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P13645 (K1C10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 151. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length584 AA.
Sequence statusComplete.
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

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 584584Keratin, 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 – 584128Tail
Compositional bias17 – 575559Gly-rich
Compositional bias477 – 579103Ser-rich

Amino acid modifications

Modified residue161Phosphoserine Ref.10
Modified residue421Phosphoserine Ref.10

Natural variations

Natural variant1011I → S. Ref.1 Ref.4
Corresponds to variant rs4261597 [ dbSNP | Ensembl ].
VAR_058202
Natural variant1261G → S. Ref.17
Corresponds to variant rs77919366 [ dbSNP | Ensembl ].
VAR_010505
Natural variant1501M → R in EHK. Ref.17
Corresponds to variant rs58901407 [ dbSNP | Ensembl ].
VAR_010506
Natural variant1501M → T in a patient with epidermal nevi hyperkeratotic type due to genetic mosaicism. Ref.19
VAR_010507
Natural variant1541N → H in EHK. Ref.16
Corresponds to variant rs57784225 [ dbSNP | Ensembl ].
VAR_003826
Natural variant1561R → C in EHK. Ref.7 Ref.16 Ref.17
VAR_003828
Natural variant1561R → H in EHK. Ref.6 Ref.13 Ref.15 Ref.16
Corresponds to variant rs58075662 [ dbSNP | Ensembl ].
VAR_003827
Natural variant1561R → P in EHK. Ref.18
VAR_003829
Natural variant1561R → S in EHK. Ref.18
Corresponds to variant rs58852768 [ dbSNP | Ensembl ].
VAR_003830
Natural variant1601Y → D in EHK; severe phenotype. Ref.16
Corresponds to variant rs58414354 [ dbSNP | Ensembl ].
VAR_003831
Natural variant1601Y → N in EHK; severe phenotype. Ref.6
VAR_010508
Natural variant1601Y → S in EHK; severe phenotype. Ref.22
Corresponds to variant rs58735429 [ dbSNP | Ensembl ].
VAR_010509
Natural variant1611L → S in EHK. Ref.15
Corresponds to variant rs60118264 [ dbSNP | Ensembl ].
VAR_003832
Natural variant4221R → E in AEI; requires 2 nucleotide substitutions. Ref.20
Corresponds to variant rs59075499 [ dbSNP | Ensembl ].
VAR_033145
Natural variant4391K → E in EHK; mild phenotype. Ref.17
Corresponds to variant rs61434181 [ dbSNP | Ensembl ].
VAR_010510
Natural variant4421L → Q in EHK. Ref.16
Corresponds to variant rs58026994 [ dbSNP | Ensembl ].
VAR_003833
Natural variant4461I → T in AEI. Ref.21
VAR_010511
Natural variant4871H → Y. Ref.1 Ref.2 Ref.4 Ref.5
Corresponds to variant rs17855579 [ dbSNP | Ensembl ].
VAR_060723

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.8
Sequence conflict2661K → Q in AAA60544. Ref.1
Sequence conflict279 – 2802EL → YV in AAA59468. Ref.5
Sequence conflict2871H → R in AAA60544. Ref.1
Sequence conflict2931D → H in AAA60544. Ref.1
Sequence conflict3121V → I in AAA59468. Ref.5
Sequence conflict3231S → N in AAA60544. Ref.1
Sequence conflict3401F → V in AAA59468. Ref.5
Sequence conflict3741A → R in AAA59468. Ref.5
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.8
Sequence conflict460 – 4612GG → RS in AAA59468. Ref.5
Sequence conflict4771S → T in AAA59468. Ref.5
Sequence conflict4821S → T in AAA59468. Ref.5
Sequence conflict487 – 4904Missing in AAA59199. Ref.8
Sequence conflict491 – 51626Missing in AAA60544. Ref.1
Sequence conflict5031S → T in AAA59468. Ref.5
Sequence conflict5081S → T in AAA59468. Ref.5
Sequence conflict513 – 5197YGGGSSS → LRGELH in AAA59468. Ref.5
Sequence conflict523 – 5275GGSSS → AHST in AAA59468. Ref.5
Sequence conflict5241G → GGSSSGGHGG in CAA32649. Ref.2
Sequence conflict5341S → N in AAA59468. Ref.5
Sequence conflict5351S → F in AAA60544. Ref.1
Sequence conflict542 – 5465YGGGS → LRGRH in AAA59468. Ref.5
Sequence conflict5651G → GGYGGGSSSGG in AAA60544. Ref.1

Secondary structure

....... 584
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13645 [UniParc].

Last modified November 24, 2009. Version 6.
Checksum: 4941ECD2AE46D417

FASTA58458,827
        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 

« 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] [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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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.

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.
PIRA31994.
KRHU0. S02158.
RefSeqNP_000412.3. NM_000421.3.
UniGeneHs.99936.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3ASWX-ray2.60B473-487[»]
4F1ZX-ray2.30Q473-486[»]
ProteinModelPortalP13645.
SMRP13645. Positions 144-287, 313-455.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110056. 50 interactions.
IntActP13645. 19 interactions.
MINTMINT-1132575.
STRING9606.ENSP00000269576.

PTM databases

PhosphoSiteP13645.

Polymorphism databases

DMDM269849769.

2D gel databases

REPRODUCTION-2DPAGEP13645.
SWISS-2DPAGEP13645.

Proteomic databases

PaxDbP13645.
PeptideAtlasP13645.
PRIDEP13645.
ProMEXP13645.

Protocols and materials databases

DNASU3858.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000269576; ENSP00000269576; ENSG00000186395.
GeneID3858.
KEGGhsa:3858.
UCSCuc002hvi.3. human.

Organism-specific databases

CTD3858.
GeneCardsGC17M038974.
HGNCHGNC:6413. KRT10.
HPACAB000132.
HPA012014.
MIM113800. phenotype.
148080. gene.
607602. phenotype.
609165. phenotype.
neXtProtNX_P13645.
Orphanet281139. Annular epidermolytic ichthyosis.
281190. Congenital reticular ichthyosiform erythroderma.
312. Epidermolytic ichthyosis.
PharmGKBPA30200.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG147548.
HOGENOMHOG000230975.
HOVERGENHBG013015.
InParanoidP13645.
KOK07604.
OMAYSSSKHY.
OrthoDBEOG7FV3Q8.
PhylomeDBP13645.
TreeFamTF332742.

Gene expression databases

BgeeP13645.
CleanExHS_KRT10.
GenevestigatorP13645.

Family and domain databases

InterProIPR001664. IF.
IPR018039. Intermediate_filament_CS.
IPR002957. Keratin_I.
IPR009053. Prefoldin.
[Graphical view]
PANTHERPTHR23239. PTHR23239. 1 hit.
PfamPF00038. Filament. 1 hit.
[Graphical view]
PRINTSPR01248. TYPE1KERATIN.
SUPFAMSSF46579. SSF46579. 1 hit.
PROSITEPS00226. IF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiKeratin_10.
GenomeRNAi3858.
NextBio15181.
PROP13645.
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: November 24, 2009
Last modified: March 19, 2014
This is version 151 of the entry and version 6 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

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