ID K1C39_HUMAN Reviewed; 491 AA. AC Q6A163; B2RXK6; Q6IFU6; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 2. DT 12-AUG-2020, entry version 129. DE RecName: Full=Keratin, type I cytoskeletal 39; DE AltName: Full=Cytokeratin-39; DE Short=CK-39; DE AltName: Full=Keratin-39; DE Short=K39; DE AltName: Full=Type I hair keratin Ka35; GN Name=KRT39; Synonyms=KA35; 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], TISSUE SPECIFICITY, AND VARIANT GLN-456. RC TISSUE=Scalp; 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] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLN-456. 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] RP IDENTIFICATION. RX PubMed=15085952; DOI=10.1078/0171-9335-00354; RA Hesse M., Zimek A., Weber K., Magin T.M.; RT "Comprehensive analysis of keratin gene clusters in humans and rodents."; RL Eur. J. Cell Biol. 83:19-26(2004). RN [5] RP POSSIBLE FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RX PubMed=17301834; DOI=10.1038/sj.jid.5700734; RA Langbein L., Rogers M.A., Praetzel-Wunder S., Boeckler D., Schirmacher P., RA Schweizer J.; RT "Novel type I hair keratins K39 and K40 are the last to be expressed in RT differentiation of the hair: completion of the human hair keratin RT catalog."; RL J. Invest. Dermatol. 127:1532-1535(2007). CC -!- FUNCTION: May play a role in late hair differentiation. CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins. CC -!- INTERACTION: CC Q6A163; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-11958242, EBI-11954519; CC Q6A163; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-11958242, EBI-742909; CC Q6A163; Q9BXY8: BEX2; NbExp=3; IntAct=EBI-11958242, EBI-745073; CC Q6A163; Q8TAB5: C1orf216; NbExp=3; IntAct=EBI-11958242, EBI-747505; CC Q6A163; A0A1B0GWI1: CCDC196; NbExp=3; IntAct=EBI-11958242, EBI-10181422; CC Q6A163; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-11958242, EBI-11980535; CC Q6A163; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-11958242, EBI-1752811; CC Q6A163; P14136: GFAP; NbExp=3; IntAct=EBI-11958242, EBI-744302; CC Q6A163; O14964: HGS; NbExp=3; IntAct=EBI-11958242, EBI-740220; CC Q6A163; Q86VF2-5: IGFN1; NbExp=3; IntAct=EBI-11958242, EBI-11955401; CC Q6A163; O60341: KDM1A; NbExp=3; IntAct=EBI-11958242, EBI-710124; CC Q6A163; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-11958242, EBI-6426443; CC Q6A163; P04264: KRT1; NbExp=3; IntAct=EBI-11958242, EBI-298429; CC Q6A163; P12035: KRT3; NbExp=3; IntAct=EBI-11958242, EBI-2430095; CC Q6A163; P04259: KRT6B; NbExp=3; IntAct=EBI-11958242, EBI-740907; CC Q6A163; Q7RTS7: KRT74; NbExp=3; IntAct=EBI-11958242, EBI-968660; CC Q6A163; Q01546: KRT76; NbExp=3; IntAct=EBI-11958242, EBI-2952745; CC Q6A163; Q8N1N4: KRT78; NbExp=3; IntAct=EBI-11958242, EBI-1056564; CC Q6A163; Q14533: KRT81; NbExp=3; IntAct=EBI-11958242, EBI-739648; CC Q6A163; P78385: KRT83; NbExp=3; IntAct=EBI-11958242, EBI-10221390; CC Q6A163; P78386: KRT85; NbExp=3; IntAct=EBI-11958242, EBI-1049371; CC Q6A163; O43790: KRT86; NbExp=5; IntAct=EBI-11958242, EBI-9996498; CC Q6A163; P61968: LMO4; NbExp=3; IntAct=EBI-11958242, EBI-2798728; CC Q6A163; O60437: PPL; NbExp=4; IntAct=EBI-11958242, EBI-368321; CC Q6A163; Q99633: PRPF18; NbExp=3; IntAct=EBI-11958242, EBI-2798416; CC Q6A163; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-11958242, EBI-748391; CC Q6A163; Q92529: SHC3; NbExp=3; IntAct=EBI-11958242, EBI-79084; CC Q6A163; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-11958242, EBI-455078; CC Q6A163; Q96PF1: TGM7; NbExp=3; IntAct=EBI-11958242, EBI-12029034; CC Q6A163; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-11958242, EBI-6116822; CC Q6A163; P57075-2: UBASH3A; NbExp=5; IntAct=EBI-11958242, EBI-7353612; CC Q6A163; Q9Y2B5: VPS9D1; NbExp=3; IntAct=EBI-11958242, EBI-9031083; CC Q6A163; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-11958242, EBI-740727; CC -!- TISSUE SPECIFICITY: Expressed in skin and scalp. In the hair follicle, CC it is present in the upper hair cuticle and the upper cortex. Also CC present in the in the upper portion of beard hairs (at protein level). CC {ECO:0000269|PubMed:15617563, ECO:0000269|PubMed:17301834}. CC -!- DEVELOPMENTAL STAGE: During differentiation of the hair, it is one of CC the last keratins expressed. {ECO:0000269|PubMed:17301834}. CC -!- MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar CC keratin, I (acidic) and II (neutral to basic) (40-55 and 56-70 kDa, CC respectively). CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ786657; CAH10352.1; -; mRNA. DR EMBL; AC004231; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC007455; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC157887; AAI57888.1; -; mRNA. DR EMBL; BK004054; DAA04487.1; -; mRNA. DR CCDS; CCDS11382.1; -. DR RefSeq; NP_998821.3; NM_213656.3. DR SMR; Q6A163; -. DR BioGRID; 133686; 1. DR IntAct; Q6A163; 34. DR STRING; 9606.ENSP00000347823; -. DR iPTMnet; Q6A163; -. DR PhosphoSitePlus; Q6A163; -. DR BioMuta; KRT39; -. DR DMDM; 166218816; -. DR jPOST; Q6A163; -. DR MassIVE; Q6A163; -. DR PaxDb; Q6A163; -. DR PeptideAtlas; Q6A163; -. DR PRIDE; Q6A163; -. DR ProteomicsDB; 66177; -. DR Antibodypedia; 55323; 32 antibodies. DR DNASU; 390792; -. DR Ensembl; ENST00000355612; ENSP00000347823; ENSG00000196859. DR Ensembl; ENST00000575391; ENSP00000459016; ENSG00000262164. DR GeneID; 390792; -. DR KEGG; hsa:390792; -. DR UCSC; uc002hvo.1; human. DR CTD; 390792; -. DR EuPathDB; HostDB:ENSG00000196859.7; -. DR GeneCards; KRT39; -. DR HGNC; HGNC:32971; KRT39. DR HPA; ENSG00000196859; Tissue enriched (skin). DR MIM; 616678; gene. DR neXtProt; NX_Q6A163; -. DR OpenTargets; ENSG00000196859; -. DR PharmGKB; PA147357633; -. DR eggNOG; ENOG502SH7Y; Eukaryota. DR GeneTree; ENSGT00940000162203; -. DR HOGENOM; CLU_012560_8_0_1; -. DR InParanoid; Q6A163; -. DR KO; K07604; -. DR OMA; CQNCSRI; -. DR OrthoDB; 798081at2759; -. DR PhylomeDB; Q6A163; -. DR TreeFam; TF332742; -. DR PathwayCommons; Q6A163; -. DR Reactome; R-HSA-6805567; Keratinization. DR Reactome; R-HSA-6809371; Formation of the cornified envelope. DR BioGRID-ORCS; 390792; 0 hits in 870 CRISPR screens. DR GenomeRNAi; 390792; -. DR Pharos; Q6A163; Tdark. DR PRO; PR:Q6A163; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q6A163; protein. DR Bgee; ENSG00000196859; Expressed in skin of abdomen and 36 other tissues. DR ExpressionAtlas; Q6A163; baseline and differential. 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:0070268; P:cornification; TAS:Reactome. DR GO; GO:0031424; P:keratinization; TAS:Reactome. DR Gene3D; 1.20.5.1160; -; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR042180; IF_rod_dom_coil1B. 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 Coiled coil; Intermediate filament; Keratin; Polymorphism; KW Reference proteome. FT CHAIN 1..491 FT /note="Keratin, type I cytoskeletal 39" FT /id="PRO_0000314853" FT DOMAIN 96..407 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..96 FT /note="Head" FT REGION 97..131 FT /note="Coil 1A" FT REGION 132..142 FT /note="Linker 1" FT REGION 143..243 FT /note="Coil 1B" FT REGION 244..259 FT /note="Linker 12" FT REGION 260..403 FT /note="Coil 2" FT REGION 404..491 FT /note="Tail" FT SITE 345 FT /note="Stutter" FT VARIANT 341 FT /note="T -> M (in dbSNP:rs17843021)" FT /id="VAR_038075" FT VARIANT 383 FT /note="L -> M (in dbSNP:rs17843023)" FT /id="VAR_038076" FT VARIANT 456 FT /note="R -> Q (in dbSNP:rs7213256)" FT /evidence="ECO:0000269|PubMed:15489334, FT ECO:0000269|PubMed:15617563" FT /id="VAR_038077" SQ SEQUENCE 491 AA; 55651 MW; 4299E51361B30BAC CRC64; MDTKGCTTTN SPSTPCQNCS RITNVSTISS NNGCHPGGLT VNNCQPAGHV LRIPWDQGCQ PTPRFCRKPI YLMNNFNARF SLDDCSWYGE GINSNEKETM QILNERLANY LQKVRMLERE NAELESKIQE ESNKELPVLC PDYLSYYTTI EELQQKILCT KAENSRLVSQ IDNTKLTADD LRAKYEAEVS LRQLVESDAN GLKQILNVLT LGKADLEAQV QSLKEELLCL KNNHKEEINS LQCQLGERLD IEVTAAPSAD LNQVLQEMRC QYEPIMETNR KDVEQWFNTQ IEELNQQVVT SSQQQQCCQK EIIELRRSVN TLEVELQAQH RMRDSQECIL TETEARYTAL LTQIQSLIDN LEAQLAEIRC ALERQNQEYE ILLDVKSRLE CEITTYRSLL ESSDGKRPCY PRATKCEPSP WTSCKSGAIE STAPACTSSS PCSLKEHCSA CGPLSRILVK ICTITKEIKD GKVISSYEHV QPCFIIRPAK V //