ID KRT86_HUMAN Reviewed; 486 AA. AC O43790; P78387; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 27-MAR-2024, entry version 187. DE RecName: Full=Keratin, type II cuticular Hb6; DE AltName: Full=Hair keratin K2.11; DE AltName: Full=Keratin-86; DE Short=K86; DE AltName: Full=Type II hair keratin Hb6; DE AltName: Full=Type-II keratin Kb26; GN Name=KRT86; Synonyms=KRTHB6; 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 [GENOMIC DNA]. RX PubMed=9457912; DOI=10.1046/j.1523-1747.1998.00097.x; RA Bowden P.E., Hainey S.D., Parker G., Jones D.O., Zimonjic D., Popescu N., RA Hodgins M.B.; RT "Characterization and chromosomal localization of human hair-specific RT keratin genes and comparative expression during the hair growth cycle."; RL J. Invest. Dermatol. 110:158-164(1998). RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-486, AND TISSUE SPECIFICITY. RX PubMed=9084137; DOI=10.1046/j.1432-0436.1997.6130187.x; RA Rogers M.A., Langbein L., Praetzel S., Krieg T., Winter H., Schweizer J.; RT "Sequences and differential expression of three novel human type-II hair RT keratins."; RL Differentiation 61:187-194(1997). RN [4] RP VARIANTS MNLIX LYS-413 AND ASP-413. RX PubMed=9402962; DOI=10.1007/s004390050607; RA Winter H., Rogers M.A., Gebhardt M., Wollina U., Boxall L., Chitayat D., RA Babul-Hirji R., Stevens H.P., Zlotogorski A., Schweizer J.; RT "A new mutation in the type II hair cortex keratin hHb1 involved in the RT inherited hair disorder monilethrix."; RL Hum. Genet. 101:165-169(1997). RN [5] RP VARIANTS MNLIX ASP-114 AND LYS-402. RX PubMed=10469314; DOI=10.1046/j.1523-1747.1999.00685.x; RA Winter H., Clark R.D., Tarras-Wahlberg C., Rogers M.A., Schweizer J.; RT "Monilethrix: a novel mutation (Glu402Lys) in the helix termination motif RT and the first causative mutation (Asn114Asp) in the helix initiation motif RT of the type II hair keratin hHb6."; RL J. Invest. Dermatol. 113:263-266(1999). RN [6] RP VARIANTS MNLIX ASP-114; HIS-114 AND LYS-413. RX PubMed=10504448; DOI=10.1046/j.1523-1747.1999.00722.x; RA Korge B.P., Hamm H., Jury C.S., Traupe H., Irvine A.D., Healy E., RA Birch-MacHin M.A., Rees J.L., Messenger A.G., Holmes S.C., Parry D.A., RA Munro C.S.; RT "Identification of novel mutations in basic hair keratins hHb1 and hHb6 in RT monilethrix: implications for protein structure and clinical phenotype."; RL J. Invest. Dermatol. 113:607-612(1999). RN [7] RP VARIANTS MNLIX GLN-402 AND LYS-402. RX PubMed=10594761; DOI=10.1046/j.1523-1747.1999.00777.x; RA Pearce E.G., Smith S.K., Lanigan S.W., Bowden P.E.; RT "Two different mutations in the same codon of a type II hair keratin (hHb6) RT in patients with monilethrix."; RL J. Invest. Dermatol. 113:1123-1127(1999). RN [8] RP VARIANTS MNLIX PRO-409 AND PRO-410. RX PubMed=25557232; DOI=10.1111/exd.12624; RA van Steensel M., Vreeburg M., Urbina M.T., Lopez P., Morice-Picard F., RA van Geel M.; RT "Novel KRT83 and KRT86 mutations associated with monilethrix."; RL Exp. Dermatol. 24:222-224(2015). CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins. CC -!