[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=2580302 [NCBI, ExPASy, EBI, Israel, Japan] Johnson L.D., Idler W.W., Zhou X.-M., Roop D.R., Steinert P.M.; "Structure of a gene for the human epidermal 67-kDa keratin."; Proc. Natl. Acad. Sci. U.S.A. 82:1896-1900(1985).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. DOI=10.1006/bbrc.2000.3110; PubMed=10903910 [NCBI, ExPASy, EBI, Israel, Japan] Whittock N.V., Eady R.A.J., McGrath J.A.; "Genomic organization and amplification of the human epidermal type II keratin genes K1 and K5."; Biochem. Biophys. Res. Commun. 274:149-152(2000).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN NEPPK. DOI=10.1046/j.1523-1747.2001.13041234.x; PubMed=11286630 [NCBI, ExPASy, EBI, Israel, Japan] Hatsell S.J., Eady R.A.J., Wennerstrand L., Dopping-Hepenstal P.J., Leigh I.M., Munro C., Kelsell D.P.; "Novel splice site mutation in keratin 1 underlies mild epidermolytic palmoplantar keratoderma in three kindreds."; J. Invest. Dermatol. 116:606-609(2001).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT TYR-358. TISSUE=Skin; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[5]	PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 152-644. PubMed=2581964 [NCBI, ExPASy, EBI, Israel, Japan] Steinert P.M., Parry D.A.D., Idler W.W., Johnson L.D., Steven A.C., Roop D.R.; "Amino acid sequences of mouse and human epidermal type II keratins of Mr 67,000 provide a systematic basis for the structural and functional diversity of the end domains of keratin intermediate filament subunits."; J. Biol. Chem. 260:7142-7149(1985).
[6]	PROTEIN SEQUENCE OF 2-8. TISSUE=Platelet; DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan] Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.; "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."; Nat. Biotechnol. 21:566-569(2003).
[7]	CITRULLINATION. DOI=10.1006/bbrc.1996.1240; PubMed=8780679 [NCBI, ExPASy, EBI, Israel, Japan] Senshu T., Kan S., Ogawa H., Manabe M., Asaga H.; "Preferential deimination of keratin K1 and filaggrin during the terminal differentiation of human epidermis."; Biochem. Biophys. Res. Commun. 225:712-719(1996).
[8]	INVOLVEMENT IN IHCM. DOI=10.1046/j.1523-1747.2001.01292.x; PubMed=11286616 [NCBI, ExPASy, EBI, Israel, Japan] Sprecher E., Ishida-Yamamoto A., Becker O.M., Marekov L.N., Miller C.J., Steinert P.M., Neldner K., Richard G.; "Evidence for novel functions of the keratin tail emerging from a mutation causing ichthyosis hystrix."; J. Invest. Dermatol. 116:511-519(2001).
[9]	CITRULLINATION. DOI=10.1046/j.0022-202x.2001.01671.x; PubMed=11841545 [NCBI, ExPASy, EBI, Israel, Japan] Ishida-Yamamoto A., Senshu T., Eady R.A.J., Takahashi H., Shimizu H., Akiyama M., Iizuka H.; "Sequential reorganization of cornified cell keratin filaments involving filaggrin-mediated compaction and keratin 1 deimination."; J. Invest. Dermatol. 118:282-287(2002).
[10]	INVOLVEMENT IN PPKS3. DOI=10.1046/j.1523-1747.2002.01750.x; PubMed=11982762 [NCBI, ExPASy, EBI, Israel, Japan] Whittock N.V., Smith F.J., Wan H., Mallipeddi R., Griffiths W.A.D., Dopping-Hepenstal P.J., Ashton G.H.S., Eady R.A.J., McLean W.H.I., McGrath J.A.; "Frameshift mutation in the V2 domain of human keratin 1 results in striate palmoplantar keratoderma."; J. Invest. Dermatol. 118:838-844(2002).
[11]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1073/pnas.0507066103; PubMed=16565220 [NCBI, ExPASy, EBI, Israel, Japan] Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.; "Phosphoproteome analysis of the human mitotic spindle."; Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
[12]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-295 AND THR-297, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan] Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; J. Proteome Res. 6:4150-4162(2007).
[13]	VARIANT BCIE PRO-161. DOI=10.1016/0092-8674(92)90315-4; PubMed=1381288 [NCBI, ExPASy, EBI, Israel, Japan] Chipev C.C., Korge B.P., Markova N., Bale S.J., Digiovanna J.J., Compton J.G., Steinert P.M.; "A leucine-->proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis."; Cell 70:821-828(1992).
[14]	VARIANT ALLELE 1B 560-GLY--TYR-566 DEL. DOI=10.1111/1523-1747.ep12614149; PubMed=1281859 [NCBI, ExPASy, EBI, Israel, Japan] Korge B.P., Compton J.G., Steinert P.M., Mischke D.; "The two size alleles of human keratin 1 are due to a deletion in the glycine-rich carboxyl-terminal V2 subdomain."; J. Invest. Dermatol. 99:697-702(1992).
[15]	VARIANT BCIE GLN-490. PubMed=1380725 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis."; Science 257:1128-1130(1992).
[16]	VARIANT BCIE CYS-482. PubMed=7512983 [NCBI, ExPASy, EBI, Israel, Japan] Syder A.J., Yu Q.-C., Paller A.S., Giudice G., Pearson R., Fuchs E.; "Genetic mutations in the K1 and K10 genes of patients with epidermolytic hyperkeratosis. Correlation between location and disease severity."; J. Clin. Invest. 93:1533-1542(1994).
[17]	VARIANTS BCIE GLY-155; SER-188 AND PRO-193. DOI=10.1111/1523-1747.ep12371725; PubMed=7507151 [NCBI, ExPASy, EBI, Israel, Japan] Yang J.-M., Chipev C.C., Digiovanna J.J., Bale S.J., Marekov L.N., Steinert P.M., Compton J.G.; "Mutations in the H1 and 1A domains in the keratin 1 gene in epidermolytic hyperkeratosis."; J. Invest. Dermatol. 102:17-23(1994).
[18]	VARIANTS BCIE PRO-186 AND SER-188. DOI=10.1111/1523-1747.ep12371726; PubMed=7507152 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "Mutations in the rod 1A domain of keratins 1 and 10 in bullous congenital ichthyosiform erythroderma (BCIE)."; J. Invest. Dermatol. 102:24-30(1994).
[19]	VARIANT NEPPK ILE-74. DOI=10.1111/1523-1747.ep12412771; PubMed=7528239 [NCBI, ExPASy, EBI, Israel, Japan] Kimonis V., DiGiovanna J.J., Yang J.-M., Doyle S.Z., Bale S.J., Compton J.G.; "A mutation in the V1 end domain of keratin 1 in non-epidermolytic palmar-plantar keratoderma."; J. Invest. Dermatol. 103:764-769(1994).
[20]	VARIANT BCIE VAL-340. DOI=10.1046/j.1523-1747.1998.00389.x; PubMed=9856846 [NCBI, ExPASy, EBI, Israel, Japan] Kremer H., Lavrijsen A.P., McLean W.H.I., Lane E.B., Melchers D., Ruiter D.J., Mariman E.C., Steijlen P.M.; "An atypical form of bullous congenital ichthyosiform erythroderma is caused by a mutation in the L12 linker region of keratin 1."; J. Invest. Dermatol. 111:1224-1226(1998).
[21]	VARIANTS AEI PHE-479 AND THR-479. DOI=10.1086/302278; PubMed=10053007 [NCBI, ExPASy, EBI, Israel, Japan] Sybert V.P., Francis J.S., Corden L.D., Smith L.T., Weaver M., Stephens K., McLean W.H.I.; "Cyclic ichthyosis with epidermolytic hyperkeratosis: a phenotype conferred by mutations in the 2B domain of keratin K1."; Am. J. Hum. Genet. 64:732-738(1999).
[22]	VARIANT BCIE THR-188. PubMed=10232403 [NCBI, ExPASy, EBI, Israel, Japan] Arin M.J., Longley M.A., Kuster W., Huber M., Hohl D., Rothnagel J.A., Roop D.R.; "An asparagine to threonine substitution in the 1A domain of keratin 1: a novel mutation that causes epidermolytic hyperkeratosis."; Exp. Dermatol. 8:124-127(1999).
[23]	VARIANT AEI PHE-479. PubMed=10597140 [NCBI, ExPASy, EBI, Israel, Japan] Michael E.J., Schneiderman P., Grossman M.E., Christiano A.M.; "Epidermolytic hyperkeratosis with polycyclic psoriasiform plaques resulting from a mutation in the keratin 1 gene."; Exp. Dermatol. 8:501-503(1999).
[24]	VARIANT BCIE PRO-214. DOI=10.1046/j.1365-2230.2000.00625.x; PubMed=10844506 [NCBI, ExPASy, EBI, Israel, Japan] Cserhalmi-Friedman P.B., Squeo R., Gordon D., Garzon M., Schneiderman P., Grossman M.E., Christiano A.M.; "Epidermolytic hyperkeratosis in a Hispanic family resulting from a mutation in the keratin 1 gene."; Clin. Exp. Dermatol. 25:241-243(2000).
[25]	VARIANT BCIE THR-479. DOI=10.1034/j.1600-0625.2000.009001016.x; PubMed=10688370 [NCBI, ExPASy, EBI, Israel, Japan] Arin M.J., Longley M.A., Epstein E.H. Jr., Rothnagel J.A., Roop D.R.; "Identification of a novel mutation in keratin 1 in a family with epidermolytic hyperkeratosis."; Exp. Dermatol. 9:16-19(2000).
[26]	VARIANT BCIE ASP-155. DOI=10.1046/j.1365-2133.2001.04327.x; PubMed=11531804 [NCBI, ExPASy, EBI, Israel, Japan] Whittock N.V., Ashton G.H.S., Griffiths W.A.D., Eady R.A.J., McGrath J.A.; "New mutations in keratin 1 that cause bullous congenital ichthyosiform erythroderma and keratin 2e that cause ichthyosis bullosa of Siemens."; Br. J. Dermatol. 145:330-335(2001).
[27]	VARIANTS PALMOPLANTAR KERATODERMA VAL-176--LYS-197 DEL AND ALA-459--466-GLN DEL. DOI=10.1046/j.1523-1747.2002.00186.x; PubMed=12406346 [NCBI, ExPASy, EBI, Israel, Japan] Terron-Kwiatkowski A., Paller A.S., Compton J., Atherton D.J., McLean W.H., Irvine A.D.; "Two cases of primarily palmoplantar keratoderma associated with novel mutations in keratin 1."; J. Invest. Dermatol. 119:966-971(2002).
[28]	VARIANTS BCIE LYS-188 AND PRO-486. DOI=10.1046/j.1523-1747.2002.00061.x; PubMed=12406348 [NCBI, ExPASy, EBI, Israel, Japan] Lee D.-Y., Ahn K.-S., Lee C.-H., Rho N.-K., Lee J.-H., Lee E.-S., Steinert P.M., Yang J.-M.; "Two novel mutations in the keratin 1 gene in epidermolytic hyperkeratosis."; J. Invest. Dermatol. 119:976-977(2002).

