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P35527 (K1C9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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 9
Alternative name(s):
Cytokeratin-9
Short name=CK-9
Keratin-9
Short name=K9
Gene names
Name:KRT9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length623 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May serve an important special function either in the mature palmar and plantar skin tissue or in the morphogenetic program of the formation of these tissues. Plays a role in keratin filament assembly. Ref.1 Ref.8

Subunit structure

Heterotetramer of two type I and two type II keratins.

Tissue specificity

Expressed in the terminally differentiated epidermis of palms and soles. Ref.1

Induction

Induced by intrinsic regulatory mechanisms and by extrinsic signals from a subset of dermal palmoplantar fibroblasts. Ref.9

Involvement in disease

Keratoderma, palmoplantar, epidermolytic (EPPK) [MIM:144200]: A dermatological disorder characterized by diffuse thickening of the epidermis on the entire surface of palms and soles sharply bordered with erythematous margins. Some patients may present knuckle pads, thick pads of skin appearing over the proximal phalangeal joints.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.5 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29

Miscellaneous

There are two types of cytoskeletal and microfibrillar keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa, respectively).

Sequence similarities

Belongs to the intermediate filament family.

Caution

Was originally (Ref.7) thought to be a 60 kDa chain of placental scatter protein.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 623623Keratin, type I cytoskeletal 9
PRO_0000063640

Regions

Region1 – 152152Head
Region153 – 461309Rod
Region153 – 18836Coil 1A
Region189 – 20719Linker 1
Region208 – 29992Coil 1B
Region300 – 32223Linker 12
Region323 – 461139Coil 2
Region462 – 623162Tail
Compositional bias15 – 2612Poly-Gly

Natural variations

Natural variant1571M → R in EPPK. Ref.29
VAR_036805
Natural variant1571M → T in EPPK. Ref.17
Corresponds to variant rs59510579 [ dbSNP | Ensembl ].
VAR_010499
Natural variant1571M → V in EPPK. Ref.12 Ref.17 Ref.21
Corresponds to variant rs58597584 [ dbSNP | Ensembl ].
VAR_010500
Natural variant1601L → F in EPPK; with knuckle pads. Ref.23
Corresponds to variant rs28940896 [ dbSNP | Ensembl ].
VAR_035438
Natural variant1601L → V in EPPK. Ref.16
VAR_010501
Natural variant1611N → H in EPPK. Ref.24 Ref.26
VAR_036806
Natural variant1611N → I in EPPK. Ref.20 Ref.22
VAR_036807
Natural variant1611N → K in EPPK. Ref.2
Corresponds to variant rs57536312 [ dbSNP | Ensembl ].
VAR_003822
Natural variant1611N → S in EPPK. Ref.13 Ref.24
Corresponds to variant rs56707768 [ dbSNP | Ensembl ].
VAR_010502
Natural variant1611N → Y in EPPK. Ref.14
Corresponds to variant rs59296273 [ dbSNP | Ensembl ].
VAR_010503
Natural variant1631R → P in EPPK. Ref.27
VAR_036808
Natural variant1631R → Q in EPPK. Ref.2 Ref.5 Ref.17 Ref.18 Ref.21
Corresponds to variant rs57758262 [ dbSNP | Ensembl ].
VAR_003823
Natural variant1631R → W in EPPK. Ref.2 Ref.15 Ref.19 Ref.21 Ref.24
Corresponds to variant rs59616921 [ dbSNP | Ensembl ].
VAR_003824
Natural variant1671Y → WL in EPPK.
VAR_036809
Natural variant1681L → S in EPPK. Ref.15
Corresponds to variant rs61157095 [ dbSNP | Ensembl ].
VAR_003825
Natural variant1711V → M in EPPK. Ref.21
Corresponds to variant rs57019720 [ dbSNP | Ensembl ].
VAR_035439
Natural variant1721Q → P in EPPK. Ref.12
Corresponds to variant rs59878153 [ dbSNP | Ensembl ].
VAR_010504
Natural variant4581L → F in EPPK. Ref.28
Corresponds to variant rs58120120 [ dbSNP | Ensembl ].
VAR_036810

Experimental info

Mutagenesis1631R → QHA: Leads to aggregate formation. Ref.8
Sequence conflict12 – 132SR → T in AAC60619. Ref.1
Sequence conflict12 – 132SR → T in CAA52924. Ref.2
Sequence conflict411G → R in AAC60619. Ref.1
Sequence conflict411G → R in CAA82315. Ref.1
Sequence conflict411G → R in CAA52924. Ref.2
Sequence conflict1341F → L in AAC60619. Ref.1
Sequence conflict1341F → L in CAA82315. Ref.1
Sequence conflict1341F → L in CAA52924. Ref.2
Sequence conflict157 – 17014MQELN…SYLDK → HLGAGSTPITASQP in AAI21171. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P35527 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: 45C833749B63873D

FASTA62362,064
        10         20         30         40         50         60 
MSCRQFSSSY LSRSGGGGGG GLGSGGSIRS SYSRFSSSGG GGGGGRFSSS SGYGGGSSRV 

        70         80         90        100        110        120 
CGRGGGGSFG YSYGGGSGGG FSASSLGGGF GGGSRGFGGA SGGGYSSSGG FGGGFGGGSG 

       130        140        150        160        170        180 
GGFGGGYGSG FGGFGGFGGG AGGGDGGILT ANEKSTMQEL NSRLASYLDK VQALEEANND 

       190        200        210        220        230        240 
LENKIQDWYD KKGPAAIQKN YSPYYNTIDD LKDQIVDLTV GNNKTLLDID NTRMTLDDFR 

       250        260        270        280        290        300 
IKFEMEQNLR QGVDADINGL RQVLDNLTME KSDLEMQYET LQEELMALKK NHKEEMSQLT 

       310        320        330        340        350        360 
GQNSGDVNVE INVAPGKDLT KTLNDMRQEY EQLIAKNRKD IENQYETQIT QIEHEVSSSG 

       370        380        390        400        410        420 
QEVQSSAKEV TQLRHGVQEL EIELQSQLSK KAALEKSLED TKNRYCGQLQ MIQEQISNLE 

       430        440        450        460        470        480 
AQITDVRQEI ECQNQEYSLL LSIKMRLEKE IETYHNLLEG GQEDFESSGA GKIGLGGRGG 

       490        500        510        520        530        540 
SGGSYGRGSR GGSGGSYGGG GSGGGYGGGS GSRGGSGGSY GGGSGSGGGS GGGYGGGSGG 

       550        560        570        580        590        600 
GHSGGSGGGH SGGSGGNYGG GSGSGGGSGG GYGGGSGSRG GSGGSHGGGS GFGGESGGSY 

