ID   KPBB_HUMAN              Reviewed;        1093 AA.
AC   Q93100; Q8N4T5;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 207.
DE   RecName: Full=Phosphorylase b kinase regulatory subunit beta;
DE            Short=Phosphorylase kinase subunit beta;
GN   Name=PHKB;
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 [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX   PubMed=8681948; DOI=10.1111/j.1432-1033.1996.0374z.x;
RA   Wuellrich-Schmoll A., Kilimann M.W.;
RT   "Structure of the human gene encoding the phosphorylase kinase beta subunit
RT   (PHKB).";
RL   Eur. J. Biochem. 238:374-380(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Uterus;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
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   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2 (ISOFORMS 2 AND 4),
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4 (ISOFORMS 2 AND 4),
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 2),
RP   CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 4), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [8]
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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11]
RP   VARIANT CYS-770.
RX   PubMed=9326319; DOI=10.1086/515502;
RA   van den Berg I.E.T., van Beurden E.A.C.M., de Klerk J.B.C.,
RA   van Diggelen O.P., Malingre H.E.M., Boer M.M., Berger R.;
RT   "Autosomal recessive phosphorylase kinase deficiency in liver, caused by
RT   mutations in the gene encoding the beta subunit (PHKB).";
RL   Am. J. Hum. Genet. 61:539-546(1997).
RN   [12]
RP   VARIANT GSD9B PRO-118.
RX   PubMed=9402963; DOI=10.1007/s004390050608;
RA   Burwinkel B., Moses S.W., Kilimann M.W.;
RT   "Phosphorylase-kinase-deficient liver glycogenosis with an unusual
RT   biochemical phenotype in blood cells associated with a missense mutation in
RT   the beta subunit gene (PHKB).";
RL   Hum. Genet. 101:170-174(1997).
RN   [13]
RP   VARIANTS LYS-657 AND CYS-770.
RX   PubMed=12825073; DOI=10.1038/sj.ejhg.5200996;
RA   Burwinkel B., Hu B., Schroers A., Clemens P.R., Moses S.W., Shin Y.S.,
RA   Pongratz D., Vorgerd M., Kilimann M.W.;
RT   "Muscle glycogenosis with low phosphorylase kinase activity: mutations in
RT   PHKA1, PHKG1 or six other candidate genes explain only a minority of
RT   cases.";
RL   Eur. J. Hum. Genet. 11:516-526(2003).
RN   [14]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-867 AND ARG-877.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Phosphorylase b kinase catalyzes the phosphorylation of
CC       serine in certain substrates, including troponin I. The beta chain acts
CC       as a regulatory unit and modulates the activity of the holoenzyme in
CC       response to phosphorylation.
CC   -!- ACTIVITY REGULATION: By phosphorylation of various serine residues.
CC       {ECO:0000250}.
CC   -!- PATHWAY: Glycan biosynthesis; glycogen metabolism.
CC   -!- SUBUNIT: Hexadecamer of 4 heterotetramers, each composed of alpha,
CC       beta, gamma, and delta subunits. Alpha (PHKA1 or PHKA2) and beta (PHKB)
CC       are regulatory subunits, gamma (PHKG1 or PHKG2) is the catalytic
CC       subunit, and delta is calmodulin.
CC   -!- INTERACTION:
CC       Q93100; Q13554: CAMK2B; NbExp=3; IntAct=EBI-740559, EBI-1058722;
CC       Q93100; Q96RG2: PASK; NbExp=2; IntAct=EBI-740559, EBI-1042651;
CC       Q93100-4; P46019: PHKA2; NbExp=3; IntAct=EBI-11064505, EBI-1642846;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q93100-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q93100-2; Sequence=VSP_012445;
CC       Name=3;
CC         IsoId=Q93100-3; Sequence=VSP_012446;
CC       Name=4;
CC         IsoId=Q93100-4; Sequence=VSP_012445, VSP_012446;
CC   -!- PTM: Ser-701 is probably phosphorylated by PKA.
CC   -!- PTM: Although the final Cys may be farnesylated, the terminal
CC       tripeptide is probably not removed, and the C-terminus is not
CC       methylated. {ECO:0000250|UniProtKB:P12798}.
CC   -!- DISEASE: Glycogen storage disease 9B (GSD9B) [MIM:261750]: A metabolic
CC       disorder characterized by hepatomegaly, only slightly elevated
CC       transaminases and plasma lipids, clinical improvement with increasing
CC       age, and remarkably no clinical muscle involvement. Biochemical
CC       observations suggest that this mild phenotype is caused by an
CC       incomplete holoenzyme that lacks the beta subunit, but that may possess
CC       residual activity. {ECO:0000269|PubMed:9402963}. Note=The disease is
CC       caused by variants affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the phosphorylase b kinase regulatory chain
CC       family. {ECO:0000305}.
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DR   EMBL; X84909; CAA59333.1; -; Genomic_DNA.
DR   EMBL; X84911; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84912; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84913; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84914; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84915; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84916; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84917; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84918; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84919; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84920; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84921; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84922; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84923; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84924; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84925; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84926; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84927; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84928; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84929; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84930; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84931; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84933; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84934; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84935; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84936; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84937; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84938; CAA59333.1; JOINED; Genomic_DNA.
DR   EMBL; X84908; CAA59332.1; -; mRNA.
DR   EMBL; BC033657; AAH33657.1; -; mRNA.
DR   CCDS; CCDS10729.1; -. [Q93100-1]
DR   CCDS; CCDS42161.1; -. [Q93100-4]
DR   CCDS; CCDS92152.1; -. [Q93100-3]
DR   PIR; S74250; S74250.
DR   PIR; S74251; S74251.
DR   RefSeq; NP_000284.1; NM_000293.2. [Q93100-1]
DR   RefSeq; NP_001027005.1; NM_001031835.2. [Q93100-4]
DR   RefSeq; XP_005256040.1; XM_005255983.4.
DR   RefSeq; XP_005256041.1; XM_005255984.4.
DR   AlphaFoldDB; Q93100; -.
DR   BioGRID; 111275; 61.
DR   CORUM; Q93100; -.
DR   IntAct; Q93100; 20.
DR   MINT; Q93100; -.
DR   STRING; 9606.ENSP00000313504; -.
DR   ChEMBL; CHEMBL2111324; -.
DR   iPTMnet; Q93100; -.
DR   PhosphoSitePlus; Q93100; -.
DR   SwissPalm; Q93100; -.
DR   BioMuta; PHKB; -.
DR   DMDM; 2499582; -.
DR   EPD; Q93100; -.
DR   jPOST; Q93100; -.
DR   MassIVE; Q93100; -.
DR   MaxQB; Q93100; -.
DR   PaxDb; 9606-ENSP00000313504; -.
DR   PeptideAtlas; Q93100; -.
DR   ProteomicsDB; 75726; -. [Q93100-1]
DR   ProteomicsDB; 75727; -. [Q93100-2]
DR   ProteomicsDB; 75728; -. [Q93100-3]
DR   ProteomicsDB; 75729; -. [Q93100-4]
DR   Pumba; Q93100; -.
DR   Antibodypedia; 28116; 206 antibodies from 29 providers.
DR   DNASU; 5257; -.
DR   Ensembl; ENST00000299167.12; ENSP00000299167.8; ENSG00000102893.18. [Q93100-3]
DR   Ensembl; ENST00000323584.10; ENSP00000313504.5; ENSG00000102893.18. [Q93100-1]
DR   Ensembl; ENST00000566044.5; ENSP00000456729.1; ENSG00000102893.18. [Q93100-4]
DR   GeneID; 5257; -.
DR   KEGG; hsa:5257; -.
DR   MANE-Select; ENST00000323584.10; ENSP00000313504.5; NM_000293.3; NP_000284.1.
DR   UCSC; uc002eeu.5; human. [Q93100-1]
DR   AGR; HGNC:8927; -.
DR   CTD; 5257; -.
DR   DisGeNET; 5257; -.
DR   GeneCards; PHKB; -.
DR   GeneReviews; PHKB; -.
DR   HGNC; HGNC:8927; PHKB.
DR   HPA; ENSG00000102893; Tissue enhanced (skeletal).
DR   MalaCards; PHKB; -.
DR   MIM; 172490; gene.
DR   MIM; 261750; phenotype.
DR   neXtProt; NX_Q93100; -.
DR   OpenTargets; ENSG00000102893; -.
DR   Orphanet; 79240; Glycogen storage disease due to liver and muscle phosphorylase kinase deficiency.
DR   PharmGKB; PA33268; -.
DR   VEuPathDB; HostDB:ENSG00000102893; -.
DR   eggNOG; KOG3635; Eukaryota.
DR   GeneTree; ENSGT00950000183118; -.
DR   HOGENOM; CLU_004177_0_1_1; -.
DR   InParanoid; Q93100; -.
DR   OMA; CWIKQAH; -.
DR   OrthoDB; 3640971at2759; -.
DR   PhylomeDB; Q93100; -.
DR   TreeFam; TF313970; -.
DR   BioCyc; MetaCyc:HS02424-MONOMER; -.
DR   BRENDA; 2.7.11.19; 2681.
DR   PathwayCommons; Q93100; -.
DR   Reactome; R-HSA-70221; Glycogen breakdown (glycogenolysis).
DR   SignaLink; Q93100; -.
DR   UniPathway; UPA00163; -.
DR   BioGRID-ORCS; 5257; 9 hits in 1153 CRISPR screens.
DR   ChiTaRS; PHKB; human.
DR   GeneWiki; PHKB; -.
DR   GenomeRNAi; 5257; -.
DR   Pharos; Q93100; Tbio.
DR   PRO; PR:Q93100; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q93100; Protein.
DR   Bgee; ENSG00000102893; Expressed in adrenal tissue and 212 other cell types or tissues.
DR   ExpressionAtlas; Q93100; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005964; C:phosphorylase kinase complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; TAS:ProtInc.
DR   GO; GO:0005977; P:glycogen metabolic process; TAS:ProtInc.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR011613; GH15-like.
DR   InterPro; IPR045583; KPBA/B_C.
DR   InterPro; IPR008734; PHK_A/B_su.
DR   PANTHER; PTHR10749; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT; 1.
DR   PANTHER; PTHR10749:SF8; PHOSPHORYLASE B KINASE REGULATORY SUBUNIT BETA; 1.
DR   Pfam; PF00723; Glyco_hydro_15; 1.
DR   Pfam; PF19292; KPBB_C; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
DR   Genevisible; Q93100; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Calmodulin-binding;
KW   Carbohydrate metabolism; Cell membrane; Disease variant;
KW   Glycogen metabolism; Glycogen storage disease; Lipoprotein; Membrane;
KW   Phosphoprotein; Prenylation; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:P12798"
FT   CHAIN           2..1093
FT                   /note="Phosphorylase b kinase regulatory subunit beta"
FT                   /id="PRO_0000057736"
FT   REGION          7..29
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          689..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..795
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          920..951
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        697..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P12798"
FT   MOD_RES         12
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P12798"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         701
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P12798"
FT   LIPID           1090
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P12798"
FT   VAR_SEQ         1..23
FT                   /note="MAGAAGLTAEVSWKVLERRARTK -> MACSPDAVVSPSSAFL (in
FT                   isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012445"
FT   VAR_SEQ         780..806
FT                   /note="LAVRYGAAFTQKFSSSIAPHITTFLVH -> SVVRRAASLLSKVVDSLAPSI
FT                   TNVLVQ (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_012446"
FT   VARIANT         118
FT                   /note="A -> P (in GSD9B; dbSNP:rs121918022)"
FT                   /evidence="ECO:0000269|PubMed:9402963"
FT                   /id="VAR_015536"
FT   VARIANT         657
FT                   /note="Q -> K (in dbSNP:rs34667348)"
FT                   /evidence="ECO:0000269|PubMed:12825073"
FT                   /id="VAR_020857"
FT   VARIANT         770
FT                   /note="Y -> C (in dbSNP:rs16945474)"
FT                   /evidence="ECO:0000269|PubMed:12825073,
FT                   ECO:0000269|PubMed:9326319"
FT                   /id="VAR_006187"
FT   VARIANT         820
FT                   /note="E -> V (in dbSNP:rs9934849)"
FT                   /id="VAR_034056"
FT   VARIANT         867
FT                   /note="L -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036486"
FT   VARIANT         877
FT                   /note="G -> R (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs150902092)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036487"
FT   INIT_MET        Q93100-2:1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         Q93100-2:2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         Q93100-2:4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   INIT_MET        Q93100-4:1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         Q93100-4:2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         Q93100-4:4
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
SQ   SEQUENCE   1093 AA;  124884 MW;  48F05EE306195472 CRC64;
     MAGAAGLTAE VSWKVLERRA RTKRSGSVYE PLKSINLPRP DNETLWDKLD HYYRIVKSTL
     LLYQSPTTGL FPTKTCGGDQ KAKIQDSLYC AAGAWALALA YRRIDDDKGR THELEHSAIK
     CMRGILYCYM RQADKVQQFK QDPRPTTCLH SVFNVHTGDE LLSYEEYGHL QINAVSLYLL
     YLVEMISSGL QIIYNTDEVS FIQNLVFCVE RVYRVPDFGV WERGSKYNNG STELHSSSVG
     LAKAALEAIN GFNLFGNQGC SWSVIFVDLD AHNRNRQTLC SLLPRESRSH NTDAALLPCI
     SYPAFALDDE VLFSQTLDKV VRKLKGKYGF KRFLRDGYRT SLEDPNRCYY KPAEIKLFDG
     IECEFPIFFL YMMIDGVFRG NPKQVQEYQD LLTPVLHHTT EGYPVVPKYY YVPADFVEYE
     KNNPGSQKRF PSNCGRDGKL FLWGQALYII AKLLADELIS PKDIDPVQRY VPLKDQRNVS
     MRFSNQGPLE NDLVVHVALI AESQRLQVFL NTYGIQTQTP QQVEPIQIWP QQELVKAYLQ
     LGINEKLGLS GRPDRPIGCL GTSKIYRILG KTVVCYPIIF DLSDFYMSQD VFLLIDDIKN
     ALQFIKQYWK MHGRPLFLVL IREDNIRGSR FNPILDMLAA LKKGIIGGVK VHVDRLQTLI
     SGAVVEQLDF LRISDTEELP EFKSFEELEP PKHSKVKRQS STPSAPELGQ QPDVNISEWK
     DKPTHEILQK LNDCSCLASQ AILLGILLKR EGPNFITKEG TVSDHIERVY RRAGSQKLWL
     AVRYGAAFTQ KFSSSIAPHI TTFLVHGKQV TLGAFGHEEE VISNPLSPRV IQNIIYYKCN
     THDEREAVIQ QELVIHIGWI ISNNPELFSG MLKIRIGWII HAMEYELQIR GGDKPALDLY
     QLSPSEVKQL LLDILQPQQN GRCWLNRRQI DGSLNRTPTG FYDRVWQILE RTPNGIIVAG
     KHLPQQPTLS DMTMYEMNFS LLVEDTLGNI DQPQYRQIVV ELLMVVSIVL ERNPELEFQD
     KVDLDRLVKE AFNEFQKDQS RLKEIEKQDD MTSFYNTPPL GKRGTCSYLT KAVMNLLLEG
     EVKPNNDDPC LIS
//