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Reviewed, UniProtKB/Swiss-Prot P13645 (K1C10_HUMAN)

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

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.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.

Ontologies

Keywords
   Cellular componentIntermediate filament
Keratin
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Ichthyosis
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processepidermis development Ref.13

Traceable author statement. Source: ProtInc

   Cellular componentintermediate filament Ref.1 Ref.13

Non-traceable author statement. Source: UniProtKB

   Molecular functionprotein 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

MDM2Q009871EBI-465144,EBI-389668

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593Keratin, type I cytoskeletal 10
PRO_0000063642

Regions

Region1 – 145145Head
Region146 – 456311Rod
Region146 – 18136Coil 1A
Region182 – 20221Linker 1
Region203 – 29492Coil 1B
Region295 – 31723Linker 12
Region318 – 456139Coil 2
Region457 – 593137Tail
Compositional bias6 – 144139Gly/Phe/Ser-rich
Compositional bias451 – 590140Gly/Ser-rich

Amino acid modifications

Modified residue161Phosphoserine Ref.9
Modified residue421Phosphoserine Ref.9

Natural variations

Natural variant1261G → S Ref.15
VAR_010505
Natural variant1501M → R in BCIE. Ref.15
VAR_010506
Natural variant1501M → T in epidermal nevus epidermolytic hyperkeratotic type. Ref.15 Ref.17
VAR_010507
Natural variant1541N → H in BCIE. Ref.14
VAR_003826
Natural variant1561R → C in BCIE. Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
VAR_003828
Natural variant1561R → H in BCIE. Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
VAR_003827
Natural variant1561R → P in BCIE. Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
VAR_003829
Natural variant1561R → S in BCIE. Ref.5 Ref.6 Ref.11 Ref.13 Ref.14 Ref.15 Ref.16
VAR_003830
Natural variant1601Y → D in BCIE; severe phenotype. Ref.5 Ref.14 Ref.20
VAR_003831
Natural variant1601Y → N in BCIE; severe phenotype. Ref.5 Ref.14 Ref.20
VAR_010508
Natural variant1601Y → S in BCIE; severe phenotype. Ref.5 Ref.14 Ref.20
VAR_010509
Natural variant1611L → S in BCIE. Ref.13
VAR_003832
Natural variant4221R → E in AEI; requires 2 nucleotide substitutions. Ref.18
VAR_033145
Natural variant4391K → E in BCIE; mild phenotype. Ref.15
VAR_010510
Natural variant4421L → Q in BCIE. Ref.14
VAR_003833
Natural variant4461I → T in AEI. Ref.19
VAR_010511

Experimental info

Sequence conflict9 – 113KHY → SKQF in AAA60544. Ref.1
Sequence conflict24 – 318Missing in AAA60544. Ref.1
Sequence conflict861R → H in CAA32649. Ref.2
Sequence conflict1061S → N in CAA32649. Ref.2
Sequence conflict181 – 1844WYEK → RYDQ in AAA60544. Ref.1
Sequence conflict1891H → R in AAA60544. Ref.1
Sequence conflict1971S → G in AAA59199. Ref.7
Sequence conflict2661K → Q in AAA60544. Ref.1
Sequence conflict279 – 2802EL → YV in AAA59468. Ref.4
Sequence conflict2871H → R in AAA60544. Ref.1
Sequence conflict2931D → H in AAA60544. Ref.1
Sequence conflict3121V → I in AAA59468. Ref.4
Sequence conflict3231S → N in AAA60544. Ref.1
Sequence conflict3401F → V in AAA59468. Ref.4
Sequence conflict3741A → R in AAA59468. Ref.4
Sequence conflict4081Q → H in CAA32649. Ref.2
Sequence conflict4201Q → E in AAA60544. Ref.1
Sequence conflict4361L → T in AAA60544. Ref.1
Sequence conflict4511S → G in AAA59199. Ref.7
Sequence conflict460 – 4612GG → RS in AAA59468. Ref.4
Sequence conflict4771S → T in AAA59468. Ref.4
Sequence conflict4821S → T in AAA59468. Ref.4
Sequence conflict487 – 4904Missing in AAA59199. Ref.7
Sequence conflict491 – 52535Missing in AAA60544. Ref.1
Sequence conflict5031S → T in AAA59468. Ref.4
Sequence conflict5081S → T in AAA59468. Ref.4
Sequence conflict513 – 5197YGGGSSS → LRGELH in AAA59468. Ref.4
Sequence conflict523 – 53614GGGSS…GGSSS → AHST in AAA59468. Ref.4
Sequence conflict525 – 5339Missing in AAH34697. Ref.3
Sequence conflict525 – 5339Missing in AAA59199. Ref.7
Sequence conflict5431S → N in AAA59468. Ref.4
Sequence conflict5441S → F in AAA60544. Ref.1
Sequence conflict551 – 5555YGGGS → LRGRH in AAA59468. Ref.4
Sequence conflict5741G → GGYGGGSSSGG in AAA60544. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P13645-1 [UniParc].

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

FASTA59359,511
        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 

« Hide

References

« Hide '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.

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.
IPIIPI00009865.
PIRA31994.
KRHU0. S02158.
RefSeqNP_000412.3.
UniGeneHs.99936

3D structure databases

HSSPHSSP built from PDB template 1GK7 based on UniProtKB P08670.
ModBaseSearch...

Protein-protein interaction databases

IntActP13645. 11 interactions.

PTM databases

PhosphoSiteP13645.

2-D gel databases

SWISS-2DPAGEP13645.
Aarhus/Ghent-2DPAGE7405. IEF.
REPRODUCTION-2DPAGEP13645.

Proteomic databases

PeptideAtlasP13645.
PRIDEP13645.

Genome annotation databases

EnsemblENSG00000186395. Homo sapiens. [Contig view]
GeneID3858.
KEGGhsa:3858.

Organism-specific databases

GeneCardsGC17M036227.
HGNCHGNC:6413. KRT10.
HPACAB000132.
MIM113800. phenotype.
148080. gene.
600648. phenotype.
607602. phenotype.
Orphanet312. Erythroderma, congenital ichthyosiform, bullous.
313. Ichthyosis, lamellar.
PharmGKBPA30200.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP13645.
HOVERGENP13645.

Gene expression databases

ArrayExpressP13645.
BgeeP13645.
CleanExHS_KRT10.
GermOnlineENSG00000186395. Homo sapiens.

Family and domain databases

InterProIPR016044. F.
IPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
[Graphical view]
PANTHERPTHR23239. IF. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01248. TYPE1KERATIN.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio15181.
SOURCESearch...

Entry information

Entry nameK1C10_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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 · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents