[1]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY. TISSUE=Foot sole tissue; PubMed=7507869 [NCBI, ExPASy, EBI, Israel, Japan] 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. DOI=10.1038/ng0294-174; PubMed=7512862 [NCBI, ExPASy, EBI, Israel, Japan] 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]	PROTEIN SEQUENCE OF 14-29, AND MASS SPECTROMETRY. TISSUE=Cervix carcinoma; Bienvenut W.V.; Submitted (AUG-2005) to UniProtKB.
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 147-372, AND VARIANT EPPK GLN-163. DOI=10.1016/0014-5793(96)00393-6; PubMed=8647270 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-623. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	PROTEIN SEQUENCE OF 450-466. DOI=10.1016/0006-291X(90)91140-N; PubMed=2140676 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	FUNCTION, AND MUTAGENESIS OF ARG-163. DOI=10.1016/S0014-5793(99)00233-1; PubMed=10218578 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	INDUCTION. DOI=10.1046/j.1523-1747.1999.00544.x; PubMed=10201533 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	VARIANTS EPPK VAL-157 AND PRO-172. DOI=10.1007/BF00201564; PubMed=7516304 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[10]	VARIANT EPPK SER-161. DOI=10.1111/1523-1747.ep12395570; PubMed=7523529 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	VARIANT EPPK TYR-161. DOI=10.1038/ng0194-106; PubMed=7511021 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[12]	VARIANTS EPPK TRP-163 AND SER-168. DOI=10.1111/1523-1747.ep12666018; PubMed=7532199 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	VARIANT EPPK VAL-160. DOI=10.1111/1523-1747.ep12276751; PubMed=9204965 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[14]	VARIANTS EPPK THR-157; VAL-157 AND GLN-163. DOI=10.1046/j.1523-1747.1998.00445.x; PubMed=9856842 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	VARIANTS EPPK GLN-163 AND STOP-170. DOI=10.1046/j.1525-1470.1999.00111.x; PubMed=10632938 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	VARIANT EPPK TRP-163. DOI=10.1046/j.1365-2230.2000.00626.x; PubMed=10844507 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	VARIANT EPPK ILE-161. DOI=10.1007/s00403-002-0328-9; PubMed=12192490 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[18]	VARIANTS EPPK VAL-157; TRP-163; GLN-163 AND MET-171. DOI=10.1046/j.1365-2133.2002.04764.x; PubMed=12072061 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	VARIANT EPPK ILE-161. DOI=10.1080/00015550310016652; PubMed=12926810 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	VARIANT EPPK PHE-160. DOI=10.1002/ajmg.a.20090; PubMed=12838553 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	VARIANTS EPPK HIS-161; SER-161 AND TRP-163. DOI=10.1111/j.0906-6705.2003.00012.x; PubMed=14675368 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	VARIANT EPPK TYR-167 DEL TRP-LEU INS. DOI=10.1111/j.0007-0963.2004.05865.x; PubMed=15099359 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	VARIANT EPPK HIS-161. DOI=10.1111/j.1365-2230.2004.01497.x; PubMed=15115518 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[24]	VARIANT EPPK PRO-163. DOI=10.1007/s00403-004-0534-8; PubMed=15605275 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[25]	VARIANT EPPK PHE-458. DOI=10.1111/j.1365-2133.2006.07358.x; PubMed=16911293 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[26]	VARIANT EPPK ARG-157. DOI=10.1111/j.1365-4632.2006.02910.x; PubMed=16961539 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

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.
SUBUNIT: Heterotetramer of two type I and two type II keratins.
INTERACTION:
Q00987:MDM2; NbExp=1; IntAct=EBI-356382, EBI-389668;
TISSUE SPECIFICITY: Expressed in the terminally differentiated epidermis of palms and soles.
INDUCTION: Induced by intrinsic regulatory mechanisms and by extrinsic signals from a subset of dermal palmoplantar fibroblasts.
DISEASE: Defects in KRT9 are a cause of palmoplantar keratoderma epidermolytic (EPPK) [MIM:144200]; also abbreviated EHPPK. EPPK is a dermatological disorder characterized by diffuse thickening of the epidermis on the entire surface of palms and soles sharply bordered with erythematous margins.
DISEASE: Knuckle pads are sometimes associated with EPPK [MIM:149100]. Knuckle pads consist of an autosomal dominant trait, in which thick pads of skin appear over the proximal phalangeal joints.
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.
CAUTION: Was originally (PubMed:2140676) thought to be a 60 kDa chain of placental scatter protein.
WEB RESOURCE: Name=Human Intermediate Filament Mutation Database; URL="http://www.interfil.org";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=KRT9";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Z29074; CAA82315.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S69510; AAC60619.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X75015; CAA52924.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB001594; BAA19418.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC121170; AAI21171.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

I37984; I37984.

UniGene

Hs.654569

3D structure databases

HSSP

P08670; 1GK7. [HSSP ENTRY / PDB]

ModBase

P35527.

Protein-protein interaction databases

IntAct

P35527; -.

PTM databases

PhosphoSite

P35527; -.

2D gel databases

DOSAC-COBS-2DPAGE

P35527; -.

Organism-specific databases

HIX0039018; -.

HGNC:6447; KRT9.

HPA007261; -.
HPA009673; -.

MIM

144200; phenotype. [NCBI / EBI]
149100; phenotype. [NCBI / EBI]
607606; gene. [NCBI / EBI]

Orphanet

2199; Hyperkeratosis palmoplantar, localized, epidermolytic.

PharmGKB

PA30235; -.

GeneCards

P35527.

Gene expression databases

ArrayExpress

P35527; -.

CleanEx

HS_KRT9; -.

GermOnline

ENSG00000171403; Homo sapiens.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0005200;	Molecular function: structural constituent of cytoskeleton (traceable author statement from ProtInc).
GO:0045109;	Biological process: intermediate filament organization (inferred from mutant phenotype from UniProtKB).
GO:0043588;	Biological process: skin development (inferred from direct assay from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR016044; F.
IPR001664; IF.
IPR002957; Keratin_I.
Graphical view of domain structure.

PANTHER

PTHR23239; IF; 1.

Pfam

PF00038; Filament; 1.
Pfam graphical view of domain structure.

PRINTS

PR01248; TYPE1KERATIN.

PS00226; IF; 1.

Proteomic databases

P35527; -.

Genome annotation databases

Ensembl

ENSG00000171403; Homo sapiens. [Contig view]

Phylogenomic databases

HOGENOM

P35527; -.

HOVERGEN

P35527; -.

Other

KRT9; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Coiled coil; Direct protein sequencing; Disease mutation; Intermediate filament; Keratin.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 623`	`623`	`Keratin, type I cytoskeletal 9.`	`PRO_0000063640`
`REGION`	`1 152`	`152`	`Head.`
`REGION`	`153 461`	`309`	`Rod.`
`REGION`	`153 188`	`36`	`Coil 1A.`
`REGION`	`189 207`	`19`	`Linker 1.`
`REGION`	`208 299`	`92`	`Coil 1B.`
`REGION`	`300 322`	`23`	`Linker 12.`
`REGION`	`323 461`	`139`	`Coil 2.`
`REGION`	`462 623`	`162`	`Tail.`
`COMPBIAS`	`15 26`	`12`	`Poly-Gly.`
`VARIANT`	`157 157`	`1`	`M -> R (in EPPK).`	`VAR_036805`
`VARIANT`	`157 157`	`1`	`M -> T (in EPPK).`	`VAR_010499`
`VARIANT`	`157 157`	`1`	`M -> V (in EPPK).`	`VAR_010500`
`VARIANT`	`160 160`	`1`	`L -> F (in EPPK; with knuckle pads).`	`VAR_035438`
`VARIANT`	`160 160`	`1`	`L -> V (in EPPK).`	`VAR_010501`
`VARIANT`	`161 161`	`1`	`N -> H (in EPPK).`	`VAR_036806`
`VARIANT`	`161 161`	`1`	`N -> I (in EPPK).`	`VAR_036807`
`VARIANT`	`161 161`	`1`	`N -> K (in EPPK).`	`VAR_003822`
`VARIANT`	`161 161`	`1`	`N -> S (in EPPK).`	`VAR_010502`
`VARIANT`	`161 161`	`1`	`N -> Y (in EPPK).`	`VAR_010503`
`VARIANT`	`163 163`	`1`	`R -> P (in EPPK).`	`VAR_036808`
`VARIANT`	`163 163`	`1`	`R -> Q (in EPPK).`	`VAR_003823`
`VARIANT`	`163 163`	`1`	`R -> W (in EPPK).`	`VAR_003824`
`VARIANT`	`167 167`	`1`	`Y -> WL (in EPPK).`	`VAR_036809`
`VARIANT`	`168 168`	`1`	`L -> S (in EPPK).`	`VAR_003825`
`VARIANT`	`171 171`	`1`	`V -> M (in EPPK).`	`VAR_035439`
`VARIANT`	`172 172`	`1`	`Q -> P (in EPPK).`	`VAR_010504`
`VARIANT`	`458 458`	`1`	`L -> F (in EPPK).`	`VAR_036810`
`MUTAGEN`	`163 163`		`R->QHA: Leads to aggregate formation.`
`CONFLICT`	`12 13`		`SR -> T (in Ref. 1; AAC60619 and 2; CAA52924).`
`CONFLICT`	`157 170`		`MQELNSRLASYLDK -> HLGAGSTPITASQP (in Ref. 5; AAI21171).`

Sequence information

Length: 623 AA [This is the length of the unprocessed precursor]

Molecular weight: 62129 Da [This is the MW of the unprocessed precursor]

CRC64: DE1D5A462FF96D10 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSCRQFSSSY LSRSGGGGGG GLGSGGSIRS SYSRFSSSGG RGGGGRFSSS SGYGGGSSRV 

        70         80         90        100        110        120 
CGRGGGGSFG YSYGGGSGGG FSASSLGGGF GGGSRGFGGA SGGGYSSSGG FGGGFGGGSG 

       130        140        150        160        170        180 
GGFGGGYGSG FGGLGGFGGG AGGGDGGILT ANEKSTMQEL NSRLASYLDK VQALEEANND 

       190        200        210        220        230        240 
LENKIQDWYD KKGPAAIQKN YSPYYNTIDD LKDQIVDLTV GNNKTLLDID NTRMTLDDFR 

       250        260        270        280        290        300 
IKFEMEQNLR QGVDADINGL RQVLDNLTME KSDLEMQYET LQEELMALKK NHKEEMSQLT 

       310        320        330        340        350        360 
GQNSGDVNVE INVAPGKDLT KTLNDMRQEY EQLIAKNRKD IENQYETQIT QIEHEVSSSG 

       370        380        390        400        410        420 
QEVQSSAKEV TQLRHGVQEL EIELQSQLSK KAALEKSLED TKNRYCGQLQ MIQEQISNLE 

       430        440        450        460        470        480 
AQITDVRQEI ECQNQEYSLL LSIKMRLEKE IETYHNLLEG GQEDFESSGA GKIGLGGRGG 

       490        500        510        520        530        540 
SGGSYGRGSR GGSGGSYGGG GSGGGYGGGS GSRGGSGGSY GGGSGSGGGS GGGYGGGSGG 

       550        560        570        580        590        600 
GHSGGSGGGH SGGSGGNYGG GSGSGGGSGG GYGGGSGSRG GSGGSHGGGS GFGGESGGSY 

       610        620 
GGGEEASGSG GGYGGGSGKS SHS

P35527 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools