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Database: UniProt
Entry: K1C26_HUMAN
LinkDB: K1C26_HUMAN
Original site: K1C26_HUMAN 
ID   K1C26_HUMAN             Reviewed;         468 AA.
AC   Q7Z3Y9; A2RUL2; B2RNH8;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   24-JAN-2024, entry version 151.
DE   RecName: Full=Keratin, type I cytoskeletal 26;
DE   AltName: Full=Cytokeratin-26;
DE            Short=CK-26;
DE   AltName: Full=Keratin-25B;
DE            Short=K25B;
DE   AltName: Full=Keratin-26;
DE            Short=K26;
DE   AltName: Full=Type I inner root sheath-specific keratin-K25irs2;
GN   Name=KRT26 {ECO:0000312|EMBL:AAI32952.1};
GN   Synonyms=KRT25B {ECO:0000312|EMBL:CAD91905.1};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:CAD91905.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT ARG-118.
RC   TISSUE=Scalp {ECO:0000312|EMBL:CAD91905.1};
RX   PubMed=15617563; DOI=10.1111/j.1432-0436.2004.07209006.x;
RA   Rogers M.A., Winter H., Langbein L., Bleiler R., Schweizer J.;
RT   "The human type I keratin gene family: characterization of new hair
RT   follicle specific members and evaluation of the chromosome 17q21.2 gene
RT   domain.";
RL   Differentiation 72:527-540(2004).
RN   [2] {ECO:0000312|EMBL:EAW60677.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000312|EMBL:AAI32952.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4] {ECO:0000305}
RP   TISSUE SPECIFICITY.
RX   PubMed=16874310; DOI=10.1038/sj.jid.5700494;
RA   Langbein L., Rogers M.A., Praetzel-Wunder S., Helmke B., Schirmacher P.,
RA   Schweizer J.;
RT   "K25 (K25irs1), K26 (K25irs2), K27 (K25irs3), and K28 (K25irs4) represent
RT   the type I inner root sheath keratins of the human hair follicle.";
RL   J. Invest. Dermatol. 126:2377-2386(2006).
CC   -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC       {ECO:0000305}.
CC   -!- INTERACTION:
CC       Q7Z3Y9; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-12084444, EBI-465872;
CC       Q7Z3Y9; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-12084444, EBI-10749669;
CC       Q7Z3Y9; Q9NVL1-2: FAM86C1P; NbExp=3; IntAct=EBI-12084444, EBI-12845222;
CC       Q7Z3Y9; O14964: HGS; NbExp=5; IntAct=EBI-12084444, EBI-740220;
CC       Q7Z3Y9; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-12084444, EBI-14069005;
CC       Q7Z3Y9; P04264: KRT1; NbExp=3; IntAct=EBI-12084444, EBI-298429;
CC       Q7Z3Y9; P12035: KRT3; NbExp=3; IntAct=EBI-12084444, EBI-2430095;
CC       Q7Z3Y9; P02538: KRT6A; NbExp=3; IntAct=EBI-12084444, EBI-702198;
CC       Q7Z3Y9; P48668: KRT6C; NbExp=5; IntAct=EBI-12084444, EBI-2564105;
CC       Q7Z3Y9; Q3SY84: KRT71; NbExp=3; IntAct=EBI-12084444, EBI-2952676;
CC       Q7Z3Y9; Q7RTS7: KRT74; NbExp=3; IntAct=EBI-12084444, EBI-968660;
CC       Q7Z3Y9; O95678: KRT75; NbExp=3; IntAct=EBI-12084444, EBI-2949715;
CC       Q7Z3Y9; Q14533: KRT81; NbExp=3; IntAct=EBI-12084444, EBI-739648;
CC       Q7Z3Y9; P78386: KRT85; NbExp=3; IntAct=EBI-12084444, EBI-1049371;
CC       Q7Z3Y9; P59942: MCCD1; NbExp=3; IntAct=EBI-12084444, EBI-11987923;
CC       Q7Z3Y9; P41440-3: SLC19A1; NbExp=3; IntAct=EBI-12084444, EBI-17438674;
CC       Q7Z3Y9; O95295: SNAPIN; NbExp=3; IntAct=EBI-12084444, EBI-296723;
CC       Q7Z3Y9; P51687: SUOX; NbExp=3; IntAct=EBI-12084444, EBI-3921347;
CC       Q7Z3Y9; Q9UM00-1: TMCO1; NbExp=3; IntAct=EBI-12084444, EBI-11614122;
CC       Q7Z3Y9; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-12084444, EBI-492476;
CC       Q7Z3Y9; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-12084444, EBI-6116822;
CC       Q7Z3Y9; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12084444, EBI-739895;
CC   -!- TISSUE SPECIFICITY: Strongly expressed in skin and scalp, and weak
CC       expression observed in thymus and tongue. In the hair follicle,
CC       expression is restricted to the mid- to upper inner root sheath
CC       cuticle, being present slightly above the apex of the dermal papilla
CC       (at protein level). {ECO:0000269|PubMed:15617563,
CC       ECO:0000269|PubMed:16874310}.
