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UniProtKB/Swiss-Prot entry P08729


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name K2C7_HUMAN
Primary accession number P08729
Secondary accession numbers Q92676 Q9BUD8 Q9Y3R7
Integrated into Swiss-Prot on August 1, 1988
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 110)
Name and origin of the protein
Protein name Keratin, type II cytoskeletal 7
Synonyms Cytokeratin-7
CK-7
Keratin-7
K7
Sarcolectin
Gene name
Name: KRT7
Synonyms: SCL
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Mesothelium;
DOI=10.1083/jcb.101.6.2366; PubMed=2415537 [NCBI, ExPASy, EBI, Israel, Japan]
Glass C., Kim K.H., Fuchs E.;
"Sequence and expression of a human type II mesothelial keratin.";
J. Cell Biol. 101:2366-2373(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
DOI=10.1083/jcb.107.4.1337; PubMed=2459129 [NCBI, ExPASy, EBI, Israel, Japan]
Glass C., Fuchs E.;
"Isolation, sequence, and differential expression of a human K7 gene in simple epithelial cells.";
J. Cell Biol. 107:1337-1350(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Placenta;
DOI=10.1016/S0300-9084(99)80128-X; PubMed=10492017 [NCBI, ExPASy, EBI, Israel, Japan]
Kaba A., Jiang P., Chany-Fournier F., Chany C.;
"Sarcolectin (SCL): structure and expression of the recombinant molecule.";
Biochimie 81:709-715(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND VARIANT GLY-364.
TISSUE=Keratinocyte;
DOI=10.1016/S0006-291X(02)02288-X; PubMed=12359226 [NCBI, ExPASy, EBI, Israel, Japan]
Smith F.J.D., Porter R.M., Corden L.D., Lunny D.P., Lane E.B., McLean W.H.I.;
"Cloning of human, murine, and marsupial keratin 7 and a survey of K7 expression in the mouse.";
Biochem. Biophys. Res. Commun. 297:818-827(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
PROTEIN SEQUENCE OF 2-48; 53-96; 102-110; 123-130; 137-161; 178-208; 215-273; 277-296; 306-313; 318-326; 330-348; 352-363 AND 374-402, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT ARG-20, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma, and Ovarian carcinoma;
Bienvenut W.V., Zebisch A., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[7]
INTERACTION WITH EIF3S10.
DOI=10.1002/1097-4644(20010315)80:4<483::AID-JCB1002>3.0.CO;2-B; PubMed=11169732 [NCBI, ExPASy, EBI, Israel, Japan]
Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.;
"Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7.";
J. Cell. Biochem. 80:483-490(2001).
[8]
FUNCTION, AND INTERACTION WITH HPV16 E7.
DOI=10.1128/JVI.76.14.7040-7048.2002; PubMed=12072504 [NCBI, ExPASy, EBI, Israel, Japan]
Kanduc D.;
"Translational regulation of human papillomavirus type 16 E7 mRNA by the peptide SEQIKA, shared by rabbit alpha(1)-globin and human cytokeratin 7.";
J. Virol. 76:7040-7048(2002).
[9]
MASS SPECTROMETRY.
TISSUE=Mammary cancer;
DOI=10.1002/1615-9861(200202)2:2<212::AID-PROT212>3.0.CO;2-H; PubMed=11840567 [NCBI, ExPASy, EBI, Israel, Japan]
Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A., Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J., Zvelebil M.J.;
"Cluster analysis of an extensive human breast cancer cell line protein expression map database.";
Proteomics 2:212-223(2002).
[10]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-20, AND MASS SPECTROMETRY.
DOI=10.1038/nmeth715; PubMed=15782174 [NCBI, ExPASy, EBI, Israel, Japan]
Ong S.E., Mittler G., Mann M.;
"Identifying and quantifying in vivo methylation sites by heavy methyl SILAC.";
Nat. Methods 1:119-126(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-254, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-205, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-375 AND SER-380, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252 AND SER-254, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[17]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
