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Keratin, type I cytoskeletal 9 (Cytokeratin-9) (CK-9) (Keratin-9) (K9)

 K1C9_HUMAN              Reviewed;         623 AA.
P35527; O00109; Q0IJ47; Q14665;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 3.
25-OCT-2017, entry version 178.
RecName: Full=Keratin, type I cytoskeletal 9;
AltName: Full=Cytokeratin-9;
Short=CK-9;
AltName: Full=Keratin-9;
Short=K9;
Name=KRT9;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
TISSUE SPECIFICITY.
TISSUE=Foot sole tissue;
PubMed=7507869; DOI=10.1111/j.1432-0436.1993.tb00033.x;
Langbein L., Heid H.W., Moll I., Franke W.W.;
"Molecular characterization of the body site-specific human epidermal
cytokeratin 9: cDNA cloning, amino acid sequence, and tissue
specificity of gene expression.";
Differentiation 55:57-72(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS EPPK LYS-161; GLN-163
AND TRP-163.
PubMed=7512862; DOI=10.1038/ng0294-174;
Reis A., Hennies H.-C., Langbein L., Digweed M., Mischke D.,
Dreschler M., Schroek E., Royer-Pokora B., Franke W.W., Sperling K.,
Kuester W.;
"Keratin 9 gene mutations in epidermolytic palmoplantar keratoderma
(EPPK).";
Nat. Genet. 6:174-179(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
PROTEIN SEQUENCE OF 14-29, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Cervix carcinoma;
Bienvenut W.V.;
Submitted (AUG-2005) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 147-372, AND VARIANT EPPK GLN-163.
PubMed=8647270; DOI=10.1016/0014-5793(96)00393-6;
Kobayashi S., Tanaka T., Matsuyoshi N., Imamura S.;
"Keratin 9 point mutation in the pedigree of epidermolytic hereditary
palmoplantar keratoderma perturbs keratin intermediate filament
network formation.";
FEBS Lett. 386:149-155(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-623.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 450-466.
PubMed=2140676; DOI=10.1016/0006-291X(90)91140-N;
Rosen E.M., Meromsky L., Romero R., Setter E., Goldberg I.;
"Human placenta contains an epithelial scatter protein.";
Biochem. Biophys. Res. Commun. 168:1082-1088(1990).
[8]
FUNCTION, AND MUTAGENESIS OF ARG-163.
PubMed=10218578; DOI=10.1016/S0014-5793(99)00233-1;
Kobayashi S., Kore-eda S., Tanaka T.;
"Demonstration of the pathogenic effect of point mutated keratin 9 in
vivo.";
FEBS Lett. 447:39-43(1999).
[9]
INDUCTION.
PubMed=10201533; DOI=10.1046/j.1523-1747.1999.00544.x;
Yamaguchi Y., Itami S., Tarutani M., Hosokawa K., Miura H.,
Yoshikawa K.;
"Regulation of keratin 9 in nonpalmoplantar keratinocytes by
palmoplantar fibroblasts through epithelial-mesenchymal
interactions.";
J. Invest. Dermatol. 112:483-488(1999).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
VARIANTS EPPK VAL-157 AND PRO-172.
PubMed=7516304; DOI=10.1007/BF00201564;
Hennies H.-C., Zehender D., Kunze J., Kuester W., Reis A.;
"Keratin 9 gene mutational heterogeneity in patients with
epidermolytic palmoplantar keratoderma.";
Hum. Genet. 93:649-654(1994).
[15]
VARIANT EPPK SER-161.
PubMed=7523529; DOI=10.1111/1523-1747.ep12395570;
Bonifas J.M., Matsumura K., Chen M.A., Berth-Jones J.,
Hutchinson P.E., Zloczower M., Fritsch P.O., Epstein E.H. Jr.;
"Mutations of keratin 9 in two families with palmoplantar
epidermolytic hyperkeratosis.";
J. Invest. Dermatol. 103:474-477(1994).
[16]
VARIANT EPPK TYR-161.
