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Keratin, type II cytoskeletal 2 epidermal (Cytokeratin-2e) (CK-2e) (Epithelial keratin-2e) (Keratin-2 epidermis) (Keratin-2e) (K2e) (Type-II keratin Kb2)

 K22E_HUMAN              Reviewed;         639 AA.
P35908; Q4VAQ2;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
27-SEP-2017, entry version 164.
RecName: Full=Keratin, type II cytoskeletal 2 epidermal;
AltName: Full=Cytokeratin-2e;
Short=CK-2e;
AltName: Full=Epithelial keratin-2e;
AltName: Full=Keratin-2 epidermis;
AltName: Full=Keratin-2e;
Short=K2e;
AltName: Full=Type-II keratin Kb2;
Name=KRT2; Synonyms=KRT2A, KRT2E;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY,
DEVELOPMENTAL STAGE, AND VARIANT GLY-101.
TISSUE=Thigh epidermis;
PubMed=1380918; DOI=10.1016/0014-4827(92)90412-2;
Collin C., Moll R., Kubicka S., Ouhayoun J.-P., Franke W.W.;
"Characterization of human cytokeratin 2, an epidermal cytoskeletal
protein synthesized late during differentiation.";
Exp. Cell Res. 202:132-141(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS IBS TYR-186 AND LYS-476,
AND VARIANT GLY-101.
PubMed=9804344; DOI=10.1046/j.1523-1747.1998.00371.x;
Smith F.J.D., Maingi C., Covello S.P., Higgins C., Schmidt M.,
Lane E.B., Uitto J., Leigh I.M., McLean W.H.I.;
"Genomic organization and fine mapping of the keratin 2e gene (KRT2E):
K2e V1 domain polymorphism and novel mutations in ichthyosis bullosa
of Siemens.";
J. Invest. Dermatol. 111:817-821(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
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]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10233306; DOI=10.1046/j.1365-2133.1999.02755.x;
Smith L.T., Underwood R.A., McLean W.H.I.;
"Ontogeny and regional variability of keratin 2e (K2e) in developing
human fetal skin: a unique spatial and temporal pattern of keratin
expression in development.";
Br. J. Dermatol. 140:582-591(1999).
[6]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12598329; DOI=10.1016/S0002-9440(10)63891-6;
Bloor B.K., Tidman N., Leigh I.M., Odell E., Dogan B., Wollina U.,
Ghali L., Waseem A.;
"Expression of keratin K2e in cutaneous and oral lesions: association
with keratinocyte activation, proliferation, and keratinization.";
Am. J. Pathol. 162:963-975(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[11]
VARIANT IBS LYS-487.
PubMed=7521371; DOI=10.1111/1523-1747.ep12394307;
McLean W.H.I., Morley S.M., Lane E.B., Eady R.A.J., Griffiths W.A.D.,
Paige D.G., Harper J.I., Higgins C., Leigh I.M.;
"Ichthyosis bullosa of Siemens -- a disease involving keratin 2e.";
J. Invest. Dermatol. 103:277-281(1994).
[12]
VARIANTS IBS PRO-181; PRO-484 AND LYS-487.
PubMed=8077693; DOI=10.1111/1523-1747.ep12394414;
Kremer H., Zeeuwen P., McLean W.H.I., Mariman E.C.M., Lane E.B.,
van de Kerkhof P.C.M., Ropers H.-H., Steijlen P.M.;
"Ichthyosis bullosa of Siemens is caused by mutations in the keratin
2e gene.";
J. Invest. Dermatol. 103:286-289(1994).
[13]
VARIANTS IBS ASP-487 AND LYS-487.
PubMed=7524919; DOI=10.1038/ng0894-485;
Rothnagel J.A., Traupe H., Wojcik S., Huber M., Hohl D.,
Pittelkow M.R., Saeki H., Ishibashi Y., Roop D.R.;
"Mutations in the rod domain of keratin 2e in patients with ichthyosis
bullosa of Siemens.";
Nat. Genet. 7:485-490(1994).
[14]
VARIANTS IBS LYS-487 AND LYS-488.
PubMed=9036938; DOI=10.1111/1523-1747.ep12286487;
Jones D.O., Watts C., Mills C., Sharpe G., Marks R., Bowden P.E.;
"A new keratin 2e mutation in ichthyosis bullosa of Siemens.";
J. Invest. Dermatol. 108:354-356(1997).
[15]
VARIANT IBS PRO-479.
PubMed=9204966; DOI=10.1111/1523-1747.ep12276775;
Yang J.-M., Lee S., Bang H.-D., Kim W.-S., Lee E.-S., Steinert P.M.;
"A novel threonine-to-proline mutation at the end of 2B rod domain in
the keratin 2e chain in ichthyosis bullosa of Siemens.";
J. Invest. Dermatol. 109:116-118(1997).
[16]
VARIANT IBS LYS-487.
PubMed=9833038; DOI=10.1080/000155598442683;
Yang J.-M., Lee E.-S., Kang H.-J., Choi G.-S., Yoneda K., Jung S.-Y.,
Park K.-B., Steinert P.M., Lee E.-S.;
"A glutamate to lysine mutation at the end of 2B rod domain of keratin
2e gene in ichthyosis bullosa of Siemens.";
Acta Derm. Venereol. 78:417-419(1998).
[17]
VARIANT IBS LYS-487.
PubMed=10233323; DOI=10.1046/j.1365-2133.1999.02772.x;
Basarab T., Smith F.J., Jolliffe V.M., McLean W.H.I., Neill S.,
Rustin M.H., Eady R.A.;
"Ichthyosis bullosa of Siemens: report of a family with evidence of a
keratin 2e mutation, and a review of the literature.";
Br. J. Dermatol. 140:689-695(1999).
[18]
VARIANT IBS ASN-182.
PubMed=10084318; DOI=10.1046/j.1523-1747.1999.00529.x;
Arin M.J., Longley M.A., Epstein E.H. Jr., Scott G., Goldsmith L.A.,
Rothnagel J.A., Roop D.R.;
"A novel mutation in the 1A domain of keratin 2e in ichthyosis bullosa
of Siemens.";
J. Invest. Dermatol. 112:380-382(1999).
[19]
VARIANT IBS VAL-476.
PubMed=10564334; DOI=10.1046/j.1365-2230.1999.00514.x;
Moraru R., Cserhalmi-Friedman P.B., Grossman M.E., Schneiderman P.,
Christiano A.M.;
"Ichthyosis bullosa of Siemens resulting from a novel missense
mutation near the helix termination motif of the keratin 2e gene.";
Clin. Exp. Dermatol. 24:412-415(1999).
[20]
VARIANT IBS ASN-477.
PubMed=11167982; DOI=10.1046/j.1365-2230.2000.00728.x;
Irvine A.D., Smith F.J., Shum K.W., Williams H.C., McLean W.H.I.;
"A novel mutation in the 2B domain of keratin 2e causing ichthyosis
bullosa of Siemens.";
Clin. Exp. Dermatol. 25:648-651(2000).
[21]
VARIANTS IBS LYS-465 AND ASP-465.
PubMed=10688369; DOI=10.1034/j.1600-0625.2000.009001011.x;
Suga Y., Arin M.J., Scott G., Goldsmith L.A., Magro C.M., Baden L.A.,
Baden H.P., Roop D.R.;
"Hot spot mutations in keratin 2e suggest a correlation between
genotype and phenotype in patients with ichthyosis bullosa of
Siemens.";
Exp. Dermatol. 9:11-15(2000).
[22]
VARIANT IBS ASP-186.
PubMed=10620137; DOI=10.1046/j.1523-1747.2000.00817.x;
Takizawa Y., Akiyama M., Nagashima M., Shimizu H.;
"A novel asparagine-->aspartic acid mutation in the rod 1A domain in
keratin 2e in a Japanese family with ichthyosis bullosa of Siemens.";
J. Invest. Dermatol. 114:193-195(2000).
[23]
VARIANT IBS LYS-186.
PubMed=11531804; DOI=10.1046/j.1365-2133.2001.04327.x;
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).
[24]
VARIANTS IBS PRO-484 AND LYS-487.
PubMed=15949009; DOI=10.1111/j.1365-2133.2005.06598.x;
Akiyama M., Tsuji-Abe Y., Yanagihara M., Nakajima K., Kodama H.,
Yaosaka M., Abe M., Sawamura D., Shimizu H.;
"Ichthyosis bullosa of Siemens: its correct diagnosis facilitated by
molecular genetic testing.";
Br. J. Dermatol. 152:1353-1356(2005).
-!- FUNCTION: Probably contributes to terminal cornification.
Associated with keratinocyte activation, proliferation and
keratinization. {ECO:0000269|PubMed:12598329,
ECO:0000269|PubMed:1380918}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
Associates with KRT10 (By similarity). {ECO:0000250}.
-!- INTERACTION:
A1A4E9:KRT13; NbExp=3; IntAct=EBI-1247312, EBI-10171552;
P13646:KRT13; NbExp=3; IntAct=EBI-1247312, EBI-1223876;
P19012:KRT15; NbExp=6; IntAct=EBI-1247312, EBI-739566;
P08727:KRT19; NbExp=8; IntAct=EBI-1247312, EBI-742756;
Q15323:KRT31; NbExp=9; IntAct=EBI-1247312, EBI-948001;
O76015:KRT38; NbExp=9; IntAct=EBI-1247312, EBI-1047263;
Q6A162:KRT40; NbExp=10; IntAct=EBI-1247312, EBI-10171697;
-!- TISSUE SPECIFICITY: Expressed in the upper spinous and granular
suprabasal layers of normal adult epidermal tissues from most body
sites including thigh, breast nipple, foot sole, penile shaft and
axilla. Not present in foreskin, squamous metaplasias and
carcinomas. Expression in hypertrophic and keloid scars begins in
the deepest suprabasal layer. Weakly expressed in normal gingiva
and tongue, however expression is induced in benign keratoses of
lingual mucosa and in mild-to-moderate oral dysplasia with
orthokeratinization. {ECO:0000269|PubMed:10233306,
ECO:0000269|PubMed:12598329, ECO:0000269|PubMed:1380918}.
-!- DEVELOPMENTAL STAGE: Synthesized during maturation of epidermal
keratinocytes and localized in the upper intermediate cells of
fetal skin. Earliest expression is at 10 weeks in the developing
embryo in the presumptive nail bed of developing digits, shifting
to the proximal nail fold by 13.5 weeks. At 12.5 weeks, detected
in scattered cells of the intermediate layer of trunk skin. At
19.3 weeks, regional expression patterns were observed in upper
intermediate keratinocytes of cheek, trunk, dorsal and ventral
knee, elbow and dorsal hand. Distal areas around the periumbilical
region showed increased number of positive cells and by 15 weeks
is expressed in small groups of cells in the fetal hair follicles.
{ECO:0000269|PubMed:10233306, ECO:0000269|PubMed:1380918}.
-!- DISEASE: Ichthyosis bullosa of Siemens (IBS) [MIM:146800]: A rare
autosomal dominant skin disorder displaying a type of
epidermolytic hyperkeratosis characterized by generalized erythema
and extensive blistering from birth. Large, dark gray
hyperkeratoses are observed in later weeks. The skin of IBS
patients is unusually fragile and has a tendency to shed the outer
layers of the epidermis, producing localized denuded areas
(molting effect). IBS usually improves with age so that in most
middle-aged patients the hyperkeratosis and keratotic
lichenification is limited to the flexural folds of the major
joints. {ECO:0000269|PubMed:10084318, ECO:0000269|PubMed:10233323,
ECO:0000269|PubMed:10564334, ECO:0000269|PubMed:10620137,
ECO:0000269|PubMed:10688369, ECO:0000269|PubMed:11167982,
ECO:0000269|PubMed:11531804, ECO:0000269|PubMed:15949009,
ECO:0000269|PubMed:7521371, ECO:0000269|PubMed:7524919,
ECO:0000269|PubMed:8077693, ECO:0000269|PubMed:9036938,
ECO:0000269|PubMed:9204966, ECO:0000269|PubMed:9804344,
ECO:0000269|PubMed:9833038}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
-!- WEB RESOURCE: Name=Wikipedia; Note=Keratin-2A entry;
URL="https://en.wikipedia.org/wiki/Keratin_2A";
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EMBL; M99061; AAC83410.1; -; mRNA.
EMBL; AF019084; AAB81946.1; -; Genomic_DNA.
EMBL; AC055715; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC055716; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC096294; AAH96294.1; -; mRNA.
EMBL; BC099643; AAH99643.1; -; mRNA.
EMBL; BC099644; AAH99644.1; -; mRNA.
CCDS; CCDS8835.1; -.
PIR; A44861; A44861.
