[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Foreskin; PubMed=2459124 [NCBI, ExPASy, EBI, Israel, Japan] Zhou X.M., Idler W.W., Steven A.C., Roop D.R., Steinert P.M.; "The complete sequence of the human intermediate filament chain keratin 10. Subdomainal divisions and model for folding of end domain sequences."; J. Biol. Chem. 263:15584-15589(1988).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1016/0022-2836(88)90045-9; PubMed=2464696 [NCBI, ExPASy, EBI, Israel, Japan] Rieger M., Franke W.W.; "Identification of an orthologous mammalian cytokeratin gene. High degree of intron sequence conservation during evolution of human cytokeratin 10."; J. Mol. Biol. 204:841-856(1988).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Skin; 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).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 130-593. DOI=10.1007/BF00444680; PubMed=2448602 [NCBI, ExPASy, EBI, Israel, Japan] Darmon M.Y., Semat A., Darmon M.C., Vasseur M.; "Sequence of a cDNA encoding human keratin No 10 selected according to structural homologies of keratins and their tissue-specific expression."; Mol. Biol. Rep. 12:277-283(1987).
[5]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, AND VARIANTS BCIE HIS-156 AND ASN-160. DOI=10.1111/1523-1747.ep12371723; PubMed=7507150 [NCBI, ExPASy, EBI, Israel, Japan] Rothnagel J.A., Longley M.A., Holder R.A., Kuster W., Roop D.R.; "Prenatal diagnosis of epidermolytic hyperkeratosis by direct gene sequencing."; J. Invest. Dermatol. 102:13-16(1994).
[6]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, AND VARIANT BCIE CYS-156. Rothnagel J.J., Dominey A., Fisher M., Axtell S., Pittelkow M., Anton-Lamprecht I., Hohl D., Roop D.; "Identification of mutational hot spots in the suprabasal keratin genes from patients with epidermolytic hyperkeratosis."; Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [MRNA] OF 197-593. DOI=10.1016/0378-1119(92)90521-P; PubMed=1378806 [NCBI, ExPASy, EBI, Israel, Japan] Tkachenko A.V., Buchman V.L., Bliskovsky V.V., Shvets Y.P., Kisselev L.L.; "Exons I and VII of the gene (Ker10) encoding human keratin 10 undergo structural rearrangements within repeats."; Gene 116:245-251(1992).
[8]	PROTEIN SEQUENCE OF 180-184 AND 577-589. TISSUE=Keratinocyte; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan] Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.; "Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."; Electrophoresis 13:960-969(1992).
[9]	VARIANT BCIE HIS-156. DOI=10.1016/0092-8674(92)90314-3; PubMed=1381287 [NCBI, ExPASy, EBI, Israel, Japan] Cheng J., Syder A.J., Yu Q.-C., Letai A., Paller A.S., Fuchs E.; "The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes."; Cell 70:811-819(1992).
[10]	VARIANTS. PubMed=1371013 [NCBI, ExPASy, EBI, Israel, Japan] Korge B.P., Gan S.-Q., McBridge O.W., Mischke D., Steinert P.M.; "Extensive size polymorphism of the human keratin 10 chain resides in the C-terminal V2 subdomain due to variable numbers and sizes of glycine loops."; Proc. Natl. Acad. Sci. U.S.A. 89:910-914(1992).
[11]	VARIANTS BCIE HIS-156 AND SER-161. PubMed=1380725 [NCBI, ExPASy, EBI, Israel, Japan] Rothnagel J.A., Dominey A.M., Dempsey L.D., Longley M.A., Greenhalgh D.A., Gagne T.A., Huber M., Frenk E., Hohl D., Roop D.R.; "Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis."; Science 257:1128-1130(1992).
[12]	VARIANTS BCIE HIS-154; CYS-156; HIS-156; ASP-160 AND GLN-442. PubMed=7508181 [NCBI, ExPASy, EBI, Israel, Japan] Chipev C.C., Yang J.-M., Digiovanna J.J., Steinert P.M., Marekov L., Compton J.G., Bale S.J.; "Preferential sites in keratin 10 that are mutated in epidermolytic hyperkeratosis."; Am. J. Hum. Genet. 54:179-190(1994).
[13]	VARIANTS BCIE ARG-150; CYS-156 AND GLU-439, AND VARIANT SER-126. PubMed=7512983 [NCBI, ExPASy, EBI, Israel, Japan] Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E.; "Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity."; J. Clin. Invest. 93:1533-1542(1994).
[14]	VARIANTS BCIE PRO-156 AND SER-156. DOI=10.1111/1523-1747.ep12371726; PubMed=7507152 [NCBI, ExPASy, EBI, Israel, Japan] McLean W.H.I., Eady R.A.J., Dopping-Hepenstal P.J.C., McMillan J.R., Leigh I.M., Navsaria H.A., Higgins C., Harper J.I., Paige D.G., Morley S.M.; "Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital ichthyosiform erythroderma (BCIE)."; J. Invest. Dermatol. 102:24-30(1994).
[15]	VARIANT EPIDERMAL NEVUS EPIDERMOLYTIC HYPERKERATOTIC TYPE THR-150. DOI=10.1056/NEJM199411243312103; PubMed=7526210 [NCBI, ExPASy, EBI, Israel, Japan] Paller A.S., Syder A.J., Chan Y.-M., Yu Q.-C., Hutton M.E., Tadini G., Fuchs E.; "Genetic and clinical mosaicism in a type of epidermal nevus."; N. Engl. J. Med. 331:1408-1415(1994).
[16]	VARIANT AEI GLU-422. DOI=10.1111/1523-1747.ep12286491; PubMed=9036939 [NCBI, ExPASy, EBI, Israel, Japan] Joh G.-Y., Traupe H., Metze D., Nashan D., Huber M., Hohl D., Longley M.A., Rothnagel J.A., Roop D.R.; "A novel dinucleotide mutation in keratin 10 in the annular epidermolytic ichthyosis variant of bullous congenital ichthyosiform erythroderma."; J. Invest. Dermatol. 108:357-361(1997).
[17]	VARIANT AEI THR-446. DOI=10.1046/j.1523-1747.1998.00451.x; PubMed=9856845 [NCBI, ExPASy, EBI, Israel, Japan] Suga Y., Duncan K.O., Heald P.W., Roop D.R.; "A novel helix termination mutation in keratin 10 in annular epidermolytic ichthyosis, a variant of bullous congenital ichthyosiform erythroderma."; J. Invest. Dermatol. 111:1220-1223(1998).
[18]	VARIANT BCIE SER-160. DOI=10.1046/j.1523-1747.1999.00557.x; PubMed=10201536 [NCBI, ExPASy, EBI, Israel, Japan] Arin M.J., Longley M.A., Anton-Lamprecht I., Kurze G., Huber M., Hohl D., Rothnagel J.A., Roop D.R.; "A novel substitution in keratin 10 in epidermolytic hyperkeratosis."; J. Invest. Dermatol. 112:506-508(1999).