PubMed=7511021; DOI=10.1038/ng0194-106;
Torchard D., Blanchet-Bardon C., Serova O., Langbein L., Narod S.,
Janin N., Goguel A.F., Bernheim A., Franke W.W., Lenoir G.M.,
Feunteun J.;
"Epidermolytic palmoplantar keratoderma cosegregates with a keratin 9
mutation in a pedigree with breast and ovarian cancer.";
Nat. Genet. 6:106-110(1994).
[17]
VARIANTS EPPK TRP-163 AND SER-168.
PubMed=7532199; DOI=10.1111/1523-1747.ep12666018;
Rothnagel J.A., Wojcik S., Liefer K.M., Dominey A.M., Huber M.,
Hohl D., Roop D.R.;
"Mutations in the 1A domain of keratin 9 in patients with
epidermolytic palmoplantar keratoderma.";
J. Invest. Dermatol. 104:430-433(1995).
[18]
VARIANT EPPK VAL-160.
PubMed=9204965; DOI=10.1111/1523-1747.ep12276751;
Endo H., Hatamochi A., Shinkai H.;
"A novel mutation of a leucine residue in coil 1A of keratin 9 in
epidermolytic palmoplantar keratoderma.";
J. Invest. Dermatol. 109:113-115(1997).
[19]
VARIANTS EPPK THR-157; VAL-157 AND GLN-163.
PubMed=9856842; DOI=10.1046/j.1523-1747.1998.00445.x;
Covello S.P., Irvine A.D., McKenna K.E., Munro C.S., Nevin N.C.,
Smith F.J.D., Uitto J., McLean W.H.I.;
"Mutations in keratin K9 in kindreds with epidermolytic palmoplantar
keratoderma and epidemiology in Northern Ireland.";
J. Invest. Dermatol. 111:1207-1209(1998).
[20]
VARIANTS EPPK GLN-163 AND STOP-170.
PubMed=10632938; DOI=10.1046/j.1525-1470.1999.00111.x;
Szalai S., Szalai C., Becker K., Torok E.;
"Keratin 9 mutations in the coil 1A region in epidermolytic
palmoplantar keratoderma.";
Pediatr. Dermatol. 16:430-435(1999).
[21]
VARIANT EPPK TRP-163.
PubMed=10844507; DOI=10.1046/j.1365-2230.2000.00626.x;
Warmuth I., Cserhalmi-Friedman P.B., Schneiderman P., Grossman M.E.,
Christiano A.M.;
"Epidermolytic palmoplantar keratoderma in a Hispanic kindred
resulting from a mutation in the keratin 9 gene.";
Clin. Exp. Dermatol. 25:244-246(2000).
[22]
VARIANT EPPK ILE-161.
PubMed=12192490; DOI=10.1007/s00403-002-0328-9;
Kuster W., Reis A., Hennies H.C.;
"Epidermolytic palmoplantar keratoderma of Vorner: re-evaluation of
Vorner's original family and identification of a novel keratin 9
mutation.";
Arch. Dermatol. Res. 294:268-272(2002).
[23]
VARIANTS EPPK VAL-157; TRP-163; GLN-163 AND MET-171.
PubMed=12072061; DOI=10.1046/j.1365-2133.2002.04764.x;
Rugg E.L., Common J.E., Wilgoss A., Stevens H.P., Buchan J.,
Leigh I.M., Kelsell D.P.;
"Diagnosis and confirmation of epidermolytic palmoplantar keratoderma
by the identification of mutations in keratin 9 using denaturing high-
performance liquid chromatography.";
Br. J. Dermatol. 146:952-957(2002).
[24]
VARIANT EPPK ILE-161.
PubMed=12926810; DOI=10.1080/00015550310016652;
Csikos M., Hollo P., Becker K., Racz E., Horvath A., Karpati S.;
"Novel N160I mutation of keratin 9 in a large pedigree from Hungary
with epidermolytic palmoplantar keratoderma.";
Acta Derm. Venereol. 83:303-305(2003).
[25]
VARIANT EPPK PHE-160.
PubMed=12838553; DOI=10.1002/ajmg.a.20090;
Lu Y., Guo C., Liu Q., Zhang X., Cheng L., Li J., Chen B., Gao G.,
Zhou H., Guo Y., Li Y., Gong Y.;
"A novel mutation of keratin 9 in epidermolytic palmoplantar
keratoderma combined with knuckle pads.";
Am. J. Med. Genet. A 120:345-349(2003).
[26]
VARIANTS EPPK HIS-161; SER-161 AND TRP-163.
PubMed=14675368; DOI=10.1111/j.0906-6705.2003.00012.x;
Lee J.-H., Ahn K.-S., Lee C.-H., Youn S.-J., Kim J.-W., Lee D.-Y.,
Lee E.-S., Steinert P.M., Yang J.-M.;
"Keratin 9 gene mutations in five Korean families with epidermolytic
palmoplantar keratoderma.";
Exp. Dermatol. 12:876-881(2003).
[27]
VARIANT EPPK TYR-167 DEL TRP-LEU INS.
PubMed=15099359; DOI=10.1111/j.0007-0963.2004.05865.x;
He X.-H., Zhang X.-N., Mao W., Chen H.-P., Xu L.-R., Chen H.,
He X.-L., Le Y.-P.;
"A novel mutation of keratin 9 in a large Chinese family with
epidermolytic palmoplantar keratoderma.";
Br. J. Dermatol. 150:647-651(2004).
[28]
VARIANT EPPK HIS-161.
PubMed=15115518; DOI=10.1111/j.1365-2230.2004.01497.x;
Lin J.-H., Lin M.-H., Yang M.-H., Chao S.-C.;
"A novel keratin 9 gene mutation (Asn160His) in a Taiwanese family
with epidermolytic palmoplantar keratoderma.";
Clin. Exp. Dermatol. 29:308-310(2004).
[29]
VARIANT EPPK PRO-163.
PubMed=15605275; DOI=10.1007/s00403-004-0534-8;
Kon A., Itagaki K., Yoneda K., Takagaki K.;
"A novel mutation of keratin 9 gene (R162P) in a Japanese family with
epidermolytic palmoplantar keratoderma.";
Arch. Dermatol. Res. 296:375-378(2005).
[30]
VARIANT EPPK PHE-458.
PubMed=16911293; DOI=10.1111/j.1365-2133.2006.07358.x;
Kon A., Ito N., Kudo Y., Nomura K., Yoneda K., Hanada K.,
Hashimoto I., Takagaki K.;
"L457F missense mutation within the 2B rod domain of keratin 9 in a
Japanese family with epidermolytic palmoplantar keratoderma.";
Br. J. Dermatol. 155:624-626(2006).
[31]
VARIANT EPPK ARG-157.
PubMed=16961539; DOI=10.1111/j.1365-4632.2006.02910.x;
Shimazu K., Tsunemi Y., Hattori N., Saeki H., Komine M., Adachi M.,
Tamaki K.;
"A novel keratin 9 gene mutation (Met156Arg) in a Japanese patient
with epidermolytic palmoplantar keratoderma.";
Int. J. Dermatol. 45:1128-1130(2006).
[32]
VARIANTS EPPK LYS-157; THR-157; GLN-163 AND HIS-454.
PubMed=19874353; DOI=10.1111/j.1365-2230.2009.03700.x;
Shimomura Y., Wajid M., Weiser J., Kraemer L., Christiano A.M.;
"Mutations in the keratin 9 gene in Pakistani families with
epidermolytic palmoplantar keratoderma.";
Clin. Exp. Dermatol. 35:759-764(2010).
[33]
VARIANT EPPK ARG-406.
PubMed=20964665; DOI=10.1111/j.1365-4632.2009.04295.x;
Wang K., He C.D., Song F., Liu J., Chen H.D.;
"A novel mutation of the keratin 9 gene in a Chinese family with
epidermolytic palmoplantar keratoderma.";
Int. J. Dermatol. 49:1342-1344(2010).
[34]
VARIANT EPPK PRO-458.
PubMed=21715251; DOI=10.1684/ejd.2011.1458;
Du Z.F., Wei W., Wang Y.F., Chen X.L., Chen C.Y., Liu W.T., Lu J.J.,
Mao L.G., Xu C.M., Fang H., Zhang X.N.;
"A novel mutation within the 2B rod domain of keratin 9 in a Chinese
pedigree with epidermolytic palmoplantar keratoderma combined with
knuckle pads and camptodactyly.";
Eur. J. Dermatol. 21:675-679(2011).
