P13645 (K1C10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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	Epidermolytic hyperkeratosis (EHK) [MIM:113800]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6 Ref.7 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.22 Ichthyosis annular epidermolytic (AEI) [MIM:607602]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Erythroderma, ichthyosiform, congenital reticular (CRIE) [MIM:609165]: A rare skin condition characterized by slowly enlarging islands of normal skin surrounded by erythematous ichthyotic patches in a reticulated pattern. The condition starts in infancy as a lamellar ichthyosis, with small islands of normal skin resembling confetti appearing in late childhood and at puberty. Histopathologic findings include band-like parakeratosis, psoriasiform acanthosis, and vacuolization of keratinocytes with binucleated cells in the upper epidermis, sometimes associated with amyloid deposition in the dermis. Ultrastructural abnormalities include perinuclear shells formed from a network of fine filaments in the upper epidermis. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11
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.
Sequence caution	The sequence AAA59468.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Cellular component	Intermediate filament Keratin
Coding sequence diversity	Polymorphism
Disease	Disease mutation Ichthyosis
Domain	Coiled coil
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular response to calcium ion Inferred from electronic annotation. Source: Compara keratinocyte differentiation Inferred from expression pattern PubMed 22170488. Source: UniProtKB
Cellular_component	cytoplasm Inferred from direct assay PubMed 22170488. Source: UniProtKB intermediate filament Non-traceable author statement Ref.1. Source: UniProtKB keratin filament Inferred from electronic annotation. Source: Compara
Molecular_function	structural constituent of epidermis Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

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. Ref.1 Ref.4
Corresponds to variant rs4261597 [ dbSNP | Ensembl ].

VAR_058202

Natural variant

126

1

G → S. Ref.17

VAR_010505

Natural variant

150

1

M → R in EHK. Ref.17
Corresponds to variant rs58901407 [ dbSNP | Ensembl ].

VAR_010506

Natural variant

150

1

M → T in a patient with epidermal nevi hyperkeratotic type due to genetic mosaicism. Ref.19

VAR_010507

Natural variant

154

1

N → H in EHK. Ref.16
Corresponds to variant rs57784225 [ dbSNP | Ensembl ].

VAR_003826

Natural variant

156

1

R → C in EHK. Ref.7 Ref.16 Ref.17

VAR_003828

Natural variant

156

1

R → H in EHK. Ref.6 Ref.13 Ref.15 Ref.16
Corresponds to variant rs58075662 [ dbSNP | Ensembl ].

VAR_003827

Natural variant

156

1

R → P in EHK. Ref.18

VAR_003829

Natural variant

156

1

R → S in EHK. Ref.18
Corresponds to variant rs58852768 [ dbSNP | Ensembl ].

VAR_003830

Natural variant

160

1

Y → D in EHK; severe phenotype. Ref.16
Corresponds to variant rs58414354 [ dbSNP | Ensembl ].

VAR_003831

Natural variant

160

1

Y → N in EHK; severe phenotype. Ref.6

VAR_010508

Natural variant

160

1

Y → S in EHK; severe phenotype. Ref.22
Corresponds to variant rs58735429 [ dbSNP | Ensembl ].

VAR_010509

Natural variant

161

1

L → S in EHK. Ref.15
Corresponds to variant rs60118264 [ dbSNP | Ensembl ].

VAR_003832

Natural variant

422

1

R → E in AEI; requires 2 nucleotide substitutions. Ref.20
Corresponds to variant rs59075499 [ dbSNP | Ensembl ].

VAR_033145

Natural variant

439

1

K → E in EHK; mild phenotype. Ref.17
Corresponds to variant rs61434181 [ dbSNP | Ensembl ].

VAR_010510

Natural variant

442

1

L → Q in EHK. Ref.16
Corresponds to variant rs58026994 [ dbSNP | Ensembl ].

VAR_003833

Natural variant

446

1

I → T in AEI. Ref.21

VAR_010511

Natural variant

487

1

H → Y. Ref.1 Ref.2 Ref.4 Ref.5

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

Secondary structure

1

.

.

.

.

584

Helix Strand Turn

Details...

Beta strand

474 – 482

9

Beta strand

483 – 486

4

Sequences

	Sequence		Length	Mass (Da)
	P13645 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 147-161, VARIANTS EHK 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 EHK 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-42, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Mitotic recombination in patients with ichthyosis causes reversion of dominant mutations in KRT10." Choate K.A., Lu Y., Zhou J., Choi M., Elias P.M., Farhi A., Nelson-Williams C., Crumrine D., Williams M.L., Nopper A.J., Bree A., Milstone L.M., Lifton R.P. Science 330:94-97(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN CRIE.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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] [Europe PMC] [Abstract] Cited for: VARIANT EHK HIS-156.
[14]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS.
[15]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS EHK HIS-156 AND SER-161.
[16]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS EHK HIS-154; CYS-156; HIS-156; ASP-160 AND GLN-442.
[17]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS EHK ARG-150; CYS-156 AND GLU-439, VARIANT SER-126.
[18]	"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] [Europe PMC] [Abstract] Cited for: VARIANTS EHK PRO-156 AND SER-156.
[19]	"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] [Europe PMC] [Abstract] Cited for: VARIANT THR-150.
[20]	"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] [Europe PMC] [Abstract] Cited for: VARIANT AEI GLU-422.
[21]	"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] [Europe PMC] [Abstract] Cited for: VARIANT AEI THR-446.
[22]	"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] [Europe PMC] [Abstract] Cited for: VARIANT EHK 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. NM_000421.3.

UniGene

Hs.99936.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3ASW	X-ray	2.60	B	473-487	[»]
4F1Z	X-ray	2.30	Q	473-486	[»]

ProteinModelPortal

P13645.

SMR

P13645. Positions 145-287, 313-455.

ModBase

Search...

Protein-protein interaction databases

IntAct

P13645. 18 interactions.

MINT

MINT-1132575.

STRING

9606.ENSP00000269576.

PTM databases

PhosphoSite

P13645.

Polymorphism databases

DMDM

269849769.

2D gel databases

REPRODUCTION-2DPAGE

P13645.

SWISS-2DPAGE

P13645.

Proteomic databases

PaxDb

P13645.

PeptideAtlas

P13645.

PRIDE

P13645.

ProMEX

P13645.

Protocols and materials databases

DNASU

3858.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000269576; ENSP00000269576; ENSG00000186395.

GeneID

3858.

KEGG

hsa:3858.

UCSC

uc002hvi.3. human.

Organism-specific databases

CTD

3858.

GeneCards

GC17M038974.

HGNC

HGNC:6413. KRT10.

HPA

CAB000132.
HPA012014.

MIM

113800. phenotype.
148080. gene.
607602. phenotype.
609165. phenotype.

neXtProt

NX_P13645.

Orphanet

281139. Annular epidermolytic ichthyosis.
281190. Congenital reticular ichthyosiform erythroderma.
312. Epidermolytic ichthyosis.

PharmGKB

PA30200.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG147548.

HOGENOM

HOG000230975.

HOVERGEN

HBG013015.

InParanoid

P13645.

KO

K07604.

OMA

YSSSKHY.

OrthoDB

EOG4P8FJH.

PhylomeDB

P13645.

Gene expression databases

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. PTHR23239. 1 hit.

Pfam

PF00038. Filament. 1 hit.
[Graphical view]

PRINTS

PR01248. TYPE1KERATIN.

PROSITE

PS00226. IF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

3858.

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:	May 1, 2013
This is version 143 of the entry and version 6 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.