Comments

SUBUNIT: Heterotetramer of two type I and two type II keratins. keratin-1 is generally associated with keratin-10.
INTERACTION:
Q00987:MDM2; NbExp=1; IntAct=EBI-298429, EBI-389668;
TISSUE SPECIFICITY: The source of this protein is neonatal foreskin. The 67-kDa type II keratins are expressed in terminally differentiating epidermis.
PTM: Undergoes deimination of some arginine residues (citrullination).
POLYMORPHISM: There are two size variants of KRT1, termed allele 1A and allele 1B with allelic frequencies of 0.61 and 0.39. Allele 1B lacks 7 residues compared to allele 1A.
DISEASE: Defects in KRT1 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.
DISEASE: Defects in KRT1 are the cause of ichthyosis hystrix Curth-Macklin type (IHCM) [MIM:146590]. IHCM is a genodermatosis with severe verrucous hyperkeratosis. Affected individuals manifest congenital verrucous black scale on the scalp, neck, and limbs with truncal erythema, palmo-plantar keratoderma and keratoses on the lips, ears, nipples and buttocks.
DISEASE: Defects in KRT1 are a cause of nonepidermolytic palmoplantar keratoderma (NEPPK) [MIM:600962]; also known as Unna-Thost disease.
DISEASE: Defects in KRT1 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.
DISEASE: Defects in KRT1 are the cause of keratosis palmoplantaris striata III (PPKS3) [MIM:607654]; also known as striate palmoplantar keratoderma III (SPPK3). PPKS3 is an autosomal dominant disorder affecting palm and sole skin where stratum corneum and epidermal layers are thickened. There is no involvement of non-palmoplantar skin, and both hair and nails are normal.
MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
SIMILARITY: Belongs to the intermediate filament family.
WEB RESOURCE: Name=Human Intermediate Filament Mutation Database; URL="http://www.interfil.org";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=KRT1";.
WEB RESOURCE: Name=Wikipedia; Note=Keratin-1 entry; URL="http://en.wikipedia.org/wiki/Keratin_1";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M98776; AAB47721.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF237621; AAF60327.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF304164; AAG41947.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC063697; AAH63697.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M10938; AAA36153.1; ALT_SEQ; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

A22940; KRHU2.

NP_006112.3; -.

3D structure databases

HSSP

P08670; 1GK7. [HSSP ENTRY / PDB]

ModBase

P04264.

Protein-protein interaction databases

IntAct

P04264; -.

PTM databases

PhosphoSite

P04264; -.

2D gel databases

SWISS-2DPAGE

P04264; -.

Aarhus/Ghent-2DPAGE

4606; NEPHGE.

REPRODUCTION-2DPAGE

P04264; -.

Organism-specific databases

HGNC:6412; KRT1.

KRT1; Homo sapiens.

CAB002153; -.

113800; phenotype. [NCBI / EBI]
139350; gene. [NCBI / EBI]
146590; phenotype. [NCBI / EBI]
600962; phenotype. [NCBI / EBI]
607602; phenotype. [NCBI / EBI]
607654; phenotype. [NCBI / EBI]

Orphanet

312; Bullous ichthyosiform erythroderma congenita.
458; Ichthyosis hystrix.
50942; Keratosis palmoplantaris striata.
313; Lamellar ichthyosis.

PharmGKB

PA30199; -.

GeneCards

P04264.

Gene expression databases

ArrayExpress

P04264; -.

CleanEx

HS_KRT1; -.

GermOnline

ENSG00000167768; Homo sapiens.

Ontologies

GO:0005882;	Cellular component: intermediate filament (traceable author statement from ProtInc).
GO:0016020;	Cellular component: membrane (inferred from direct assay from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from mutant phenotype from UniProtKB).
GO:0004872;	Molecular function: receptor activity (non-traceable author statement from UniProtKB).
GO:0005200;	Molecular function: structural constituent of cytoskeleton (traceable author statement from ProtInc).
GO:0005529;	Molecular function: sugar binding (inferred from physical interaction from UniProtKB).
GO:0001867;	Biological process: complement activation, lectin pathway (inferred from physical interaction from UniProtKB).
GO:0008544;	Biological process: epidermis development (traceable author statement from ProtInc).
GO:0042730;	Biological process: fibrinolysis (non-traceable author statement from UniProtKB).
GO:0045765;	Biological process: regulation of angiogenesis (non-traceable author statement from UniProtKB).
GO:0006979;	Biological process: response to oxidative stress (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

IPR016044; F.
IPR001664; IF.
IPR003054; Keratin_II.
Graphical view of domain structure.

PANTHER

PTHR23239; IF; 1.
PTHR23239:SF18; Keratin_II; 1.

Pfam

PF00038; Filament; 1.
Pfam graphical view of domain structure.

PRINTS

PR01276; TYPE2KERATIN.

PROSITE

PS00226; IF; 1.

BLOCKS

P04264.

Genome annotation databases

Ensembl

ENSG00000167768; Homo sapiens. [Contig view]

GeneID

3848; -.

KEGG

hsa:3848; -.

Phylogenomic databases

HOGENOM

P04264; -.

HOVERGEN

P04264; -.