-!- FUNCTION: May serve an important special function either in the
mature palmar and plantar skin tissue or in the morphogenetic
program of the formation of these tissues. Plays a role in keratin
filament assembly. {ECO:0000269|PubMed:10218578,
ECO:0000269|PubMed:7507869}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
-!- TISSUE SPECIFICITY: Expressed in the terminally differentiated
epidermis of palms and soles. {ECO:0000269|PubMed:7507869}.
-!- INDUCTION: Induced by intrinsic regulatory mechanisms and by
extrinsic signals from a subset of dermal palmoplantar
fibroblasts. {ECO:0000269|PubMed:10201533}.
-!- DISEASE: Keratoderma, palmoplantar, epidermolytic (EPPK)
[MIM:144200]: A dermatological disorder characterized by diffuse
thickening of the epidermis on the entire surface of palms and
soles sharply bordered with erythematous margins. Some patients
may present knuckle pads, thick pads of skin appearing over the
proximal phalangeal joints. {ECO:0000269|PubMed:10632938,
ECO:0000269|PubMed:10844507, ECO:0000269|PubMed:12072061,
ECO:0000269|PubMed:12192490, ECO:0000269|PubMed:12838553,
ECO:0000269|PubMed:12926810, ECO:0000269|PubMed:14675368,
ECO:0000269|PubMed:15099359, ECO:0000269|PubMed:15115518,
ECO:0000269|PubMed:15605275, ECO:0000269|PubMed:16911293,
ECO:0000269|PubMed:16961539, ECO:0000269|PubMed:19874353,
ECO:0000269|PubMed:20964665, ECO:0000269|PubMed:21715251,
ECO:0000269|PubMed:7511021, ECO:0000269|PubMed:7512862,
ECO:0000269|PubMed:7516304, ECO:0000269|PubMed:7523529,
ECO:0000269|PubMed:7532199, ECO:0000269|PubMed:8647270,
ECO:0000269|PubMed:9204965, ECO:0000269|PubMed:9856842}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin, I (acidic) and II (neutral to basic) (40-
55 and 56-70 kDa, respectively).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-!- CAUTION: Was originally thought to be a 60 kDa chain of placental
scatter protein. {ECO:0000305|PubMed:2140676}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
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EMBL; Z29074; CAA82315.1; -; mRNA.
EMBL; S69510; AAC60619.1; -; mRNA.
EMBL; X75015; CAA52924.1; -; Genomic_DNA.
EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB001594; BAA19418.1; -; mRNA.
EMBL; BC121170; AAI21171.1; -; mRNA.
CCDS; CCDS32654.1; -.
PIR; I37984; I37984.
RefSeq; NP_000217.2; NM_000226.3.
UniGene; Hs.654569; -.
ProteinModelPortal; P35527; -.
SMR; P35527; -.
BioGrid; 110055; 48.
IntAct; P35527; 19.
MINT; MINT-4998976; -.
STRING; 9606.ENSP00000246662; -.
iPTMnet; P35527; -.
PhosphoSitePlus; P35527; -.
SwissPalm; P35527; -.
BioMuta; KRT9; -.
DMDM; 239938886; -.
DOSAC-COBS-2DPAGE; P35527; -.
EPD; P35527; -.
PaxDb; P35527; -.
PeptideAtlas; P35527; -.
PRIDE; P35527; -.
TopDownProteomics; P35527; -.
DNASU; 3857; -.
Ensembl; ENST00000246662; ENSP00000246662; ENSG00000171403.
GeneID; 3857; -.
KEGG; hsa:3857; -.
UCSC; uc002hxe.5; human.
CTD; 3857; -.
DisGeNET; 3857; -.
EuPathDB; HostDB:ENSG00000171403.9; -.
GeneCards; KRT9; -.
H-InvDB; HIX0039018; -.
HGNC; HGNC:6447; KRT9.
MalaCards; KRT9; -.
MIM; 144200; phenotype.
MIM; 149100; phenotype.
MIM; 607606; gene.
neXtProt; NX_P35527; -.