Comments

SUBUNIT: Heterotetramer of two type I and two type II keratins. keratin-10 is generally associated with keratin-1.
INTERACTION:
Q00987:MDM2; NbExp=1; IntAct=EBI-465144, EBI-389668;
TISSUE SPECIFICITY: Seen in all suprabasal cell layers including stratum corneum.
POLYMORPHISM: A number of alleles are known that mainly differ in the Gly-rich region (positions 490-560).
DISEASE: Defects in KRT10 are a cause of bullous congenital ichthyosiform erythroderma (BCIE) [MIM:113800]; also known as epidermolytic hyperkeratosis (EHK) or bullous erythroderma ichthyosiformis congenita of Brocq. BCIE is an autosomal dominant skin disorder characterized by widespread blistering and an ichthyotic erythroderma at birth that persist into adulthood. Histologically there is a diffuse epidermolytic degeneration in the lower spinous layer of the epidermis. Within a few weeks from birth, erythroderma and blister formation diminish and hyperkeratoses develop.
DISEASE: Defects in KRT10 are a cause of ichthyosis annular epidermolytic (AEI) [MIM:607602]; also known as cyclic ichthyosis with epidermolytic hyperkeratosis. AEI is a skin disorder resembling bullous congenital ichthyosiform erythroderma. Affected individuals present with bullous ichthyosis in early childhood and hyperkeratotic lichenified plaques in the flexural areas and extensor surfaces at later ages. The feature that distinguishes AEI from BCIE is dramatic episodes of flares of annular polycyclic plaques with scale, which coalesce to involve most of the body surface and can persist for several weeks or even months.
DISEASE: Defects in KRT10 are a cause of epidermal nevus epidermolytic hyperkeratotic type [MIM:600648]. Epidermal nevi affect about 1 in 1,000 people. They appear at or shortly after birth as localized lines of epidermal thickening. The extent of skin involvement varies widely.
MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
SIMILARITY: Belongs to the intermediate filament family.
WEB RESOURCE: Name=Human Intermediate Filament Mutation Database; URL="http://www.interfil.org";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=KRT10";.
WEB RESOURCE: Name=Wikipedia; Note=Keratin-10 entry; URL="http://en.wikipedia.org/wiki/Keratin_10";.

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

J04029; AAA60544.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X14487; CAA32649.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC034697; AAH34697.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M19156; AAA59468.1; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M77663; AAA59199.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L20218; AAB59438.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L20219; AAB59439.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A31994; A31994.
S02158; KRHU0.