Other

KRT1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Citrullination; Coiled coil; Direct protein sequencing; Disease mutation; Ichthyosis; Intermediate filament; Keratin; Phosphoprotein; Polymorphism.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 644`	`643`	`Keratin, type II cytoskeletal 1.`	`PRO_0000063709`
`REGION`	`2 179`	`178`	`Head.`
`REGION`	`180 489`	`310`	`Rod.`
`REGION`	`180 215`	`36`	`Coil 1A.`
`REGION`	`216 234`	`19`	`Linker 1.`
`REGION`	`235 326`	`92`	`Coil 1B.`
`REGION`	`327 350`	`24`	`Linker 12.`
`REGION`	`351 489`	`139`	`Coil 2.`
`REGION`	`490 644`	`155`	`Tail.`
`COMPBIAS`	`2 151`	`150`	`Gly/Phe/Ser-rich.`
`COMPBIAS`	`502 641`	`140`	`Gly/Ser-rich.`
`SITE`	`433 433`	`1`	`Stutter.`
`MOD_RES`	`21 21`		`Phosphoserine.`
`MOD_RES`	`66 66`		`Phosphoserine (By similarity).`
`MOD_RES`	`295 295`		`Phosphotyrosine.`
`MOD_RES`	`297 297`		`Phosphothreonine.`
`VARIANT`	`74 74`	`1`	`K -> I (in NEPPK).`	`VAR_017819`
`VARIANT`	`155 155`	`1`	`V -> D (in BCIE).`	`VAR_017820`
`VARIANT`	`155 155`	`1`	`V -> G (in BCIE).`	`VAR_003853`
`VARIANT`	`161 161`	`1`	`L -> P (in BCIE).`	`VAR_003854`
`VARIANT`	`176 197`	`22`	`Missing (in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas).`	`VAR_038627`
`VARIANT`	`186 186`	`1`	`S -> P (in BCIE).`	`VAR_003855`
`VARIANT`	`188 188`	`1`	`N -> K (in BCIE).`	`VAR_017821`
`VARIANT`	`188 188`	`1`	`N -> S (in BCIE).`	`VAR_003856`
`VARIANT`	`188 188`	`1`	`N -> T (in BCIE; severe).`	`VAR_017822`
`VARIANT`	`193 193`	`1`	`S -> P (in BCIE).`	`VAR_003857`
`VARIANT`	`214 214`	`1`	`L -> P (in BCIE).`	`VAR_017823`
`VARIANT`	`312 312`	`1`	`I -> V.`	`VAR_003858`
`VARIANT`	`330 330`	`1`	`I -> T.`	`VAR_003859`
`VARIANT`	`340 340`	`1`	`D -> V (in BCIE).`	`VAR_017824`
`VARIANT`	`358 358`	`1`	`N -> Y (in dbSNP:rs1050872 [NCBI]).`	`VAR_003860`
`VARIANT`	`454 454`	`1`	`A -> S (in dbSNP:rs17678945 [NCBI]).`	`VAR_038628`
`VARIANT`	`459 466`	`8`	`Missing (in palmoplantar keratoderma; and mild ichthyosis largely limited to the flexural areas).`	`VAR_038629`
`VARIANT`	`479 479`	`1`	`I -> F (in AEI).`	`VAR_017825`
`VARIANT`	`479 479`	`1`	`I -> T (in AEI and BCIE).`	`VAR_017826`
`VARIANT`	`482 482`	`1`	`Y -> C (in BCIE).`	`VAR_017827`
`VARIANT`	`486 486`	`1`	`L -> P (in BCIE).`	`VAR_017828`
`VARIANT`	`490 490`	`1`	`E -> Q (in BCIE).`	`VAR_003861`
`VARIANT`	`537 537`	`1`	`G -> C.`	`VAR_003862`
`VARIANT`	`560 566`	`7`	`Missing (in allele 1B).`	`VAR_003864`
`VARIANT`	`633 633`	`1`	`R -> K (in dbSNP:rs14024 [NCBI]).`	`VAR_003863`

Sequence information

Length: 644 AA [This is the length of the unprocessed precursor]

Molecular weight: 66018 Da [This is the MW of the unprocessed precursor]

CRC64: 468F83CA61A455C4 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSRQFSSRSG YRSGGGFSSG SAGIINYQRR TTSSSTRRSG GGGGRFSSCG GGGGSFGAGG 

        70         80         90        100        110        120 
GFGSRSLVNL GGSKSISISV ARGGGRGSGF GGGYGGGGFG GGGFGGGGFG GGGIGGGGFG 

       130        140        150        160        170        180 
GFGSGGGGFG GGGFGGGGYG GGYGPVCPPG GIQEVTINQS LLQPLNVEID PEIQKVKSRE 

       190        200        210        220        230        240 
REQIKSLNNQ FASFIDKVRF LEQQNQVLQT KWELLQQVDT STRTHNLEPY FESFINNLRR 

       250        260        270        280        290        300 
RVDQLKSDQS RLDSELKNMQ DMVEDYRNKY EDEINKRTNA ENEFVTIKKD VDGAYMTKVD 

       310        320        330        340        350        360 
LQAKLDNLQQ EIDFLTALYQ AELSQMQTQI SETNVILSMD NNRSLDLDSI IAEVKAQNED 

       370        380        390        400        410        420 
IAQKSKAEAE SLYQSKYEEL QITAGRHGDS VRNSKIEISE LNRVIQRLRS EIDNVKKQIS 

       430        440        450        460        470        480 
NLQQSISDAE QRGENALKDA KNKLNDLEDA LQQAKEDLAR LLRDYQELMN TKLALDLEIA 

       490        500        510        520        530        540 
TYRTLLEGEE SRMSGECAPN VSVSVSTSHT TISGGGSRGG GGGGYGSGGS SYGSGGGSYG 

       550        560        570        580        590        600 
SGGGGGGGRG SYGSGGSSYG SGGGSYGSGG GGGGHGSYGS GSSSGGYRGG SGGGGGGSSG 

       610        620        630        640 
GRGSGGGSSG GSIGGRGSSS GGVKSSGGSS SVRFVSTTYS GVTR

P04264 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools