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UniProtKB - P02533 (K1C14_HUMAN)

Entry version 224 (02 Jun 2021)
Sequence version 4 (05 May 2009)
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Protein

Keratin, type I cytoskeletal 14

Gene

KRT14

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

The nonhelical tail domain is involved in promoting KRT5-KRT14 filaments to self-organize into large bundles and enhances the mechanical properties involved in resilience of keratin intermediate filaments in vitro.

1 Publication

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>Sitei364Stutter1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P02533

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-446107, Type I hemidesmosome assembly
R-HSA-6805567, Keratinization
R-HSA-6809371, Formation of the cornified envelope

SIGNOR Signaling Network Open Resource

More...SIGNORi		P02533

<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%5Fand%5Ftaxonomy%5Fsection">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 14
Alternative name(s):
Cytokeratin-14
Short name:
CK-14
Keratin-14
Short name:
K14
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:KRT14
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 17

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:6416, KRT14

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		148066, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P02533

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000186847.5

<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

<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, 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

Epidermolysis bullosa simplex, Dowling-Meara type (DM-EBS)18 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA severe form of intraepidermal epidermolysis bullosa characterized by generalized herpetiform blistering, milia formation, dystrophic nails, and mucous membrane involvement.
Related information in OMIM
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_010440119M → T in DM-EBS. 2 PublicationsCorresponds to variant dbSNP:rs28928893EnsemblClinVar.1
Natural variantiVAR_010441120Q → R in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60993843EnsemblClinVar.1
Natural variantiVAR_010442122L → F in DM-EBS and K-EBS. 2 PublicationsCorresponds to variant dbSNP:rs59110575EnsemblClinVar.1
Natural variantiVAR_023720123N → K in DM-EBS. 2 PublicationsCorresponds to variant dbSNP:rs3826549EnsemblClinVar.1
Natural variantiVAR_010443123N → S in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60171927EnsemblClinVar.1
Natural variantiVAR_003837125R → C in DM-EBS. 7 PublicationsCorresponds to variant dbSNP:rs60399023EnsemblClinVar.1
Natural variantiVAR_023721125R → G in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60399023EnsemblClinVar.1
Natural variantiVAR_003838125R → H in DM-EBS. 7 PublicationsCorresponds to variant dbSNP:rs58330629EnsemblClinVar.1
Natural variantiVAR_010444125R → S in DM-EBS. 1 Publication1
Natural variantiVAR_031634128Missing in DM-EBS. 1 Publication1
Natural variantiVAR_010445129Y → D in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60470268EnsemblClinVar.1
Natural variantiVAR_023722130L → P in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs57522245EnsemblClinVar.1
Natural variantiVAR_031639416R → P in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60622724EnsemblClinVar.1
Natural variantiVAR_027721417R → P in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs61085704EnsemblClinVar.1
Natural variantiVAR_003845419L → Q in DM-EBS. 3 PublicationsCorresponds to variant dbSNP:rs57364972EnsemblClinVar.1
Epidermolysis bullosa simplex, Weber-Cockayne type (WC-EBS)13 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of intraepidermal epidermolysis bullosa characterized by blistering limited to palmar and plantar areas of the skin.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_010438116K → N in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs59271739EnsemblClinVar.1
Natural variantiVAR_023719119M → V in K-EBS and WC-EBS. 2 PublicationsCorresponds to variant dbSNP:rs61263401EnsemblClinVar.1
Natural variantiVAR_023723133V → L in WC-EBS and K-EBS. 2 PublicationsCorresponds to variant dbSNP:rs61027685EnsemblClinVar.1
Natural variantiVAR_031636148R → C in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58378809EnsemblClinVar.1
Natural variantiVAR_027718211R → P in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs60589227EnsemblClinVar.1
Natural variantiVAR_003840270V → M in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58560979EnsemblClinVar.1
Natural variantiVAR_010448273D → G in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs59375065EnsemblClinVar.1
Natural variantiVAR_010449274A → D in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58785777EnsemblClinVar.1
Natural variantiVAR_003842375Missing in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs56974573Ensembl.1
Natural variantiVAR_010450377I → N in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs61536893EnsemblClinVar.1
Natural variantiVAR_010451388R → C in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs59966597EnsemblClinVar.1
Natural variantiVAR_031637388R → H in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58645163EnsemblClinVar.1
Natural variantiVAR_023724408L → M in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs57200223EnsemblClinVar.1
Natural variantiVAR_027720411Missing in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs267607389Ensembl.1
Natural variantiVAR_031638415Y → C in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs59442925EnsemblClinVar.1
Natural variantiVAR_010452422E → K in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58762773EnsemblClinVar.1
Epidermolysis bullosa simplex, Koebner type (K-EBS)10 Publications
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of intraepidermal epidermolysis bullosa characterized by generalized skin blistering. The phenotype is not fundamentally distinct from the Dowling-Meara type, although it is less severe.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023719119M → V in K-EBS and WC-EBS. 2 PublicationsCorresponds to variant dbSNP:rs61263401EnsemblClinVar.1
Natural variantiVAR_010442122L → F in DM-EBS and K-EBS. 2 PublicationsCorresponds to variant dbSNP:rs59110575EnsemblClinVar.1
Natural variantiVAR_023723133V → L in WC-EBS and K-EBS. 2 PublicationsCorresponds to variant dbSNP:rs61027685EnsemblClinVar.1
Natural variantiVAR_031635134R → P in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs61540016EnsemblClinVar.1
Natural variantiVAR_010446143L → P in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs61326242EnsemblClinVar.1
Natural variantiVAR_010447247A → D in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs147611635Ensembl.1
Natural variantiVAR_003841272M → R in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs61371557EnsemblClinVar.1
Natural variantiVAR_027719272M → T in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs61371557EnsemblClinVar.1
Natural variantiVAR_003843384L → P in K-EBS. 2 PublicationsCorresponds to variant dbSNP:rs59629244EnsemblClinVar.1
Natural variantiVAR_023725413A → T in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs59780231EnsemblClinVar.1
Natural variantiVAR_003844415Y → H in K-EBS. 3 PublicationsCorresponds to variant dbSNP:rs58380626EnsemblClinVar.1
Epidermolysis bullosa simplex, autosomal recessive 1 (EBSB1)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA form of epidermolysis bullosa, a genodermatosis characterized by recurrent blistering and cleavage within basal keratinocytes, fragility of the skin and mucosal epithelia, and erosions caused by minor mechanical trauma.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_003839144E → A in EBSB1. 1 PublicationCorresponds to variant dbSNP:rs57121345EnsemblClinVar.1
Naegeli-Franceschetti-Jadassohn syndrome (NFJS)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA rare autosomal dominant form of ectodermal dysplasia. The cardinal features are absence of dermatoglyphics (fingerprints), reticular cutaneous hyperpigmentation (starting at about the age of 2 years without a preceding inflammatory stage), palmoplantar keratoderma, hypohidrosis with diminished sweat gland function and discomfort provoked by heat, nail dystrophy, and tooth enamel defects.
Related information in OMIM
Dermatopathia pigmentosa reticularis (DPR)1 Publication
The disease is caused by variants affecting the gene represented in this entry.
Disease descriptionA rare ectodermal dysplasia characterized by lifelong persistent reticulate hyperpigmentation, non-cicatricial alopecia, and nail dystrophy. Variable features include adermatoglyphia, hypohidrosis or hyperhidrosis, and palmoplantar hyperkeratosis.
Related information in OMIM

Keywords - Diseasei

Disease variant, Ectodermal dysplasia, Epidermolysis bullosa, Palmoplantar keratoderma

Organism-specific databases

DisGeNET

More...DisGeNETi		3861

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

More...GeneReviewsi		KRT14

MalaCards human disease database

More...MalaCardsi		KRT14
MIMi125595, phenotype
131760, phenotype
131800, phenotype
131900, phenotype
161000, phenotype
601001, phenotype

Open Targets

More...OpenTargetsi		ENSG00000186847

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...Orphaneti		79399, Autosomal dominant generalized epidermolysis bullosa simplex, intermediate form
79396, Autosomal dominant generalized epidermolysis bullosa simplex, severe form
89838, Autosomal recessive generalized epidermolysis bullosa simplex
86920, Dermatopathia pigmentosa reticularis
79397, Epidermolysis bullosa simplex with mottled pigmentation
79400, Localized epidermolysis bullosa simplex
69087, Naegeli-Franceschetti-Jadassohn syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA30203

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P02533, Tbio

Chemistry databases

Drug and drug target database

More...DrugBanki		DB01593, Zinc
DB14487, Zinc acetate

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		KRT14

Domain mapping of disease mutations (DMDM)

More...DMDMi		229463044

<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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000636531 – 472Keratin, type I cytoskeletal 14Add BLAST472

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi367Interchain1 Publication
<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 residuei435PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

A disulfide bond is formed between rather than within filaments and promotes the formation of a keratin filament cage around the nucleus.
Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P02533

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P02533

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

More...PaxDbi		P02533

PeptideAtlas

More...PeptideAtlasi		P02533

PRoteomics IDEntifications database

More...PRIDEi		P02533

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		51528

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P02533

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

More...PhosphoSitePlusi		P02533

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P02533

<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 the corneal epithelium (at protein level) (PubMed:26758872). Detected in the basal layer, lowered within the more apically located layers specifically in the stratum spinosum, stratum granulosum but is not detected in stratum corneum. Strongly expressed in the outer root sheath of anagen follicles but not in the germinative matrix, inner root sheath or hair (PubMed:9457912). Found in keratinocytes surrounding the club hair during telogen (PubMed:9457912).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000186847, Expressed in gingival epithelium and 141 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P02533, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000186847, Group enriched (skin, tongue)

<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%5Fsection">'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%5Fsection">'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. disulfide-linked keratin-14 associates with keratin-5.

Interacts with TRADD and with keratin filaments. Associates with other type I keratins.

Interacts with EPPK1 (By similarity).

Interacts with KLHL24 (PubMed:27798626).

By similarity4 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		110059, 103 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-888, Keratin-5 - Keratin-14 dimer complex

Database of interacting proteins

More...DIPi		DIP-33874N

Protein interaction database and analysis system

More...IntActi		P02533, 63 interactors

Molecular INTeraction database

More...MINTi		P02533

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000167586

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P02533, protein

<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

Secondary structure

1472
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P02533

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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%5Fand%5Fdomains%5Fsection">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>Domaini115 – 426IF 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>Regioni1 – 114HeadAdd BLAST114
Regioni115 – 150Coil 1AAdd BLAST36
Regioni151 – 168Linker 1Add BLAST18
Regioni169 – 260Coil 1BAdd BLAST92
Regioni261 – 283Linker 12Add BLAST23
Regioni284 – 422Coil 2Add BLAST139
Regioni423 – 472TailAdd BLAST50
Regioni425 – 472Interaction with Type I keratins and keratin filamentsAdd BLAST48
Regioni426 – 472DisorderedSequence analysisAdd BLAST47

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi426 – 449Polar residuesSequence analysisAdd BLAST24
Compositional biasi450 – 472Basic and acidic residuesSequence analysisAdd BLAST23

<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

More...eggNOGi		ENOG502R8V7, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000154602

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_012560_8_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P02533

Identification of Orthologs from Complete Genome Data

More...OMAi		YWATIND

Database of Orthologous Groups

More...OrthoDBi		798081at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P02533

TreeFam database of animal gene trees

More...TreeFami		TF332742

Family and domain databases

Database of protein disorder

More...DisProti		DP02605

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.20.5.1160, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR018039, IF_conserved
IPR039008, IF_rod_dom
IPR042180, IF_rod_dom_coil1B
IPR002957, Keratin_I

The PANTHER Classification System

More...PANTHERi		PTHR23239, PTHR23239, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00038, Filament, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01248, TYPE1KERATIN

