UniProtKB - P08729 (K2C7_HUMAN)
(max 400 entries)x
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
- BLAST>sp|P08729|K2C7_HUMAN Keratin, type II cytoskeletal 7 OS=Homo sapiens OX=9606 GN=KRT7 PE=1 SV=5 MSIHFSSPVFTSRSAAFSGRGAQVRLSSARPGGLGSSSLYGLGASRPRVAVRSAYGGPVG AGIREVTINQSLLAPLRLDADPSLQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLE TKWTLLQEQKSAKSSRLPDIFEAQIAGLRGQLEALQVDGGRLEAELRSMQDVVEDFKNKY EDEINHRTAAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTLNETELTELQSQI SDTSVVLSMDNSRSLDLDGIIAEVKAQYEEMAKCSRAEAEAWYQTKFETLQAQAGKHGDD LRNTRNEISEMNRAIQRLQAEIDNIKNQRAKLEAAIAEAEERGELALKDARAKQEELEAA LQRGKQDMARQLREYQELMSVKLALDIEIATYRKLLEGEESRLAGDGVGAVNISVMNSTG GSSSGGGIGLTLGGTMGSNALSFSSSAGPGLLKAYSIRTASASRRSARD
- Align
Protein
Keratin, type II cytoskeletal 7
Gene
KRT7
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
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).2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.3"Sarcolectin (SCL): structure and expression of the recombinant molecule."
Kaba A., Jiang P., Chany-Fournier F., Chany C.
Biochimie 81:709-715(1999) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS ARG-186 AND ALA-364. - Ref.9"Translational regulation of human papillomavirus type 16 E7 mRNA by the peptide SEQIKA, shared by rabbit alpha(1)-globin and human cytokeratin 7."
Kanduc D.
J. Virol. 76:7040-7048(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HPV16 E7.
Miscellaneous
There are two types of cytoskeletal and microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to basic; 56-70 kDa).
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 343 | Stutter | 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- structural molecule activity Source: InterPro
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cornification Source: Reactome
- keratinization Source: Reactome
- viral process Source: UniProtKB-KW
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Biological process | Host-virus interaction |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-6805567. Keratinization. R-HSA-6809371. Formation of the cornified envelope. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P08729. |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Keratin, type II cytoskeletal 7Alternative name(s): Cytokeratin-7 Short name: CK-7 Keratin-7 Short name: K7 Sarcolectin Type-II keratin Kb7 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:KRT7 Synonyms:SCL |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000135480.14. |
Human Gene Nomenclature Database More...HGNCi | HGNC:6445. KRT7. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 148059. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P08729. |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Other locations
- Cytoplasm 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Isolation, sequence, and differential expression of a human K7 gene in simple epithelial cells."
Glass C., Fuchs E.
J. Cell Biol. 107:1337-1350(1988) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, VARIANTS ARG-186 AND ALA-364.
- Cytoplasm 1 Publication
Cytoskeleton
- intermediate filament Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- keratin filament Source: InterPro
Cytosol
- cytosol Source: Reactome
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Nucleus
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Intermediate filament, Keratin<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Organism-specific databases
DisGeNET More...DisGeNETi | 3855. |
Open Targets More...OpenTargetsi | ENSG00000135480. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30233. |
Chemistry databases
Drug and drug target database More...DrugBanki | DB04959. HspE7. DB01087. Primaquine. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | KRT7. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 317373583. |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000063725 | 2 – 469 | Keratin, type II cytoskeletal 7Add BLAST | 468 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 6 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 7 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 20 | Dimethylated arginine; alternate1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 20 | Omega-N-methylarginine; alternate1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 53 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 71 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 83 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 97 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 130 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 179 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 252 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 254 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 265 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 286 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 289 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 296 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span> / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">‘Disulfide bond’</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 331 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
|
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section"><span class="caps">PTM</span>/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
Arg-20 is dimethylated, probably to asymmetric dimethylarginine.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P08729. |
PeptideAtlas More...PeptideAtlasi | P08729. |
PRoteomics IDEntifications database More...PRIDEi | P08729. |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P08729. |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P08729. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P08729. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P08729. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P08729. |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression"><span class="caps">P92958</span></a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="http://www.uniprot.org/uniprot/O14734#expression"><span class="caps">O14734</span></a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
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.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.1"Sequence and expression of a human type II mesothelial keratin."
Glass C., Kim K.H., Fuchs E.
J. Cell Biol. 101:2366-2373(1985) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANTS ARG-186 AND ALA-364. - Ref.4"Cloning of human, murine, and marsupial keratin 7 and a survey of K7 expression in the mouse."
Smith F.J.D., Porter R.M., Corden L.D., Lunny D.P., Lane E.B., McLean W.H.I.
Biochem. Biophys. Res. Commun. 297:818-827(2002) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANTS ARG-186 AND ALA-364.
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Up-regulated by retinoic acid.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.2"Isolation, sequence, and differential expression of a human K7 gene in simple epithelial cells."
Glass C., Fuchs E.
J. Cell Biol. 107:1337-1350(1988) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, VARIANTS ARG-186 AND ALA-364.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000135480. |
CleanEx database of gene expression profiles More...CleanExi | HS_KRT7. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P08729. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P08729. HS. |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB000028. HPA007272. |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">‘Interaction’</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">‘Function’</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Heterotetramer of two type I and two type II keratins. Interacts with eukaryotic translation initiator factor 3 (eIF3) subunit EIF3S10 and with HPV16 E7. Interacts with GPER1.3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.8"Molecular interaction between human tumor marker protein p150, the largest subunit of eIF3, and intermediate filament protein K7."
Lin L., Holbro T., Alonso G., Gerosa D., Burger M.M.
J. Cell. Biochem. 80:483-490(2001) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH EIF3S10. - Ref.9"Translational regulation of human papillomavirus type 16 E7 mRNA by the peptide SEQIKA, shared by rabbit alpha(1)-globin and human cytokeratin 7."
Kanduc D.
J. Virol. 76:7040-7048(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, INTERACTION WITH HPV16 E7. - Ref.15"G protein-coupled estrogen receptor 1/G protein-coupled receptor 30 localizes in the plasma membrane and traffics intracellularly on cytokeratin intermediate filaments."
Sanden C., Broselid S., Cornmark L., Andersson K., Daszkiewicz-Nilsson J., Martensson U.E., Olde B., Leeb-Lundberg L.M.
Mol. Pharmacol. 79:400-410(2011) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH GPER1.
<p>This subsection of the ‘<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>’ section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| EIF3A | Q14152 | 3 | EBI-297833,EBI-366617 |
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110053. 12 interactors. |
Protein interaction database and analysis system More...IntActi | P08729. 7 interactors. |
Molecular INTeraction database More...MINTi | P08729. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000329243. |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 4XIF | X-ray | 3.20 | E/F/G/H | 8-16 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P08729. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08729. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 91 – 403 | IF rodPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi Add BLAST | 313 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 2 – 90 | HeadAdd BLAST | 89 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 90 – 126 | Coil 1AAdd BLAST | 37 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 92 – 97 | Interaction with HPV16 E71 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 6 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 127 – 144 | Linker 1Add BLAST | 18 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 145 – 236 | Coil 1BAdd BLAST | 92 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 237 – 260 | Linker 12Add BLAST | 24 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 261 – 399 | Coil 2Add BLAST | 139 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 400 – 469 | TailAdd BLAST | 70 |
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Belongs to the intermediate filament family.PROSITE-ProRule annotation
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More…</a></p> Manual assertion according to rulesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
Coiled coilPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IG4R. Eukaryota. ENOG410YY6B. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118796. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000230976. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG013015. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P08729. |
KEGG Orthology (KO) More...KOi | K07605. |
Identification of Orthologs from Complete Genome Data More...OMAi | PGIFEAQ. |
Database of Orthologous Groups More...OrthoDBi | EOG091G09KR. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P08729. |
TreeFam database of animal gene trees More...TreeFami | TF317854. |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR032444. Keratin_2_head. IPR003054. Keratin_II. |
The PANTHER Classification System More...PANTHERi | PTHR23239. PTHR23239. 1 hit. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00038. Filament. 1 hit. PF16208. Keratin_2_head. 1 hit. |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01276. TYPE2KERATIN. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01391. Filament. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00226. IF_ROD_1. 1 hit. PS51842. IF_ROD_2. 1 hit. |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
P08729-1 [UniParc]FASTAAdd to basketAdded to basketShow »
10 20 30 40 50
MSIHFSSPVF TSRSAAFSGR GAQVRLSSAR PGGLGSSSLY GLGASRPRVA
60 70 80 90 100
VRSAYGGPVG AGIREVTINQ SLLAPLRLDA DPSLQRVRQE ESEQIKTLNN
110 120 130 140 150
KFASFIDKVR FLEQQNKLLE TKWTLLQEQK SAKSSRLPDI FEAQIAGLRG
160 170 180 190 200
QLEALQVDGG RLEAELRSMQ DVVEDFKNKY EDEINHRTAA ENEFVVLKKD
210 220 230 240 250
VDAAYMSKVE LEAKVDALND EINFLRTLNE TELTELQSQI SDTSVVLSMD
260 270 280 290 300
NSRSLDLDGI IAEVKAQYEE MAKCSRAEAE AWYQTKFETL QAQAGKHGDD
310 320 330 340 350
LRNTRNEISE MNRAIQRLQA EIDNIKNQRA KLEAAIAEAE ERGELALKDA
360 370 380 390 400
RAKQEELEAA LQRGKQDMAR QLREYQELMS VKLALDIEIA TYRKLLEGEE
410 420 430 440 450
SRLAGDGVGA VNISVMNSTG GSSSGGGIGL TLGGTMGSNA LSFSSSAGPG
460
LLKAYSIRTA SASRRSARD
Length:469
Mass (Da):51,386
Last modified:January 11, 2011 - v5
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i070CBE8F66A62497
<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence CAA26956 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.Curated
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 79 | D → G in CAB41416 (PubMed:10492017).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 83 – 84 | SL → FS in CAB41416 (PubMed:10492017).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 97 | T → A in CAA26956 (PubMed:2415537).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 97 | T → A in CAA31695 (PubMed:2459129).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 155 | L → M in CAB41416 (PubMed:10492017).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 164 | A → Q in CAA26956 (PubMed:2415537).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 164 | A → Q in CAA31695 (PubMed:2459129).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 164 | A → Q in CAB41416 (PubMed:10492017).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 165 | E → G in CAA26956 (PubMed:2415537).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 165 | E → G in CAA31695 (PubMed:2459129).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 165 | E → G in CAB41416 (PubMed:10492017).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 168 | S → T in CAA26956 (PubMed:2415537).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 168 | S → T in CAA31695 (PubMed:2459129).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 168 | S → T in CAB41416 (PubMed:10492017).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 342 | R → C in CAA26956 (PubMed:2415537).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 342 | R → C in CAA31695 (PubMed:2459129).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 411 | V → A in CAB41416 (PubMed:10492017).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 467 | A → T in CAB41416 (PubMed:10492017).Curated | 1 |
<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi
Molecular mass is 51203.48 Da from positions 2 - 469. Determined by MALDI. 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
- Ref.10"Cluster analysis of an extensive human breast cancer cell line protein expression map database."
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.
Proteomics 2:212-223(2002) [PubMed] [Europe PMC] [Abstract]Cited for: MASS SPECTROMETRY.
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_060731 | 186 | H → RCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_016321 | 364 | G → A5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
| 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X03212 mRNA. Translation: CAA26956.2. Sequence problems. X13320 , X13346, X13347, X13348, X13349, X13350, X13351, X13352, X13353 Genomic DNA. Translation: CAA31695.1. AJ238246 mRNA. Translation: CAB41416.1. AF509887 mRNA. Translation: AAN64031.1. AF509892, AF509891 Genomic DNA. Translation: AAN64035.1. AC007338 Genomic DNA. No translation available. AC007494 Genomic DNA. No translation available. BC002700 mRNA. Translation: AAH02700.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS8822.1. |
Protein sequence database of the Protein Information Resource More...PIRi | B24177. S05602. |
NCBI Reference Sequences More...RefSeqi | NP_005547.3. NM_005556.3. |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.411501. |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000331817; ENSP00000329243; ENSG00000135480. |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3855. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3855. |
UCSC genome browser More...UCSCi | uc001saa.2. human. |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | X03212 mRNA. Translation: CAA26956.2. Sequence problems. X13320 , X13346, X13347, X13348, X13349, X13350, X13351, X13352, X13353 Genomic DNA. Translation: CAA31695.1. AJ238246 mRNA. Translation: CAB41416.1. AF509887 mRNA. Translation: AAN64031.1. AF509892, AF509891 Genomic DNA. Translation: AAN64035.1. AC007338 Genomic DNA. No translation available. AC007494 Genomic DNA. No translation available. BC002700 mRNA. Translation: AAH02700.1. |
The Consensus CDS (CCDS) project More...CCDSi | CCDS8822.1. |
Protein sequence database of the Protein Information Resource More...PIRi | B24177. S05602. |
NCBI Reference Sequences More...RefSeqi | NP_005547.3. NM_005556.3. |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.411501. |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 4XIF | X-ray | 3.20 | E/F/G/H | 8-16 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P08729. | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P08729. | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 110053. 12 interactors. |
Protein interaction database and analysis system More...IntActi | P08729. 7 interactors. |
Molecular INTeraction database More...MINTi | P08729. |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000329243. |
Chemistry databases
Drug and drug target database More...DrugBanki | DB04959. HspE7. DB01087. Primaquine. |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P08729. |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P08729. |
SwissPalm database of S-palmitoylation events More...SwissPalmi | P08729. |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | KRT7. |
Domain mapping of disease mutations (DMDM) More...DMDMi | 317373583. |
2D gel databases
Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital More...SWISS-2DPAGEi | P08729. |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P08729. |
PeptideAtlas More...PeptideAtlasi | P08729. |
PRoteomics IDEntifications database More...PRIDEi | P08729. |
Consortium for Top Down Proteomics More...TopDownProteomicsi | P08729. |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 3855. |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000331817; ENSP00000329243; ENSG00000135480. |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 3855. |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:3855. |
UCSC genome browser More...UCSCi | uc001saa.2. human. |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 3855. |
DisGeNET More...DisGeNETi | 3855. |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000135480.14. |
GeneCards: human genes, protein and diseases More...GeneCardsi | KRT7. |
H-Invitational Database, human transcriptome db More...H-InvDBi | HIX0010643. HIX0079487. |
Human Gene Nomenclature Database More...HGNCi | HGNC:6445. KRT7. |
Human Protein Atlas More...HPAi | CAB000028. HPA007272. |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 148059. gene. |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P08729. |
Open Targets More...OpenTargetsi | ENSG00000135480. |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA30233. |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG410IG4R. Eukaryota. ENOG410YY6B. LUCA. |
Ensembl GeneTree More...GeneTreei | ENSGT00760000118796. |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000230976. |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG013015. |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P08729. |
KEGG Orthology (KO) More...KOi | K07605. |
Identification of Orthologs from Complete Genome Data More...OMAi | PGIFEAQ. |
Database of Orthologous Groups More...OrthoDBi | EOG091G09KR. |
Database for complete collections of gene phylogenies More...PhylomeDBi | P08729. |
TreeFam database of animal gene trees More...TreeFami | TF317854. |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-6805567. Keratinization. R-HSA-6809371. Formation of the cornified envelope. |
SIGNOR Signaling Network Open Resource More...SIGNORi | P08729. |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | KRT7. human. |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Keratin_7. |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 3855. |
Protein Ontology More...PROi | PR:P08729. |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000135480. |
CleanEx database of gene expression profiles More...CleanExi | HS_KRT7. |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P08729. baseline and differential. |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P08729. HS. |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001664. IF. IPR018039. Intermediate_filament_CS. IPR032444. Keratin_2_head. IPR003054. Keratin_II. |
The PANTHER Classification System More...PANTHERi | PTHR23239. PTHR23239. 1 hit. |
Pfam protein domain database More...Pfami | View protein in Pfam PF00038. Filament. 1 hit. PF16208. Keratin_2_head. 1 hit. |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR01276. TYPE2KERATIN. |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM01391. Filament. 1 hit. |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00226. IF_ROD_1. 1 hit. PS51842. IF_ROD_2. 1 hit. |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | K2C7_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P08729Primary (citable) accession number: P08729 Secondary accession number(s): Q92676, Q9BUD8, Q9Y3R7 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1988 |
| Last sequence update: | January 11, 2011 | |
| Last modified: | February 28, 2018 | |
| This is version 192 of the entry and version 5 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |