KPCB_HUMAN
ID KPCB_HUMAN Reviewed; 671 AA.
AC P05771; C5IFJ8; D3DWF5; O43744; P05127; Q15138; Q93060; Q9UE49; Q9UE50;
AC Q9UEH8; Q9UJ30; Q9UJ33;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 253.
DE RecName: Full=Protein kinase C beta type;
DE Short=PKC-B;
DE Short=PKC-beta;
DE EC=2.7.11.13 {ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:25982116};
GN Name=PRKCB; Synonyms=PKCB, PRKCB1;
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] (ISOFORM BETA-II).
RX PubMed=3755548; DOI=10.1126/science.3755548;
RA Coussens L., Parker P.J., Rhee L., Yang-Feng T.L., Chen E.,
RA Waterfield M.D., Francke U., Ullrich A.;
RT "Multiple, distinct forms of bovine and human protein kinase C suggest
RT diversity in cellular signaling pathways.";
RL Science 233:859-866(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BETA-I AND BETA-II).
RX PubMed=3666134; DOI=10.1016/0014-5793(87)80524-0;
RA Kubo K., Ohno S., Suzuki K.;
RT "Primary structures of human protein kinase C beta I and beta II differ
RT only in their C-terminal sequences.";
RL FEBS Lett. 223:138-142(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Hippocampus;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RX PubMed=7880442; DOI=10.1089/dna.1995.14.213;
RA Mahajna J., King P., Parker P., Haley J.;
RT "Autoregulation of cloned human protein kinase C beta and gamma gene
RT promoters in U937 cells.";
RL DNA Cell Biol. 14:213-222(1995).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58.
RX PubMed=1556124; DOI=10.1016/s0021-9258(18)42675-0;
RA Niino Y.S., Ohno S., Suzuki K.;
RT "Positive and negative regulation of the transcription of the human protein
RT kinase C beta gene.";
RL J. Biol. Chem. 267:6158-6163(1992).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-57.
RX PubMed=1400396; DOI=10.1016/s0021-9258(19)36758-4;
RA Obeid L.M., Blobe G.C., Karolak L.A., Hannun Y.A.;
RT "Cloning and characterization of the major promoter of the human protein
RT kinase C beta gene. Regulation by phorbol esters.";
RL J. Biol. Chem. 267:20804-20810(1992).
RN [10]
RP PROTEIN SEQUENCE OF 2-19, AND ACETYLATION AT ALA-2.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 97-176.
RA Greenham J.A., Adams M.D., Doggett N.A., Mole S.E.;
RT "The genomic structure of the human protein kinase C beta gene (PRKCB).";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 609-671.
RC TISSUE=Fetal brain;
RX PubMed=3677994; DOI=10.1089/dna.1987.6.389;
RA Coussens L., Rhee L., Parker P.J., Ullrich A.;
RT "Alternative splicing increases the diversity of the human protein kinase C
RT family.";
RL DNA 6:389-394(1987).
RN [13]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 622-671.
RX PubMed=3658678; DOI=10.1093/nar/15.17.7179;
RA Kubo K., Ohno S., Suzuki K.;
RT "Nucleotide sequence of the 3' portion of a human gene for protein kinase C
RT beta-I/beta-II.";
RL Nucleic Acids Res. 15:7179-7180(1987).
RN [14]
RP FUNCTION IN PHOSPHORYLATION OF BTK.
RX PubMed=11598012; DOI=10.1093/emboj/20.20.5692;
RA Kang S.W., Wahl M.I., Chu J., Kitaura J., Kawakami Y., Kato R.M.,
RA Tabuchi R., Tarakhovsky A., Kawakami T., Turck C.W., Witte O.N.,
RA Rawlings D.J.;
RT "PKCbeta modulates antigen receptor signaling via regulation of Btk
RT membrane localization.";
RL EMBO J. 20:5692-5702(2001).
RN [15]
RP ACTIVITY REGULATION.
RX PubMed=16103100; DOI=10.1158/0008-5472.can-05-0071;
RA Graff J.R., McNulty A.M., Hanna K.R., Konicek B.W., Lynch R.L.,
RA Bailey S.N., Banks C., Capen A., Goode R., Lewis J.E., Sams L., Huss K.L.,
RA Campbell R.M., Iversen P.W., Neubauer B.L., Brown T.J., Musib L.,
RA Geeganage S., Thornton D.;
RT "The protein kinase Cbeta-selective inhibitor, enzastaurin (LY317615.HCl),
RT suppresses signaling through the AKT pathway, induces apoptosis, and
RT suppresses growth of human colon cancer and glioblastoma xenografts.";
RL Cancer Res. 65:7462-7469(2005).
RN [16]
RP INTERACTION WITH PHLPP1 AND PHLPP2.
RX PubMed=18162466; DOI=10.1074/jbc.m707319200;
RA Gao T., Brognard J., Newton A.C.;
RT "The phosphatase PHLPP controls the cellular levels of protein kinase C.";
RL J. Biol. Chem. 283:6300-6311(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [18]
RP FUNCTION.
RX PubMed=19176525; DOI=10.1074/jbc.m808719200;
RA Yamasaki T., Takahashi A., Pan J., Yamaguchi N., Yokoyama K.K.;
RT "Phosphorylation of activation transcription factor-2 at serine 121 by
RT protein kinase c controls c-Jun-mediated activation of transcription.";
RL J. Biol. Chem. 284:8567-8581(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-504, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-641 AND SER-660 (ISOFORM BETA-II), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP FUNCTION IN HISTONE H3 PHOSPHORYLATION, CATALYTIC ACTIVITY, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH KDM1A; PKN1 AND AR.
RX PubMed=20228790; DOI=10.1038/nature08839;
RA Metzger E., Imhof A., Patel D., Kahl P., Hoffmeyer K., Friedrichs N.,
RA Muller J.M., Greschik H., Kirfel J., Ji S., Kunowska N.,
RA Beisenherz-Huss C., Gunther T., Buettner R., Schule R.;
RT "Phosphorylation of histone H3T6 by PKCbeta(I) controls demethylation at
RT histone H3K4.";
RL Nature 464:792-796(2010).
RN [21]
RP REVIEW ON FUNCTION.
RX PubMed=12417015; DOI=10.1093/oxfordjournals.jbchem.a003273;
RA Kawakami T., Kawakami Y., Kitaura J.;
RT "Protein kinase C beta (PKC beta): normal functions and diseases.";
RL J. Biochem. 132:677-682(2002).
RN [22]
RP REVIEW ON FUNCTION.
RX PubMed=20186491; DOI=10.1007/s11154-010-9134-4;
RA Tabit C.E., Chung W.B., Hamburg N.M., Vita J.A.;
RT "Endothelial dysfunction in diabetes mellitus: molecular mechanisms and
RT clinical implications.";
RL Rev. Endocr. Metab. Disord. 11:61-74(2010).
RN [23]
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., Buerckstuemmer 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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-11; THR-17; SER-206; SER-311;
RP THR-314 AND THR-642, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-641 AND SER-660 (ISOFORM
RP BETA-II), AND IDENTIFICATION BY 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 [26]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25982116; DOI=10.1016/j.molcel.2015.04.015;
RA Lee E.E., Ma J., Sacharidou A., Mi W., Salato V.K., Nguyen N., Jiang Y.,
RA Pascual J.M., North P.E., Shaul P.W., Mettlen M., Wang R.C.;
RT "A protein kinase C phosphorylation motif in GLUT1 affects glucose
RT transport and is mutated in GLUT1 deficiency syndrome.";
RL Mol. Cell 58:845-853(2015).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 321-660 IN COMPLEX WITH INHIBITOR,
RP AND PHOSPHORYLATION AT THR-500; THR-642 AND SER-661.
