Keratin, type I cytoskeletal 10 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P13645 (K1C10_HUMAN)

Last modified June 16, 2009. Version 101. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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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)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

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

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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.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.20 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.18 Ref.19 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. Ref.17
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.

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Ontologies

Keywords
Cellular component	Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Disease	Disease mutation Ichthyosis
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	epidermis development Ref.13 Traceable author statement. Source: ProtInc
Cellular component	intermediate filament Ref.1 Ref.13 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...

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Binary interactions

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

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 593

593

Keratin, type I cytoskeletal 10

PRO_0000063642

Regions

Region

1 – 145

145

Head

Region

146 – 456

311

Rod

Region

146 – 181

Coil 1A

Region

182 – 202

Linker 1

Region

203 – 294

Coil 1B

Region

295 – 317

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

Amino acid modifications

Modified residue

Phosphoserine Ref.9

Modified residue

Phosphoserine Ref.9

Natural variations

Natural variant

126

G → S Ref.15

VAR_010505

Natural variant

150

M → R in BCIE. Ref.15

VAR_010506

Natural variant

150

M → T in epidermal nevus epidermolytic hyperkeratotic type. Ref.15 Ref.17

VAR_010507

Natural variant

154

N → H in BCIE. Ref.14

VAR_003826

Natural variant

156

R → C in BCIE. Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

VAR_003828

Natural variant

156

R → H in BCIE. Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

VAR_003827

Natural variant

156

R → P in BCIE. Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

VAR_003829

Natural variant

156

R → S in BCIE. Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16

VAR_003830

Natural variant

160

Y → D in BCIE; severe phenotype. Ref.5 Ref.14 Ref.20

VAR_003831

Natural variant

160

Y → N in BCIE; severe phenotype. Ref.5 Ref.14 Ref.20

VAR_010508

Natural variant

160

Y → S in BCIE; severe phenotype. Ref.5 Ref.14 Ref.20

VAR_010509

Natural variant

161

L → S in BCIE. Ref.13

VAR_003832

Natural variant

422

R → E in AEI; requires 2 nucleotide substitutions. Ref.18

VAR_033145

Natural variant

439

K → E in BCIE; mild phenotype. Ref.15

VAR_010510

Natural variant

442

L → Q in BCIE. Ref.14

VAR_003833

Natural variant

446

I → T in AEI. Ref.19

VAR_010511

Experimental info

Sequence conflict

9 – 11

KHY → SKQF in AAA60544. Ref.1

Sequence conflict

24 – 31

Missing in AAA60544. Ref.1

Sequence conflict

R → H in CAA32649. Ref.2

Sequence conflict

106

S → N in CAA32649. Ref.2

Sequence conflict

181 – 184

WYEK → RYDQ in AAA60544. Ref.1

Sequence conflict

189

H → R in AAA60544. Ref.1

Sequence conflict

197

S → G in AAA59199. Ref.7

Sequence conflict

266

K → Q in AAA60544. Ref.1

Sequence conflict

279 – 280

EL → YV in AAA59468. Ref.4

Sequence conflict

287

H → R in AAA60544. Ref.1

Sequence conflict

293

D → H in AAA60544. Ref.1

Sequence conflict

312

V → I in AAA59468. Ref.4

Sequence conflict

323

S → N in AAA60544. Ref.1

Sequence conflict

340

F → V in AAA59468. Ref.4

Sequence conflict

374

A → R in AAA59468. Ref.4

Sequence conflict

408

Q → H in CAA32649. Ref.2

Sequence conflict

420

Q → E in AAA60544. Ref.1

Sequence conflict

436

L → T in AAA60544. Ref.1

Sequence conflict

451

S → G in AAA59199. Ref.7

Sequence conflict

460 – 461

GG → RS in AAA59468. Ref.4

Sequence conflict

477

S → T in AAA59468. Ref.4

Sequence conflict

482

S → T in AAA59468. Ref.4

Sequence conflict

487 – 490

Missing in AAA59199. Ref.7

Sequence conflict

491 – 525

Missing in AAA60544. Ref.1

Sequence conflict

503

S → T in AAA59468. Ref.4

Sequence conflict

508

S → T in AAA59468. Ref.4

Sequence conflict

513 – 519

YGGGSSS → LRGELH in AAA59468. Ref.4

Sequence conflict

523 – 536

GGGSS…GGSSS → AHST in AAA59468. Ref.4

Sequence conflict

525 – 533

Missing in AAH34697. Ref.3

Sequence conflict

525 – 533

Missing in AAA59199. Ref.7

Sequence conflict

543

S → N in AAA59468. Ref.4

Sequence conflict

544

S → F in AAA60544. Ref.1

Sequence conflict

551 – 555

YGGGS → LRGRH in AAA59468. Ref.4

Sequence conflict

574

G → GGYGGGSSSGG in AAA60544. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P13645-1 [UniParc].

Last modified May 15, 2007. Version 4.
Checksum: B86B29834355A2D0
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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

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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]	"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.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.
[17]	"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.
[18]	"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.
[19]	"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.
[20]	"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.

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Web resources

Human Intermediate Filament Mutation Database

GeneReviews

Wikipedia

Keratin-10 entry

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Cross-references

Sequence databases
	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. Translation: AAB59439.1.
IPI	IPI00009865.
PIR	A31994. KRHU0. S02158.
RefSeq	NP_000412.3.
UniGene	Hs.99936
3D structure databases
HSSP	HSSP built from PDB template 1GK7 based on UniProtKB P08670.
ModBase	Search...
Protein-protein interaction databases
IntAct	P13645. 11 interactions.
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	ENSG00000186395. Homo sapiens. [Contig view]
GeneID	3858.
KEGG	hsa:3858.
Organism-specific databases
GeneCards	GC17M036227.
HGNC	HGNC:6413. KRT10.
HPA	CAB000132.
MIM	113800. phenotype. 148080. gene. 600648. phenotype. 607602. phenotype.
Orphanet	312. Erythroderma, congenital ichthyosiform, bullous. 313. Ichthyosis, lamellar.
PharmGKB	PA30200.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	P13645.
HOVERGEN	P13645.
Gene expression databases
ArrayExpress	P13645.
Bgee	P13645.
CleanEx	HS_KRT10.
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...

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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:	May 15, 2007
Last modified:	June 16, 2009
This is version 101 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents