K1C23_HUMAN
ID K1C23_HUMAN Reviewed; 422 AA.
AC Q9C075; A8K084; B7Z7J2; I3L3Q6; Q9NUR6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Keratin, type I cytoskeletal 23;
DE AltName: Full=Cytokeratin-23;
DE Short=CK-23;
DE AltName: Full=Keratin-23;
DE Short=K23;
GN Name=KRT23;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11135429;
RX DOI=10.1002/1098-2264(2000)9999:9999<::aid-gcc1070>3.0.co;2-w;
RA Zhang J.-S., Wang L., Huang H., Nelson M., Smith D.I.;
RT "Keratin 23 (K23), a novel acidic keratin, is highly induced by histone
RT deacetylase inhibitors during differentiation of pancreatic cancer cells.";
RL Genes Chromosomes Cancer 30:123-135(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ALA-303.
RC TISSUE=Placenta, Testis, and Urinary bladder;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9C075; Q06455-2: RUNX1T1; NbExp=3; IntAct=EBI-3211278, EBI-11984663;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9C075-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9C075-2; Sequence=VSP_055662;
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 -!- SIMILARITY: Belongs to the intermediate filament family.
CC {ECO:0000255|PROSITE-ProRule:PRU01188}.
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DR EMBL; AF102848; AAK00050.1; -; mRNA.
DR EMBL; AK002047; BAA92054.1; -; mRNA.
DR EMBL; AK289449; BAF82138.1; -; mRNA.
DR EMBL; AK302109; BAH13628.1; -; mRNA.
DR EMBL; AC004231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS11380.1; -. [Q9C075-1]
DR CCDS; CCDS62182.1; -. [Q9C075-2]
DR RefSeq; NP_001269362.1; NM_001282433.1. [Q9C075-2]
DR RefSeq; NP_056330.3; NM_015515.4. [Q9C075-1]
DR RefSeq; XP_005257257.1; XM_005257200.4. [Q9C075-2]
DR RefSeq; XP_011522897.1; XM_011524595.1. [Q9C075-2]
DR AlphaFoldDB; Q9C075; -.
DR SMR; Q9C075; -.
DR BioGRID; 117467; 25.
DR IntAct; Q9C075; 2.
DR STRING; 9606.ENSP00000209718; -.
DR iPTMnet; Q9C075; -.
DR PhosphoSitePlus; Q9C075; -.
DR SwissPalm; Q9C075; -.
DR BioMuta; KRT23; -.
DR DMDM; 143811410; -.
DR jPOST; Q9C075; -.
DR MassIVE; Q9C075; -.
DR PaxDb; Q9C075; -.
DR PeptideAtlas; Q9C075; -.
DR PRIDE; Q9C075; -.
DR ProteomicsDB; 47295; -.
DR ProteomicsDB; 79963; -. [Q9C075-1]
DR Antibodypedia; 1978; 293 antibodies from 29 providers.
DR DNASU; 25984; -.
DR Ensembl; ENST00000209718.8; ENSP00000209718.3; ENSG00000108244.17. [Q9C075-1]
DR Ensembl; ENST00000436344.7; ENSP00000414056.3; ENSG00000108244.17. [Q9C075-2]
DR Ensembl; ENST00000571258.6; ENSP00000460637.2; ENSG00000263309.6. [Q9C075-2]
DR Ensembl; ENST00000574480.5; ENSP00000459021.1; ENSG00000263309.6. [Q9C075-1]
DR GeneID; 25984; -.
DR KEGG; hsa:25984; -.
DR MANE-Select; ENST00000209718.8; ENSP00000209718.3; NM_015515.5; NP_056330.3.
DR UCSC; uc002hvm.3; human. [Q9C075-1]
DR CTD; 25984; -.
DR DisGeNET; 25984; -.
DR GeneCards; KRT23; -.
DR HGNC; HGNC:6438; KRT23.
DR HPA; ENSG00000108244; Group enriched (salivary gland, skin).
DR MIM; 606194; gene.
DR neXtProt; NX_Q9C075; -.
DR OpenTargets; ENSG00000108244; -.
DR PharmGKB; PA134914537; -.
DR VEuPathDB; HostDB:ENSG00000108244; -.
DR eggNOG; ENOG502QTH0; Eukaryota.
DR GeneTree; ENSGT00940000161077; -.
DR HOGENOM; CLU_012560_8_1_1; -.
DR InParanoid; Q9C075; -.
DR OMA; SQDFKVN; -.
DR PhylomeDB; Q9C075; -.
DR TreeFam; TF332742; -.
DR PathwayCommons; Q9C075; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q9C075; -.
DR BioGRID-ORCS; 25984; 14 hits in 1061 CRISPR screens.
DR ChiTaRS; KRT23; human.
DR GeneWiki; KRT23; -.
DR GenomeRNAi; 25984; -.
DR Pharos; Q9C075; Tbio.
DR PRO; PR:Q9C075; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9C075; protein.
DR Bgee; ENSG00000108244; Expressed in placenta and 91 other tissues.
DR ExpressionAtlas; Q9C075; baseline and differential.
DR Genevisible; Q9C075; HS.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
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 InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR002957; Keratin_I.
DR PANTHER; PTHR23239; PTHR23239; 1.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01248; TYPE1KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS00226; IF_ROD_1; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Intermediate filament; Keratin;
KW Reference proteome.
FT CHAIN 1..422
FT /note="Keratin, type I cytoskeletal 23"
FT /id="PRO_0000063677"
FT DOMAIN 72..382
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..71
FT /note="Head"
FT REGION 72..107
FT /note="Coil 1A"
FT REGION 108..125
FT /note="Linker 1"
FT REGION 126..217
FT /note="Coil 1B"
FT REGION 218..240
FT /note="Linker 12"
FT REGION 241..378
FT /note="Coil 2"
FT REGION 379..422
FT /note="Rod-like helical tail"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..137
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055662"
FT VARIANT 303
FT /note="T -> A (in dbSNP:rs9257)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_031608"
FT VARIANT 393
FT /note="S -> F (in dbSNP:rs17856805)"
FT /id="VAR_049785"
FT CONFLICT 137
FT /note="K -> N (in Ref. 1; AAK00050)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="K -> E (in Ref. 2; BAA92054)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="K -> E (in Ref. 2; BAA92054)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="Y -> N (in Ref. 1; AAK00050)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 422 AA; 48131 MW; A43876CCBA9CBE7D CRC64;
MNSGHSFSQT PSASFHGAGG GWGRPRSFPR APTVHGGAGG ARISLSFTTR SCPPPGGSWG
SGRSSPLLGG NGKATMQNLN DRLASYLEKV RALEEANMKL ESRILKWHQQ RDPGSKKDYS
QYEENITHLQ EQIVDGKMTN AQIILLIDNA RMAVDDFNLK YENEHSFKKD LEIEVEGLRR
TLDNLTIVTT DLEQEVEGMR KELILMKKHH EQEMEKHHVP SDFNVNVKVD TGPREDLIKV
LEDMRQEYEL IIKKKHRDLD TWYKEQSAAM SQEAASPATV QSRQGDIHEL KRTFQALEID
LQTQYSTKSA LENMLSETQS RYSCKLQDMQ EIISHYEEEL TQLRHELERQ NNEYQVLLGI
KTHLEKEITT YRRLLEGESE GTREESKSSM KVSATPKIKA ITQETINGRL VLCQVNEIQK
HA