RefSeq

NP_000412.2; -.

UniGene

Hs.99936

3D structure databases

HSSP

P08670; 1GK7. [HSSP ENTRY / PDB]

ModBase

P13645.

Protein-protein interaction databases

IntAct

P13645; -.

PTM databases

PhosphoSite

P13645; -.

2D gel databases

SWISS-2DPAGE

P13645; -.

Aarhus/Ghent-2DPAGE

7405; IEF.

REPRODUCTION-2DPAGE

P13645; -.

Organism-specific databases

HGNC:6413; KRT10.

KRT10; Homo sapiens.

CAB000132; -.

113800; phenotype. [NCBI / EBI]
148080; gene. [NCBI / EBI]
600648; phenotype. [NCBI / EBI]
607602; phenotype. [NCBI / EBI]

Orphanet

312; Bullous ichthyosiform erythroderma congenita.
313; Lamellar ichthyosis.

PharmGKB

PA30200; -.

GeneCards

P13645.

Gene expression databases

ArrayExpress

P13645; -.

CleanEx

HS_KRT10; -.

GermOnline

ENSG00000186395; Homo sapiens.

Ontologies

GO:0005882;	Cellular component: intermediate filament (non-traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0030280;	Molecular function: structural constituent of epidermis (non-traceable author statement from UniProtKB).
GO:0008544;	Biological process: epidermis development (traceable author statement from ProtInc).
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

P13645; -.

Genome annotation databases

Ensembl

ENSG00000186395; Homo sapiens. [Contig view]

GeneID

3858; -.

KEGG

hsa:3858; -.

Phylogenomic databases

HOGENOM

P13645; -.

HOVERGEN

P13645; -.

Other

KRT10; Homo sapiens.

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 593`	`593`	`Keratin, type I cytoskeletal 10.`	`PRO_0000063642`
`REGION`	`1 145`	`145`	`Head.`
`REGION`	`146 456`	`311`	`Rod.`
`REGION`	`146 181`	`36`	`Coil 1A.`
`REGION`	`182 202`	`21`	`Linker 1.`
`REGION`	`203 294`	`92`	`Coil 1B.`
`REGION`	`295 317`	`23`	`Linker 12.`
`REGION`	`318 456`	`139`	`Coil 2.`
`REGION`	`457 593`	`137`	`Tail.`
`COMPBIAS`	`6 144`	`139`	`Gly/Phe/Ser-rich.`
`COMPBIAS`	`451 590`	`140`	`Gly/Ser-rich.`
`VARIANT`	`126 126`	`1`	`G -> S.`	`VAR_010505`
`VARIANT`	`150 150`	`1`	`M -> R (in BCIE).`	`VAR_010506`
`VARIANT`	`150 150`	`1`	`M -> T (in epidermal nevus epidermolytic hyperkeratotic type).`	`VAR_010507`
`VARIANT`	`154 154`	`1`	`N -> H (in BCIE).`	`VAR_003826`
`VARIANT`	`156 156`	`1`	`R -> C (in BCIE).`	`VAR_003828`
`VARIANT`	`156 156`	`1`	`R -> H (in BCIE).`	`VAR_003827`
`VARIANT`	`156 156`	`1`	`R -> P (in BCIE).`	`VAR_003829`
`VARIANT`	`156 156`	`1`	`R -> S (in BCIE).`	`VAR_003830`
`VARIANT`	`160 160`	`1`	`Y -> D (in BCIE; severe phenotype).`	`VAR_003831`
`VARIANT`	`160 160`	`1`	`Y -> N (in BCIE; severe phenotype).`	`VAR_010508`
`VARIANT`	`160 160`	`1`	`Y -> S (in BCIE; severe phenotype).`	`VAR_010509`
`VARIANT`	`161 161`	`1`	`L -> S (in BCIE).`	`VAR_003832`
`VARIANT`	`422 422`	`1`	`R -> E (in AEI; requires 2 nucleotide substitutions).`	`VAR_033145`
`VARIANT`	`439 439`	`1`	`K -> E (in BCIE; mild phenotype).`	`VAR_010510`
`VARIANT`	`442 442`	`1`	`L -> Q (in BCIE).`	`VAR_003833`
`VARIANT`	`446 446`	`1`	`I -> T (in AEI).`	`VAR_010511`
`CONFLICT`	`9 11`		`KHY -> SKQF (in Ref. 1; AAA60544).`
`CONFLICT`	`24 31`		`Missing (in Ref. 1; AAA60544).`
`CONFLICT`	`86 86`		`R -> H (in Ref. 2; CAA32649).`
`CONFLICT`	`106 106`		`S -> N (in Ref. 2; CAA32649).`
`CONFLICT`	`181 184`		`WYEK -> RYDQ (in Ref. 1; AAA60544).`
`CONFLICT`	`189 189`		`H -> R (in Ref. 1; AAA60544).`
`CONFLICT`	`197 197`		`S -> G (in Ref. 7; AAA59199).`
`CONFLICT`	`266 266`		`K -> Q (in Ref. 1; AAA60544).`
`CONFLICT`	`279 280`		`EL -> YV (in Ref. 4; AAA59468).`
`CONFLICT`	`287 287`		`H -> R (in Ref. 1; AAA60544).`
`CONFLICT`	`293 293`		`D -> H (in Ref. 1; AAA60544).`
`CONFLICT`	`312 312`		`V -> I (in Ref. 4; AAA59468).`
`CONFLICT`	`323 323`		`S -> N (in Ref. 1; AAA60544).`
`CONFLICT`	`340 340`		`F -> V (in Ref. 4; AAA59468).`
`CONFLICT`	`374 374`		`A -> R (in Ref. 4; AAA59468).`
`CONFLICT`	`408 408`		`Q -> H (in Ref. 2; CAA32649).`
`CONFLICT`	`420 420`		`Q -> E (in Ref. 1; AAA60544).`
`CONFLICT`	`436 436`		`L -> T (in Ref. 1; AAA60544).`
`CONFLICT`	`451 451`		`S -> G (in Ref. 7; AAA59199).`
`CONFLICT`	`460 461`		`GG -> RS (in Ref. 4; AAA59468).`
`CONFLICT`	`477 477`		`S -> T (in Ref. 4; AAA59468).`
`CONFLICT`	`482 482`		`S -> T (in Ref. 4; AAA59468).`
`CONFLICT`	`487 490`		`Missing (in Ref. 7; AAA59199).`
`CONFLICT`	`491 525`		`Missing (in Ref. 1; AAA60544).`
`CONFLICT`	`503 503`		`S -> T (in Ref. 4; AAA59468).`
`CONFLICT`	`508 508`		`S -> T (in Ref. 4; AAA59468).`
`CONFLICT`	`513 519`		`YGGGSSS -> LRGELH (in Ref. 4; AAA59468).`
`CONFLICT`	`523 536`		`GGGSSSGGHGGSSS -> AHST (in Ref. 4; AAA59468).`
`CONFLICT`	`525 533`		`Missing (in Ref. 3; AAH34697 and 7; AAA59199).`
`CONFLICT`	`543 543`		`S -> N (in Ref. 4; AAA59468).`
`CONFLICT`	`544 544`		`S -> F (in Ref. 1; AAA60544).`
`CONFLICT`	`551 555`		`YGGGS -> LRGRH (in Ref. 4; AAA59468).`
`CONFLICT`	`574 574`		`G -> GGYGGGSSSGG (in Ref. 1; AAA60544).`