  • FUNCTION: Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. Involved in the translational regulation of the human papillomavirus type 16 E7 mRNA (HPV16 E7).
  • SUBUNIT: Heterotetramer of two type I and two type II keratins. Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit EIF3S10 and with HPV16 E7.
  • INTERACTION:
    Q14152:EIF3A; NbExp=2; IntAct=EBI-297833, EBI-366617;
  • SUBCELLULAR LOCATION: Cytoplasm.
  • TISSUE SPECIFICITY: Expressed in cultured epidermal, bronchial and mesothelial cells but absent in colon, ectocervix and liver. Observed throughout the glandular cells in the junction between stomach and esophagus but is absent in the esophagus.
  • INDUCTION: Up-regulated by retinoic acid.
  • PTM: Arg-20 is dimethylated, probably to asymmetric dimethylarginine.
  • MASS SPECTROMETRY: Mass=51203.48; Method=MALDI; Range=2-469; Source=PubMed:11840567;.
  • MISCELLANEOUS: There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
  • SIMILARITY: Belongs to the intermediate filament family.
  • SEQUENCE CAUTION:
    • Sequence=CAA26956.2; Type=Frameshift; Positions=22;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03212; CAA26956.2; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13320; CAA31695.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13346; CAA31695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13347; CAA31695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13348; CAA31695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13349; CAA31695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13350; CAA31695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13351; CAA31695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13352; CAA31695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X13353; CAA31695.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ238246; CAB41416.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF509887; AAN64031.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF509892; AAN64035.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF509891; AAN64035.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002700; AAH02700.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00306959; -.
PIR B24177; B24177.
S05602; S05602.
RefSeq NP_005547.3; -.
UniGene Hs.411501
3D structure databases
HSSP P08670; 1GK7. [HSSP ENTRY / PDB]
ModBase P08729.
Protein-protein interaction databases
IntAct P08729; 4.
PTM databases
PhosphoSite P08729; -.
2D gel databases
SWISS-2DPAGE P08729; -.
Organism-specific databases
GeneCards GC12P050913; -.
H-InvDB HIX0037105; -.
HIX0079487; -.
HGNC HGNC:6445; KRT7.
GenAtlas KRT7.
HPA CAB000028; -.
HPA007272; -.
MIM 148059; gene. [NCBI / EBI]
PharmGKB PA30233; -.
Gene expression databases
ArrayExpress P08729; -.
Bgee P08729; -.
CleanEx HS_KRT7; -.
GermOnline ENSG00000135480; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from UniProtKB).
GO:0045095; Cellular component: keratin filament (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0005198; Molecular function: structural molecule activity (non-traceable author statement from UniProtKB).
GO:0007010; Biological process: cytoskeleton organization (non-traceable author statement from UniProtKB).
GO:0006260; Biological process: DNA replication (inferred from direct assay from UniProtKB).
GO:0051325; Biological process: interphase (inferred from direct assay from UniProtKB).
GO:0044419; Biological process: interspecies interaction between organisms (inferred from electronic annotation from UniProtKB-KW).
GO:0006417; Biological process: regulation of translation (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR016044; F.
IPR001664; IF.
IPR018039; Intermediate_filament_CS.
IPR003054; Keratin_II.
Graphical view of domain structure.
PANTHER PTHR23239; IF; 1.
PTHR23239:SF18; Keratin_II; 1.
Pfam PF00038; Filament; 1.
Pfam graphical view of domain structure.
PRINTS PR01276; TYPE2KERATIN.
PROSITE PS00226; IF; 1.
Proteomic databases
PRIDE P08729; -.
Genome annotation databases
Ensembl ENSG00000135480; Homo sapiens. [Contig view]
GeneID 3855; -.
KEGG hsa:3855; -.
Phylogenomic databases
HOGENOM P08729; -.
HOVERGEN P08729; -.
Other
NextBio 15169; -.
SOURCE KRT7; Homo sapiens.
ProtoNet P08729.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Coiled coil; Cytoplasm; Direct protein sequencing; Host-virus interaction; Intermediate filament; Keratin; Methylation; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   469  468     Keratin, type II cytoskeletal 7. PRO_0000063725
REGION   2    90  89     Head. 
REGION   90   126  37     Coil 1A. 
REGION   91   399  309     Rod. 
REGION   92    97  6     Interaction with HPV16 E7. 
REGION   127   144  18     Linker 1. 
REGION   145   236  92     Coil 1B. 
REGION   237   260  24     Linker 12. 
REGION   261   399  139     Coil 2. 
REGION   400   469  70     Tail. 
SITE   343   343  1     Stutter. 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   7     7        Phosphoserine. 
MOD_RES   14    14        Phosphoserine (By similarity). 
MOD_RES   20    20        Dimethylated arginine; alternate. 
MOD_RES   20    20        Omega-N-methylarginine; alternate. 
MOD_RES   45    45        Phosphoserine. 
MOD_RES   205   205        Phosphotyrosine. 
MOD_RES   252   252        Phosphoserine. 
MOD_RES   254   254        Phosphoserine. 
MOD_RES   375   375        Phosphotyrosine. 
MOD_RES   380   380        Phosphoserine. 
VARIANT   364   364  1     A -> G. VAR_016321 
CONFLICT   79    79        D -> G (in Ref. 3; CAB41416). 
CONFLICT   83    84        SL -> FS (in Ref. 3; CAB41416). 
CONFLICT   97    97        T -> A (in Ref. 1; CAA26956 and 2; CAA31695). 
CONFLICT   155   155        L -> M (in Ref. 3; CAB41416). 
CONFLICT   164   165        QG -> AE (in Ref. 4; AAN64031/AAN64035 and 5; AAH02700). 
CONFLICT   168   168        T -> S (in Ref. 4; AAN64031/AAN64035 and 5; AAH02700). 
CONFLICT   342   342        R -> C (in Ref. 1; CAA26956 and 2; CAA31695). 
CONFLICT   411   411        V -> A (in Ref. 3; CAB41416). 
CONFLICT   467   467        A -> T (in Ref. 3; CAB41416). 
Sequence information
Length: 469 AA [This is the length of the unprocessed precursor] Molecular weight: 51418 Da [This is the MW of the unprocessed precursor] CRC64: 26578B9D40DFF5CF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSIHFSSPVF TSRSAAFSGR GAQVRLSSAR PGGLGSSSLY GLGASRPRVA VRSAYGGPVG 

        70         80         90        100        110        120 
AGIREVTINQ SLLAPLRLDA DPSLQRVRQE ESEQIKTLNN KFASFIDKVR FLEQQNKLLE 

       130        140        150        160        170        180 
TKWTLLQEQK SAKSSRLPDI FEAQIAGLRG QLEALQVDGG RLEQGLRTMQ DVVEDFKNKY 

       190        200        210        220        230        240 
EDEINRRTAA ENEFVVLKKD VDAAYMSKVE LEAKVDALND EINFLRTLNE TELTELQSQI 

       250        260        270        280        290        300 
SDTSVVLSMD NSRSLDLDGI IAEVKAQYEE MAKCSRAEAE AWYQTKFETL QAQAGKHGDD 

       310        320        330        340        350        360 
LRNTRNEISE MNRAIQRLQA EIDNIKNQRA KLEAAIAEAE ERGELALKDA RAKQEELEAA 

       370        380        390        400        410        420 
LQRAKQDMAR QLREYQELMS VKLALDIEIA TYRKLLEGEE SRLAGDGVGA VNISVMNSTG 

       430        440        450        460 
GSSSGGGIGL TLGGTMGSNA LSFSSSAGPG LLKAYSIRTA SASRRSARD 

P08729 in FASTA format

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