- INTERACTION: CC O43790; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-9996498, EBI-11523526; CC O43790; Q8IYE0: CCDC146; NbExp=3; IntAct=EBI-9996498, EBI-10749669; CC O43790; Q07002: CDK18; NbExp=3; IntAct=EBI-9996498, EBI-746238; CC O43790; Q86XR8-3: CEP57; NbExp=3; IntAct=EBI-9996498, EBI-11752486; CC O43790; Q02930-3: CREB5; NbExp=3; IntAct=EBI-9996498, EBI-10192698; CC O43790; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-9996498, EBI-3867333; CC O43790; Q9Y223-2: GNE; NbExp=3; IntAct=EBI-9996498, EBI-11975289; CC O43790; O14964: HGS; NbExp=3; IntAct=EBI-9996498, EBI-740220; CC O43790; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-9996498, EBI-3918847; CC O43790; Q14005-2: IL16; NbExp=3; IntAct=EBI-9996498, EBI-17178971; CC O43790; Q15040: JOSD1; NbExp=3; IntAct=EBI-9996498, EBI-2510602; CC O43790; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-9996498, EBI-2556193; CC O43790; P02533: KRT14; NbExp=3; IntAct=EBI-9996498, EBI-702178; CC O43790; P19012: KRT15; NbExp=7; IntAct=EBI-9996498, EBI-739566; CC O43790; P08779: KRT16; NbExp=3; IntAct=EBI-9996498, EBI-356410; CC O43790; P08727: KRT19; NbExp=3; IntAct=EBI-9996498, EBI-742756; CC O43790; Q7Z3Z0: KRT25; NbExp=3; IntAct=EBI-9996498, EBI-11980019; CC O43790; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-9996498, EBI-3044087; CC O43790; Q7Z3Y7: KRT28; NbExp=3; IntAct=EBI-9996498, EBI-11980489; CC O43790; Q15323: KRT31; NbExp=3; IntAct=EBI-9996498, EBI-948001; CC O43790; Q14532: KRT32; NbExp=3; IntAct=EBI-9996498, EBI-1044146; CC O43790; Q14525: KRT33B; NbExp=3; IntAct=EBI-9996498, EBI-1049638; CC O43790; O76011: KRT34; NbExp=3; IntAct=EBI-9996498, EBI-1047093; CC O43790; Q92764: KRT35; NbExp=3; IntAct=EBI-9996498, EBI-1058674; CC O43790; O76013-2: KRT36; NbExp=5; IntAct=EBI-9996498, EBI-11958506; CC O43790; O76014: KRT37; NbExp=3; IntAct=EBI-9996498, EBI-1045716; CC O43790; O76015: KRT38; NbExp=3; IntAct=EBI-9996498, EBI-1047263; CC O43790; Q6A163: KRT39; NbExp=5; IntAct=EBI-9996498, EBI-11958242; CC O43790; Q6A162: KRT40; NbExp=3; IntAct=EBI-9996498, EBI-10171697; CC O43790; Q01546: KRT76; NbExp=3; IntAct=EBI-9996498, EBI-2952745; CC O43790; O60336: MAPKBP1; NbExp=3; IntAct=EBI-9996498, EBI-947402; CC O43790; P50222: MEOX2; NbExp=3; IntAct=EBI-9996498, EBI-748397; CC O43790; Q13064: MKRN3; NbExp=3; IntAct=EBI-9996498, EBI-2340269; CC O43790; P61970: NUTF2; NbExp=3; IntAct=EBI-9996498, EBI-591778; CC O43790; Q14990: ODF1; NbExp=3; IntAct=EBI-9996498, EBI-10234557; CC O43790; O43482: OIP5; NbExp=3; IntAct=EBI-9996498, EBI-536879; CC O43790; Q7RTU3: OLIG3; NbExp=3; IntAct=EBI-9996498, EBI-10225049; CC O43790; Q9HCM1: RESF1; NbExp=3; IntAct=EBI-9996498, EBI-308368; CC O43790; Q14D33: RTP5; NbExp=3; IntAct=EBI-9996498, EBI-10217913; CC O43790; Q92529: SHC3; NbExp=3; IntAct=EBI-9996498, EBI-79084; CC O43790; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-9996498, EBI-750487; CC O43790; Q3SY00: TSGA10IP; NbExp=3; IntAct=EBI-9996498, EBI-10241197; CC O43790; Q96IQ9: ZNF414; NbExp=3; IntAct=EBI-9996498, EBI-744257; CC O43790; Q8N720: ZNF655; NbExp=3; IntAct=EBI-9996498, EBI-625509; CC -!- TISSUE SPECIFICITY: Synthesis begins slightly higher in the hair shaft CC than HB1 and HB3 and continues much farther up, ending in the CC keratogeneous zone. {ECO:0000269|PubMed:9084137}. CC -!- DISEASE: Monilethrix (MNLIX) [MIM:158000]: A disorder clinically CC characterized by alopecia and follicular papules. Affected hairs have CC uniform elliptical nodes of normal thickness and intermittent CC constrictions, internodes at which the hair easily breaks. Usually only CC the scalp is involved, but in severe forms, the secondary sexual hair, CC eyebrows, eyelashes, and nails may also be affected. CC {ECO:0000269|PubMed:10469314, ECO:0000269|PubMed:10504448, CC ECO:0000269|PubMed:10594761, ECO:0000269|PubMed:25557232, CC ECO:0000269|PubMed:9402962}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: There are two types of hair/microfibrillar keratin, I CC (acidic) and II (neutral to basic). 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; AJ000263; CAA03979.1; -; Genomic_DNA. DR EMBL; BC069585; AAH69585.1; -; mRNA. DR EMBL; X99142; CAA67579.1; -; mRNA. DR CCDS; CCDS41785.1; -. DR RefSeq; NP_001307127.1; NM_001320198.1. DR RefSeq; XP_016874785.1; XM_017019296.1. DR AlphaFoldDB; O43790; -. DR SMR; O43790; -. DR BioGRID; 110090; 76. DR ComplexPortal; CPX-5663; Keratin-36 - Keratin-86 dimer complex. DR IntAct; O43790; 50. DR STRING; 9606.ENSP00000444533; -. DR ChEMBL; CHEMBL4523139; -. DR GlyGen; O43790; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; O43790; -. DR PhosphoSitePlus; O43790; -. DR SwissPalm; O43790; -. DR BioMuta; KRT86; -. DR jPOST; O43790; -. DR MassIVE; O43790; -. DR PaxDb; 9606-ENSP00000444533; -. DR PeptideAtlas; O43790; -. DR ProteomicsDB; 49170; -. DR Antibodypedia; 56637; 77 antibodies from 17 providers. DR DNASU; 3892; -. DR Ensembl; ENST00000293525.5; ENSP00000293525.5; ENSG00000170442.12. DR Ensembl; ENST00000423955.7; ENSP00000444533.1; ENSG00000170442.12. DR GeneID; 3892; -. DR KEGG; hsa:3892; -. DR MANE-Select; ENST00000423955.7; ENSP00000444533.1; NM_001320198.2; NP_001307127.1. DR UCSC; uc001sad.3; human. DR AGR; HGNC:6463; -. DR CTD; 3892; -. DR DisGeNET; 3892; -. DR GeneCards; KRT86; -. DR HGNC; HGNC:6463; KRT86. DR HPA; ENSG00000170442; Tissue enriched (skin). DR MalaCards; KRT86; -. DR MIM; 158000; phenotype. DR MIM; 601928; gene. DR neXtProt; NX_O43790; -. DR OpenTargets; ENSG00000170442; -. DR Orphanet; 573; Monilethrix. DR PharmGKB; PA30252; -. DR VEuPathDB; HostDB:ENSG00000170442; -. DR eggNOG; ENOG502RTZU; Eukaryota. DR GeneTree; ENSGT00940000161838; -. DR HOGENOM; CLU_012560_5_0_1; -. DR InParanoid; O43790; -. DR OMA; AVNDAKC; -. DR PhylomeDB; O43790; -. DR TreeFam; TF317854; -. DR PathwayCommons; O43790; -. DR Reactome; R-HSA-6805567; Keratinization. DR Reactome; R-HSA-6809371; Formation of the cornified envelope. DR SignaLink; O43790; -. DR BioGRID-ORCS; 3892; 131 hits in 1133 CRISPR screens. DR ChiTaRS; KRT86; human. DR GeneWiki; KRT86; -. DR GenomeRNAi; 3892; -. DR Pharos; O43790; Tbio. DR PRO; PR:O43790; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; O43790; Protein. DR Bgee; ENSG00000170442; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 112 other cell types or tissues. DR ExpressionAtlas; O43790; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB. DR GO; GO:0045095; C:keratin filament; IPI:ComplexPortal. DR GO; GO:0030280; F:structural constituent of skin epidermis; IBA:GO_Central. DR GO; GO:0045109; P:intermediate filament organization; IBA:GO_Central. DR GO; GO:0031424; P:keratinization; 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; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR032444; Keratin_2_head. DR InterPro; IPR003054; Keratin_II. DR PANTHER; PTHR45616; GATA-TYPE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR45616:SF52; KERATIN, TYPE II CUTICULAR HB6; 1. DR Pfam; PF00038; Filament; 1. DR Pfam; PF16208; Keratin_2_head; 1. DR PRINTS; PR01276; TYPE2KERATIN. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR Genevisible; O43790; HS. PE 1: Evidence at protein level; KW Coiled coil; Disease variant; Intermediate filament; Isopeptide bond; KW Keratin; Reference proteome; Ubl conjugation. FT CHAIN 1..486 FT /note="Keratin, type II cuticular Hb6" FT /id="PRO_0000063704" FT DOMAIN 106..417 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 1..106 FT /note="Head" FT REGION 107..141 FT /note="Coil 1A" FT REGION 142..151 FT /note="Linker 1" FT REGION 152..252 FT /note="Coil 1B" FT REGION 253..269 FT /note="Linker 12" FT REGION 270..413 FT /note="Coil 2" FT REGION 414..486 FT /note="Tail" FT CROSSLNK 212 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000250|UniProtKB:P78386" FT VARIANT 114 FT /note="N -> D (in MNLIX; dbSNP:rs61091894)" FT /evidence="ECO:0000269|PubMed:10469314, FT ECO:0000269|PubMed:10504448" FT /id="VAR_018125" FT VARIANT 114 FT /note="N -> H (in MNLIX; dbSNP:rs61091894)" FT /evidence="ECO:0000269|PubMed:10504448" FT /id="VAR_023053" FT VARIANT 402 FT /note="E -> K (in MNLIX; dbSNP:rs60687604)" FT /evidence="ECO:0000269|PubMed:10469314, FT ECO:0000269|PubMed:10594761" FT /id="VAR_018127" FT VARIANT 402 FT /note="E -> Q (in MNLIX; dbSNP:rs60687604)" FT /evidence="ECO:0000269|PubMed:10594761" FT /id="VAR_018126" FT VARIANT 409 FT /note="L -> P (in MNLIX)" FT /evidence="ECO:0000269|PubMed:25557232" FT /id="VAR_073050" FT VARIANT 410 FT /note="L -> P (in MNLIX)" FT /evidence="ECO:0000269|PubMed:25557232" FT /id="VAR_073051" FT VARIANT 413 FT /note="E -> D (in MNLIX; dbSNP:rs121909130)" FT /evidence="ECO:0000269|PubMed:9402962" FT /id="VAR_018129" FT VARIANT 413 FT /note="E -> K (in MNLIX; dbSNP:rs121909129)" FT /evidence="ECO:0000269|PubMed:10504448, FT ECO:0000269|PubMed:9402962" FT /id="VAR_018128" FT CONFLICT 62 FT /note="S -> D (in Ref. 3; CAA67579)" FT /evidence="ECO:0000305" SQ SEQUENCE 486 AA; 53501 MW; 5ED86FB4CCA62688 CRC64; MTCGSYCGGR AFSCISACGP RPGRCCITAA PYRGISCYRG LTGGFGSHSV CGGFRAGSCG RSFGYRSGGV CGPSPPCITT VSVNESLLTP LNLEIDPNAQ CVKQEEKEQI KSLNSRFAAF IDKVRFLEQQ NKLLETKLQF YQNRECCQSN LEPLFEGYIE TLRREAECVE ADSGRLASEL NHVQEVLEGY KKKYEEEVSL RATAENEFVA LKKDVDCAYL RKSDLEANVE ALIQEIDFLR RLYEEEIRVL QSHISDTSVV VKLDNSRDLN MDCIIAEIKA QYDDIVTRSR AEAESWYRSK CEEMKATVIR HGETLRRTKE EINELNRMIQ RLTAEVENAK CQNSKLEAAV AQSEQQGEAA LSDARCKLAE LEGALQKAKQ DMACLIREYQ EVMNSKLGLD IEIATYRRLL EGEEQRLCEG VGSVNVCVSS SRGGVVCGDL CASTTAPVVS TRVSSVPSNS NVVVGTTNAC APSARVGVCG GSCKRC //