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Protein

Keratin, type I cytoskeletal 18

Gene

KRT18

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. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<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>

<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

Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.By similarity7 Publications

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei271Stutter1
Sitei331Stutter1

<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

GO - Biological processi

<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 processCell cycle, 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

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P05783

SIGNOR Signaling Network Open Resource

More...
SIGNORi
P05783

<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 I cytoskeletal 18
Alternative name(s):
Cell proliferation-inducing gene 46 protein
Cytokeratin-18
Short name:
CK-18
Keratin-18
Short name:
K18
<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:KRT18
Synonyms:CYK18
ORF Names:PIG46
<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>OrganismiHomo 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 NCBI 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000111057.10

Human Gene Nomenclature Database

More...
HGNCi
HGNC:6430 KRT18

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
148070 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P05783

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Intermediate filament, Keratin, Nucleus

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Cirrhosis (CIRRH)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA liver disease characterized by severe panlobular liver-cell swelling with Mallory body formation, prominent pericellular fibrosis, and marked deposits of copper. Clinical features include abdomen swelling, jaundice and pulmonary hypertension.
See also OMIM:215600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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_023054103T → A in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs61136606EnsemblClinVar.1
Natural variantiVAR_003852128H → L in CIRRH; interfers with the ability to form normal filaments. 2 PublicationsCorresponds to variant dbSNP:rs57758506EnsemblClinVar.1
Natural variantiVAR_023056261R → Q in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs57354642EnsemblClinVar.1
Natural variantiVAR_023057340G → R in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs57370769EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi2S → A: No effect on phosphorylation; when associated with A-7 and A-10. 1 Publication1
Mutagenesisi7S → A: No effect on phosphorylation; when associated with A-2 and A-10. 1 Publication1
Mutagenesisi10S → A: No effect on phosphorylation; when associated with A-2 and A-7. 1 Publication1
Mutagenesisi15S → A: No effect on phosphorylation; when associated with A-18 and A-23. Abolishes phosphorylation; when associated with A-18; A-34; A-47; A-49; A-51 and A-53. 1 Publication1
Mutagenesisi18S → A: No effect on phosphorylation; when associated with A-15 and A-23. Abolishes phosphorylation; when associated with A-15; A-34; A-47; A-49; A-51 and A-53. 1 Publication1
Mutagenesisi23S → A: No effect on phosphorylation; when associated with A-15 and A-18. 1 Publication1
Mutagenesisi30S → A: No effect on phosphorylation; when associated with A-31 and A-34, or with A-31; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-31 and A-49. 2 Publications1
Mutagenesisi31S → A: No effect on phosphorylation; when associated with A-30 and A-34, or with A-30; A-44 and A-51. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-49. 2 Publications1
Mutagenesisi34S → A: No effect on phosphorylation; when associated with A-30 and A-31. Abolishes phosphorylation; when associated with A-15; A-18; A-47; A-49; A-51 and A-53. Abolishes binding to YWHAE and YWHAZ; and when associated with A-53. 2 Publications1
Mutagenesisi34S → D or E: Abolishes binding to YWHAE and YWHAZ. 2 Publications1
Mutagenesisi42S → A: No effect on phosphorylation; when associated with A-44. 1 Publication1
Mutagenesisi44S → A: No effect on phosphorylation; when associated with A-42, or with A-30; A-31 and A-51. 1 Publication1
Mutagenesisi47S → A: No effect on phosphorylation; when associated with A-49. Abolishes phosphorylation; when associated with A-49; A-51 and A-53, or with A-15; A-18; A-34; A-49; A-51 and A-53. 1 Publication1
Mutagenesisi49S → A: No effect on phosphorylation; when associated with A-47. Abolishes phosphorylation; when associated with A-47; A-51 and A-53, or with A-15; A-18; A-34; A-47; A-51 and A-53. Abolishes glycosylation but does not affect binding to YWHAE and YWHAZ; when associated with A-30 and A-31. 2 Publications1
Mutagenesisi51S → A: No effect on phosphorylation; when associated with A-30; A-31 and A-47. Abolishes phosphorylation; when associated with A-47; A-49 and A-53, or with A-15; A-18; A-34; A-47; A-49 and A-53. 1 Publication1
Mutagenesisi53S → A: Abolishes phosphorylation; when associated with A-47; A-49 and A-51, or with A-15; A-18; A-34; A-47; A-49 and A-51. Abolishes binding to YWHAE and YWHAZ; when associated with A-34. No effect on caspase cleavage during apoptosis. 3 Publications1
Mutagenesisi90R → C or H in transgenic mice, induces marked disruption of liver and pancreas keratin filament network. Increases phosphorylation and glycosylation. 1 Publication1
Mutagenesisi238D → E: Prevents cleavage by caspase-6 during apoptosis. Induces aggregates of keratin filaments in an altered organization. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
3875
MIMi215600 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000111057