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 <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P02533-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL 
        60         70         80         90        100
SVSSSRFSSG GACGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGAGLGGGF 
       110        120        130        140        150
GGGFAGGDGL LVGSEKVTMQ NLNDRLASYL DKVRALEEAN ADLEVKIRDW 
       160        170        180        190        200
YQRQRPAEIK DYSPYFKTIE DLRNKILTAT VDNANVLLQI DNARLAADDF 
       210        220        230        240        250
RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE SLKEELAYLK 
       260        270        280        290        300
KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK 
       310        320        330        340        350
DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN LEIELQSQLS 
       360        370        380        390        400
MKASLENSLE ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI 
       410        420        430        440        450
LLDVKTRLEQ EIATYRRLLE GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT 
       460        470 
KVMDVHDGKV VSTHEQVLRT KN
Length:472
Mass (Da):51,561
Last modified:May 5, 2009 - v4
<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:i120BA30BA2F8E397
GO

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 conflicti26G → A (PubMed:6210150).Curated1
Sequence conflicti26G → A in AAB59562 (PubMed:2580298).Curated1
Sequence conflicti44S → N (PubMed:6210150).Curated1
Sequence conflicti44S → N in AAB59562 (PubMed:2580298).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05534763C → Y3 PublicationsCorresponds to variant dbSNP:rs6503640Ensembl.1
Natural variantiVAR_01043794A → T3 PublicationsCorresponds to variant dbSNP:rs3826550EnsemblClinVar.1
Natural variantiVAR_010438116K → N in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs59271739EnsemblClinVar.1
Natural variantiVAR_010439119M → I in WC-EBS at heterozygosity; more severe phenotype is associated with homozygosity. 2 PublicationsCorresponds to variant dbSNP:rs57358989EnsemblClinVar.1
Natural variantiVAR_010440119M → T in DM-EBS. 2 PublicationsCorresponds to variant dbSNP:rs28928893EnsemblClinVar.1
Natural variantiVAR_023719119M → V in K-EBS and WC-EBS. 2 PublicationsCorresponds to variant dbSNP:rs61263401EnsemblClinVar.1
Natural variantiVAR_010441120Q → R in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60993843EnsemblClinVar.1
Natural variantiVAR_010442122L → F in DM-EBS and K-EBS. 2 PublicationsCorresponds to variant dbSNP:rs59110575EnsemblClinVar.1
Natural variantiVAR_023720123N → K in DM-EBS. 2 PublicationsCorresponds to variant dbSNP:rs3826549EnsemblClinVar.1
Natural variantiVAR_010443123N → S in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60171927EnsemblClinVar.1
Natural variantiVAR_003837125R → C in DM-EBS. 7 PublicationsCorresponds to variant dbSNP:rs60399023EnsemblClinVar.1
Natural variantiVAR_023721125R → G in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60399023EnsemblClinVar.1
Natural variantiVAR_003838125R → H in DM-EBS. 7 PublicationsCorresponds to variant dbSNP:rs58330629EnsemblClinVar.1
Natural variantiVAR_010444125R → S in DM-EBS. 1 Publication1
Natural variantiVAR_031634128Missing in DM-EBS. 1 Publication1
Natural variantiVAR_010445129Y → D in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60470268EnsemblClinVar.1
Natural variantiVAR_023722130L → P in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs57522245EnsemblClinVar.1
Natural variantiVAR_033496133V → A. Corresponds to variant dbSNP:rs56798071Ensembl.1
Natural variantiVAR_023723133V → L in WC-EBS and K-EBS. 2 PublicationsCorresponds to variant dbSNP:rs61027685EnsemblClinVar.1
Natural variantiVAR_031635134R → P in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs61540016EnsemblClinVar.1
Natural variantiVAR_010446143L → P in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs61326242EnsemblClinVar.1
Natural variantiVAR_003839144E → A in EBSB1. 1 PublicationCorresponds to variant dbSNP:rs57121345EnsemblClinVar.1
Natural variantiVAR_031636148R → C in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58378809EnsemblClinVar.1
Natural variantiVAR_027718211R → P in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs60589227EnsemblClinVar.1
Natural variantiVAR_049784215E → K. Corresponds to variant dbSNP:rs11551755Ensembl.1
Natural variantiVAR_010447247A → D in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs147611635Ensembl.1
Natural variantiVAR_003840270V → M in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58560979EnsemblClinVar.1
Natural variantiVAR_003841272M → R in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs61371557EnsemblClinVar.1
Natural variantiVAR_027719272M → T in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs61371557EnsemblClinVar.1
Natural variantiVAR_010448273D → G in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs59375065EnsemblClinVar.1
Natural variantiVAR_010449274A → D in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58785777EnsemblClinVar.1
Natural variantiVAR_003842375Missing in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs56974573Ensembl.1
Natural variantiVAR_010450377I → N in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs61536893EnsemblClinVar.1
Natural variantiVAR_003843384L → P in K-EBS. 2 PublicationsCorresponds to variant dbSNP:rs59629244EnsemblClinVar.1
Natural variantiVAR_010451388R → C in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs59966597EnsemblClinVar.1
Natural variantiVAR_031637388R → H in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58645163EnsemblClinVar.1
Natural variantiVAR_023724408L → M in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs57200223EnsemblClinVar.1
Natural variantiVAR_027720411Missing in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs267607389Ensembl.1
Natural variantiVAR_023725413A → T in K-EBS. 1 PublicationCorresponds to variant dbSNP:rs59780231EnsemblClinVar.1
Natural variantiVAR_031638415Y → C in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs59442925EnsemblClinVar.1
Natural variantiVAR_003844415Y → H in K-EBS. 3 PublicationsCorresponds to variant dbSNP:rs58380626EnsemblClinVar.1
Natural variantiVAR_031639416R → P in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs60622724EnsemblClinVar.1
Natural variantiVAR_027721417R → P in DM-EBS. 1 PublicationCorresponds to variant dbSNP:rs61085704EnsemblClinVar.1
Natural variantiVAR_071705418L → Q Probable disease-associated variant found in epidermolysis bullosa simplex with variable phenotype. 1 Publication1
Natural variantiVAR_003845419L → Q in DM-EBS. 3 PublicationsCorresponds to variant dbSNP:rs57364972EnsemblClinVar.1
Natural variantiVAR_010452422E → K in WC-EBS. 1 PublicationCorresponds to variant dbSNP:rs58762773EnsemblClinVar.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
J00124 Genomic DNA Translation: AAB59562.1
BT007186 mRNA Translation: AAP35850.1
AC019349 Genomic DNA No translation available.
BC002690 mRNA Translation: AAH02690.1
BC019097 mRNA Translation: AAH19097.1
BC042437 mRNA Translation: AAH42437.1
BC094830 mRNA Translation: AAH94830.1
D28807 Genomic DNA Translation: BAA05967.1
AF186085 Genomic DNA Translation: AAF04034.1
AF186086 Genomic DNA Translation: AAF04035.1
AF186087 Genomic DNA Translation: AAF04036.1
AF186088 Genomic DNA Translation: AAF04037.1
AF186089 Genomic DNA Translation: AAF04038.1
AF186090 Genomic DNA Translation: AAF04039.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS11400.1

Protein sequence database of the Protein Information Resource

More...PIRi		A26763, KRHUE

NCBI Reference Sequences

More...RefSeqi		NP_000517.2, NM_000526.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000167586; ENSP00000167586; ENSG00000186847

Database of genes from NCBI RefSeq genomes

More...GeneIDi		3861

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:3861

UCSC genome browser

More...UCSCi		uc002hxf.3, human

<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%5Freferences%5Fsection">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
J00124 Genomic DNA Translation: AAB59562.1
BT007186 mRNA Translation: AAP35850.1
AC019349 Genomic DNA No translation available.
BC002690 mRNA Translation: AAH02690.1
BC019097 mRNA Translation: AAH19097.1
BC042437 mRNA Translation: AAH42437.1
BC094830 mRNA Translation: AAH94830.1
D28807 Genomic DNA Translation: BAA05967.1
AF186085 Genomic DNA Translation: AAF04034.1
AF186086 Genomic DNA Translation: AAF04035.1
AF186087 Genomic DNA Translation: AAF04036.1
AF186088 Genomic DNA Translation: AAF04037.1
AF186089 Genomic DNA Translation: AAF04038.1
AF186090 Genomic DNA Translation: AAF04039.1
CCDSiCCDS11400.1
PIRiA26763, KRHUE
RefSeqiNP_000517.2, NM_000526.4

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3TNUX-ray3.00A295-422[»]
6JFVX-ray2.60A/C327-421[»]
SMRiP02533
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi110059, 103 interactors
ComplexPortaliCPX-888, Keratin-5 - Keratin-14 dimer complex
DIPiDIP-33874N
IntActiP02533, 63 interactors
MINTiP02533
STRINGi9606.ENSP00000167586

Chemistry databases

DrugBankiDB01593, Zinc
DB14487, Zinc acetate

PTM databases

iPTMnetiP02533
PhosphoSitePlusiP02533
SwissPalmiP02533

Genetic variation databases

BioMutaiKRT14
DMDMi229463044

Proteomic databases

jPOSTiP02533
MassIVEiP02533
PaxDbiP02533
PeptideAtlasiP02533
PRIDEiP02533
ProteomicsDBi51528

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3600, 1249 antibodies

The DNASU plasmid repository

More...DNASUi		3861

Genome annotation databases

EnsembliENST00000167586; ENSP00000167586; ENSG00000186847
GeneIDi3861
KEGGihsa:3861
UCSCiuc002hxf.3, human

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		3861
DisGeNETi3861

GeneCards: human genes, protein and diseases

More...GeneCardsi		KRT14
GeneReviewsiKRT14
HGNCiHGNC:6416, KRT14
HPAiENSG00000186847, Group enriched (skin, tongue)
MalaCardsiKRT14
MIMi125595, phenotype
131760, phenotype
131800, phenotype
131900, phenotype
148066, gene
161000, phenotype
601001, phenotype
neXtProtiNX_P02533
OpenTargetsiENSG00000186847
Orphaneti79399, Autosomal dominant generalized epidermolysis bullosa simplex, intermediate form
79396, Autosomal dominant generalized epidermolysis bullosa simplex, severe form
89838, Autosomal recessive generalized epidermolysis bullosa simplex
86920, Dermatopathia pigmentosa reticularis
79397, Epidermolysis bullosa simplex with mottled pigmentation
79400, Localized epidermolysis bullosa simplex
69087, Naegeli-Franceschetti-Jadassohn syndrome
PharmGKBiPA30203
VEuPathDBiHostDB:ENSG00000186847.5

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiENOG502R8V7, Eukaryota
GeneTreeiENSGT00940000154602
HOGENOMiCLU_012560_8_1_1
InParanoidiP02533
OMAiYWATIND
OrthoDBi798081at2759
PhylomeDBiP02533
TreeFamiTF332742

Enzyme and pathway databases

PathwayCommonsiP02533
ReactomeiR-HSA-446107, Type I hemidesmosome assembly
R-HSA-6805567, Keratinization
R-HSA-6809371, Formation of the cornified envelope
SIGNORiP02533

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		3861, 12 hits in 959 CRISPR screens

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

More...ChiTaRSi		KRT14, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Keratin_14

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

More...GenomeRNAii		3861
PharosiP02533, Tbio

Protein Ontology

More...PROi		PR:P02533
RNActiP02533, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000186847, Expressed in gingival epithelium and 141 other tissues
GenevisibleiP02533, HS

Family and domain databases

DisProtiDP02605
Gene3Di1.20.5.1160, 1 hit
InterProiView protein in InterPro
IPR018039, IF_conserved
IPR039008, IF_rod_dom
IPR042180, IF_rod_dom_coil1B
IPR002957, Keratin_I
PANTHERiPTHR23239, PTHR23239, 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

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiK1C14_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: P02533
Secondary accession number(s): Q14715
, Q53XY3, Q9BUE3, Q9UBN2, Q9UBN3, Q9UCY4
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 5, 2009
Last modified: June 2, 2021
This is version 224 of the entry and version 4 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

3D-structure, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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