Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - Q07157 (ZO1_HUMAN)

Entry version 218 (13 Nov 2019)
Sequence version 3 (24 Jan 2006)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Tight junction protein ZO-1

Gene

TJP1

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

TJP1, TJP2, and TJP3 are closely related scaffolding proteins that link tight junction (TJ) transmembrane proteins such as claudins, junctional adhesion molecules, and occludin to the actin cytoskeleton (PubMed:7798316, PubMed:9792688). The tight junction acts to limit movement of substances through the paracellular space and as a boundary between the compositionally distinct apical and basolateral plasma membrane domains of epithelial and endothelial cells. Necessary for lumenogenesis, and particularly efficient epithelial polarization and barrier formation (By similarity). Plays a role in the regulation of cell migration by targeting CDC42BPB to the leading edge of migrating cells (PubMed:21240187). Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (PubMed:20930113). With TJP2 and TJP3, participates to the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (By similarity).By similarity2 Publications

<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 ...

<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

Molecular functionCalmodulin-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-191650 Regulation of gap junction activity
R-HSA-2028269 Signaling by Hippo
R-HSA-351906 Apoptotic cleavage of cell adhesion proteins
R-HSA-8935964 RUNX1 regulates expression of components of tight junctions

SIGNOR Signaling Network Open Resource

More...SIGNORi		Q07157

Protein family/group databases

Transport Classification Database

More...TCDBi		8.A.24.1.9 the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family

<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:
Tight junction protein ZO-1
Alternative name(s):
Tight junction protein 1
Zona occludens protein 1
Zonula occludens protein 1
<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:TJP1
Synonyms:ZO1
<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 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_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 15

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:11827 TJP1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		601009 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q07157

<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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Gap junction, Membrane, Tight junction

<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

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>Mutagenesisi201R → A: Strongly reduced interaction with GJA1. 1 Publication1
Mutagenesisi209K → A: Abolishes interaction with GJA1. 1 Publication1
Mutagenesisi1699 – 1700MC → AA: Abolishes interaction with CDC42BPB. 1 Publication2
Mutagenesisi1748Missing : Abolishes interaction with CDC42BPB and MYZAP. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		7082

Open Targets

More...OpenTargetsi		ENSG00000104067

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA36532

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q07157

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		TJP1

Domain mapping of disease mutations (DMDM)

More...DMDMi		85700443

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000945401 – 1748Tight junction protein ZO-1Add BLAST1748

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 residuei125PhosphoserineCombined sources1
Modified residuei132PhosphotyrosineBy similarity1
Modified residuei175PhosphoserineCombined sources1
Modified residuei178PhosphoserineCombined sources1
Modified residuei179PhosphoserineCombined sources1
Modified residuei185PhosphothreonineCombined sources1
Modified residuei212PhosphoserineCombined sources1
Modified residuei241PhosphoserineBy similarity1
Modified residuei267PhosphothreonineCombined sources1
Modified residuei275PhosphoserineCombined sources1
Modified residuei277PhosphoserineCombined sources1
Modified residuei280PhosphoserineCombined sources1
Modified residuei284PhosphoserineCombined sources1
Modified residuei290PhosphoserineCombined sources1
Modified residuei294PhosphoserineCombined sources1
Modified residuei297PhosphoserineCombined sources1
Modified residuei300PhosphoserineCombined sources1
Modified residuei323PhosphoserineBy similarity1
Modified residuei329PhosphoserineCombined sources1
Modified residuei334PhosphoserineCombined sources1
Modified residuei337PhosphoserineCombined sources1
Modified residuei353PhosphoserineCombined sources1
Modified residuei354PhosphothreonineCombined sources1
Modified residuei617PhosphoserineCombined sources1
Modified residuei622PhosphoserineCombined sources1
Modified residuei809PhosphothreonineCombined sources1
Modified residuei810PhosphoserineBy similarity1
Modified residuei821PhosphoserineCombined sources1
Modified residuei822PhosphotyrosineBy similarity1
Modified residuei824PhosphoserineBy similarity1
Modified residuei828PhosphoserineBy similarity1
Modified residuei837PhosphoserineCombined sources1
Modified residuei846PhosphothreonineBy similarity1
Modified residuei848PhosphothreonineBy similarity1
Modified residuei854PhosphothreonineCombined sources1
Modified residuei861PhosphothreonineCombined sources1
Modified residuei868PhosphothreonineCombined sources1
Modified residuei912PhosphoserineCombined sources1
Modified residuei968PhosphoserineCombined sources1
Modified residuei1071PhosphoserineBy similarity1
Modified residuei1111PhosphoserineCombined sources1
Modified residuei1139PhosphoserineBy similarity1
Modified residuei1140PhosphotyrosineBy similarity1
Modified residuei1165PhosphotyrosineBy similarity1
Modified residuei1354PhosphotyrosineBy similarity1
Modified residuei1366PhosphoserineCombined sources1
Modified residuei1413PhosphoserineCombined sources1
Modified residuei1545PhosphoserineCombined sources1
Modified residuei1617PhosphoserineCombined sources1
Isoform Short (identifier: Q07157-2)
Modified residuei912PhosphoserineCombined sources1

<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

Phosphorylated at tyrosine redidues in response to epidermal growth factor (EGF) (PubMed:19332538, PubMed:7542259). This response is dependent on an intact actin microfilament system (PubMed:7542259). Dephosphorylated by PTPRJ (PubMed:19332538).2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		Q07157

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q07157

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q07157

MaxQB - The MaxQuant DataBase

More...MaxQBi		Q07157

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

More...PaxDbi		Q07157

PeptideAtlas

More...PeptideAtlasi		Q07157

PRoteomics IDEntifications database

More...PRIDEi		Q07157

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		58506 [Q07157-1]
58507 [Q07157-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q07157

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

More...PhosphoSitePlusi		Q07157

<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

The alpha-containing isoform is found in most epithelial cell junctions. The short isoform is found both in endothelial cells and the highly specialized epithelial junctions of renal glomeruli and Sertoli cells of the seminiferous tubules.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000104067 Expressed in 241 organ(s), highest expression level in brain

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q07157 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q07157 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB010822
HPA001636
HPA001637

<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

Homodimer (PubMed:17928286). Forms heterodimers (via the PDZ2 domain) with TJP2 and TJP3 (PubMed:9792688, PubMed:17928286, PubMed:16737969).

Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1 (PubMed:7798316, PubMed:11734628, PubMed:12023291, PubMed:12154091, PubMed:15183511, PubMed:18823282, PubMed:20200156).

Interacts (via ZU5 domain) with CDC42BPB and MYZAP (PubMed:20093627, PubMed:21240187).

Interacts (via PDZ domain) with GJA1 (PubMed:18636092).

Interacts (via PDZ domains) with ANKRD2 (PubMed:22016770).

Interacts with BVES (via the C-terminus cytoplasmic tail) (By similarity).

Interacts with HSPA4 and KIRREL1 (By similarity).

Interacts with DLL1 (By similarity).

Interacts with USP53 (via the C-terminal region) (By similarity).

Interacts (via ABR region) with F-actin (PubMed:9792688, PubMed:12354695, PubMed:20930113).

Interacts with DNMBP (via C-terminal domain); required for the apical cell-cell junction localization of DNMBP (PubMed:17015620).

By similarity16 Publications

<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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		112937, 131 interactors

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q07157

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...ELMi		Q07157

Protein interaction database and analysis system

More...IntActi		Q07157, 70 interactors

Molecular INTeraction database

More...MINTi		Q07157

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000281537

<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

11748
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		Q07157

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q07157

<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>Domaini23 – 110PDZ 1PROSITE-ProRule annotationAdd BLAST88
Domaini186 – 264PDZ 2PROSITE-ProRule annotationAdd BLAST79
Domaini421 – 502PDZ 3PROSITE-ProRule annotationAdd BLAST82
Domaini516 – 584SH3PROSITE-ProRule annotationAdd BLAST69
Domaini598 – 779Guanylate kinase-likePROSITE-ProRule annotationAdd BLAST182
Domaini1634 – 1748ZU5PROSITE-ProRule annotationAdd BLAST115

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>Regioni633 – 876Occludin (OCLN)-binding region1 PublicationAdd BLAST244
Regioni1151 – 1371Actin-binding region (ABR)1 PublicationAdd BLAST221

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1243 – 1248Poly-Pro6
Compositional biasi1426 – 1432Poly-Pro7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The 244-aa domain between residues 633 and 876 is the primary occludin (OCLN)-binding site and is required for stable association with the tight junction (PubMed:9792688).1 Publication
The C-terminal region (residues 1151-1372) is an actin-binding region (ABR) that interacts directly with F-actin and plays an important role in the localization of TJP1 at junctions (PubMed:9792688, PubMed:12354695, PubMed:20930113). The ABR is also required for the localization to puncta at the free edge of cells before initiation of cell-cell contact (PubMed:12354695). The ABR is also necessary for TJP1 recruitment to podosomes (PubMed:20930113).3 Publications
The second PDZ domain (PDZ2) mediates homodimerization and heterodimerization with TJP2 and TJP3 (PubMed:9792688, PubMed:17928286).2 Publications

<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 MAGUK family.Curated

Keywords - Domaini

Repeat, SH3 domain

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3580 Eukaryota
ENOG410XQP3 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000155164

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q07157

KEGG Orthology (KO)

More...KOi		K05701

Database of Orthologous Groups

More...OrthoDBi		179316at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q07157

TreeFam database of animal gene trees

More...TreeFami		TF315957

Family and domain databases

Conserved Domains Database

More...CDDi		cd12026 SH3_ZO-1, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008145 GK/Ca_channel_bsu
IPR008144 Guanylate_kin-like_dom
IPR027417 P-loop_NTPase
IPR001478 PDZ
IPR036034 PDZ_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR005417 ZO
IPR005418 ZO-1
IPR035597 ZO-1_SH3
IPR000906 ZU5_dom

The PANTHER Classification System

More...PANTHERi		PTHR13865:SF25 PTHR13865:SF25, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00625 Guanylate_kin, 1 hit
PF00595 PDZ, 3 hits
PF07653 SH3_2, 1 hit
PF00791 ZU5, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR01597 ZONOCCLUDNS
PR01598 ZONOCCLUDNS1

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00072 GuKc, 1 hit
SM00228 PDZ, 3 hits
SM00218 ZU5, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50044 SSF50044, 1 hit
SSF50156 SSF50156, 3 hits
SSF52540 SSF52540, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS50052 GUANYLATE_KINASE_2, 1 hit
PS50106 PDZ, 3 hits
PS50002 SH3, 1 hit
PS51145 ZU5, 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>. 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>Sequences (2+)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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

Isoform Long (identifier: Q07157-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSARAAAAKS TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG 
        60         70         80         90        100
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK 
       110        120        130        140        150
NAKITIRRKK KVQIPVSRPD PEPVSDNEED SYDEEIHDPR SGRSGVVNRR 
       160        170        180        190        200
SEKIWPRDRS ASRERSLSPR SDRRSVASSQ PAKPTKVTLV KSRKNEEYGL 
       210        220        230        240        250
RLASHIFVKE ISQDSLAARD GNIQEGDVVL KINGTVTENM SLTDAKTLIE 
       260        270        280        290        300
RSKGKLKMVV QRDERATLLN VPDLSDSIHS ANASERDDIS EIQSLASDHS 
       310        320        330        340        350
GRSHDRPPRR SRSRSPDQRS EPSDHSRHSP QQPSNGSLRS RDEERISKPG 
       360        370        380        390        400
AVSTPVKHAD DHTPKTVEEV TVERNEKQTP SLPEPKPVYA QVGQPDVDLP 
       410        420        430        440        450
VSPSDGVLPN STHEDGILRP SMKLVKFRKG DSVGLRLAGG NDVGIFVAGV 
       460        470        480        490        500
LEDSPAAKEG LEEGDQILRV NNVDFTNIIR EEAVLFLLDL PKGEEVTILA 
       510        520        530        540        550
QKKKDVYRRI VESDVGDSFY IRTHFEYEKE SPYGLSFNKG EVFRVVDTLY 
       560        570        580        590        600
NGKLGSWLAI RIGKNHKEVE RGIIPNKNRA EQLASVQYTL PKTAGGDRAD 
       610        620        630        640        650
FWRFRGLRSS KRNLRKSRED LSAQPVQTKF PAYERVVLRE AGFLRPVTIF 
       660        670        680        690        700
GPIADVAREK LAREEPDIYQ IAKSEPRDAG TDQRSSGIIR LHTIKQIIDQ 
       710        720        730        740        750
DKHALLDVTP NAVDRLNYAQ WYPIVVFLNP DSKQGVKTMR MRLCPESRKS 
       760        770        780        790        800
ARKLYERSHK LRKNNHHLFT TTINLNSMND GWYGALKEAI QQQQNQLVWV 
       810        820        830        840        850
SEGKADGATS DDLDLHDDRL SYLSAPGSEY SMYSTDSRHT SDYEDTDTEG 
       860        870        880        890        900
GAYTDQELDE TLNDEVGTPP ESAITRSSEP VREDSSGMHH ENQTYPPYSP 
       910        920        930        940        950
QAQPQPIHRI DSPGFKPASQ QKAEASSPVP YLSPETNPAS STSAVNHNVN 
       960        970        980        990       1000
LTNVRLEEPT PAPSTSYSPQ ADSLRTPSTE AAHIMLRDQE PSLSSHVDPT 
      1010       1020       1030       1040       1050
KVYRKDPYPE EMMRQNHVLK QPAVSHPGHR PDKEPNLTYE PQLPYVEKQA 
      1060       1070       1080       1090       1100
SRDLEQPTYR YESSSYTDQF SRNYEHRLRY EDRVPMYEEQ WSYYDDKQPY 
      1110       1120       1130       1140       1150
PSRPPFDNQH SQDLDSRQHP EESSERGYFP RFEEPAPLSY DSRPRYEQAP 
      1160       1170       1180       1190       1200
RASALRHEEQ PAPGYDTHGR LRPEAQPHPS AGPKPAESKQ YFEQYSRSYE 
      1210       1220       1230       1240       1250
QVPPQGFTSR AGHFEPLHGA AAVPPLIPSS QHKPEALPSN TKPLPPPPTQ 
      1260       1270       1280       1290       1300
TEEEEDPAMK PQSVLTRVKM FENKRSASLE TKKDVNDTGS FKPPEVASKP 
      1310       1320       1330       1340       1350
SGAPIIGPKP TSQNQFSEHD KTLYRIPEPQ KPQLKPPEDI VRSNHYDPEE 
      1360       1370       1380       1390       1400
DEEYYRKQLS YFDRRSFENK PPAHIAASHL SEPAKPAHSQ NQSNFSSYSS 
      1410       1420       1430       1440       1450
KGKPPEADGV DRSFGEKRYE PIQATPPPPP LPSQYAQPSQ PVTSASLHIH 
      1460       1470       1480       1490       1500
SKGAHGEGNS VSLDFQNSLV SKPDPPPSQN KPATFRPPNR EDTAQAAFYP 
      1510       1520       1530       1540       1550
QKSFPDKAPV NGTEQTQKTV TPAYNRFTPK PYTSSARPFE RKFESPKFNH 
      1560       1570       1580       1590       1600
NLLPSETAHK PDLSSKTPTS PKTLVKSHSL AQPPEFDSGV ETFSIHAEKP 
      1610       1620       1630       1640       1650
KYQINNISTV PKAIPVSPSA VEEDEDEDGH TVVATARGIF NSNGGVLSSI 
      1660       1670       1680       1690       1700
ETGVSIIIPQ GAIPEGVEQE IYFKVCRDNS ILPPLDKEKG ETLLSPLVMC 
      1710       1720       1730       1740 
GPHGLKFLKP VELRLPHCDP KTWQNKCLPG DPNYLVGANC VSVLIDHF
Length:1,748
Mass (Da):195,459
Last modified:January 24, 2006 - v3
<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:i189E31617084C0CC
GO
Isoform Short (identifier: Q07157-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     922-1001: Missing.

Show »
Length:1,668
Mass (Da):186,966
Checksum:i5AD0570EC32FD9C3
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 are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V1L9G3V1L9_HUMAN
Tight junction protein 1 (Zona occl...
TJP1 hCG_27621
1,768Annotation score:

Annotation score:4 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>
G5E9E7G5E9E7_HUMAN
Tight junction protein 1 (Zona occl...
TJP1 hCG_27621
1,692Annotation 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>
A0A087X0K9A0A087X0K9_HUMAN
Tight junction protein ZO-1
TJP1
1,676Annotation 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>
H0YKB1H0YKB1_HUMAN
Tight junction protein 1 (Zona occl...
TJP1 hCG_27621
383Annotation 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>
H0YLT6H0YLT6_HUMAN
Tight junction protein ZO-1
TJP1
231Annotation score:

Annotation score:1 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>
H0Y3R8H0Y3R8_HUMAN
Tight junction protein ZO-1
TJP1
227Annotation score:

Annotation score:1 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>

<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 AAA02891 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated

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 conflicti394 – 417QPDVD…HEDGI → NQMWIYLSVHLMVSYLIQLM KMGF in AAA02891 (PubMed:8395056).CuratedAdd BLAST24
Sequence conflicti545V → A in AAA02891 (PubMed:8395056).Curated1
Sequence conflicti688I → Y in AAA02891 (PubMed:8395056).Curated1
Sequence conflicti762R → A in AAA02891 (PubMed:8395056).Curated1

Natural variant

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_025153471N → S1 PublicationCorresponds to variant dbSNP:rs2229517Ensembl.1
Natural variantiVAR_025154790I → V3 PublicationsCorresponds to variant dbSNP:rs2229515Ensembl.1
Natural variantiVAR_025155930P → L1 PublicationCorresponds to variant dbSNP:rs45529137Ensembl.1
Natural variantiVAR_0251561110H → R1 PublicationCorresponds to variant dbSNP:rs45567033Ensembl.1
Natural variantiVAR_0251571347D → A1 PublicationCorresponds to variant dbSNP:rs2291166Ensembl.1
Natural variantiVAR_0251581605N → S1 PublicationCorresponds to variant dbSNP:rs45578638Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_003148922 – 1001Missing in isoform Short. CuratedAdd BLAST80

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
L14837 mRNA Translation: AAA02891.1 Different initiation.
AK304758 mRNA Translation: BAG65513.1
DQ015919 Genomic DNA Translation: AAY22179.1
AC022613 Genomic DNA No translation available.
BC111712 mRNA Translation: AAI11713.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS42007.1 [Q07157-1]
CCDS45199.1 [Q07157-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A47747

NCBI Reference Sequences

More...RefSeqi		NP_003248.3, NM_003257.4 [Q07157-1]
NP_783297.2, NM_175610.3 [Q07157-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000346128; ENSP00000281537; ENSG00000104067 [Q07157-1]
ENST00000545208; ENSP00000441202; ENSG00000104067 [Q07157-2]
ENST00000621049; ENSP00000484535; ENSG00000277401

Database of genes from NCBI RefSeq genomes

More...GeneIDi		7082

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:7082

UCSC genome browser

More...UCSCi		uc001zcr.4 human [Q07157-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L14837 mRNA Translation: AAA02891.1 Different initiation.
AK304758 mRNA Translation: BAG65513.1
DQ015919 Genomic DNA Translation: AAY22179.1
AC022613 Genomic DNA No translation available.
BC111712 mRNA Translation: AAI11713.1
CCDSiCCDS42007.1 [Q07157-1]
CCDS45199.1 [Q07157-2]
PIRiA47747
RefSeqiNP_003248.3, NM_003257.4 [Q07157-1]
NP_783297.2, NM_175610.3 [Q07157-2]

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
2H2BX-ray1.60A18-110[»]
2H2CX-ray2.00A18-110[»]
2H3MX-ray2.90A18-110[»]
2JWENMR-A/B185-264[»]
2KXRNMR-A1631-1748[»]
2KXSNMR-A1631-1748[»]
2RCZX-ray1.70A/B186-264[»]
3CYYX-ray2.40A/B182-273[»]
3LH5X-ray2.60A516-803[»]
3SHUX-ray2.75A/B421-512[»]
3SHWX-ray2.90A421-888[»]
3TSVX-ray1.99A417-516[»]
3TSWX-ray2.85A/B/C/D417-803[»]
3TSZX-ray2.50A417-803[»]
4OEOX-ray1.90A/B/C18-110[»]
4OEPX-ray2.35A/B18-110[»]
4Q2QX-ray1.45A419-504[»]
4YYXX-ray1.79A/B18-110[»]
SMRiQ07157
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi112937, 131 interactors
CORUMiQ07157
ELMiQ07157
IntActiQ07157, 70 interactors
MINTiQ07157
STRINGi9606.ENSP00000281537

Protein family/group databases

TCDBi8.A.24.1.9 the ezrin/radixin/moesin-binding phosphoprotein 50 (ebp50) family

PTM databases

iPTMnetiQ07157
PhosphoSitePlusiQ07157

Polymorphism and mutation databases

BioMutaiTJP1
DMDMi85700443

Proteomic databases

EPDiQ07157
jPOSTiQ07157
MassIVEiQ07157
MaxQBiQ07157
PaxDbiQ07157
PeptideAtlasiQ07157
PRIDEiQ07157
ProteomicsDBi58506 [Q07157-1]
58507 [Q07157-2]

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		7082

Genome annotation databases

EnsembliENST00000346128; ENSP00000281537; ENSG00000104067 [Q07157-1]
ENST00000545208; ENSP00000441202; ENSG00000104067 [Q07157-2]
ENST00000621049; ENSP00000484535; ENSG00000277401
GeneIDi7082
KEGGihsa:7082
UCSCiuc001zcr.4 human [Q07157-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7082
DisGeNETi7082

GeneCards: human genes, protein and diseases

More...GeneCardsi		TJP1
HGNCiHGNC:11827 TJP1
HPAiCAB010822
HPA001636
HPA001637
MIMi601009 gene
neXtProtiNX_Q07157
OpenTargetsiENSG00000104067
PharmGKBiPA36532

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3580 Eukaryota
ENOG410XQP3 LUCA
GeneTreeiENSGT00940000155164
InParanoidiQ07157
KOiK05701
OrthoDBi179316at2759
PhylomeDBiQ07157
TreeFamiTF315957

Enzyme and pathway databases

ReactomeiR-HSA-191650 Regulation of gap junction activity
R-HSA-2028269 Signaling by Hippo
R-HSA-351906 Apoptotic cleavage of cell adhesion proteins
R-HSA-8935964 RUNX1 regulates expression of components of tight junctions
SIGNORiQ07157

Miscellaneous databases

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

More...ChiTaRSi		TJP1 human
EvolutionaryTraceiQ07157

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Tight_junction_protein_1

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

More...GenomeRNAii		7082
PharosiQ07157

Protein Ontology

More...PROi		PR:Q07157

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000104067 Expressed in 241 organ(s), highest expression level in brain
ExpressionAtlasiQ07157 baseline and differential
GenevisibleiQ07157 HS

Family and domain databases

CDDicd12026 SH3_ZO-1, 1 hit
InterProiView protein in InterPro
IPR008145 GK/Ca_channel_bsu
IPR008144 Guanylate_kin-like_dom
IPR027417 P-loop_NTPase
IPR001478 PDZ
IPR036034 PDZ_sf
IPR036028 SH3-like_dom_sf
IPR001452 SH3_domain
IPR005417 ZO
IPR005418 ZO-1
IPR035597 ZO-1_SH3
IPR000906 ZU5_dom
PANTHERiPTHR13865:SF25 PTHR13865:SF25, 1 hit
PfamiView protein in Pfam
PF00625 Guanylate_kin, 1 hit
PF00595 PDZ, 3 hits
PF07653 SH3_2, 1 hit
PF00791 ZU5, 1 hit
PRINTSiPR01597 ZONOCCLUDNS
PR01598 ZONOCCLUDNS1
SMARTiView protein in SMART
SM00072 GuKc, 1 hit
SM00228 PDZ, 3 hits
SM00218 ZU5, 1 hit
SUPFAMiSSF50044 SSF50044, 1 hit
SSF50156 SSF50156, 3 hits
SSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS50052 GUANYLATE_KINASE_2, 1 hit
PS50106 PDZ, 3 hits
PS50002 SH3, 1 hit
PS51145 ZU5, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiZO1_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: Q07157
Secondary accession number(s): B4E3K1, Q2NKP3, Q4ZGJ6
<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: October 1, 1994
Last sequence update: January 24, 2006
Last modified: November 13, 2019
This is version 218 of the entry and version 3 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again