RX PubMed=17115692; DOI=10.1021/bi061128h;
RA Grodsky N., Li Y., Bouzida D., Love R., Jensen J., Nodes B., Nonomiya J.,
RA Grant S.;
RT "Structure of the catalytic domain of human protein kinase C beta II
RT complexed with a bisindolylmaleimide inhibitor.";
RL Biochemistry 45:13970-13981(2006).
RN [28]
RP VARIANTS [LARGE SCALE ANALYSIS] MET-144; MET-496 AND HIS-588.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-
CC dependent serine/threonine-protein kinase involved in various cellular
CC processes such as regulation of the B-cell receptor (BCR) signalosome,
CC oxidative stress-induced apoptosis, androgen receptor-dependent
CC transcription regulation, insulin signaling and endothelial cells
CC proliferation. Plays a key role in B-cell activation by regulating BCR-
CC induced NF-kappa-B activation. Mediates the activation of the canonical
CC NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11/CARMA1
CC at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces
CC CARD11/CARMA1 association with lipid rafts and recruitment of the
CC BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK
CC complex, resulting in nuclear translocation and activation of NFKB1.
CC Plays a direct role in the negative feedback regulation of the BCR
CC signaling, by down-modulating BTK function via direct phosphorylation
CC of BTK at 'Ser-180', which results in the alteration of BTK plasma
CC membrane localization and in turn inhibition of BTK activity
CC (PubMed:11598012). Involved in apoptosis following oxidative damage: in
CC case of oxidative conditions, specifically phosphorylates 'Ser-36' of
CC isoform p66Shc of SHC1, leading to mitochondrial accumulation of
CC p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts
CC as a coactivator of androgen receptor (AR)-dependent transcription, by
CC being recruited to AR target genes and specifically mediating
CC phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for
CC epigenetic transcriptional activation that prevents demethylation of
CC histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A (PubMed:20228790). In insulin
CC signaling, may function downstream of IRS1 in muscle cells and mediate
CC insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling
CC cascade. Participates in the regulation of glucose transport in
CC adipocytes by negatively modulating the insulin-stimulated
CC translocation of the glucose transporter SLC2A4/GLUT4. Phosphorylates
CC SLC2A1/GLUT1, promoting glucose uptake by SLC2A1/GLUT1
CC (PubMed:25982116). Under high glucose in pancreatic beta-cells, is
CC probably involved in the inhibition of the insulin gene transcription,
CC via regulation of MYC expression. In endothelial cells, activation of
CC PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced
CC cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide
CC synthase (NOS3/eNOS) regulation by insulin, which causes endothelial
CC dysfunction. Also involved in triglyceride homeostasis (By similarity).
CC Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN,
CC activating transcription (PubMed:19176525).
CC {ECO:0000250|UniProtKB:P68404, ECO:0000269|PubMed:11598012,
CC ECO:0000269|PubMed:19176525, ECO:0000269|PubMed:20228790,
CC ECO:0000269|PubMed:25982116}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13;
CC Evidence={ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:25982116};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17990;
CC Evidence={ECO:0000269|PubMed:20228790, ECO:0000269|PubMed:25982116};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.13; Evidence={ECO:0000269|PubMed:20228790};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:46609;
CC Evidence={ECO:0000269|PubMed:20228790};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2
CC domain. {ECO:0000250|UniProtKB:P68403};
CC -!- ACTIVITY REGULATION: Classical (or conventional) PKCs (PRKCA, PRKCB and
CC PRKCG) are activated by calcium and diacylglycerol (DAG) in the
CC presence of phosphatidylserine. Three specific sites; Thr-500
CC (activation loop of the kinase domain), Thr-642 (turn motif) and Ser-
CC 661 (hydrophobic region), need to be phosphorylated for its full
CC activation. Specifically inhibited by enzastaurin (LY317615).
CC {ECO:0000269|PubMed:16103100}.
CC -!- SUBUNIT: Interacts with PDK1 (By similarity). Interacts in vitro with
CC PRKCBP1. Interacts with PHLPP1 and PHLPP2; both proteins mediate its
CC dephosphorylation. Interacts with KDM1A/LSD1, PKN1 and AR.
CC {ECO:0000250, ECO:0000269|PubMed:17115692, ECO:0000269|PubMed:18162466,
CC ECO:0000269|PubMed:20228790}.
CC -!- INTERACTION:
CC P05771; Q8NEM2: SHCBP1; NbExp=3; IntAct=EBI-706216, EBI-744700;
CC P05771; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-706216, EBI-717399;
CC P05771-1; O60341-1: KDM1A; NbExp=2; IntAct=EBI-5774492, EBI-15599570;
CC P05771-2; Q6DHV7-2: ADAL; NbExp=3; IntAct=EBI-5774511, EBI-18899653;
CC P05771-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-5774511, EBI-1383687;
CC P05771-2; Q6ZQX7-4: LIAT1; NbExp=3; IntAct=EBI-5774511, EBI-25830459;
CC P05771-2; O60346: PHLPP1; NbExp=5; IntAct=EBI-5774511, EBI-2511516;
CC P05771-2; Q6ZVD8: PHLPP2; NbExp=2; IntAct=EBI-5774511, EBI-2511496;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:20228790}. Membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Beta-I; Synonyms=PRKCB1;
CC IsoId=P05771-1; Sequence=Displayed;
CC Name=Beta-II; Synonyms=PRKCB2;
CC IsoId=P05771-2; Sequence=VSP_004738;
CC -!- PTM: Phosphorylation on Thr-500 within the activation loop renders it
CC competent to autophosphorylate. Subsequent autophosphorylation of Thr-
CC 642 maintains catalytic competence, and autophosphorylation on Ser-661
CC appears to release the kinase into the cytosol. Autophosphorylation on
CC other sites i.e. in the N-terminal and hinge regions have no effect on
CC enzyme activity. Phosphorylation at Tyr-662 by SYK induces binding with
CC GRB2 and contributes to the activation of MAPK/ERK signaling cascade
CC (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. PKC subfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/prkcb1/";
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DR EMBL; M13975; AAA60095.1; -; mRNA.
DR EMBL; X06318; CAA29634.1; -; mRNA.
DR EMBL; X07109; CAA30130.1; -; mRNA.
DR EMBL; FJ907246; ACS14045.1; -; Genomic_DNA.
DR EMBL; AC130454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC002299; AAB97933.1; -; Genomic_DNA.
DR EMBL; AC002299; AAB97934.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55797.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55798.1; -; Genomic_DNA.
DR EMBL; BC036472; AAH36472.1; -; mRNA.
DR EMBL; X62532; CAA44393.1; -; Genomic_DNA.
DR EMBL; S47311; AAD13852.1; -; Genomic_DNA.
DR EMBL; D10022; BAA00912.1; -; Genomic_DNA.
DR EMBL; AJ002799; CAA05725.1; -; Genomic_DNA.
DR EMBL; AJ002800; CAA05725.1; JOINED; Genomic_DNA.
DR EMBL; M18254; AAA60096.1; -; Genomic_DNA.
DR EMBL; M18255; AAA60097.1; -; Genomic_DNA.
DR EMBL; X05972; CAA29396.1; -; Genomic_DNA.
DR EMBL; X05971; CAA29395.1; -; Genomic_DNA.
DR CCDS; CCDS10618.1; -. [P05771-1]
DR CCDS; CCDS10619.1; -. [P05771-2]
DR PIR; B24664; KIHUC2.
DR PIR; S00159; KIHUC1.
DR RefSeq; NP_002729.2; NM_002738.6. [P05771-2]
DR RefSeq; NP_997700.1; NM_212535.2. [P05771-1]
DR PDB; 2I0E; X-ray; 2.60 A; A/B=321-671.
DR PDBsum; 2I0E; -.
DR AlphaFoldDB; P05771; -.
DR SMR; P05771; -.
DR BioGRID; 111565; 196.
DR DIP; DIP-34187N; -.
DR IntAct; P05771; 144.
DR MINT; P05771; -.
DR STRING; 9606.ENSP00000305355; -.
DR BindingDB; P05771; -.
DR ChEMBL; CHEMBL3045; -.
DR DrugBank; DB14001; alpha-Tocopherol succinate.
DR DrugBank; DB09096; Benzoyl peroxide.
DR DrugBank; DB08862; Cholecystokinin.
DR DrugBank; DB14002; D-alpha-Tocopherol acetate.
DR DrugBank; DB08846; Ellagic acid.
DR DrugBank; DB06486; Enzastaurin.
DR DrugBank; DB01738; Phosphorylcolamine.
DR DrugBank; DB00675; Tamoxifen.
DR DrugBank; DB00163; Vitamin E.
DR DrugCentral; P05771; -.
DR GuidetoPHARMACOLOGY; 1483; -.
DR TCDB; 8.A.104.1.4; the 5'-amp-activated protein kinase (ampk) family.
DR iPTMnet; P05771; -.
DR MetOSite; P05771; -.
DR PhosphoSitePlus; P05771; -.
DR BioMuta; PRKCB; -.
DR DMDM; 20141488; -.
DR CPTAC; CPTAC-1338; -.
DR EPD; P05771; -.
DR jPOST; P05771; -.
DR MassIVE; P05771; -.
DR MaxQB; P05771; -.
DR PaxDb; P05771; -.
DR PeptideAtlas; P05771; -.
DR PRIDE; P05771; -.
DR ProteomicsDB; 51855; -. [P05771-1]
DR ProteomicsDB; 51856; -. [P05771-2]
DR Antibodypedia; 3547; 899 antibodies from 46 providers.
DR DNASU; 5579; -.
DR Ensembl; ENST00000321728.12; ENSP00000318315.7; ENSG00000166501.14. [P05771-1]
DR Ensembl; ENST00000643927.1; ENSP00000496129.1; ENSG00000166501.14. [P05771-2]
DR GeneID; 5579; -.
DR KEGG; hsa:5579; -.
DR MANE-Select; ENST00000643927.1; ENSP00000496129.1; NM_002738.7; NP_002729.2. [P05771-2]
DR UCSC; uc002dmd.4; human. [P05771-1]
DR CTD; 5579; -.
DR DisGeNET; 5579; -.
DR GeneCards; PRKCB; -.
DR HGNC; HGNC:9395; PRKCB.
DR HPA; ENSG00000166501; Tissue enhanced (brain, lymphoid tissue).
DR MIM; 176970; gene.
DR neXtProt; NX_P05771; -.
DR OpenTargets; ENSG00000166501; -.
DR PharmGKB; PA33761; -.
DR VEuPathDB; HostDB:ENSG00000166501; -.
DR eggNOG; KOG0696; Eukaryota.
DR GeneTree; ENSGT00940000155217; -.
DR HOGENOM; CLU_000288_54_2_1; -.
DR InParanoid; P05771; -.
DR OMA; YIAPEXA; -.
DR OrthoDB; 614710at2759; -.
DR PhylomeDB; P05771; -.
DR TreeFam; TF351133; -.
DR BRENDA; 2.7.11.13; 2681.
DR PathwayCommons; P05771; -.
DR Reactome; R-HSA-114516; Disinhibition of SNARE formation.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-HSA-418597; G alpha (z) signalling events.
DR Reactome; R-HSA-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-HSA-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-HSA-5218921; VEGFR2 mediated cell proliferation.
DR Reactome; R-HSA-5668599; RHO GTPases Activate NADPH Oxidases.
