Reviewed, UniProtKB/Swiss-Prot P13645 (K1C10_HUMAN)

Names and origin

Protein names

Recommended name:
    Keratin, type I cytoskeletal 10
Alternative name(s):
    Cytokeratin-10
      Short name=CK-10
      Short name=Keratin-10
      Short name=K10

Gene names

Name:	KRT10
Synonyms:	KPP

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	593 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Subunit structure	Heterotetramer of two type I and two type II keratins. keratin-10 is generally associated with keratin-1.
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).
Involvement in 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. 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. 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).
Sequence similarities	Belongs to the intermediate filament family.

Ontologies

Keywords
Cellular component	Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Disease	Disease mutation Ichthyosis
Domain	Coiled coil
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	epidermis development Ref.11 Traceable author statement. Source: ProtInc
Cellular component	intermediate filament Ref.1 Ref.11 Non-traceable author statement. Source: UniProtKB
Molecular function	protein binding Inferred from physical interaction. Source: IntAct structural constituent of epidermis Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MDM2	Q00987	1	EBI-465144,EBI-389668

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 593	593	Keratin, type I cytoskeletal 10
Regions
	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
	Compositional bias	6 – 144	139	Gly/Phe/Ser-rich
	Compositional bias	451 – 590	140	Gly/Ser-rich
Natural variations
	Natural variant	126	1	G → S
	Natural variant	150	1	M → R in BCIE.
	Natural variant	150	1	M → T in epidermal nevus epidermolytic hyperkeratotic type.
	Natural variant	154	1	N → H in BCIE.
	Natural variant	156	1	R → C in BCIE.
	Natural variant	156	1	R → H in BCIE.
	Natural variant	156	1	R → P in BCIE.
	Natural variant	156	1	R → S in BCIE.
	Natural variant	160	1	Y → D in BCIE; severe phenotype.
	Natural variant	160	1	Y → N in BCIE; severe phenotype.
	Natural variant	160	1	Y → S in BCIE; severe phenotype.
	Natural variant	161	1	L → S in BCIE.
	Natural variant	422	1	R → E in AEI; requires 2 nucleotide substitutions.
	Natural variant	439	1	K → E in BCIE; mild phenotype.
	Natural variant	442	1	L → Q in BCIE.
	Natural variant	446	1	I → T in AEI.
Experimental info
	Sequence conflict	9 – 11	3	KHY → SKQF in AAA60544. Ref.1
	Sequence conflict	24 – 31	8	Missing in AAA60544. Ref.1
	Sequence conflict	86	1	R → H in CAA32649. Ref.2
	Sequence conflict	106	1	S → N in CAA32649. Ref.2
	Sequence conflict	181 – 184	4	WYEK → RYDQ in AAA60544. Ref.1
	Sequence conflict	189	1	H → R in AAA60544. Ref.1
	Sequence conflict	197	1	S → G in AAA59199. Ref.7
	Sequence conflict	266	1	K → Q in AAA60544. Ref.1
	Sequence conflict	279 – 280	2	EL → YV in AAA59468. Ref.4
	Sequence conflict	287	1	H → R in AAA60544. Ref.1
	Sequence conflict	293	1	D → H in AAA60544. Ref.1
	Sequence conflict	312	1	V → I in AAA59468. Ref.4
	Sequence conflict	323	1	S → N in AAA60544. Ref.1
	Sequence conflict	340	1	F → V in AAA59468. Ref.4
	Sequence conflict	374	1	A → R in AAA59468. Ref.4
	Sequence conflict	408	1	Q → H in CAA32649. Ref.2
	Sequence conflict	420	1	Q → E in AAA60544. Ref.1
	Sequence conflict	436	1	L → T in AAA60544. Ref.1
	Sequence conflict	451	1	S → G in AAA59199. Ref.7
	Sequence conflict	460 – 461	2	GG → RS in AAA59468. Ref.4
	Sequence conflict	477	1	S → T in AAA59468. Ref.4
	Sequence conflict	482	1	S → T in AAA59468. Ref.4
	Sequence conflict	487 – 490	4	Missing in AAA59199. Ref.7
	Sequence conflict	491 – 525	35	Missing in AAA60544. Ref.1
	Sequence conflict	503	1	S → T in AAA59468. Ref.4
	Sequence conflict	508	1	S → T in AAA59468. Ref.4
	Sequence conflict	513 – 519	7	YGGGSSS → LRGELH in AAA59468. Ref.4
	Sequence conflict	523 – 536	14	GGGSS…GGSSS → AHST in AAA59468. Ref.4
	Sequence conflict	525 – 533	9	Missing in AAH34697. Ref.3
	Sequence conflict	525 – 533	9	Missing in AAA59199. Ref.7
	Sequence conflict	543	1	S → N in AAA59468. Ref.4
	Sequence conflict	544	1	S → F in AAA60544. Ref.1
	Sequence conflict	551 – 555	5	YGGGS → LRGRH in AAA59468. Ref.4
	Sequence conflict	574	1	G → GGYGGGSSSGG in AAA60544. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P13645-1 [UniParc]. Last modified May 15, 2007. Version 4. Checksum: B86B29834355A2D0	FASTA	593	59,511
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete sequence of the human intermediate filament chain keratin 10. Subdomainal divisions and model for folding of end domain sequences." Zhou X.M., Idler W.W., Steven A.C., Roop D.R., Steinert P.M. J. Biol. Chem. 263:15584-15589(1988) [PubMed: 2459124] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Foreskin.
[2]	"Identification of an orthologous mammalian cytokeratin gene. High degree of intron sequence conservation during evolution of human cytokeratin 10." Rieger M., Franke W.W. J. Mol. Biol. 204:841-856(1988) [PubMed: 2464696] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Skin.
[4]	"Sequence of a cDNA encoding human keratin No 10 selected according to structural homologies of keratins and their tissue-specific expression." Darmon M.Y., Semat A., Darmon M.C., Vasseur M. Mol. Biol. Rep. 12:277-283(1987) [PubMed: 2448602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 130-593.
[5]	"Prenatal diagnosis of epidermolytic hyperkeratosis by direct gene sequencing." Rothnagel J.A., Longley M.A., Holder R.A., Kuster W., Roop D.R. J. Invest. Dermatol. 102:13-16(1994) [PubMed: 7507150] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, VARIANTS BCIE HIS-156 AND ASN-160.
[6]	"Identification of mutational hot spots in the suprabasal keratin genes from patients with epidermolytic hyperkeratosis." Rothnagel J.J., Dominey A., Fisher M., Axtell S., Pittelkow M., Anton-Lamprecht I., Hohl D., Roop D. Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, VARIANT BCIE CYS-156.
[7]	"Exons I and VII of the gene (Ker10) encoding human keratin 10 undergo structural rearrangements within repeats." Tkachenko A.V., Buchman V.L., Bliskovsky V.V., Shvets Y.P., Kisselev L.L. Gene 116:245-251(1992) [PubMed: 1378806] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 197-593.
[8]	"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes." Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J. Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract] Cited for: PROTEIN SEQUENCE OF 180-184 AND 577-589. Tissue: Keratinocyte.
[9]	"The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes." Cheng J., Syder A.J., Yu Q.-C., Letai A., Paller A.S., Fuchs E. Cell 70:811-819(1992) [PubMed: 1381287] [Abstract] Cited for: VARIANT BCIE HIS-156.
[10]	"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." Korge B.P., Gan S.-Q., McBridge O.W., Mischke D., Steinert P.M. Proc. Natl. Acad. Sci. U.S.A. 89:910-914(1992) [PubMed: 1371013] [Abstract] Cited for: VARIANTS.
[11]	"Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis." 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. Science 257:1128-1130(1992) [PubMed: 1380725] [Abstract] Cited for: VARIANTS BCIE HIS-156 AND SER-161.
[12]	"Preferential sites in keratin 10 that are mutated in epidermolytic hyperkeratosis." Chipev C.C., Yang J.-M., Digiovanna J.J., Steinert P.M., Marekov L., Compton J.G., Bale S.J. Am. J. Hum. Genet. 54:179-190(1994) [PubMed: 7508181] [Abstract] Cited for: VARIANTS BCIE HIS-154; CYS-156; HIS-156; ASP-160 AND GLN-442.
[13]	"Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity." Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E. J. Clin. Invest. 93:1533-1542(1994) [PubMed: 7512983] [Abstract] Cited for: VARIANTS BCIE ARG-150; CYS-156 AND GLU-439, VARIANT SER-126.
[14]	"Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital ichthyosiform erythroderma (BCIE)." 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. J. Invest. Dermatol. 102:24-30(1994) [PubMed: 7507152] [Abstract] Cited for: VARIANTS BCIE PRO-156 AND SER-156.
[15]	"Genetic and clinical mosaicism in a type of epidermal nevus." Paller A.S., Syder A.J., Chan Y.-M., Yu Q.-C., Hutton M.E., Tadini G., Fuchs E. N. Engl. J. Med. 331:1408-1415(1994) [PubMed: 7526210] [Abstract] Cited for: VARIANT EPIDERMAL NEVUS EPIDERMOLYTIC HYPERKERATOTIC TYPE THR-150.
[16]	"A novel dinucleotide mutation in keratin 10 in the annular epidermolytic ichthyosis variant of bullous congenital ichthyosiform erythroderma." Joh G.-Y., Traupe H., Metze D., Nashan D., Huber M., Hohl D., Longley M.A., Rothnagel J.A., Roop D.R. J. Invest. Dermatol. 108:357-361(1997) [PubMed: 9036939] [Abstract] Cited for: VARIANT AEI GLU-422.
[17]	"A novel helix termination mutation in keratin 10 in annular epidermolytic ichthyosis, a variant of bullous congenital ichthyosiform erythroderma." Suga Y., Duncan K.O., Heald P.W., Roop D.R. J. Invest. Dermatol. 111:1220-1223(1998) [PubMed: 9856845] [Abstract] Cited for: VARIANT AEI THR-446.
[18]	"A novel substitution in keratin 10 in epidermolytic hyperkeratosis." Arin M.J., Longley M.A., Anton-Lamprecht I., Kurze G., Huber M., Hohl D., Rothnagel J.A., Roop D.R. J. Invest. Dermatol. 112:506-508(1999) [PubMed: 10201536] [Abstract] Cited for: VARIANT BCIE SER-160.
+	Additional computationally mapped references.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

Wikipedia

Keratin-10 entry

Cross-references

Sequence databases
EMBLGenBankDDBJ	J04029 mRNA. Translation: AAA60544.1. X14487 Genomic DNA. Translation: CAA32649.1. BC034697 mRNA. Translation: AAH34697.1. M19156 mRNA. Translation: AAA59468.1. Different initiation. M77663 mRNA. Translation: AAA59199.1. L20218 Genomic DNA. Translation: AAB59438.1. L20219 Genomic DNA. T