text>
<dbReference type="Rhea" id="RHEA:46608"/>
<dbReference type="Rhea" id="RHEA-COMP:11060"/>
<dbReference type="Rhea" id="RHEA-COMP:11605"/>
<dbReference type="ChEBI" id="CHEBI:15378"/>
<dbReference type="ChEBI" id="CHEBI:30013"/>
<dbReference type="ChEBI" id="CHEBI:30616"/>
<dbReference type="ChEBI" id="CHEBI:61977"/>
<dbReference type="ChEBI" id="CHEBI:456216"/>
<dbReference type="EC" id="2.7.11.13"/>
</reaction>
<physiologicalReaction direction="left-to-right" evidence="18">
<dbReference type="Rhea" id="RHEA:46609"/>
</physiologicalReaction>
</comment>
<comment type="cofactor">
<cofactor evidence="5">
<name>Ca(2+)</name>
<dbReference type="ChEBI" id="CHEBI:29108"/>
</cofactor>
<text evidence="2">Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain.</text>
</comment>
<comment type="activity regulation">
<text evidence="13">Classical (or conventional) PKCs (PRKCA, PRKCB and PRKCG) are activated by calcium and diacylglycerol (DAG) in the presence of phosphatidylserine. Three specific sites; Thr-500 (activation loop of the kinase domain), Thr-642 (turn motif) and Ser-661 (hydrophobic region), need to be phosphorylated for its full activation. Specifically inhibited by enzastaurin (LY317615).</text>
</comment>
<comment type="subunit">
<text evidence="1 14 16 18">Interacts with PDK1 (By similarity). Interacts in vitro with PRKCBP1. Interacts with PHLPP1 and PHLPP2; both proteins mediate its dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and AR.</text>
</comment>
<comment type="interaction">
<interactant intactId="EBI-706216">
<id>P05771</id>
</interactant>
<interactant intactId="EBI-744700">
<id>Q8NEM2</id>
<label>SHCBP1</label>
</interactant>
<organismsDiffer>false</organismsDiffer>
<experiments>3</experiments>
</comment>
<comment type="interaction">
<interactant intactId="EBI-706216">
<id>P05771</id>
</interactant>
<interactant intactId="EBI-717399">
<id>Q9BSI4</id>
<label>TINF2</label>
</interactant>
<organismsDiffer>false</organismsDiffer>
<experiments>2</experiments>
</comment>
<comment type="interaction">
<interactant intactId="EBI-5774492">
<id>P05771-1</id>
</interactant>
<interactant intactId="EBI-15599570">
<id>O60341-1</id>
<label>KDM1A</label>
</interactant>
<organismsDiffer>false</organismsDiffer>
<experiments>2</experiments>
</comment>
<comment type="interaction">
<interactant intactId="EBI-5774511">
<id>P05771-2</id>
</interactant>
<interactant intactId="EBI-18899653">
<id>Q6DHV7-2</id>
<label>ADAL</label>
</interactant>
<organismsDiffer>false</organismsDiffer>
<experiments>3</experiments>
</comment>
<comment type="interaction">
<interactant intactId="EBI-5774511">
<id>P05771-2</id>
</interactant>
<interactant intactId="EBI-1383687">
<id>Q9UQM7</id>
<label>CAMK2A</label>
</interactant>
<organismsDiffer>false</organismsDiffer>
<experiments>3</experiments>
</comment>
<comment type="interaction">
<interactant intactId="EBI-5774511">
<id>P05771-2</id>
</interactant>
<interactant intactId="EBI-25830459">
<id>Q6ZQX7-4</id>
<label>LIAT1</label>
</interactant>
<organismsDiffer>false</organismsDiffer>
<experiments>3</experiments>
</comment>
<comment type="interaction">
<interactant intactId="EBI-5774511">
<id>P05771-2</id>
</interactant>
<interactant intactId="EBI-2511516">
<id>O60346</id>
<label>PHLPP1</label>
</interactant>
<organismsDiffer>false</organismsDiffer>
<experiments>5</experiments>
</comment>
<comment type="interaction">
<interactant intactId="EBI-5774511">
<id>P05771-2</id>
</interactant>
<interactant intactId="EBI-2511496">
<id>Q6ZVD8</id>
<label>PHLPP2</label>
</interactant>
<organismsDiffer>false</organismsDiffer>
<experiments>2</experiments>
</comment>
<comment type="subcellular location">
<subcellularLocation>
<location evidence="1">Cytoplasm</location>
</subcellularLocation>
<subcellularLocation>
<location evidence="18">Nucleus</location>
</subcellularLocation>
<subcellularLocation>
<location evidence="1">Membrane</location>
<topology evidence="1">Peripheral membrane protein</topology>
</subcellularLocation>
</comment>
<comment type="alternative products">
<event type="alternative splicing"/>
<isoform>
<id>P05771-1</id>
<name>Beta-I</name>
<name>PRKCB1</name>
<sequence type="displayed"/>
</isoform>
<isoform>
<id>P05771-2</id>
<name>Beta-II</name>
<name>PRKCB2</name>
<sequence type="described" ref="VSP_004738"/>
</isoform>
</comment>
<comment type="PTM">
<text evidence="1">Phosphorylation on Thr-500 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Autophosphorylation on other sites i.e. in the N-terminal and hinge regions have no effect on enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with GRB2 and contributes to the activation of MAPK/ERK signaling cascade (By similarity).</text>
</comment>
<comment type="similarity">
<text evidence="22">Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.</text>
</comment>
<comment type="online information" name="NIEHS-SNPs">
<link uri="http://egp.gs.washington.edu/data/prkcb1/"/>
</comment>
<dbReference type="EC" id="2.7.11.13" evidence="18 19"/>
<dbReference type="EMBL" id="M13975">
<property type="protein sequence ID" value="AAA60095.1"/>
<property type="molecule type" value="mRNA"/>
</dbReference>
<dbReference type="EMBL" id="X06318">
<property type="protein sequence ID" value="CAA29634.1"/>
<property type="molecule type" value="mRNA"/>
</dbReference>
<dbReference type="EMBL" id="X07109">
<property type="protein sequence ID" value="CAA30130.1"/>
<property type="molecule type" value="mRNA"/>
</dbReference>
<dbReference type="EMBL" id="FJ907246">
<property type="protein sequence ID" value="ACS14045.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="AC130454">
<property type="status" value="NOT_ANNOTATED_CDS"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="AC002299">
<property type="protein sequence ID" value="AAB97933.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="AC002299">
<property type="protein sequence ID" value="AAB97934.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="CH471145">
<property type="protein sequence ID" value="EAW55797.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="CH471145">
<property type="protein sequence ID" value="EAW55798.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="BC036472">
<property type="protein sequence ID" value="AAH36472.1"/>
<property type="molecule type" value="mRNA"/>
</dbReference>
<dbReference type="EMBL" id="X62532">
<property type="protein sequence ID" value="CAA44393.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="S47311">
<property type="protein sequence ID" value="AAD13852.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="D10022">
<property type="protein sequence ID" value="BAA00912.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="AJ002799">
<property type="protein sequence ID" value="CAA05725.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="AJ002800">
<property type="protein sequence ID" value="CAA05725.1"/>
<property type="status" value="JOINED"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="M18254">
<property type="protein sequence ID" value="AAA60096.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="M18255">
<property type="protein sequence ID" value="AAA60097.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="X05972">
<property type="protein sequence ID" value="CAA29396.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="EMBL" id="X05971">
<property type="protein sequence ID" value="CAA29395.1"/>
<property type="molecule type" value="Genomic_DNA"/>
</dbReference>
<dbReference type="CCDS" id="CCDS10618.1">
<molecule id="P05771-1"/>
</dbReference>
<dbReference type="CCDS" id="CCDS10619.1">
<molecule id="P05771-2"/>
</dbReference>
<dbReference type="PIR" id="B24664">
<property type="entry name" value="KIHUC2"/>
</dbReference>
<dbReference type="PIR" id="S00159">
<property type="entry name" value="KIHUC1"/>
</dbReference>
<dbReference type="RefSeq" id="NP_002729.2">
<molecule id="P05771-2"/>
<property type="nucleotide sequence ID" value="NM_002738.6"/>
</dbReference>
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