K2C80_HUMAN
ID K2C80_HUMAN Reviewed; 452 AA.
AC Q6KB66; Q6P1A5; Q7Z3Q0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Keratin, type II cytoskeletal 80;
DE AltName: Full=Cytokeratin-80;
DE Short=CK-80;
DE AltName: Full=Keratin-80;
DE Short=K80;
DE AltName: Full=Type-II keratin Kb20;
GN Name=KRT80; Synonyms=KB20;
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), AND TISSUE SPECIFICITY.
RC TISSUE=Scalp;
RX PubMed=15737194; DOI=10.1111/j.0022-202x.2004.23530.x;
RA Rogers M.A., Edler L., Winter H., Langbein L., Beckmann I., Schweizer J.;
RT "Characterization of new members of the human type II keratin gene family
RT and a general evaluation of the keratin gene domain on chromosome
RT 12q13.13.";
RL J. Invest. Dermatol. 124:536-544(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Endometrial adenocarcinoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Prostate;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-396, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [7]
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).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
CC -!- INTERACTION:
CC Q6KB66; P19012: KRT15; NbExp=3; IntAct=EBI-3046635, EBI-739566;
CC Q6KB66; P35900: KRT20; NbExp=3; IntAct=EBI-3046635, EBI-742094;
CC Q6KB66; P50222: MEOX2; NbExp=3; IntAct=EBI-3046635, EBI-748397;
CC Q6KB66-2; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-11999246, EBI-8643161;
CC Q6KB66-2; Q9UNS2: COPS3; NbExp=3; IntAct=EBI-11999246, EBI-350590;
CC Q6KB66-2; Q9BRX5: GINS3; NbExp=3; IntAct=EBI-11999246, EBI-2857315;
CC Q6KB66-2; P02533: KRT14; NbExp=3; IntAct=EBI-11999246, EBI-702178;
CC Q6KB66-2; P19012: KRT15; NbExp=3; IntAct=EBI-11999246, EBI-739566;
CC Q6KB66-2; P08779: KRT16; NbExp=3; IntAct=EBI-11999246, EBI-356410;
CC Q6KB66-2; P08727: KRT19; NbExp=5; IntAct=EBI-11999246, EBI-742756;
CC Q6KB66-2; P35900: KRT20; NbExp=3; IntAct=EBI-11999246, EBI-742094;
CC Q6KB66-2; Q2M2I5: KRT24; NbExp=5; IntAct=EBI-11999246, EBI-2952736;
CC Q6KB66-2; Q7Z3Y7: KRT28; NbExp=3; IntAct=EBI-11999246, EBI-11980489;
CC Q6KB66-2; Q15323: KRT31; NbExp=3; IntAct=EBI-11999246, EBI-948001;
CC Q6KB66-2; Q14532: KRT32; NbExp=4; IntAct=EBI-11999246, EBI-1044146;
CC Q6KB66-2; Q14525: KRT33B; NbExp=3; IntAct=EBI-11999246, EBI-1049638;
CC Q6KB66-2; O76011: KRT34; NbExp=5; IntAct=EBI-11999246, EBI-1047093;
CC Q6KB66-2; Q92764: KRT35; NbExp=3; IntAct=EBI-11999246, EBI-1058674;
CC Q6KB66-2; O76013-2: KRT36; NbExp=3; IntAct=EBI-11999246, EBI-11958506;
CC Q6KB66-2; O76015: KRT38; NbExp=5; IntAct=EBI-11999246, EBI-1047263;
CC Q6KB66-2; O95447: LCA5L; NbExp=3; IntAct=EBI-11999246, EBI-8473670;
CC Q6KB66-2; P25791-3: LMO2; NbExp=5; IntAct=EBI-11999246, EBI-11959475;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6KB66-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6KB66-2; Sequence=VSP_030423;
CC Name=3;
CC IsoId=Q6KB66-3; Sequence=VSP_030421, VSP_030422;
CC -!- TISSUE SPECIFICITY: Weakly expressed in tongue, but not skin or in any
CC other tissues or organs examined. {ECO:0000269|PubMed:15737194}.
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}.
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DR EMBL; AJ717743; CAG30732.1; -; mRNA.
DR EMBL; BX537567; CAD97784.1; -; mRNA.
DR EMBL; CH471111; EAW58237.1; -; Genomic_DNA.
DR EMBL; BC065180; AAH65180.1; -; mRNA.
DR CCDS; CCDS41784.1; -. [Q6KB66-2]
DR CCDS; CCDS8821.2; -. [Q6KB66-1]
DR RefSeq; NP_001074961.1; NM_001081492.1. [Q6KB66-2]
DR RefSeq; NP_872313.2; NM_182507.2. [Q6KB66-1]
DR AlphaFoldDB; Q6KB66; -.
DR SMR; Q6KB66; -.
DR BioGRID; 126858; 58.
DR ComplexPortal; CPX-5664; Keratin-80- Keratin-82 dimer complex.
DR IntAct; Q6KB66; 31.
DR STRING; 9606.ENSP00000378292; -.
DR GlyGen; Q6KB66; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6KB66; -.
DR PhosphoSitePlus; Q6KB66; -.
DR BioMuta; KRT80; -.
DR DMDM; 166218808; -.
DR EPD; Q6KB66; -.
DR jPOST; Q6KB66; -.
DR MassIVE; Q6KB66; -.
DR PaxDb; Q6KB66; -.
DR PeptideAtlas; Q6KB66; -.
DR PRIDE; Q6KB66; -.
DR ProteomicsDB; 66535; -. [Q6KB66-1]
DR ProteomicsDB; 66536; -. [Q6KB66-2]
DR ProteomicsDB; 66537; -. [Q6KB66-3]
DR Antibodypedia; 43038; 162 antibodies from 24 providers.
