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
Keratin-10
Short name=K10

Gene names

Name:	KRT10
Synonyms:	KPP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	584 AA.
Sequence status	Complete.
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. Ref.6 Ref.7 Ref.12 Ref.14 Ref.15 Ref.16 Ref.17 Ref.21 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. Ref.19 Ref.20
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
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	epidermis development Ref.14 Traceable author statement. Source: ProtInc
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	Feature identifier
Molecule processing
	Chain	1 – 584	584	Keratin, type I cytoskeletal 10		PRO_0000063642
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 – 584	128	Tail
	Compositional bias	17 – 575	559	Gly-rich
	Compositional bias	477 – 579	103	Ser-rich
Amino acid modifications
	Modified residue	16	1	Phosphoserine Ref.10
	Modified residue	42	1	Phosphoserine Ref.10
	Modified residue	56	1	Phosphoserine By similarity
Natural variations
	Natural variant	101	1	I → S: dbSNP rs4261597. Ref.1 Ref.4		VAR_058202
	Natural variant	126	1	G → S		VAR_010505
	Natural variant	150	1	M → R in BCIE. dbSNP rs58901407. Ref.16		VAR_010506
	Natural variant	150	1	M → T in a patient with epidermal nevi hyperkeratotic type due to genetic mosaicism. Ref.18		VAR_010507
	Natural variant	154	1	N → H in BCIE. dbSNP rs57784225. Ref.15		VAR_003826
	Natural variant	156	1	R → C in BCIE. Ref.7 Ref.15 Ref.16		VAR_003828
	Natural variant	156	1	R → H in BCIE. dbSNP rs58075662. Ref.6 Ref.12 Ref.14 Ref.15		VAR_003827
	Natural variant	156	1	R → P in BCIE. Ref.17		VAR_003829
	Natural variant	156	1	R → S in BCIE. dbSNP rs58852768. Ref.17		VAR_003830
	Natural variant	160	1	Y → D in BCIE; severe phenotype. dbSNP rs58414354. Ref.15		VAR_003831
	Natural variant	160	1	Y → N in BCIE; severe phenotype. Ref.6		VAR_010508
	Natural variant	160	1	Y → S in BCIE; severe phenotype. dbSNP rs58735429. Ref.21		VAR_010509
	Natural variant	161	1	L → S in BCIE. dbSNP rs60118264. Ref.14		VAR_003832
	Natural variant	422	1	R → E in AEI; requires 2 nucleotide substitutions. dbSNP rs59075499. Ref.19		VAR_033145
	Natural variant	439	1	K → E in BCIE; mild phenotype. dbSNP rs61434181. Ref.16		VAR_010510
	Natural variant	442	1	L → Q in BCIE. dbSNP rs58026994. Ref.15		VAR_003833
	Natural variant	446	1	I → T in AEI. Ref.20		VAR_010511
	Natural variant	487	1	H → Y		VAR_060723
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.8
	Sequence conflict	266	1	K → Q in AAA60544. Ref.1
	Sequence conflict	279 – 280	2	EL → YV in AAA59468. Ref.5
	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.5
	Sequence conflict	323	1	S → N in AAA60544. Ref.1
	Sequence conflict	340	1	F → V in AAA59468. Ref.5
	Sequence conflict	374	1	A → R in AAA59468. Ref.5
	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.8
	Sequence conflict	460 – 461	2	GG → RS in AAA59468. Ref.5
	Sequence conflict	477	1	S → T in AAA59468. Ref.5
	Sequence conflict	482	1	S → T in AAA59468. Ref.5
	Sequence conflict	487 – 490	4	Missing in AAA59199. Ref.8
	Sequence conflict	491 – 516	26	Missing in AAA60544. Ref.1
	Sequence conflict	503	1	S → T in AAA59468. Ref.5
	Sequence conflict	508	1	S → T in AAA59468. Ref.5
	Sequence conflict	513 – 519	7	YGGGSSS → LRGELH in AAA59468. Ref.5
	Sequence conflict	523 – 527	5	GGSSS → AHST in AAA59468. Ref.5
	Sequence conflict	524	1	G → GGSSSGGHGG in CAA32649. Ref.2
	Sequence conflict	534	1	S → N in AAA59468. Ref.5
	Sequence conflict	535	1	S → F in AAA60544. Ref.1
	Sequence conflict	542 – 546	5	YGGGS → LRGRH in AAA59468. Ref.5
	Sequence conflict	565	1	G → GGYGGGSSSGG in AAA60544. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P13645-1 [UniParc]. Last modified November 24, 2009. Version 6. Checksum: 4941ECD2AE46D417	FASTA	584	58,827
	10 20 30 40 50 60 MSVRYSSSKH YSSSRSGGGG GGGGCGGGGG VSSLRISSSK GSLGGGFSSG GFSGGSFSRG 70 80 90 100 110 120 SSGGGCFGGS SGGYGGLGGF GGGSFRGSYG SSSFGGSYGG IFGGGSFGGG 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 GSSGGGHGGG HGGSSGGGYG GGSSGGGSSG GGYGGGSSSG GHGGSSSGGY GGGSSGGGGG 550 560 570 580 GYGGGSSGGG SSSGGGYGGG SSSGGHKSSS SGSVGESSSK GPRY

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], VARIANTS SER-101 AND TYR-487. 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], VARIANT TYR-487.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." 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. Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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], VARIANTS SER-101 AND TYR-487. Tissue: Skin.
[5]	"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 130-584, VARIANT TYR-487.
[6]	"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.
[7]	"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.
[8]	"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 197-584.
[9]	"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 568-580. Tissue: Keratinocyte.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-42, MASS SPECTROMETRY.
[11]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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 THR-150.
[19]	"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.
[20]	"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.
[21]	"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
EMBL GenBank DDBJ	J04029 mRNA. Translation: AAA60544.1. X14487 Genomic DNA. Translation: CAA32649.1. AC090283 mRNA. No translation available. BC034697 mRNA. Translation: AAH34697.1. M19156 mRNA. Translation: AAA59468.1. Different initiation. L20218 Genomic DNA. Translation: AAB59438.1. L20219 Genomic DNA. Translation: AAB59439.1. M77663 mRNA. Translation: AAA59199.1.
IPI	IPI00009865.
PIR	A31994. KRHU0. S02158.
RefSeq	NP_000412.3.
UniGene	Hs.99936
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P13645. 11 interactions.
STRING	P13645.
PTM databases
PhosphoSite	P13645.
2-D gel databases
SWISS-2DPAGE	P13645.
Aarhus/Ghent-2DPAGE	7405. IEF.
REPRODUCTION-2DPAGE	P13645.
Proteomic databases
PeptideAtlas	P13645.
PRIDE	P13645.
Genome annotation databases
Ensembl	ENST00000269576; ENSP00000269576; ENSG00000186395; Homo sapiens. [Genome view]
GeneID	3858.
KEGG	hsa:3858.
UCSC	uc002hvi.1. human.
Organism-specific databases
CTD	3858.
GeneCards	GC17M036227.
HGNC	HGNC:6413. KRT10.
HPA	CAB000132. HPA012014.
MIM	113800. phenotype. 148080. gene. 607602. phenotype.
Orphanet	312. Erythroderma, congenital ichthyosiform, bullous. 313. Ichthyosis, lamellar.
PharmGKB	PA30200.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05122.
HOGENOM	HBG715391.
HOVERGEN	HBG013015.
InParanoid	P13645.
OMA	YSSSKHY.
Gene expression databases
ArrayExpress	P13645.
Bgee	P13645.
CleanEx	HS_KRT10.
Genevestigator	P13645.
GermOnline	ENSG00000186395. Homo sapiens.
Family and domain databases
InterPro	IPR016044. F. IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR002957. Keratin_I. [Graphical view]
PANTHER	PTHR23239. IF. 1 hit.
Pfam	PF00038. Filament. 1 hit. [Graphical view]
PRINTS	PR01248. TYPE1KERATIN.
PROSITE	PS00226. IF. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	15181.
SOURCE	Search...

Entry information

Entry name

K1C10_HUMAN

Accession

Primary (citable) accession number: P13645
Secondary accession number(s): Q14664, Q8N175

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 24, 2009
Last modified:	March 2, 2010
This is version 110 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.