RefSeq; NP_000414.2; NM_000423.2.
UniGene; Hs.707; -.
ProteinModelPortal; P35908; -.
SMR; P35908; -.
BioGrid; 110047; 57.
IntAct; P35908; 22.
MINT; MINT-1208580; -.
STRING; 9606.ENSP00000310861; -.
iPTMnet; P35908; -.
PhosphoSitePlus; P35908; -.
SwissPalm; P35908; -.
BioMuta; KRT2; -.
DMDM; 239938650; -.
EPD; P35908; -.
PaxDb; P35908; -.
PeptideAtlas; P35908; -.
PRIDE; P35908; -.
Ensembl; ENST00000309680; ENSP00000310861; ENSG00000172867.
GeneID; 3849; -.
KEGG; hsa:3849; -.
UCSC; uc001sat.4; human.
CTD; 3849; -.
DisGeNET; 3849; -.
EuPathDB; HostDB:ENSG00000172867.3; -.
GeneCards; KRT2; -.
H-InvDB; HIX0036877; -.
HGNC; HGNC:6439; KRT2.
HPA; CAB037321; -.
HPA; HPA006299; -.
MalaCards; KRT2; -.
MIM; 146800; phenotype.
MIM; 600194; gene.
neXtProt; NX_P35908; -.
OpenTargets; ENSG00000172867; -.
Orphanet; 455; Superficial epidermolytic ichthyosis.
PharmGKB; PA30227; -.
eggNOG; ENOG410IJPR; Eukaryota.
eggNOG; ENOG410XWGZ; LUCA.
GeneTree; ENSGT00760000118796; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; P35908; -.
KO; K07605; -.
OMA; GEHAIKD; -.
OrthoDB; EOG091G09KR; -.
PhylomeDB; P35908; -.
TreeFam; TF317854; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GeneWiki; Keratin_2A; -.
GenomeRNAi; 3849; -.
PRO; PR:P35908; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000172867; -.
CleanEx; HS_KRT2; -.
Genevisible; P35908; HS.
GO; GO:0001533; C:cornified envelope; IDA:CAFA.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; TAS:ProtInc.
GO; GO:0045095; C:keratin filament; IEA:Ensembl.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:Ensembl.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0030280; F:structural constituent of epidermis; IDA:CAFA.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0045109; P:intermediate filament organization; IEA:Ensembl.
GO; GO:0031424; P:keratinization; IDA:UniProtKB.
GO; GO:0032980; P:keratinocyte activation; IDA:UniProtKB.
GO; GO:0003334; P:keratinocyte development; IEA:Ensembl.
GO; GO:0051546; P:keratinocyte migration; IDA:UniProtKB.
GO; GO:0043616; P:keratinocyte proliferation; IDA:UniProtKB.
GO; GO:0018149; P:peptide cross-linking; IDA:CAFA.
GO; GO:0098773; P:skin epidermis development; IC:CAFA.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR032444; Keratin_2_head.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
Pfam; PF16208; Keratin_2_head; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF; 1.
1: Evidence at protein level;
Coiled coil; Complete proteome; Disease mutation; Ichthyosis;
Intermediate filament; Keratin; Methylation; Phosphoprotein;
Polymorphism; Reference proteome.
CHAIN 1 639 Keratin, type II cytoskeletal 2
epidermal.
/FTId=PRO_0000063715.
REGION 1 177 Head.
REGION 178 487 Rod.
REGION 178 213 Coil 1A.
REGION 214 232 Linker 1.
REGION 233 324 Coil 1B.
REGION 325 348 Linker 12.
REGION 349 487 Coil 2.
REGION 488 639 Tail.
SITE 429 429 Stutter.
MOD_RES 20 20 Asymmetric dimethylarginine.
{ECO:0000250|UniProtKB:Q3TTY5}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
VARIANT 101 101 S -> G (in dbSNP:rs2634041).
{ECO:0000269|PubMed:1380918,
ECO:0000269|PubMed:9804344}.
/FTId=VAR_058293.
VARIANT 181 181 Q -> P (in IBS; dbSNP:rs57510142).
{ECO:0000269|PubMed:8077693}.
/FTId=VAR_003865.
VARIANT 182 182 I -> N (in IBS; dbSNP:rs61622714).
{ECO:0000269|PubMed:10084318}.
/FTId=VAR_010514.
VARIANT 186 186 N -> D (in IBS; dbSNP:rs137852631).
{ECO:0000269|PubMed:10620137}.
/FTId=VAR_010515.
VARIANT 186 186 N -> K (in IBS; dbSNP:rs61726457).
{ECO:0000269|PubMed:11531804}.
/FTId=VAR_017829.
VARIANT 186 186 N -> Y (in IBS; dbSNP:rs61726454).
{ECO:0000269|PubMed:9804344}.
/FTId=VAR_009185.
VARIANT 219 219 G -> D (in dbSNP:rs638043).
/FTId=VAR_058294.
VARIANT 465 465 E -> D (in IBS).
{ECO:0000269|PubMed:10688369}.
/FTId=VAR_031082.
VARIANT 465 465 E -> K (in IBS; dbSNP:rs758760389).
{ECO:0000269|PubMed:10688369}.
/FTId=VAR_031083.
VARIANT 476 476 E -> K (in IBS; dbSNP:rs56829062).
{ECO:0000269|PubMed:9804344}.
/FTId=VAR_009186.
VARIANT 476 476 E -> V (in IBS; dbSNP:rs60537449).
{ECO:0000269|PubMed:10564334}.
/FTId=VAR_031084.
VARIANT 477 477 I -> N (in IBS).
{ECO:0000269|PubMed:11167982}.
/FTId=VAR_031085.
VARIANT 479 479 T -> P (in IBS; dbSNP:rs61726453).
{ECO:0000269|PubMed:9204966}.
/FTId=VAR_009187.
VARIANT 484 484 L -> P (in IBS; dbSNP:rs61726451).
{ECO:0000269|PubMed:15949009,
ECO:0000269|PubMed:8077693}.
/FTId=VAR_010516.
VARIANT 487 487 E -> D (in IBS; dbSNP:rs61726450).
{ECO:0000269|PubMed:7524919}.
/FTId=VAR_003866.
VARIANT 487 487 E -> K (in IBS; dbSNP:rs61726449).
{ECO:0000269|PubMed:10233323,
ECO:0000269|PubMed:15949009,
ECO:0000269|PubMed:7521371,
ECO:0000269|PubMed:7524919,
ECO:0000269|PubMed:8077693,
ECO:0000269|PubMed:9036938,
ECO:0000269|PubMed:9833038}.
/FTId=VAR_003867.
VARIANT 488 488 E -> K (in IBS; dbSNP:rs61726452).
{ECO:0000269|PubMed:9036938}.
/FTId=VAR_031086.
CONFLICT 108 108 F -> FGGGSGF (in Ref. 1; AAC83410 and 2;
AAB81946). {ECO:0000305}.
SEQUENCE 639 AA; 65433 MW; B80526BAF70078A7 CRC64;
MSCQISCKSR GRGGGGGGFR GFSSGSAVVS GGSRRSTSSF SCLSRHGGGG GGFGGGGFGS
RSLVGLGGTK SISISVAGGG GGFGAAGGFG GRGGGFGGGS SFGGGSGFSG GGFGGGGFGG
GRFGGFGGPG GVGGLGGPGG FGPGGYPGGI HEVSVNQSLL QPLNVKVDPE IQNVKAQERE
QIKTLNNKFA SFIDKVRFLE QQNQVLQTKW ELLQQMNVGT RPINLEPIFQ GYIDSLKRYL
DGLTAERTSQ NSELNNMQDL VEDYKKKYED EINKRTAAEN DFVTLKKDVD NAYMIKVELQ
SKVDLLNQEI EFLKVLYDAE ISQIHQSVTD TNVILSMDNS RNLDLDSIIA EVKAQYEEIA
QRSKEEAEAL YHSKYEELQV TVGRHGDSLK EIKIEISELN RVIQRLQGEI AHVKKQCKNV
QDAIADAEQR GEHALKDARN KLNDLEEALQ QAKEDLARLL RDYQELMNVK LALDVEIATY
RKLLEGEECR MSGDLSSNVT VSVTSSTISS NVASKAAFGG SGGRGSSSGG GYSSGSSSYG
SGGRQSGSRG GSGGGGSISG GGYGSGGGSG GRYGSGGGSK GGSISGGGYG SGGGKHSSGG
GSRGGSSSGG GYGSGGGGSS SVKGSSGEAF GSSVTFSFR


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