PEPL_HUMAN
ID PEPL_HUMAN Reviewed; 1756 AA.
AC O60437; O60314; O60454; Q14C98;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Periplakin;
DE AltName: Full=190 kDa paraneoplastic pemphigus antigen;
DE AltName: Full=195 kDa cornified envelope precursor protein;
GN Name=PPL; Synonyms=KIAA0568;
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], FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INDUCTION, INTERACTION WITH EVPL, AND VARIANTS GLN-589 AND
RP SER-819.
RC TISSUE=Keratinocyte;
RX PubMed=9412476; DOI=10.1083/jcb.139.7.1835;
RA Ruhrberg C., Hajibagheri M.A.N., Parry D.A.D., Watt F.M.;
RT "Periplakin, a novel component of cornified envelopes and desmosomes that
RT belongs to the plakin family and forms complexes with envoplakin.";
RL J. Cell Biol. 139:1835-1849(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT SER-819.
RC TISSUE=Keratinocyte;
RX PubMed=9521878; DOI=10.1006/geno.1997.5188;
RA Aho S., McLean W.H.I., Li K., Uitto J.;
RT "cDNA cloning, mRNA expression, and chromosomal mapping of human and mouse
RT periplakin genes.";
RL Genomics 48:242-247(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT SER-819.
RX PubMed=10051401; DOI=10.1006/geno.1998.5704;
RA Aho S., Rothenberger K., Tan E.M.L., Ryoo Y.W., Cho B.H., McLean W.H.I.,
RA Uitto J.;
RT "Human periplakin: genomic organization in a clonally unstable region of
RT chromosome 16p with an abundance of repetitive sequence elements.";
RL Genomics 56:160-168(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLN-589;
RP SER-819 AND GLU-1573.
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], AND VARIANTS GLN-589; SER-819 AND
RP GLU-1573.
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 [LARGE SCALE MRNA] OF 331-1756, AND VARIANTS GLN-589;
RP SER-819 AND GLU-1573.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [8]
RP INTERACTION WITH AKT1.
RC TISSUE=Embryo;
RX PubMed=12244133; DOI=10.1242/jcs.00069;
RA van den Heuvel A.P., de Vries-Smits A.M.M., van Weeren P.C., Dijkers P.F.,
RA de Bruyn K.M., Riedl J.A., Burgering B.M.T.;
RT "Binding of protein kinase B to the plakin family member periplakin.";
RL J. Cell Sci. 115:3957-3966(2002).
RN [9]
RP INTERACTION WITH PPHLN1, AND DEVELOPMENTAL STAGE.
RX PubMed=12853457; DOI=10.1074/jbc.m303896200;
RA Kazerounian S., Aho S.;
RT "Characterization of periphilin, a widespread, highly insoluble nuclear
RT protein and potential constituent of the keratinocyte cornified envelope.";
RL J. Biol. Chem. 278:36707-36717(2003).
RN [10]
RP INTERACTION WITH FCGR1A.
RX PubMed=15229321; DOI=10.1073/pnas.0401217101;
RA Beekman J.M., Bakema J.E., van de Winkel J.G.J., Leusen J.H.W.;
RT "Direct interaction between FcgammaRI (CD64) and periplakin controls
RT receptor endocytosis and ligand binding capacity.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10392-10397(2004).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-887 AND SER-1657, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-1657, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465; SER-949; SER-1584 AND
RP SER-1657, 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).
CC -!- FUNCTION: Component of the cornified envelope of keratinocytes. May
CC link the cornified envelope to desmosomes and intermediate filaments.
CC May act as a localization signal in PKB/AKT-mediated signaling.
CC {ECO:0000269|PubMed:9412476}.
CC -!- SUBUNIT: Homodimer or a heterodimer with EVPL (PubMed:9412476). Found
CC in a complex composed of PPL (via C-terminal linker domain), BFSP1 and
CC BFSP2 in the retinal lens (By similarity). Within the complex interacts
CC (via C-terminal linker domain) with BFSP2 (By similarity). Interacts
CC with VIM (By similarity). Binds to the PH domain of AKT1
CC (PubMed:12244133). Interacts with FCGR1A (PubMed:15229321). May
CC interact with PPHLN1 (PubMed:12853457). {ECO:0000250|UniProtKB:Q9R269,
CC ECO:0000269|PubMed:12244133, ECO:0000269|PubMed:12853457,
CC ECO:0000269|PubMed:15229321, ECO:0000269|PubMed:9412476}.
CC -!- INTERACTION:
CC O60437; Q9H9F9: ACTR5; NbExp=3; IntAct=EBI-368321, EBI-769418;
CC O60437; O43865: AHCYL1; NbExp=3; IntAct=EBI-368321, EBI-2371423;
CC O60437; P31749: AKT1; NbExp=2; IntAct=EBI-368321, EBI-296087;
CC O60437; P13196: ALAS1; NbExp=6; IntAct=EBI-368321, EBI-3905054;
CC O60437; O76027: ANXA9; NbExp=6; IntAct=EBI-368321, EBI-720960;
CC O60437; O00481: BTN3A1; NbExp=6; IntAct=EBI-368321, EBI-2809309;
CC O60437; O00481-2: BTN3A1; NbExp=5; IntAct=EBI-368321, EBI-14033666;
CC O60437; Q5SZD1: C6orf141; NbExp=3; IntAct=EBI-368321, EBI-10697767;
CC O60437; Q8IYX8-2: CEP57L1; NbExp=3; IntAct=EBI-368321, EBI-10181988;
CC O60437; P17661: DES; NbExp=3; IntAct=EBI-368321, EBI-1055572;
CC O60437; Q5T447: HECTD3; NbExp=3; IntAct=EBI-368321, EBI-2691157;
CC O60437; P42858: HTT; NbExp=8; IntAct=EBI-368321, EBI-466029;
CC O60437; Q13422-7: IKZF1; NbExp=3; IntAct=EBI-368321, EBI-11522367;
CC O60437; Q4G0X4: KCTD21; NbExp=3; IntAct=EBI-368321, EBI-11976683;
CC O60437; Q9Y448: KNSTRN; NbExp=3; IntAct=EBI-368321, EBI-373334;
CC O60437; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-368321, EBI-11980019;
CC O60437; Q6A163: KRT39; NbExp=4; IntAct=EBI-368321, EBI-11958242;
CC O60437; Q13084: MRPL28; NbExp=3; IntAct=EBI-368321, EBI-723426;
CC O60437; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-368321, EBI-10302990;
CC O60437; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-368321, EBI-79165;
CC O60437; Q6IQ23-2: PLEKHA7; NbExp=3; IntAct=EBI-368321, EBI-12069346;
CC O60437; Q8WVV4-1: POF1B; NbExp=3; IntAct=EBI-368321, EBI-11986735;
CC O60437; Q96QF0: RAB3IP; NbExp=3; IntAct=EBI-368321, EBI-747844;
CC O60437; Q96QF0-7: RAB3IP; NbExp=3; IntAct=EBI-368321, EBI-11984839;
CC O60437; Q15311: RALBP1; NbExp=5; IntAct=EBI-368321, EBI-749285;
CC O60437; Q12933: TRAF2; NbExp=6; IntAct=EBI-368321, EBI-355744;
CC O60437; P14373: TRIM27; NbExp=3; IntAct=EBI-368321, EBI-719493;
CC O60437; Q9Y3Q8: TSC22D4; NbExp=3; IntAct=EBI-368321, EBI-739485;
CC O60437; Q96BW1: UPRT; NbExp=3; IntAct=EBI-368321, EBI-742943;
CC O60437; P08670: VIM; NbExp=3; IntAct=EBI-368321, EBI-353844;
CC O60437; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-368321, EBI-3918996;
CC O60437; P49910: ZNF165; NbExp=3; IntAct=EBI-368321, EBI-741694;
CC O60437; O14771: ZNF213; NbExp=3; IntAct=EBI-368321, EBI-12838388;
CC O60437; O14978: ZNF263; NbExp=3; IntAct=EBI-368321, EBI-744493;
CC O60437; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-368321, EBI-17269964;
CC O60437; Q8NBB4: ZSCAN1; NbExp=3; IntAct=EBI-368321, EBI-5292994;
CC O60437; Q8NBB4-2: ZSCAN1; NbExp=3; IntAct=EBI-368321, EBI-12021938;
CC O60437; Q9H4T2: ZSCAN16; NbExp=3; IntAct=EBI-368321, EBI-723596;
CC -!- SUBCELLULAR LOCATION: Cell junction, desmosome
CC {ECO:0000269|PubMed:9412476}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:9412476}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9R269}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9R269}.
CC -!- TISSUE SPECIFICITY: Expressed in stratified squamous epithelia and in
CC some other epithelia. {ECO:0000269|PubMed:9412476,
CC ECO:0000269|PubMed:9521878}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the epidermis, nuclei of dermal
CC fibroblasts, cell periphery of flattened keratinocytes, and dermal and
CC epithelial cells lining the excretory ducts of the sweat glands in
CC neonatal foreskin. {ECO:0000269|PubMed:12853457}.
CC -!- INDUCTION: During differentiation of epidermal keratinocytes.
CC {ECO:0000269|PubMed:9412476}.
CC -!- SIMILARITY: Belongs to the plakin or cytolinker family. {ECO:0000305}.
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DR EMBL; AF001691; AAC17738.1; -; mRNA.
DR EMBL; AF013717; AAC39668.1; -; mRNA.
DR EMBL; AF041004; AAD17459.1; -; Genomic_DNA.
DR EMBL; AF040999; AAD17459.1; JOINED; Genomic_DNA.
DR EMBL; AF041000; AAD17459.1; JOINED; Genomic_DNA.
DR EMBL; AF041002; AAD17459.1; JOINED; Genomic_DNA.
DR EMBL; AF041003; AAD17459.1; JOINED; Genomic_DNA.
DR EMBL; AC027687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471112; EAW85248.1; -; Genomic_DNA.
DR EMBL; BC114620; AAI14621.1; -; mRNA.
DR EMBL; AB011140; BAA25494.1; -; mRNA.
DR CCDS; CCDS10526.1; -.
DR PIR; T00337; T00337.
DR RefSeq; NP_002696.3; NM_002705.4.
DR PDB; 4Q28; X-ray; 2.64 A; A/B/C/D=1655-1756.
DR PDBsum; 4Q28; -.
DR AlphaFoldDB; O60437; -.
DR SMR; O60437; -.
DR BioGRID; 111488; 181.
DR IntAct; O60437; 66.
DR MINT; O60437; -.
DR STRING; 9606.ENSP00000340510; -.
DR iPTMnet; O60437; -.
DR PhosphoSitePlus; O60437; -.
DR SwissPalm; O60437; -.
DR BioMuta; PPL; -.
DR EPD; O60437; -.
DR jPOST; O60437; -.
DR MassIVE; O60437; -.
DR MaxQB; O60437; -.
DR PaxDb; O60437; -.
DR PeptideAtlas; O60437; -.
DR PRIDE; O60437; -.
DR ProteomicsDB; 49402; -.
DR Antibodypedia; 24458; 194 antibodies from 25 providers.
DR DNASU; 5493; -.
DR Ensembl; ENST00000345988.7; ENSP00000340510.2; ENSG00000118898.16.
DR GeneID; 5493; -.
DR KEGG; hsa:5493; -.
DR MANE-Select; ENST00000345988.7; ENSP00000340510.2; NM_002705.5; NP_002696.4.
DR UCSC; uc002cyd.1; human.
DR CTD; 5493; -.
DR DisGeNET; 5493; -.
DR GeneCards; PPL; -.
DR HGNC; HGNC:9273; PPL.
DR HPA; ENSG00000118898; Tissue enhanced (esophagus, vagina).
DR MIM; 602871; gene.
DR neXtProt; NX_O60437; -.
DR OpenTargets; ENSG00000118898; -.
DR PharmGKB; PA33602; -.
DR VEuPathDB; HostDB:ENSG00000118898; -.
DR eggNOG; KOG0516; Eukaryota.
DR GeneTree; ENSGT00940000153578; -.
DR InParanoid; O60437; -.
DR OMA; CADIERQ; -.
DR OrthoDB; 35436at2759; -.
DR PhylomeDB; O60437; -.
DR TreeFam; TF342779; -.
DR PathwayCommons; O60437; -.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR Reactome; R-HSA-8851680; Butyrophilin (BTN) family interactions.
DR SignaLink; O60437; -.
DR BioGRID-ORCS; 5493; 23 hits in 1076 CRISPR screens.
DR ChiTaRS; PPL; human.
DR GeneWiki; Periplakin; -.
DR GenomeRNAi; 5493; -.
DR Pharos; O60437; Tbio.
DR PRO; PR:O60437; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; O60437; protein.
DR Bgee; ENSG00000118898; Expressed in oral cavity and 182 other tissues.
DR ExpressionAtlas; O60437; baseline and differential.
DR Genevisible; O60437; HS.
DR GO; GO:0001533; C:cornified envelope; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030057; C:desmosome; IEA:UniProtKB-SubCell.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
DR GO; GO:0005198; F:structural molecule activity; IBA:GO_Central.
DR GO; GO:0045104; P:intermediate filament cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0031424; P:keratinization; IEA:UniProtKB-KW.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:BHF-UCL.
DR GO; GO:0042060; P:wound healing; IBA:GO_Central.
DR InterPro; IPR041615; Desmoplakin_SH3.
DR InterPro; IPR043197; Plakin.
DR InterPro; IPR035915; Plakin_repeat_sf.
DR InterPro; IPR001101; Plectin_repeat.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR PANTHER; PTHR23169; PTHR23169; 1.
DR Pfam; PF17902; SH3_10; 1.
DR SMART; SM00250; PLEC; 2.
DR SMART; SM00150; SPEC; 5.
DR SUPFAM; SSF75399; SSF75399; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Keratinization; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; SH3 domain.
FT CHAIN 1..1756
FT /note="Periplakin"
FT /id="PRO_0000078149"
FT REPEAT 216..317
FT /note="Spectrin 1"
FT REPEAT 323..485
FT /note="Spectrin 2"
FT DOMAIN 399..455
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REPEAT 505..612
FT /note="Spectrin 3"
FT REPEAT 733..861
FT /note="Spectrin 4"
FT REPEAT 1651..1685
FT /note="Plectin 1"
FT REPEAT 1700..1735
FT /note="Plectin 2"
FT REGION 1557..1756
FT /note="Interacts with BFSP2 and VIM"
FT /evidence="ECO:0000250|UniProtKB:Q9R269"
FT COILED 16..125
FT /evidence="ECO:0000255"
FT COILED 188..389
FT /evidence="ECO:0000255"
FT COILED 585..820
FT /evidence="ECO:0000255"
FT COILED 886..1645
FT /evidence="ECO:0000255"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 887
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 949
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1584
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VARIANT 520
FT /note="R -> Q (in dbSNP:rs8063727)"
FT /id="VAR_055125"
FT VARIANT 572
FT /note="A -> S (in dbSNP:rs35300633)"
FT /id="VAR_055126"
FT VARIANT 589
FT /note="R -> Q (in dbSNP:rs1049205)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9412476, ECO:0000269|PubMed:9628581,
FT ECO:0000269|Ref.5"
FT /id="VAR_055127"
FT VARIANT 631
FT /note="H -> Y (in dbSNP:rs34936263)"
FT /id="VAR_055128"
FT VARIANT 819
FT /note="R -> S (in dbSNP:rs2734742)"
FT /evidence="ECO:0000269|PubMed:10051401,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9412476,
FT ECO:0000269|PubMed:9521878, ECO:0000269|PubMed:9628581,
FT ECO:0000269|Ref.5"
FT /id="VAR_055129"
FT VARIANT 891
FT /note="E -> Q (in dbSNP:rs35869286)"
FT /id="VAR_055130"
FT VARIANT 1007
FT /note="A -> V (in dbSNP:rs2075639)"
FT /id="VAR_055131"
FT VARIANT 1199
FT /note="E -> Q (in dbSNP:rs12446946)"
FT /id="VAR_055132"
FT VARIANT 1573
FT /note="Q -> E (in dbSNP:rs2037912)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9628581, ECO:0000269|Ref.5"
FT /id="VAR_055133"
FT VARIANT 1754
FT /note="G -> R (in dbSNP:rs35865314)"
FT /id="VAR_055134"
FT CONFLICT 657
FT /note="A -> P (in Ref. 2; AAC39668 and 3; AAD17459)"
FT /evidence="ECO:0000305"
FT CONFLICT 994
FT /note="V -> F (in Ref. 1; AAC17738)"
FT /evidence="ECO:0000305"
FT CONFLICT 1663
FT /note="P -> L (in Ref. 1; AAC17738)"
FT /evidence="ECO:0000305"
FT STRAND 1655..1661
FT /evidence="ECO:0007829|PDB:4Q28"
FT TURN 1663..1665
FT /evidence="ECO:0007829|PDB:4Q28"
FT HELIX 1671..1676
FT /evidence="ECO:0007829|PDB:4Q28"
FT HELIX 1682..1689
FT /evidence="ECO:0007829|PDB:4Q28"
FT STRAND 1693..1701
FT /evidence="ECO:0007829|PDB:4Q28"
FT STRAND 1706..1712
FT /evidence="ECO:0007829|PDB:4Q28"
FT TURN 1713..1716
FT /evidence="ECO:0007829|PDB:4Q28"
FT STRAND 1717..1721
FT /evidence="ECO:0007829|PDB:4Q28"
FT HELIX 1722..1726
FT /evidence="ECO:0007829|PDB:4Q28"
FT HELIX 1732..1739
FT /evidence="ECO:0007829|PDB:4Q28"
FT HELIX 1745..1753
FT /evidence="ECO:0007829|PDB:4Q28"
SQ SEQUENCE 1756 AA; 204747 MW; EA7EAF3E756D78B4 CRC64;
MNSLFRKRNK GKYSPTVQTR SISNKELSEL IEQLQKNADQ VEKNIVDTEA KMQSDLARLQ
EGRQPEHRDV TLQKVLDSEK LLYVLEADAA IAKHMKHPQG DMIAEDIRQL KERVTNLRGK
HKQIYRLAVK EVDPQVNWAA LVEEKLDKLN NQSFGTDLPL VDHQVEEHNI FHNEVKAIGP
HLAKDGDKEQ NSELRAKYQK LLAASQARQQ HLSSLQDYMQ RCTNELYWLD QQAKGRMQYD
WSDRNLDYPS RRRQYENFIN RNLEAKEERI NKLHSEGDQL LAAEHPGRNS IEAHMEAVHA
DWKEYLNLLI CEESHLKYME DYHQFHEDVK DAQELLRKVD SDLNQKYGPD FKDRYQIELL
LRELDDQEKV LDKYEDVVQG LQKRGQQVVP LKYRRETPLK PIPVEALCDF EGEQGLISRG
YSYTLQKNNG ESWELMDSAG NKLIAPAVCF VIPPTDPEAL ALADSLGSQY RSVRQKAAGS
KRTLQQRYEV LKTENPGDAS DLQGRQLLAG LDKVASDLDR QEKAITGILR PPLEQGRAVQ
DSAERAKDLK NITNELLRIE PEKTRSTAEG EAFIQALPGS GTTPLLRTRV EDTNRKYEHL
LQLLDLAQEK VDVANRLEKS LQQSWELLAT HENHLNQDDT VPESSRVLDS KGQELAAMAC
ELQAQKSLLG EVEQNLQAAK QCSSTLASRF QEHCPDLERQ EAEVHKLGQR FNNLRQQVER
RAQSLQSAKA AYEHFHRGHD HVLQFLVSIP SYEPQETDSL SQMETKLKNQ KNLLDEIASR
EQEVQKICAN SQQYQQAVKD YELEAEKLRS LLDLENGRRS HVSKRARLQS PATKVKEEEA
ALAAKFTEVY AINRQRLQNL EFALNLLRQQ PEVEVTHETL QRNRPDSGVE EAWKIRKELD
EETERRRQLE NEVKSTQEEI WTLRNQGPQE SVVRKEVLKK VPDPVLEESF QQLQRTLAEE
QHKNQLLQEE LEALQLQLRA LEQETRDGGQ EYVVKEVLRI EPDRAQADEV LQLREELEAL
RRQKGAREAE VLLLQQRVAA LAEEKSRAQE KVTEKEVVKL QNDPQLEAEY QQLQEDHQRQ
DQLREKQEEE LSFLQDKLKR LEKERAMAEG KITVKEVLKV EKDAATEREV SDLTRQYEDE
AAKARASQRE KTELLRKIWA LEEENAKVVV QEKVREIVRP DPKAESEVAN LRLELVEQER
KYRGAEEQLR SYQSELEALR RRGPQVEVKE VTKEVIKYKT DPEMEKELQR LREEIVDKTR
LIERCDLEIY QLKKEIQALK DTKPQVQTKE VVQEILQFQE DPQTKEEVAS LRAKLSEEQK
KQVDLERERA SQEEQIARKE EELSRVKERV VQQEVVRYEE EPGLRAEASA FAESIDVELR
QIDKLRAELR RLQRRRTELE RQLEELERER QARREAEREV QRLQQRLAAL EQEEAEAREK
VTHTQKVVLQ QDPQQAREHA LLRLQLEEEQ HRRQLLEGEL ETLRRKLAAL EKAEVKEKVV
LSESVQVEKG DTEQEIQRLK SSLEEESRSK RELDVEVSRL EARLSELEFH NSKSSKELDF
LREENHKLQL ERQNLQLETR RLQSEINMAA TETRDLRNMT VADSGTNHDS RLWSLERELD
DLKRLSKDKD LEIDELQKRL GSVAVKREQR ENHLRRSIVV IHPDTGRELS PEEAHRAGLI
DWNMFVKLRS QECDWEEISV KGPNGESSVI HDRKSGKKFS IEEALQSGRL TPAQYDRYVN
KDMSIQELAV LVSGQK