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA30217

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
KRT18

Domain mapping of disease mutations (DMDM)

More...
DMDMi
125083

<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 keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / 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 methionineiRemoved1 Publication
<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_00000636662 – 430Keratin, type I cytoskeletal 18Add BLAST429

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei2N-acetylserine1 Publication1
Modified residuei7PhosphoserineCombined sources1
Modified residuei10PhosphoserineCombined sources1
Modified residuei15PhosphoserineCombined sources1
Modified residuei18PhosphoserineCombined sources1
Modified residuei30Phosphoserine; alternateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>GlycosylationiCAR_00017530O-linked (GlcNAc) serine; alternate2 Publications1
Modified residuei31Phosphoserine; alternateBy similarity1
GlycosylationiCAR_00019331O-linked (GlcNAc) serine; alternate2 Publications1
Modified residuei34Phosphoserine; by CDK1Combined sources2 Publications1
Modified residuei36PhosphotyrosineBy similarity1
Modified residuei42PhosphoserineCombined sources1
Modified residuei45Omega-N-methylarginineCombined sources1
Modified residuei49Phosphoserine; alternateCombined sources1
GlycosylationiCAR_00019449O-linked (GlcNAc) serine; alternate2 Publications1
Modified residuei51Phosphoserine; by MAPKAPK2 and MAPKAPK3By similarityCurated1
Modified residuei52PhosphothreonineCombined sources1
Modified residuei53Phosphoserine; by CAMK, PKC/PRKCE and AURKA3 Publications1
Modified residuei55Omega-N-methylarginineCombined sources1
Modified residuei60PhosphoserineCombined sources1
Modified residuei65PhosphothreonineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, 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-linki81Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei93PhosphoserineCombined sources1
Modified residuei100PhosphoserineCombined sources1
Modified residuei131N6-acetyllysineCombined sources1
Modified residuei177PhosphoserineCombined sources1
Cross-linki247Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei302PhosphothreonineCombined sources1
Modified residuei305PhosphoserineCombined sources1
Modified residuei319PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1
Cross-linki370Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki372Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei398PhosphoserineCombined sources1
Modified residuei399PhosphoserineCombined sources1
Modified residuei401PhosphoserineCombined sources1
Modified residuei404PhosphothreonineCombined sources1
Cross-linki417Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei426N6-acetyllysine; alternateCombined sources1
Cross-linki426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki426Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/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

Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6.6 Publications
Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-238 by either caspase-3, caspase-6 or caspase-7.1 Publication
O-GlcNAcylation increases solubility, and decreases stability by inducing proteasomal degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei238 – 239Cleavage; by caspase-3, caspase-6 or caspase-72

Keywords - PTMi

Acetylation, Glycoprotein, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P05783

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P05783

MaxQB - The MaxQuant DataBase

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MaxQBi
P05783

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P05783

PeptideAtlas

More...
PeptideAtlasi
P05783

PRoteomics IDEntifications database

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PRIDEi
P05783

ProteomicsDB human proteome resource

More...
ProteomicsDBi
51857

Consortium for Top Down Proteomics

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TopDownProteomicsi
P05783

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
P05783

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
312

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P05783

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P05783

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P05783

UniCarbKB; an annotated and curated database of glycan structures

More...
UniCarbKBi
P05783

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P05783

<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">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in colon, placenta, liver and very weakly in exocervix. Increased expression observed in lymph nodes of breast carcinoma.4 Publications

<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

By IL6/interleukin-6.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000111057 Expressed in 90 organ(s), highest expression level in adenohypophysis

CleanEx database of gene expression profiles

More...
CleanExi
HS_KRT18

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P05783 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P05783 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB000008
CAB000030
HPA001605

<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. KRT18 associates with KRT8. Interacts with the thrombin-antithrombin complex (By similarity). Interacts with PNN and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when phosphorylated. Interacts with DNAJB6, TCHP and TRADD. Interacts with FAM83H (PubMed:23902688). Interacts with EPPK1 (By similarity).By similarity8 Publications
(Microbial infection) Interacts with hepatitis C virus/HCV core protein.1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
110073, 102 interactors

Database of interacting proteins

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DIPi
DIP-633N

Protein interaction database and analysis system

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IntActi
P05783, 80 interactors

Molecular INTeraction database

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MINTi
P05783

STRING: functional protein association networks

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STRINGi
9606.ENSP00000373487

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P05783

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P05783

Database of comparative protein structure models

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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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini80 – 391IF rodPROSITE-ProRule annotationAdd BLAST312

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni2 – 79HeadAdd BLAST78
Regioni70 – 373Necessary for interaction with PNN1 PublicationAdd BLAST304
Regioni77 – 128Interaction with TRADD1 PublicationAdd BLAST52
Regioni80 – 115Coil 1AAdd BLAST36
Regioni116 – 132Linker 1Add BLAST17
Regioni133 – 224Coil 1BAdd BLAST92
Regioni225 – 248Linker 12Add BLAST24
Regioni243 – 391Interaction with DNAJB61 PublicationAdd BLAST149
Regioni249 – 387Coil 2Add BLAST139
Regioni388 – 430TailAdd BLAST43

<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

Keywords - Domaini

Coiled coil

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
ENOG410IEYR Eukaryota
ENOG4111DJ8 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153309

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000230975

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG013015

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P05783

KEGG Orthology (KO)

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KOi
K07604

Identification of Orthologs from Complete Genome Data

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OMAi
RAKYEKM

Database of Orthologous Groups

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OrthoDBi
856254at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P05783

TreeFam database of animal gene trees

More...
TreeFami
TF332742

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR027695 Keratin-18
IPR002957 Keratin_I

The PANTHER Classification System

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PANTHERi
PTHR23239 PTHR23239, 1 hit
PTHR23239:SF35 PTHR23239:SF35, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00038 Filament, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR01248 TYPE1KERATIN

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01391 Filament, 1 hit

PROSITE; a protein domain and family database

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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 <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P05783-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSFTTRSTFS TNYRSLGSVQ APSYGARPVS SAASVYAGAG GSGSRISVSR
60 70 80 90 100
STSFRGGMGS GGLATGIAGG LAGMGGIQNE KETMQSLNDR LASYLDRVRS
110 120 130 140 150
LETENRRLES KIREHLEKKG PQVRDWSHYF KIIEDLRAQI FANTVDNARI
160 170 180 190 200
VLQIDNARLA ADDFRVKYET ELAMRQSVEN DIHGLRKVID DTNITRLQLE
210 220 230 240 250
TEIEALKEEL LFMKKNHEEE VKGLQAQIAS SGLTVEVDAP KSQDLAKIMA
260 270 280 290 300
DIRAQYDELA RKNREELDKY WSQQIEESTT VVTTQSAEVG AAETTLTELR
310 320 330 340 350
RTVQSLEIDL DSMRNLKASL ENSLREVEAR YALQMEQLNG ILLHLESELA
360 370 380 390 400
QTRAEGQRQA QEYEALLNIK VKLEAEIATY RRLLEDGEDF NLGDALDSSN
410 420 430
SMQTIQKTTT RRIVDGKVVS ETNDTKVLRH
Length:430
Mass (Da):48,058
Last modified:January 23, 2007 - v2
<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:i1E5604C6BCC7A17A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8VZY9F8VZY9_HUMAN
Keratin, type I cytoskeletal 18
KRT18
391Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti168Y → H in AAH00698 (PubMed:15489334).Curated1
Sequence conflicti202E → Q in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti208E → G in BAD96813 (Ref. 3) Curated1
Sequence conflicti246A → S in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti309D → R in CAA31369 (PubMed:2422083).Curated1
Sequence conflicti312S → R in CAA31369 (PubMed:2422083).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023054103T → A in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs61136606EnsemblClinVar.1
Natural variantiVAR_003852128H → L in CIRRH; interfers with the ability to form normal filaments. 2 PublicationsCorresponds to variant dbSNP:rs57758506EnsemblClinVar.1
Natural variantiVAR_023055230S → T1 PublicationCorresponds to variant dbSNP:rs58472472EnsemblClinVar.1
Natural variantiVAR_023056261R → Q in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs57354642EnsemblClinVar.1
Natural variantiVAR_023057340G → R in CIRRH. 1 PublicationCorresponds to variant dbSNP:rs57370769EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
X12881 mRNA Translation: CAA31375.1
AY762101 mRNA Translation: AAX07828.1
BT019412 mRNA Translation: AAV38219.1
AK223093 mRNA Translation: BAD96813.1
BC000180 mRNA Translation: AAH00180.1
BC000698 mRNA Translation: AAH00698.1
BC004253 mRNA Translation: AAH04253.1
BC008636 mRNA Translation: AAH08636.1
BC020982 mRNA Translation: AAH20982.1
BC072017 mRNA Translation: AAH72017.1
AF179904 Genomic DNA Translation: AAA59461.1
X12883 mRNA Translation: CAA31377.1
X12876 mRNA Translation: CAA31369.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS31809.1