OpenTargets; ENSG00000171403; -.
Orphanet; 2199; Epidermolytic palmoplantar keratoderma.
PharmGKB; PA30235; -.
eggNOG; ENOG410IEYG; Eukaryota.
eggNOG; ENOG4111C5Z; LUCA.
GeneTree; ENSGT00900000140890; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; P35527; -.
KO; K07604; -.
OMA; EMQYETL; -.
OrthoDB; EOG091G087I; -.
PhylomeDB; P35527; -.
TreeFam; TF332742; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GeneWiki; Keratin_9; -.
GenomeRNAi; 3857; -.
PRO; PR:P35527; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000171403; -.
CleanEx; HS_KRT9; -.
ExpressionAtlas; P35527; baseline and differential.
Genevisible; P35527; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0045109; P:intermediate filament organization; IMP:UniProtKB.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0043588; P:skin development; IDA:UniProtKB.
GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 3.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Direct protein sequencing;
Disease mutation; Intermediate filament; Keratin;
Palmoplantar keratoderma; Phosphoprotein; Reference proteome.
CHAIN 1 623 Keratin, type I cytoskeletal 9.
/FTId=PRO_0000063640.
DOMAIN 153 465 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 152 Head.
REGION 153 188 Coil 1A.
REGION 189 207 Linker 1.
REGION 208 299 Coil 1B.
REGION 300 322 Linker 12.
REGION 323 461 Coil 2.
REGION 462 623 Tail.
COMPBIAS 15 26 Poly-Gly.
MOD_RES 14 14 Phosphoserine.
{ECO:0000250|UniProtKB:P13645}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000250|UniProtKB:P13645}.
VARIANT 157 157 M -> K (in EPPK; dbSNP:rs59510579).
{ECO:0000269|PubMed:19874353}.
/FTId=VAR_071977.
VARIANT 157 157 M -> R (in EPPK; dbSNP:rs59510579).
{ECO:0000269|PubMed:16961539}.
/FTId=VAR_036805.
VARIANT 157 157 M -> T (in EPPK; dbSNP:rs59510579).
{ECO:0000269|PubMed:19874353,
ECO:0000269|PubMed:9856842}.
/FTId=VAR_010499.
VARIANT 157 157 M -> V (in EPPK; dbSNP:rs58597584).
{ECO:0000269|PubMed:12072061,
ECO:0000269|PubMed:7516304,
ECO:0000269|PubMed:9856842}.
/FTId=VAR_010500.
VARIANT 160 160 L -> F (in EPPK; with knuckle pads;
dbSNP:rs28940896).
{ECO:0000269|PubMed:12838553}.
/FTId=VAR_035438.
VARIANT 160 160 L -> V (in EPPK; dbSNP:rs28940896).
{ECO:0000269|PubMed:9204965}.
/FTId=VAR_010501.
VARIANT 161 161 N -> H (in EPPK; dbSNP:rs59296273).
{ECO:0000269|PubMed:14675368,
ECO:0000269|PubMed:15115518}.
/FTId=VAR_036806.
VARIANT 161 161 N -> I (in EPPK; dbSNP:rs56707768).
{ECO:0000269|PubMed:12192490,
ECO:0000269|PubMed:12926810}.
/FTId=VAR_036807.
VARIANT 161 161 N -> K (in EPPK; dbSNP:rs57536312).
{ECO:0000269|PubMed:7512862}.
/FTId=VAR_003822.
VARIANT 161 161 N -> S (in EPPK; dbSNP:rs56707768).
{ECO:0000269|PubMed:14675368,
ECO:0000269|PubMed:7523529}.
/FTId=VAR_010502.
VARIANT 161 161 N -> Y (in EPPK; dbSNP:rs59296273).
{ECO:0000269|PubMed:7511021}.
/FTId=VAR_010503.
VARIANT 163 163 R -> P (in EPPK; dbSNP:rs57758262).
{ECO:0000269|PubMed:15605275}.
/FTId=VAR_036808.
VARIANT 163 163 R -> Q (in EPPK; dbSNP:rs57758262).