DR Reactome; R-HSA-76005; Response to elevated platelet cytosolic Ca2+.
DR Reactome; R-HSA-8939246; RUNX1 regulates transcription of genes involved in differentiation of myeloid cells.
DR SABIO-RK; P05771; -.
DR SignaLink; P05771; -.
DR SIGNOR; P05771; -.
DR BioGRID-ORCS; 5579; 14 hits in 1113 CRISPR screens.
DR ChiTaRS; PRKCB; human.
DR EvolutionaryTrace; P05771; -.
DR GeneWiki; PRKCB1; -.
DR GenomeRNAi; 5579; -.
DR Pharos; P05771; Tchem.
DR PRO; PR:P05771; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; P05771; protein.
DR Bgee; ENSG00000166501; Expressed in middle temporal gyrus and 187 other tissues.
DR ExpressionAtlas; P05771; baseline and differential.
DR Genevisible; P05771; HS.
DR GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0099523; C:presynaptic cytosol; IEA:Ensembl.
DR GO; GO:0008091; C:spectrin; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005246; F:calcium channel regulator activity; IEA:Ensembl.
DR GO; GO:0004698; F:calcium-dependent protein kinase C activity; IEA:UniProtKB-EC.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IDA:UniProtKB.
DR GO; GO:0035403; F:histone kinase activity (H3-T6 specific); IDA:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IMP:UniProtKB.
DR GO; GO:0004697; F:protein kinase C activity; IDA:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; IPI:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0042113; P:B cell activation; ISS:UniProtKB.
DR GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0006816; P:calcium ion transport; IEA:Ensembl.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0071322; P:cellular response to carbohydrate stimulus; IEA:Ensembl.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0042953; P:lipoprotein transport; TAS:BHF-UCL.
DR GO; GO:0007077; P:mitotic nuclear membrane disassembly; TAS:Reactome.
DR GO; GO:0010829; P:negative regulation of glucose transmembrane transport; ISS:UniProtKB.
DR GO; GO:0046627; P:negative regulation of insulin receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045766; P:positive regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0050861; P:positive regulation of B cell receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0030949; P:positive regulation of vascular endothelial growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0043687; P:post-translational protein modification; IDA:UniProtKB.
DR GO; GO:0099171; P:presynaptic modulation of chemical synaptic transmission; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0010827; P:regulation of glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR CDD; cd00029; C1; 2.
DR CDD; cd05616; STKc_cPKC_beta; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR034664; cPKC-beta.
DR InterPro; IPR020454; DAG/PE-bd.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014375; Protein_kinase_C_a/b/g.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00130; C1_1; 2.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00433; Pkinase_C; 1.
DR PIRSF; PIRSF000550; PKC_alpha; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR PRINTS; PR00008; DAGPEDOMAIN.
DR SMART; SM00109; C1; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF57889; SSF57889; 2.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 2.
