KRT86_HUMAN
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 03-AUG-2022, entry version 178.
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 -!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
CC URL="http://www.interfil.org";
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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; 73.
DR ComplexPortal; CPX-5663; Keratin-36 - Keratin-86 dimer complex.
DR IntAct; O43790; 46.
DR STRING; 9606.ENSP00000444533; -.
DR ChEMBL; CHEMBL4523139; -.
DR iPTMnet; O43790; -.
DR PhosphoSitePlus; O43790; -.
DR SwissPalm; O43790; -.
DR BioMuta; KRT86; -.
DR jPOST; O43790; -.
DR MassIVE; O43790; -.
DR PaxDb; O43790; -.
DR PeptideAtlas; O43790; -.
DR PRIDE; O43790; -.
DR ProteomicsDB; 49170; -.
DR Antibodypedia; 56637; 65 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 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; HSLCGGY; -.
DR OrthoDB; 557821at2759; -.
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 1056 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 right coronary artery and 110 other tissues.
DR ExpressionAtlas; O43790; baseline and differential.
DR Genevisible; O43790; HS.
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 InterPro; IPR018039; IF_conserved.
DR InterPro; IPR039008; IF_rod_dom.
DR InterPro; IPR032444; Keratin_2_head.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR Pfam; PF16208; Keratin_2_head; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
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; 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
