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Entry version 141 (02 Jun 2021)
Sequence version 1 (01 May 1999)
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Protein

Tight junction protein ZO-1

Gene

TJP1

Organism
Canis lupus familiaris (Dog) (Canis familiaris)
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:9792688, PubMed:10575001, PubMed:27802160).

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 (PubMed:27802160).

Plays a role in the regulation of cell migration by targeting CDC42BPBb to the leading edge of migrating cells (By similarity).

With TJP2 and TJP3, participates in the junctional retention and stability of the transcription factor DBPA, but is not involved in its shuttling to the nucleus (PubMed:24986862).

By similarity3 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

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalmodulin-binding

<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:
Tight junction protein ZO-1By similarity
Alternative name(s):
Tight junction protein 1By similarity
Zona occludens protein 11 Publication
Zonula occludens protein 1By similarity
<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:TJP1
Synonyms:ZO11 Publication
<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>OrganismiCanis lupus familiaris (Dog) (Canis familiaris)
<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 identifieri9615 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis
<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
  • UP000002254 <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: Unplaced

<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

Keywords - Cellular componenti

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

<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_00000945391 – 1769Tight junction protein ZO-1Add BLAST1769

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 residuei125PhosphoserineBy similarity1
Modified residuei131PhosphotyrosineBy similarity1
Modified residuei174PhosphoserineBy similarity1
Modified residuei177PhosphoserineBy similarity1
Modified residuei178PhosphoserineBy similarity1
Modified residuei184PhosphothreonineBy similarity1
Modified residuei211PhosphoserineBy similarity1
Modified residuei240PhosphoserineBy similarity1
Modified residuei266PhosphothreonineBy similarity1
Modified residuei274PhosphoserineBy similarity1
Modified residuei276PhosphoserineBy similarity1
Modified residuei279PhosphoserineBy similarity1
Modified residuei283PhosphoserineBy similarity1
Modified residuei289PhosphoserineBy similarity1
Modified residuei293PhosphoserineBy similarity1
Modified residuei296PhosphoserineBy similarity1
Modified residuei299PhosphoserineBy similarity1
Modified residuei322PhosphoserineBy similarity1
Modified residuei328PhosphoserineBy similarity1
Modified residuei333PhosphoserineBy similarity1
Modified residuei336PhosphoserineBy similarity1
Modified residuei352PhosphoserineBy similarity1
Modified residuei353PhosphothreonineBy similarity1
Modified residuei616PhosphoserineBy similarity1
Modified residuei621PhosphoserineBy similarity1
Modified residuei808PhosphothreonineBy similarity1
Modified residuei809PhosphoserineBy similarity1
Modified residuei820PhosphoserineBy similarity1
Modified residuei821PhosphotyrosineBy similarity1
Modified residuei823PhosphoserineBy similarity1
Modified residuei827PhosphoserineBy similarity1
Modified residuei836PhosphoserineBy similarity1
Modified residuei845PhosphothreonineBy similarity1
Modified residuei847PhosphothreonineBy similarity1
Modified residuei853PhosphothreonineBy similarity1
Modified residuei860PhosphothreonineBy similarity1
Modified residuei867PhosphothreonineBy similarity1
Modified residuei911PhosphoserineBy similarity1
Modified residuei967PhosphoserineBy similarity1
Modified residuei1070PhosphoserineBy similarity1
Modified residuei1138PhosphoserineBy similarity1
Modified residuei1139PhosphotyrosineBy similarity1
Modified residuei1164PhosphotyrosineBy similarity1
Modified residuei1353PhosphotyrosineBy similarity1
Modified residuei1365PhosphoserineBy similarity1
Modified residuei1412PhosphoserineBy similarity1
Modified residuei1546PhosphoserineBy similarity1
Modified residuei1618PhosphoserineBy 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

Phosphorylated at tyrosine redidues in response to epidermal growth factor (EGF) (By similarity). This response is dependent on an intact actin microfilament system (By similarity). Dephosphorylated by PTPRJ (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
O97758

PRoteomics IDEntifications database

More...
PRIDEi
O97758

<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

Homodimer, and heterodimer with TJP2 and TJP3 (PubMed:9792688, PubMed:10575001).

Interacts with OCLN (PubMed:9792688, PubMed:27802160).

Interacts with CALM, claudins, CGN/cingulin, CXADR, GJA12, GJD3 and UBN1 (By similarity).

Interacts (via ZU5 domain) with CDC42BPB and MYZAP (By similarity).

Interacts (via PDZ domain) with GJA1 (By similarity).

Interacts (via PDZ domains) with ANKRD2 (By similarity).

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

Interacts with HSPA4 (PubMed:16407410).

Interacts with KIRREL1 (By similarity) (PubMed:16407410).

Interacts with DLL1 (By similarity).

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

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

Interacts with SPEF1 (By similarity).

By similarity3 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
139675, 3 interactors

CORUM comprehensive resource of mammalian protein complexes

More...
CORUMi
O97758

Protein interaction database and analysis system

More...
IntActi
O97758, 8 interactors

Molecular INTeraction database

More...
MINTi
O97758

STRING: functional protein association networks

More...
STRINGi
9612.ENSCAFP00000015301

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
O97758

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

More...
SMRi
O97758

Database of comparative protein structure models

More...
ModBasei
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>Domaini23 – 110PDZ 1PROSITE-ProRule annotationAdd BLAST88
Domaini185 – 263PDZ 2PROSITE-ProRule annotationAdd BLAST79
Domaini420 – 501PDZ 3PROSITE-ProRule annotationAdd BLAST82
Domaini515 – 583SH3PROSITE-ProRule annotationAdd BLAST69
Domaini609 – 790Guanylate kinase-likePROSITE-ProRule annotationAdd BLAST182
Domaini1635 – 1769ZU5PROSITE-ProRule annotationAdd BLAST135

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>Regioni102 – 188DisorderedSequence analysisAdd BLAST87
Regioni295 – 362DisorderedSequence analysisAdd BLAST68
Regioni632 – 875Occludin (OCLN)-binding regionBy similarityAdd BLAST244
Regioni824 – 976DisorderedSequence analysisAdd BLAST153
Regioni1010 – 1067DisorderedSequence analysisAdd BLAST58
Regioni1091 – 1212DisorderedSequence analysisAdd BLAST122
Regioni1150 – 1370Actin-binding region (ABR)By similarityAdd BLAST221
Regioni1224 – 1261DisorderedSequence analysisAdd BLAST38
Regioni1273 – 1589DisorderedSequence analysisAdd BLAST317

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 biasi132 – 170Basic and acidic residuesSequence analysisAdd BLAST39
Compositional biasi171 – 185Polar residuesSequence analysisAdd BLAST15
Compositional biasi297 – 325Basic and acidic residuesSequence analysisAdd BLAST29
Compositional biasi847 – 863Acidic residuesSequence analysisAdd BLAST17
Compositional biasi913 – 976Polar residuesSequence analysisAdd BLAST64
Compositional biasi1107 – 1128Basic and acidic residuesSequence analysisAdd BLAST22
Compositional biasi1273 – 1289Basic and acidic residuesSequence analysisAdd BLAST17
Compositional biasi1337 – 1369Basic and acidic residuesSequence analysisAdd BLAST33
Compositional biasi1384 – 1402Polar residuesSequence analysisAdd BLAST19
Compositional biasi1421 – 1435Pro residuesSequence analysisAdd BLAST15
Compositional biasi1461 – 1475Polar residuesSequence analysisAdd BLAST15
Compositional biasi1485 – 1503Polar residuesSequence analysisAdd BLAST19
Compositional biasi1511 – 1533Polar residuesSequence analysisAdd BLAST23

<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 (By similarity).By similarity
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:27802160). The ABR is also required for the localization to puncta at the free edge of cells before initiation of cell-cell contact (By similarity). The ABR is also necessary for Tjp1 recruitment to podosomes (By similarity).By similarity1 Publication
The second PDZ domain (PDZ2) mediates homodimerization and heterodimerization with Tjp2 and Tjp3 (By similarity). PDZ2 domain also mediates interaction with Gja12 (By similarity).By similarity

<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

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eggNOGi
KOG3580, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
O97758

Database of Orthologous Groups

More...
OrthoDBi
1175136at2759

Family and domain databases

Conserved Domains Database

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

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.30.42.10, 3 hits

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

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PANTHERi
PTHR13865:SF25, PTHR13865:SF25, 1 hit

Pfam protein domain database

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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%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.

O97758-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSARAAAAKN TAMEETAIWE QHTVTLHRAP GFGFGIAISG GRDNPHFQSG
60 70 80 90 100
ETSIVISDVL KGGPAEGQLQ ENDRVAMVNG VSMDNVEHAF AVQQLRKSGK
110 120 130 140 150
NAKITIRRKK KVQIPVSRPD PEPVSENEDS YDEEVHDPRS SRGGLVSRRS
160 170 180 190 200
EKSWARDRSA SRERSLSPRS DRRSVASSQP PKPTKVTLVK SRKNEEYGLR
210 220 230 240 250
LASHIFVKEI SQDSLAARDG NIQEGDVVLK INGTVTENMS LTDAKTLIER
260 270 280 290 300
SKGKLKMVVQ RDERATLLNV PDLSDSIHSA NASERDDISE IQSLASDHSG
310 320 330 340 350
RSHDRPPRHS RSRSPDQRSE PSDHSRHSPQ QPSSGSLRSR EEERISKPGA
360 370 380 390 400
VSTPVKHADD HTHKTVEEVV VERNEKQAPS LPEPKPVYAQ VGQPDVDLPV
410 420 430 440 450
SPSDGVLPNS THEDGILRPS MKLVKFRKGD SVGLRLAGGN DVGIFVAGVL
460 470 480 490 500
EDSPAAKEGL EEGDQILRVN NVDFTNIIRE EAVLFLLDLP KGEEVTILAQ
510 520 530 540 550
KKKDVYRRIV ESDVGDSFYI RTHFEYEKES PYGLSFNKGE VFRVVDTLYN
560 570 580 590 600
GKLGSWLAIR IGKNHKEVER GIIPNKNRAE QLASVQYTLP KTAGGDRADF
610 620 630 640 650
WRFRGLRSSK RNLRKSREDL SAQPVQTKFP AYERVVLREA GFLRPVTIFG
660 670 680 690 700
PIADVAREKL AREEPDIYQI AKSEPRDAGT DQRSSGIIRL HTIKQIIDQD
710 720 730 740 750
KHALLDVTPN AVDRLNYAQW YPIVVFLNPD SKQGVKTMRM RLCPESRKSA
760 770 780 790 800
RKLYERSHKL RKNNHHLFTT TINLNSMNDG WYGALKEAIQ QQQNQLVWVS
810 820 830 840 850
EGKADGATSD DLDLHDDRLS YLSAPGSEYS MYSTDSRHTS DYEDTDTEGG
860 870 880 890 900
AYTDQELDET LNDEVGTPPE SAITRSSEPV REDSSGMHHE NQTYPPYSPQ
910 920 930 940 950
AQPQPIHRID SPGFKTASQQ KAEASSPVPY LSPETNPASS TSAVNHNVTL
960 970 980 990 1000
TNVRLEGPTP APSTSYSPQA DSLRTPSTEA AHIMLRDQEP SLPSHVEPAK
1010 1020 1030 1040 1050
VYRKDPYPEE MMRQNHVLKQ PAVGHPGQRP DKEPNLSYES QPPYVEKQAN
1060 1070 1080 1090 1100
RDLEQPTYRY DSSSYTDQFS RNYDHRLRYE ERIPTYEEQW SYYDDKQPYQ
1110 1120 1130 1140 1150
PRPSLDNQHP RDLDSRQHPE ESSERGSYPR FEEPAPLSYD SRPRYDQPPR
1160 1170 1180 1190 1200
TSTLRHEEQP TPGYDMHNRY RPEAQSYSSA GPKASEPKQY FDQYPRSYEQ
1210 1220 1230 1240 1250
VPSQGFSSKA GHYEPLHGAA VVPPLIPASQ HKPEVLPSNT KPLPPPPTLT
1260 1270 1280 1290 1300
EEEEDPAMKP QSVLTRVKMF ENKRSASLEN KKDENHTAGF KPPEVASKPP
1310 1320 1330 1340 1350
GAPIIGPKPT PQNQFSEHDK TLYRIPEPQK PQMKPPEDIV RSNHYDPEED
1360 1370 1380 1390 1400
EEYYRKQLSY FDRRSFENKP STHIPAGHLS EPAKPVHSQN QTNFSSYSSK
1410 1420 1430 1440 1450
GKSPEADAPD RSFGEKRYEP VQATPPPPPL PSQYAQPSQP GTSSSLALHT
1460 1470 1480 1490 1500
HAKGAHGEGN SISLDFQNSL VSKPDPPPSQ NKPATFRPPN REDTVQSTFY
1510 1520 1530 1540 1550
PQKSFPDKAP VNGAEQTQKT VTPAYNRFTP KPYTSSARPF ERKFESPKFN
1560 1570 1580 1590 1600
HNLLPSETAH KPDLSSKAPA SPKTLAKAHS RAQPPEFDSG VETFSIHADK
1610 1620 1630 1640 1650
PKYQMNNLST VPKAIPVSPS AVEEDEDEDG HTVVATARGV FNNNGGVLSS
1660 1670 1680 1690 1700
IETGVSIIIP QGAIPEGVEQ EIYFKVCRDN SILPPLDKEK GETLLSPLVM
1710 1720 1730 1740 1750
CGPHGLKFLK PVELRLPHCA SMTPDGWSFA LKSSDSSSGD PKTWQNKCLP
1760
GDPNYLVGAN CVSVLIDHF
Length:1,769
Mass (Da):197,607
Last modified:May 1, 1999 - v1
<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:i181E9F36CEBC96EF
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U55935 mRNA Translation: AAD11529.1

NCBI Reference Sequences

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RefSeqi
NP_001003140.1, NM_001003140.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
403752

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cfa:403752

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U55935 mRNA Translation: AAD11529.1
RefSeqiNP_001003140.1, NM_001003140.1

3D structure databases

BMRBiO97758
SMRiO97758
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi139675, 3 interactors
CORUMiO97758
IntActiO97758, 8 interactors
MINTiO97758
STRINGi9612.ENSCAFP00000015301

Proteomic databases

PaxDbiO97758
PRIDEiO97758

Genome annotation databases

GeneIDi403752
KEGGicfa:403752

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7082

Phylogenomic databases

eggNOGiKOG3580, Eukaryota
InParanoidiO97758
OrthoDBi1175136at2759

Family and domain databases

CDDicd12026, SH3_ZO-1, 1 hit
Gene3Di2.30.42.10, 3 hits
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

MobiDB: a database of protein disorder and mobility annotations

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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_CANLF
<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: O97758
<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: April 26, 2005
Last sequence update: May 1, 1999
Last modified: June 2, 2021
This is version 141 of the entry and version 1 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

<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

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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