Sequence information

Length: 593 AA [This is the length of the unprocessed precursor]

Molecular weight: 59511 Da [This is the MW of the unprocessed precursor]

CRC64: B86B29834355A2D0 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSVRYSSSKH YSSSRSGGGG GGGGCGGGGG VSSLRISSSK GSLGGGFSSG GFSGGSFSRG 

        70         80         90        100        110        120 
SSGGGCFGGS SGGYGGLGGF GGGSFRGSYG SSSFGGSYGG SFGGGSFGGG SFGGGSFGGG 

       130        140        150        160        170        180 
GFGGGGFGGG FGGGFGGDGG LLSGNEKVTM QNLNDRLASY LDKVRALEES NYELEGKIKE 

       190        200        210        220        230        240 
WYEKHGNSHQ GEPRDYSKYY KTIDDLKNQI LNLTTDNANI LLQIDNARLA ADDFRLKYEN 

       250        260        270        280        290        300 
EVALRQSVEA DINGLRRVLD ELTLTKADLE MQIESLTEEL AYLKKNHEEE MKDLRNVSTG 

       310        320        330        340        350        360 
DVNVEMNAAP GVDLTQLLNN MRSQYEQLAE QNRKDAEAWF NEKSKELTTE IDNNIEQISS 

       370        380        390        400        410        420 
YKSEITELRR NVQALEIELQ SQLALKQSLE ASLAETEGRY CVQLSQIQAQ ISALEEQLQQ 

       430        440        450        460        470        480 
IRAETECQNT EYQQLLDIKI RLENEIQTYR SLLEGEGSSG GGGRGGGSFG GGYGGGSSGG 

       490        500        510        520        530        540 
GSSGGGYGGG HGGSSGGGYG GGSSGGGSSG GGYGGGSSSG GHGGGSSSGG HGGSSSGGYG 

       550        560        570        580        590 
GGSSGGGGGG YGGGSSGGGS SSGGGYGGGS SSGGHKSSSS GSVGESSSKG PRY

P13645 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