P35527 (K1C9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Keratin, type I cytoskeletal 9

Alternative name(s):
Cytokeratin-9
Short name=CK-9
Keratin-9
Short name=K9

Gene names

Name:

KRT9

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	623 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Intermediate filament Keratin
Disease	Disease mutation Palmoplantar keratoderma
Domain	Coiled coil
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	intermediate filament organization Inferred from mutant phenotype Ref.8. Source: UniProtKB skin development Inferred from direct assay Ref.1. Source: UniProtKB spermatogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	intermediate filament Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	structural constituent of cytoskeleton Traceable author statement Ref.5. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 623	623	Keratin, type I cytoskeletal 9		PRO_0000063640
Regions
	Region	1 – 152	152	Head
	Region	153 – 461	309	Rod
	Region	153 – 188	36	Coil 1A
	Region	189 – 207	19	Linker 1
	Region	208 – 299	92	Coil 1B
	Region	300 – 322	23	Linker 12
	Region	323 – 461	139	Coil 2
	Region	462 – 623	162	Tail
	Compositional bias	15 – 26	12	Poly-Gly
Natural variations
	Natural variant	157	1	M → R in EPPK. Ref.29		VAR_036805
	Natural variant	157	1	M → T in EPPK. Ref.17 Corresponds to variant rs59510579 [ dbSNP | Ensembl ].		VAR_010499
	Natural variant	157	1	M → V in EPPK. Ref.12 Ref.17 Ref.21 Corresponds to variant rs58597584 [ dbSNP | Ensembl ].		VAR_010500
	Natural variant	160	1	L → F in EPPK; with knuckle pads. Ref.23 Corresponds to variant rs28940896 [ dbSNP | Ensembl ].		VAR_035438
	Natural variant	160	1	L → V in EPPK. Ref.16		VAR_010501
	Natural variant	161	1	N → H in EPPK. Ref.24 Ref.26		VAR_036806
	Natural variant	161	1	N → I in EPPK. Ref.20 Ref.22		VAR_036807
	Natural variant	161	1	N → K in EPPK. Ref.2 Corresponds to variant rs57536312 [ dbSNP | Ensembl ].		VAR_003822
	Natural variant	161	1	N → S in EPPK. Ref.13 Ref.24 Corresponds to variant rs56707768 [ dbSNP | Ensembl ].		VAR_010502
	Natural variant	161	1	N → Y in EPPK. Ref.14 Corresponds to variant rs59296273 [ dbSNP | Ensembl ].		VAR_010503
	Natural variant	163	1	R → P in EPPK. Ref.27		VAR_036808
	Natural variant	163	1	R → Q in EPPK. Ref.2 Ref.5 Ref.17 Ref.18 Ref.21 Corresponds to variant rs57758262 [ dbSNP | Ensembl ].		VAR_003823
	Natural variant	163	1	R → W in EPPK. Ref.2 Ref.15 Ref.19 Ref.21 Ref.24 Corresponds to variant rs59616921 [ dbSNP | Ensembl ].		VAR_003824
	Natural variant	167	1	Y → WL in EPPK.		VAR_036809
	Natural variant	168	1	L → S in EPPK. Ref.15 Corresponds to variant rs61157095 [ dbSNP | Ensembl ].		VAR_003825
	Natural variant	171	1	V → M in EPPK. Ref.21 Corresponds to variant rs57019720 [ dbSNP | Ensembl ].		VAR_035439
	Natural variant	172	1	Q → P in EPPK. Ref.12 Corresponds to variant rs59878153 [ dbSNP | Ensembl ].		VAR_010504
	Natural variant	458	1	L → F in EPPK. Ref.28 Corresponds to variant rs58120120 [ dbSNP | Ensembl ].		VAR_036810
Experimental info
	Mutagenesis	163	1	R → QHA: Leads to aggregate formation. Ref.8
	Sequence conflict	12 – 13	2	SR → T in AAC60619. Ref.1
	Sequence conflict	12 – 13	2	SR → T in CAA52924. Ref.2
	Sequence conflict	41	1	G → R in AAC60619. Ref.1
	Sequence conflict	41	1	G → R in CAA82315. Ref.1
	Sequence conflict	41	1	G → R in CAA52924. Ref.2
	Sequence conflict	134	1	F → L in AAC60619. Ref.1
	Sequence conflict	134	1	F → L in CAA82315. Ref.1
	Sequence conflict	134	1	F → L in CAA52924. Ref.2
	Sequence conflict	157 – 170	14	MQELN…SYLDK → HLGAGSTPITASQP in AAI21171. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P35527 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: 45C833749B63873D	FASTA	623	62,064
	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

References

	« Hide 'large scale' referencesShow '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. , 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, 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.

Web resources

Human Intermediate Filament Mutation Database

GeneReviews

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.
IPI	IPI00019359.
PIR	I37984.
RefSeq	NP_000217.2. NM_000226.3.
UniGene	Hs.654569.
3D structure databases
ProteinModelPortal	P35527.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35527. 17 interactions.
MINT	MINT-4998976.
STRING	9606.ENSP00000246662.
PTM databases
PhosphoSite	P35527.
Polymorphism databases
DMDM	239938886.
2D gel databases
DOSAC-COBS-2DPAGE	P35527.
Proteomic databases
PaxDb	P35527.
PeptideAtlas	P35527.
PRIDE	P35527.
ProMEX	P35527.
Protocols and materials databases
DNASU	3857.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000246662; ENSP00000246662; ENSG00000171403.
GeneID	3857.
KEGG	hsa:3857.
UCSC	uc002hxe.4. human.
Organism-specific databases
CTD	3857.
GeneCards	GC17M039722.
H-InvDB	HIX0039018.
HGNC	HGNC:6447. KRT9.
HPA	HPA007261. HPA009673.
MIM	144200. phenotype. 149100. phenotype. 607606. gene.
neXtProt	NX_P35527.
Orphanet	2199. Epidermolytic palmoplantar keratoderma.
PharmGKB	PA30235.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG148410.
HOGENOM	HOG000230975.
HOVERGEN	HBG013015.
InParanoid	P35527.
KO	K07604.
OMA	MALKKNH.
OrthoDB	EOG4BCDNC.
PhylomeDB	P35527.
Gene expression databases
Bgee	P35527.
CleanEx	HS_KRT9.
Genevestigator	P35527.
GermOnline	ENSG00000171403. 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	3857.
NextBio	15177.
SOURCE	Search...

Entry information

Entry name

K1C9_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 134 of the entry and version 3 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.