{ECO:0000269|PubMed:10632938,
ECO:0000269|PubMed:12072061,
ECO:0000269|PubMed:19874353,
ECO:0000269|PubMed:7512862,
ECO:0000269|PubMed:8647270,
ECO:0000269|PubMed:9856842}.
/FTId=VAR_003823.
VARIANT 163 163 R -> W (in EPPK; dbSNP:rs59616921).
{ECO:0000269|PubMed:10844507,
ECO:0000269|PubMed:12072061,
ECO:0000269|PubMed:14675368,
ECO:0000269|PubMed:7512862,
ECO:0000269|PubMed:7532199}.
/FTId=VAR_003824.
VARIANT 167 167 Y -> WL (in EPPK).
/FTId=VAR_036809.
VARIANT 168 168 L -> S (in EPPK; dbSNP:rs61157095).
{ECO:0000269|PubMed:7532199}.
/FTId=VAR_003825.
VARIANT 171 171 V -> M (in EPPK; dbSNP:rs57019720).
{ECO:0000269|PubMed:12072061}.
/FTId=VAR_035439.
VARIANT 172 172 Q -> P (in EPPK; dbSNP:rs59878153).
{ECO:0000269|PubMed:7516304}.
/FTId=VAR_010504.
VARIANT 406 406 C -> R (in EPPK; dbSNP:rs77688767).
{ECO:0000269|PubMed:20964665}.
/FTId=VAR_071978.
VARIANT 454 454 Y -> H (in EPPK; dbSNP:rs267607420).
{ECO:0000269|PubMed:19874353}.
/FTId=VAR_071979.
VARIANT 458 458 L -> F (in EPPK; dbSNP:rs58120120).
{ECO:0000269|PubMed:16911293}.
/FTId=VAR_036810.
VARIANT 458 458 L -> P (in EPPK).
{ECO:0000269|PubMed:21715251}.
/FTId=VAR_071980.
MUTAGEN 163 163 R->QHA: Leads to aggregate formation.
{ECO:0000269|PubMed:10218578}.
CONFLICT 12 13 SR -> T (in Ref. 1; AAC60619 and 2;
CAA52924). {ECO:0000305}.
CONFLICT 41 41 G -> R (in Ref. 1; AAC60619/CAA82315 and
2; CAA52924). {ECO:0000305}.
CONFLICT 134 134 F -> L (in Ref. 1; AAC60619/CAA82315 and
2; CAA52924). {ECO:0000305}.
CONFLICT 157 170 MQELNSRLASYLDK -> HLGAGSTPITASQP (in Ref.
6; AAI21171). {ECO:0000305}.
SEQUENCE 623 AA; 62064 MW; 45C833749B63873D CRC64;
MSCRQFSSSY LSRSGGGGGG GLGSGGSIRS SYSRFSSSGG GGGGGRFSSS SGYGGGSSRV
CGRGGGGSFG YSYGGGSGGG FSASSLGGGF GGGSRGFGGA SGGGYSSSGG FGGGFGGGSG
GGFGGGYGSG FGGFGGFGGG AGGGDGGILT ANEKSTMQEL NSRLASYLDK VQALEEANND
LENKIQDWYD KKGPAAIQKN YSPYYNTIDD LKDQIVDLTV GNNKTLLDID NTRMTLDDFR
IKFEMEQNLR QGVDADINGL RQVLDNLTME KSDLEMQYET LQEELMALKK NHKEEMSQLT
GQNSGDVNVE INVAPGKDLT KTLNDMRQEY EQLIAKNRKD IENQYETQIT QIEHEVSSSG
QEVQSSAKEV TQLRHGVQEL EIELQSQLSK KAALEKSLED TKNRYCGQLQ MIQEQISNLE
AQITDVRQEI ECQNQEYSLL LSIKMRLEKE IETYHNLLEG GQEDFESSGA GKIGLGGRGG
SGGSYGRGSR GGSGGSYGGG GSGGGYGGGS GSRGGSGGSY GGGSGSGGGS GGGYGGGSGG
GHSGGSGGGH SGGSGGNYGG GSGSGGGSGG GYGGGSGSRG GSGGSHGGGS GFGGESGGSY
GGGEEASGSG GGYGGGSGKS SHS


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