DR PROSITE; PS50081; ZF_DAG_PE_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Adaptive immunity; Alternative splicing;
KW Apoptosis; ATP-binding; Calcium; Chromatin regulator; Cytoplasm;
KW Direct protein sequencing; Immunity; Kinase; Membrane; Metal-binding;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transcription; Transcription regulation;
KW Transferase; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..671
FT /note="Protein kinase C beta type"
FT /id="PRO_0000055684"
FT DOMAIN 158..275
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 342..600
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 601..671
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT ZN_FING 36..86
FT /note="Phorbol-ester/DAG-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT ZN_FING 101..151
FT /note="Phorbol-ester/DAG-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00226"
FT REGION 311..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..635
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..633
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 466
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 246
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 247
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 251
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 252
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 254
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT BINDING 348..356
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 371
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:12665801"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 16
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403, ECO:0000255"
FT MOD_RES 17
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 250
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 324
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403, ECO:0000255"
FT MOD_RES 500
FT /note="Phosphothreonine; by PDPK1"
FT /evidence="ECO:0000305|PubMed:17115692"
FT MOD_RES 504
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 635
FT /note="Phosphothreonine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P68403"
FT MOD_RES 642
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17115692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 661
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:17115692"
FT MOD_RES 662
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000250|UniProtKB:P68404"
FT VAR_SEQ 622..671
FT /note="RDKRDTSNFDKEFTRQPVELTPTDKLFIMNLDQNEFAGFSYTNPEFVINV
FT -> CGRNAENFDRFFTRHPPVLTPPDQEVIRNIDQSEFEGFSFVNSEFLKPEVKS (in
FT isoform Beta-II)"
FT /evidence="ECO:0000303|PubMed:3666134,
FT ECO:0000303|PubMed:3755548"
FT /id="VSP_004738"
FT VARIANT 144
FT /note="V -> M (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs764534677)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042304"
FT VARIANT 496
FT /note="V -> M (in a glioblastoma multiforme sample; somatic
FT mutation; dbSNP:rs1466858740)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042305"
FT VARIANT 588
FT /note="P -> H (in dbSNP:rs35631544)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042306"
FT CONFLICT 69
FT /note="V -> G (in Ref. 7; CAA44393)"
FT /evidence="ECO:0000305"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:2I0E"
FT STRAND 354..361
FT /evidence="ECO:0007829|PDB:2I0E"
FT STRAND 364..374
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 375..380
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:2I0E"
FT STRAND 406..411
FT /evidence="ECO:0007829|PDB:2I0E"
FT STRAND 413..421
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 428..435
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 440..459
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:2I0E"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:2I0E"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 505..507
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 510..513
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 521..536
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 546..555
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 566..575
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 590..595
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 598..600
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 605..609
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 629..636
FT /evidence="ECO:0007829|PDB:2I0E"
FT HELIX 646..651
FT /evidence="ECO:0007829|PDB:2I0E"
FT TURN 654..657
FT /evidence="ECO:0007829|PDB:2I0E"
FT MOD_RES P05771-2:641
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES P05771-2:660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:24275569"
SQ SEQUENCE 671 AA; 76869 MW; 3937E7B667108C68 CRC64;
MADPAAGPPP SEGEESTVRF ARKGALRQKN VHEVKNHKFT ARFFKQPTFC SHCTDFIWGF
GKQGFQCQVC CFVVHKRCHE FVTFSCPGAD KGPASDDPRS KHKFKIHTYS SPTFCDHCGS
LLYGLIHQGM KCDTCMMNVH KRCVMNVPSL CGTDHTERRG RIYIQAHIDR DVLIVLVRDA
KNLVPMDPNG LSDPYVKLKL IPDPKSESKQ KTKTIKCSLN PEWNETFRFQ LKESDKDRRL
SVEIWDWDLT SRNDFMGSLS FGISELQKAS VDGWFKLLSQ EEGEYFNVPV PPEGSEANEE
LRQKFERAKI SQGTKVPEEK TTNTVSKFDN NGNRDRMKLT DFNFLMVLGK GSFGKVMLSE
RKGTDELYAV KILKKDVVIQ DDDVECTMVE KRVLALPGKP PFLTQLHSCF QTMDRLYFVM
EYVNGGDLMY HIQQVGRFKE PHAVFYAAEI AIGLFFLQSK GIIYRDLKLD NVMLDSEGHI
KIADFGMCKE NIWDGVTTKT FCGTPDYIAP EIIAYQPYGK SVDWWAFGVL LYEMLAGQAP
FEGEDEDELF QSIMEHNVAY PKSMSKEAVA ICKGLMTKHP GKRLGCGPEG ERDIKEHAFF
RYIDWEKLER KEIQPPYKPK ARDKRDTSNF DKEFTRQPVE LTPTDKLFIM NLDQNEFAGF
SYTNPEFVIN V