       610        620 
GGGEEASGSG GGYGGGSGKS SHS 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of the body site-specific human epidermal cytokeratin 9: cDNA cloning, amino acid sequence, and tissue specificity of gene expression."
Langbein L., Heid H.W., Moll I., Franke W.W.
Differentiation 55:57-72(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, TISSUE SPECIFICITY.
Tissue: Foot sole tissue.
[2]"Keratin 9 gene mutations in epidermolytic palmoplantar keratoderma (EPPK)."
Reis A., Hennies H.-C., Langbein L., Digweed M., Mischke D., Dreschler M., Schroek E., Royer-Pokora B., Franke W.W., Sperling K., Kuester W.
Nat. Genet. 6:174-179(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS EPPK LYS-161; GLN-163 AND TRP-163.
[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]Bienvenut W.V.
Submitted (AUG-2005) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 14-29, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]"Keratin 9 point mutation in the pedigree of epidermolytic hereditary palmoplantar keratoderma perturbs keratin intermediate filament network formation."
Kobayashi S., Tanaka T., Matsuyoshi N., Imamura S.
FEBS Lett. 386:149-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 147-372, VARIANT EPPK GLN-163.
[6]"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] OF 157-623.
[7]"Human placenta contains an epithelial scatter protein."
Rosen E.M., Meromsky L., Romero R., Setter E., Goldberg I.
Biochem. Biophys. Res. Commun. 168:1082-1088(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 450-466.
[8]"Demonstration of the pathogenic effect of point mutated keratin 9 in vivo."
Kobayashi S., Kore-eda S., Tanaka T.
FEBS Lett. 447:39-43(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-163.
[9]"Regulation of keratin 9 in nonpalmoplantar keratinocytes by palmoplantar fibroblasts through epithelial-mesenchymal interactions."
Yamaguchi Y., Itami S., Tarutani M., Hosokawa K., Miura H., Yoshikawa K.
J. Invest. Dermatol. 112:483-488(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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].
[12]"Keratin 9 gene mutational heterogeneity in patients with epidermolytic palmoplantar keratoderma."
Hennies H.-C., Zehender D., Kunze J., Kuester W., Reis A.
Hum. Genet. 93:649-654(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPPK VAL-157 AND PRO-172.
[13]"Mutations of keratin 9 in two families with palmoplantar epidermolytic hyperkeratosis."
Bonifas J.M., Matsumura K., Chen M.A., Berth-Jones J., Hutchinson P.E., Zloczower M., Fritsch P.O., Epstein E.H. Jr.
J. Invest. Dermatol. 103:474-477(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK SER-161.
[14]"Epidermolytic palmoplantar keratoderma cosegregates with a keratin 9 mutation in a pedigree with breast and ovarian cancer."
Torchard D., Blanchet-Bardon C., Serova O., Langbein L., Narod S., Janin N., Goguel A.F., Bernheim A., Franke W.W., Lenoir G.M., Feunteun J.
Nat. Genet. 6:106-110(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK TYR-161.
[15]"Mutations in the 1A domain of keratin 9 in patients with epidermolytic palmoplantar keratoderma."
Rothnagel J.A., Wojcik S., Liefer K.M., Dominey A.M., Huber M., Hohl D., Roop D.R.
J. Invest. Dermatol. 104:430-433(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPPK TRP-163 AND SER-168.
[16]"A novel mutation of a leucine residue in coil 1A of keratin 9 in epidermolytic palmoplantar keratoderma."
Endo H., Hatamochi A., Shinkai H.
J. Invest. Dermatol. 109:113-115(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK VAL-160.
[17]"Mutations in keratin K9 in kindreds with epidermolytic palmoplantar keratoderma and epidemiology in Northern Ireland."
Covello S.P., Irvine A.D., McKenna K.E., Munro C.S., Nevin N.C., Smith F.J.D., Uitto J., McLean W.H.I.
J. Invest. Dermatol. 111:1207-1209(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPPK THR-157; VAL-157 AND GLN-163.
[18]"Keratin 9 mutations in the coil 1A region in epidermolytic palmoplantar keratoderma."
Szalai S., Szalai C., Becker K., Torok E.
Pediatr. Dermatol. 16:430-435(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPPK GLN-163 AND STOP-170.
[19]"Epidermolytic palmoplantar keratoderma in a Hispanic kindred resulting from a mutation in the keratin 9 gene."
Warmuth I., Cserhalmi-Friedman P.B., Schneiderman P., Grossman M.E., Christiano A.M.
Clin. Exp. Dermatol. 25:244-246(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK TRP-163.
[20]"Epidermolytic palmoplantar keratoderma of Vorner: re-evaluation of Vorner's original family and identification of a novel keratin 9 mutation."
Kuster W., Reis A., Hennies H.C.
Arch. Dermatol. Res. 294:268-272(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK ILE-161.
[21]"Diagnosis and confirmation of epidermolytic palmoplantar keratoderma by the identification of mutations in keratin 9 using denaturing high-performance liquid chromatography."
Rugg E.L., Common J.E., Wilgoss A., Stevens H.P., Buchan J., Leigh I.M., Kelsell D.P.
Br. J. Dermatol. 146:952-957(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPPK VAL-157; TRP-163; GLN-163 AND MET-171.
[22]"Novel N160I mutation of keratin 9 in a large pedigree from Hungary with epidermolytic palmoplantar keratoderma."
Csikos M., Hollo P., Becker K., Racz E., Horvath A., Karpati S.
Acta Derm. Venereol. 83:303-305(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK ILE-161.
[23]"A novel mutation of keratin 9 in epidermolytic palmoplantar keratoderma combined with knuckle pads."
Lu Y., Guo C., Liu Q., Zhang X., Cheng L., Li J., Chen B., Gao G., Zhou H., Guo Y., Li Y., Gong Y.
Am. J. Med. Genet. A 120:345-349(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK PHE-160.
[24]"Keratin 9 gene mutations in five Korean families with epidermolytic palmoplantar keratoderma."
Lee J.-H., Ahn K.-S., Lee C.-H., Youn S.-J., Kim J.-W., Lee D.-Y., Lee E.-S., Steinert P.M., Yang J.-M.
Exp. Dermatol. 12:876-881(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS EPPK HIS-161; SER-161 AND TRP-163.
[25]"A novel mutation of keratin 9 in a large Chinese family with epidermolytic palmoplantar keratoderma."
He X.-H., Zhang X.-N., Mao W., Chen H.-P., Xu L.-R., Chen H., He X.-L., Le Y.-P.
Br. J. Dermatol. 150:647-651(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK TYR-167 DEL TRP-LEU INS.
[26]"A novel keratin 9 gene mutation (Asn160His) in a Taiwanese family with epidermolytic palmoplantar keratoderma."
Lin J.-H., Lin M.-H., Yang M.-H., Chao S.-C.
Clin. Exp. Dermatol. 29:308-310(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK HIS-161.
[27]"A novel mutation of keratin 9 gene (R162P) in a Japanese family with epidermolytic palmoplantar keratoderma."
Kon A., Itagaki K., Yoneda K., Takagaki K.
Arch. Dermatol. Res. 296:375-378(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK PRO-163.
[28]"L457F missense mutation within the 2B rod domain of keratin 9 in a Japanese family with epidermolytic palmoplantar keratoderma."
Kon A., Ito N., Kudo Y., Nomura K., Yoneda K., Hanada K., Hashimoto I., Takagaki K.
Br. J. Dermatol. 155:624-626(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK PHE-458.
[29]"A novel keratin 9 gene mutation (Met156Arg) in a Japanese patient with epidermolytic palmoplantar keratoderma."
Shimazu K., Tsunemi Y., Hattori N., Saeki H., Komine M., Adachi M., Tamaki K.
Int. J. Dermatol. 45:1128-1130(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT EPPK ARG-157.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z29074 mRNA. Translation: CAA82315.1.
S69510 mRNA. Translation: AAC60619.1.
X75015 Genomic DNA. Translation: CAA52924.1.
AC019349 Genomic DNA. No translation available.
AB001594 mRNA. Translation: BAA19418.1.
BC121170 mRNA. Translation: AAI21171.1.
PIRI37984.
RefSeqNP_000217.2. NM_000226.3.
UniGeneHs.654569.

3D structure databases

ProteinModelPortalP35527.
SMRP35527. Positions 151-302, 318-460.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110055. 42 interactions.
IntActP35527. 19 interactions.
MINTMINT-4998976.
STRING9606.ENSP00000246662.

PTM databases

PhosphoSiteP35527.

Polymorphism databases

DMDM239938886.

2D gel databases

DOSAC-COBS-2DPAGEP35527.

Proteomic databases

PaxDbP35527.
PeptideAtlasP35527.
PRIDEP35527.
ProMEXP35527.

Protocols and materials databases

DNASU3857.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246662; ENSP00000246662; ENSG00000171403.
GeneID3857.
KEGGhsa:3857.
UCSCuc002hxe.4. human.

Organism-specific databases

CTD3857.
GeneCardsGC17M039722.
H-InvDBHIX0039018.
HGNCHGNC:6447. KRT9.
HPAHPA007261.
HPA009673.
MIM144200. phenotype.
149100. phenotype.
607606. gene.
neXtProtNX_P35527.
Orphanet2199. Epidermolytic palmoplantar keratoderma.
PharmGKBPA30235.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148410.
HOGENOMHOG000230975.
HOVERGENHBG013015.
InParanoidP35527.
KOK07604.
OMAEMQYETL.
OrthoDBEOG7FV3Q8.
PhylomeDBP35527.
TreeFamTF332742.

Gene expression databases

ArrayExpressP35527.
BgeeP35527.
CleanExHS_KRT9.
GenevestigatorP35527.

Family and domain databases

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

Other

GeneWikiKeratin_9.
GenomeRNAi3857.
NextBio15177.
PROP35527.
SOURCESearch...

Entry information

Entry nameK1C9_HUMAN
AccessionPrimary (citable) accession number: P35527
Secondary accession number(s): O00109, Q0IJ47, Q14665
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 16, 2009
Last modified: April 16, 2014
This is version 142 of the entry and version 3 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

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