Protein sequence database of the Protein Information Resource

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PIRi
S05481

NCBI Reference Sequences

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RefSeqi
NP_000215.1, NM_000224.2
NP_954657.1, NM_199187.1

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.406013

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000388835; ENSP00000373487; ENSG00000111057
ENST00000388837; ENSP00000373489; ENSG00000111057

Database of genes from NCBI RefSeq genomes

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GeneIDi
3875

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:3875

UCSC genome browser

More...
UCSCi
uc001sbe.4 human

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Human Intermediate Filament Mutation Database

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12881 mRNA Translation: CAA31375.1
AY762101 mRNA Translation: AAX07828.1
BT019412 mRNA Translation: AAV38219.1
AK223093 mRNA Translation: BAD96813.1
BC000180 mRNA Translation: AAH00180.1
BC000698 mRNA Translation: AAH00698.1
BC004253 mRNA Translation: AAH04253.1
BC008636 mRNA Translation: AAH08636.1
BC020982 mRNA Translation: AAH20982.1
BC072017 mRNA Translation: AAH72017.1
AF179904 Genomic DNA Translation: AAA59461.1
X12883 mRNA Translation: CAA31377.1
X12876 mRNA Translation: CAA31369.1
CCDSiCCDS31809.1
PIRiS05481
RefSeqiNP_000215.1, NM_000224.2
NP_954657.1, NM_199187.1
UniGeneiHs.406013

3D structure databases

ProteinModelPortaliP05783
SMRiP05783
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110073, 102 interactors
DIPiDIP-633N
IntActiP05783, 80 interactors
MINTiP05783
STRINGi9606.ENSP00000373487

PTM databases

GlyConnecti312
iPTMnetiP05783
PhosphoSitePlusiP05783
SwissPalmiP05783
UniCarbKBiP05783

Polymorphism and mutation databases

BioMutaiKRT18
DMDMi125083

2D gel databases

SWISS-2DPAGEiP05783

Proteomic databases

EPDiP05783
jPOSTiP05783
MaxQBiP05783
PaxDbiP05783
PeptideAtlasiP05783
PRIDEiP05783
ProteomicsDBi51857
TopDownProteomicsiP05783

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
3875
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388835; ENSP00000373487; ENSG00000111057
ENST00000388837; ENSP00000373489; ENSG00000111057
GeneIDi3875
KEGGihsa:3875
UCSCiuc001sbe.4 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
3875
DisGeNETi3875
EuPathDBiHostDB:ENSG00000111057.10

GeneCards: human genes, protein and diseases

More...
GeneCardsi
KRT18

H-Invitational Database, human transcriptome db

More...
H-InvDBi
HIX0040371
HGNCiHGNC:6430 KRT18
HPAiCAB000008
CAB000030
HPA001605
MIMi148070 gene
215600 phenotype
neXtProtiNX_P05783
OpenTargetsiENSG00000111057
PharmGKBiPA30217

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG410IEYR Eukaryota
ENOG4111DJ8 LUCA
GeneTreeiENSGT00940000153309
HOGENOMiHOG000230975
HOVERGENiHBG013015
InParanoidiP05783
KOiK07604
OMAiRAKYEKM
OrthoDBi856254at2759
PhylomeDBiP05783
TreeFamiTF332742

Enzyme and pathway databases

ReactomeiR-HSA-6805567 Keratinization
R-HSA-6809371 Formation of the cornified envelope
SignaLinkiP05783
SIGNORiP05783

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
KRT18 human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Keratin_18

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
3875
PMAP-CutDBiP05783

Protein Ontology

More...
PROi
PR:P05783

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000111057 Expressed in 90 organ(s), highest expression level in adenohypophysis
CleanExiHS_KRT18
ExpressionAtlasiP05783 baseline and differential
GenevisibleiP05783 HS

Family and domain databases

InterProiView protein in InterPro
IPR001664 IF
IPR018039 IF_conserved
IPR039008 IF_rod_dom
IPR027695 Keratin-18
IPR002957 Keratin_I
PANTHERiPTHR23239 PTHR23239, 1 hit
PTHR23239:SF35 PTHR23239:SF35, 1 hit
PfamiView protein in Pfam
PF00038 Filament, 1 hit
PRINTSiPR01248 TYPE1KERATIN
SMARTiView protein in SMART
SM01391 Filament, 1 hit
PROSITEiView 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 nameiK1C18_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>AccessioniPrimary (citable) accession number: P05783
Secondary accession number(s): Q53G38, Q5U0N8, Q9BW26
<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 historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 213 of the entry and version 2 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
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