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Keratin, type II cytoskeletal 80 (Cytokeratin-80) (CK-80) (Keratin-80) (K80) (Type-II keratin Kb20)

 K2C80_HUMAN             Reviewed;         452 AA.
Q6KB66; Q6P1A5; Q7Z3Q0;
15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
15-JAN-2008, sequence version 2.
18-JUL-2018, entry version 118.
RecName: Full=Keratin, type II cytoskeletal 80;
AltName: Full=Cytokeratin-80;
Short=CK-80;
AltName: Full=Keratin-80;
Short=K80;
AltName: Full=Type-II keratin Kb20;
Name=KRT80; Synonyms=KB20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Scalp;
PubMed=15737194; DOI=10.1111/j.0022-202X.2004.23530.x;
Rogers M.A., Edler L., Winter H., Langbein L., Beckmann I.,
Schweizer J.;
"Characterization of new members of the human type II keratin gene
family and a general evaluation of the keratin gene domain on
chromosome 12q13.13.";
J. Invest. Dermatol. 124:536-544(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Endometrial adenocarcinoma;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Prostate;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45 AND SER-396, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-396, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
-!- INTERACTION:
P19012:KRT15; NbExp=3; IntAct=EBI-3046635, EBI-739566;
P35900:KRT20; NbExp=3; IntAct=EBI-3046635, EBI-742094;
P50222:MEOX2; NbExp=3; IntAct=EBI-3046635, EBI-748397;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q6KB66-1; Sequence=Displayed;
Name=2;
IsoId=Q6KB66-2; Sequence=VSP_030423;
Name=3;
IsoId=Q6KB66-3; Sequence=VSP_030421, VSP_030422;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Weakly expressed in tongue, but not skin or in
any other tissues or organs examined.
{ECO:0000269|PubMed:15737194}.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin, I (acidic) and II (neutral to basic) (40-
55 and 56-70 kDa, respectively).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000255|PROSITE-ProRule:PRU01188}.
-----------------------------------------------------------------------
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EMBL; AJ717743; CAG30732.1; -; mRNA.
EMBL; BX537567; CAD97784.1; -; mRNA.
EMBL; CH471111; EAW58237.1; -; Genomic_DNA.
EMBL; BC065180; AAH65180.1; -; mRNA.
CCDS; CCDS41784.1; -. [Q6KB66-2]
CCDS; CCDS8821.2; -. [Q6KB66-1]
RefSeq; NP_001074961.1; NM_001081492.1. [Q6KB66-2]
RefSeq; NP_872313.2; NM_182507.2. [Q6KB66-1]
UniGene; Hs.140978; -.
ProteinModelPortal; Q6KB66; -.
SMR; Q6KB66; -.
BioGrid; 126858; 10.
IntAct; Q6KB66; 24.
iPTMnet; Q6KB66; -.
PhosphoSitePlus; Q6KB66; -.
BioMuta; KRT80; -.
DMDM; 166218808; -.
EPD; Q6KB66; -.
PaxDb; Q6KB66; -.
PeptideAtlas; Q6KB66; -.
PRIDE; Q6KB66; -.
ProteomicsDB; 66535; -.
ProteomicsDB; 66536; -. [Q6KB66-2]
ProteomicsDB; 66537; -. [Q6KB66-3]
DNASU; 144501; -.
Ensembl; ENST00000313234; ENSP00000369361; ENSG00000167767. [Q6KB66-2]
Ensembl; ENST00000394815; ENSP00000378292; ENSG00000167767. [Q6KB66-1]
GeneID; 144501; -.
KEGG; hsa:144501; -.
UCSC; uc001rzx.3; human. [Q6KB66-1]
CTD; 144501; -.
DisGeNET; 144501; -.
EuPathDB; HostDB:ENSG00000167767.13; -.
GeneCards; KRT80; -.
HGNC; HGNC:27056; KRT80.
HPA; HPA077836; -.
HPA; HPA077918; -.
MIM; 611161; gene.
neXtProt; NX_Q6KB66; -.
OpenTargets; ENSG00000167767; -.
PharmGKB; PA147357831; -.
eggNOG; ENOG410IGH5; Eukaryota.
eggNOG; ENOG411183I; LUCA.
GeneTree; ENSGT00910000144006; -.
HOGENOM; HOG000230976; -.
HOVERGEN; HBG013015; -.
InParanoid; Q6KB66; -.
KO; K07605; -.
OMA; MACRSCV; -.
OrthoDB; EOG091G0AOP; -.
PhylomeDB; Q6KB66; -.
TreeFam; TF317854; -.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GeneWiki; KRT80; -.
GenomeRNAi; 144501; -.
PRO; PR:Q6KB66; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000167767; -.
CleanEx; HS_KRT80; -.
Genevisible; Q6KB66; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005882; C:intermediate filament; IDA:UniProtKB.
GO; GO:0045111; C:intermediate filament cytoskeleton; IDA:HPA.
GO; GO:0045095; C:keratin filament; IEA:InterPro.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0031424; P:keratinization; TAS:Reactome.
InterPro; IPR001664; IF.
InterPro; IPR039008; IF_rod_dom.
InterPro; IPR003054; Keratin_II.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01276; TYPE2KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Alternative splicing; Coiled coil; Complete proteome;
Intermediate filament; Keratin; Phosphoprotein; Polymorphism;
Reference proteome.
CHAIN 1 452 Keratin, type II cytoskeletal 80.
/FTId=PRO_0000314896.
DOMAIN 83 394 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 1 82 Head.
REGION 82 118 Coil 1A.
REGION 119 135 Linker 1.
REGION 136 227 Coil 1B.
REGION 228 251 Linker 12.
REGION 252 390 Coil 2.
REGION 391 452 Tail.
SITE 334 334 Stutter.
MOD_RES 45 45 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 396 396 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 100 MACRSCVVGFSSLSSCEVTPVGSPRPGTSGWDSCRAPGPGF
SSRSLTGCWSAGTISKVTVNPGLLVPLDVKLDPAVQQLKNQ
EKEEMKALNDKFASLIGK -> MSCHFPGSPPWALAGQPGA
SAPDWSTPDPFAAFLLSQ (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_030421.
VAR_SEQ 190 190 K -> KVACPACPRGSFLMGPGPSFPPDILLSFMPNQSPQR
LKSQDQQTDRGIPPSPSSSFFEALSQISSGITPTLTQEAAP
QPTPALGPSIPSPTTHHCCQPQ (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_030422.
VAR_SEQ 413 452 ASRSGLSKAPSRKKKGSKGPVIKITEMSEKYFSQESEVSE
-> PSLPYPLCSL (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_030423.
VARIANT 238 238 V -> I (in dbSNP:rs35725856).
/FTId=VAR_049807.
CONFLICT 230 230 Q -> L (in Ref. 1; CAG30732).
{ECO:0000305}.
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


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