CC   -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar
CC       keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the intermediate filament family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR   EMBL; AJ564205; CAD91905.1; -; mRNA.
DR   EMBL; CH471152; EAW60677.1; -; Genomic_DNA.
DR   EMBL; BC132951; AAI32952.1; -; mRNA.
DR   EMBL; BC136896; AAI36897.1; -; mRNA.
DR   CCDS; CCDS11374.1; -.
DR   RefSeq; NP_853517.2; NM_181539.4.
DR   AlphaFoldDB; Q7Z3Y9; -.
DR   SMR; Q7Z3Y9; -.
DR   BioGRID; 131677; 27.
DR   IntAct; Q7Z3Y9; 23.
DR   STRING; 9606.ENSP00000334798; -.
DR   iPTMnet; Q7Z3Y9; -.
DR   PhosphoSitePlus; Q7Z3Y9; -.
DR   SwissPalm; Q7Z3Y9; -.
DR   BioMuta; KRT26; -.
DR   DMDM; 162416254; -.
DR   jPOST; Q7Z3Y9; -.
DR   MassIVE; Q7Z3Y9; -.
DR   PaxDb; 9606-ENSP00000334798; -.
DR   PeptideAtlas; Q7Z3Y9; -.
DR   ProteomicsDB; 69097; -.
DR   Antibodypedia; 57607; 106 antibodies from 18 providers.
DR   DNASU; 353288; -.
DR   Ensembl; ENST00000335552.5; ENSP00000334798.4; ENSG00000186393.6.
DR   GeneID; 353288; -.
DR   KEGG; hsa:353288; -.
DR   MANE-Select; ENST00000335552.5; ENSP00000334798.4; NM_181539.5; NP_853517.2.
DR   UCSC; uc002hvf.4; human.
DR   AGR; HGNC:30840; -.
DR   CTD; 353288; -.
DR   GeneCards; KRT26; -.
DR   HGNC; HGNC:30840; KRT26.
DR   HPA; ENSG00000186393; Tissue enriched (skin).
DR   MIM; 616675; gene.
DR   neXtProt; NX_Q7Z3Y9; -.
DR   OpenTargets; ENSG00000186393; -.
DR   PharmGKB; PA134863261; -.
DR   VEuPathDB; HostDB:ENSG00000186393; -.
DR   eggNOG; ENOG502SMDE; Eukaryota.
DR   GeneTree; ENSGT00940000161950; -.
DR   HOGENOM; CLU_012560_8_3_1; -.
DR   InParanoid; Q7Z3Y9; -.
DR   OMA; IQCETLS; -.
DR   OrthoDB; 4640531at2759; -.
DR   PhylomeDB; Q7Z3Y9; -.
DR   TreeFam; TF332742; -.
DR   PathwayCommons; Q7Z3Y9; -.
DR   Reactome; R-HSA-6805567; Keratinization.
DR   Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR   SignaLink; Q7Z3Y9; -.
DR   BioGRID-ORCS; 353288; 10 hits in 1130 CRISPR screens.
DR   GenomeRNAi; 353288; -.
DR   Pharos; Q7Z3Y9; Tbio.
DR   PRO; PR:Q7Z3Y9; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q7Z3Y9; Protein.
DR   Bgee; ENSG00000186393; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 7 other cell types or tissues.
DR   GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005882; C:intermediate filament; IEA:UniProtKB-KW.
DR   GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR   GO; GO:0030855; P:epithelial cell differentiation; IBA:GO_Central.
DR   GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central.
DR   Gene3D; 1.20.5.170; -; 1.
DR   Gene3D; 1.20.5.500; Single helix bin; 1.
DR   Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1.
DR   InterPro; IPR039008; IF_rod_dom.
DR   InterPro; IPR002957; Keratin_I.
DR   PANTHER; PTHR23239; INTERMEDIATE FILAMENT; 1.
DR   PANTHER; PTHR23239:SF162; KERATIN, TYPE I CYTOSKELETAL 26; 1.
DR   Pfam; PF00038; Filament; 1.
DR   PRINTS; PR01248; TYPE1KERATIN.
DR   SMART; SM01391; Filament; 1.
DR   SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2.
DR   PROSITE; PS51842; IF_ROD_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Intermediate filament; Keratin; Reference proteome.
FT   CHAIN           1..468
FT                   /note="Keratin, type I cytoskeletal 26"
FT                   /id="PRO_0000312697"
FT   DOMAIN          83..398
FT                   /note="IF rod"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT   REGION          1..82
FT                   /note="Head"
FT                   /evidence="ECO:0000255"
FT   REGION          83..118
FT                   /note="Coil 1A"
FT                   /evidence="ECO:0000255"
FT   REGION          119..140
FT                   /note="Linker 1"
FT                   /evidence="ECO:0000255"
FT   REGION          141..232
FT                   /note="Coil 1B"
FT                   /evidence="ECO:0000255"
FT   REGION          233..255
FT                   /note="Linker 12"
FT                   /evidence="ECO:0000255"
FT   REGION          256..394
FT                   /note="Coil 2"
FT                   /evidence="ECO:0000255"
FT   REGION          395..465
FT                   /note="Tail"
FT                   /evidence="ECO:0000255"
FT   VARIANT         118
FT                   /note="W -> R (in dbSNP:rs9898164)"
FT                   /evidence="ECO:0000269|PubMed:15617563"
FT                   /id="VAR_056006"
FT   CONFLICT        149
FT                   /note="I -> T (in Ref. 1; CAD91905)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   468 AA;  51911 MW;  E21E4E13443C5209 CRC64;
     MSFRLSGGSR RICSRTGSGR LSGGGTGFVA GNVCVGSGAR SSFSCTLEGI SSGGSFCNSG
     GGLGSGACAG FLGNEHSLLS GNEKVTMQNL NDRLASYLDH VHALEEANAD LEQKIKGWYE
     KCEPGSSREH DHDYSRYFSV IEDLKRQIIS ATICNASIVL QNDNARLTAD DFRLKYENEL
     ALHHSVEADT SGLRRVLDEL TLCTTDLEIQ CETLSEELTY LKKSHEEEME VLQYTAGGNV
     NVEMNATPGV DLTVLLNNMR AEYEDLAEQN RKDAEAWFNE RSATLQQQIS DHEGAATAAR
     NELTELKRNL QTLEIELQSL MAVKHSYECS LAETEGNYCN QLQQIQDQIG VMEEQLQQIR
     TETEGQKLEY EQLLDVKIFL EKEIDIYCNL LDGEERKSKS TCYKSKGYRP VNSGNQAKDS
     TEETIVKTVV EELDQIGNLL SLRVHSVEEK SSKISNITVE QRVPSKAP
//
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