DR DNASU; 144501; -.
DR Ensembl; ENST00000313234.9; ENSP00000369361.2; ENSG00000167767.14. [Q6KB66-2]
DR Ensembl; ENST00000394815.3; ENSP00000378292.2; ENSG00000167767.14. [Q6KB66-1]
DR GeneID; 144501; -.
DR KEGG; hsa:144501; -.
DR MANE-Select; ENST00000394815.3; ENSP00000378292.2; NM_182507.3; NP_872313.2.
DR UCSC; uc001rzx.3; human. [Q6KB66-1]
DR CTD; 144501; -.
DR DisGeNET; 144501; -.
DR GeneCards; KRT80; -.
DR HGNC; HGNC:27056; KRT80.
DR HPA; ENSG00000167767; Tissue enriched (skin).
DR MIM; 611161; gene.
DR neXtProt; NX_Q6KB66; -.
DR OpenTargets; ENSG00000167767; -.
DR PharmGKB; PA147357831; -.
DR VEuPathDB; HostDB:ENSG00000167767; -.
DR eggNOG; ENOG502RVYD; Eukaryota.
DR GeneTree; ENSGT00940000161279; -.
DR HOGENOM; CLU_012560_5_4_1; -.
DR InParanoid; Q6KB66; -.
DR OMA; HHYEEYQ; -.
DR OrthoDB; 669704at2759; -.
DR PhylomeDB; Q6KB66; -.
DR TreeFam; TF317854; -.
DR PathwayCommons; Q6KB66; -.
DR Reactome; R-HSA-6805567; Keratinization.
DR Reactome; R-HSA-6809371; Formation of the cornified envelope.
DR SignaLink; Q6KB66; -.
DR BioGRID-ORCS; 144501; 12 hits in 1064 CRISPR screens.
DR ChiTaRS; KRT80; human.
DR GeneWiki; KRT80; -.
DR GenomeRNAi; 144501; -.
DR Pharos; Q6KB66; Tbio.
DR PRO; PR:Q6KB66; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q6KB66; protein.
DR Bgee; ENSG00000167767; Expressed in skin of abdomen and 115 other tissues.
DR Genevisible; Q6KB66; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
DR GO; GO:0045095; C:keratin filament; IBA:GO_Central.
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; IPR039008; IF_rod_dom.
DR InterPro; IPR003054; Keratin_II.
DR Pfam; PF00038; Filament; 1.
DR PRINTS; PR01276; TYPE2KERATIN.
DR SMART; SM01391; Filament; 1.
DR PROSITE; PS51842; IF_ROD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Intermediate filament; Keratin;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..452
FT /note="Keratin, type II cytoskeletal 80"
FT /id="PRO_0000314896"
FT DOMAIN 83..394
FT /note="IF rod"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188"
FT REGION 1..82
FT /note="Head"
FT REGION 82..118
FT /note="Coil 1A"
FT REGION 119..135
FT /note="Linker 1"
FT REGION 136..227
FT /note="Coil 1B"
FT REGION 228..251
FT /note="Linker 12"
FT REGION 252..390
FT /note="Coil 2"
FT REGION 391..452
FT /note="Tail"
FT REGION 412..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 334
FT /note="Stutter"
FT MOD_RES 45
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 396
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..100
FT /note="MACRSCVVGFSSLSSCEVTPVGSPRPGTSGWDSCRAPGPGFSSRSLTGCWSA
FT GTISKVTVNPGLLVPLDVKLDPAVQQLKNQEKEEMKALNDKFASLIGK -> MSCHFPG
FT SPPWALAGQPGASAPDWSTPDPFAAFLLSQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030421"
FT VAR_SEQ 190
FT /note="K -> KVACPACPRGSFLMGPGPSFPPDILLSFMPNQSPQRLKSQDQQTDRG
FT IPPSPSSSFFEALSQISSGITPTLTQEAAPQPTPALGPSIPSPTTHHCCQPQ (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_030422"
FT VAR_SEQ 413..452
FT /note="ASRSGLSKAPSRKKKGSKGPVIKITEMSEKYFSQESEVSE -> PSLPYPLC
FT SL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_030423"
FT VARIANT 238
FT /note="V -> I (in dbSNP:rs35725856)"
FT /id="VAR_049807"
FT CONFLICT 230
FT /note="Q -> L (in Ref. 1; CAG30732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 452 AA; 50525 MW; BC54C53D0566FEA3 CRC64;
MACRSCVVGF SSLSSCEVTP VGSPRPGTSG WDSCRAPGPG FSSRSLTGCW SAGTISKVTV
NPGLLVPLDV KLDPAVQQLK NQEKEEMKAL NDKFASLIGK VQALEQRNQL LETRWSFLQG
QDSAIFDLGH LYEEYQGRLQ EELRKVSQER GQLEANLLQV LEKVEEFRIR YEDEISKRTD
MEFTFVQLKK DLDAECLHRT ELETKLKSLE SFVELMKTIY EQELKDLAAQ VKDVSVTVGM
DSRCHIDLSG IVEEVKAQYD AVAARSLEEA EAYSRSQLEE QAARSAEYGS SLQSSRSEIA
DLNVRIQKLR SQILSVKSHC LKLEENIKTA EEQGELAFQD AKTKLAQLEA ALQQAKQDMA
RQLRKYQELM NVKLALDIEI ATYRKLVEGE EGRMDSPSAT VVSAVQSRCK TAASRSGLSK
APSRKKKGSK GPVIKITEMS EKYFSQESEV SE
