P39447 · ZO1_MOUSE
- ProteinTight junction protein ZO-1
- GeneTjp1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1745 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Tjp1, TjpP2, 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 (By similarity).
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 (By similarity).
Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (By similarity).
With Tjp2 and TJjp3, participates in the junctional retention and stability of the transcription factor Dbpa, but is not involved in its shuttling to the nucleus (By similarity).
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 (By similarity).
Plays an important role in podosome formation and associated function, thus regulating cell adhesion and matrix remodeling (By similarity).
With Tjp2 and TJjp3, participates in the junctional retention and stability of the transcription factor Dbpa, but is not involved in its shuttling to the nucleus (By similarity).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTight junction protein ZO-1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP39447
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact (By similarity).
Detected at the leading edge of migrating and wounded cells (By similarity).
Colocalizes with SPEF1 at sites of cell-cell contact in intestinal epithelial cells (By similarity).
Detected at the leading edge of migrating and wounded cells (By similarity).
Colocalizes with SPEF1 at sites of cell-cell contact in intestinal epithelial cells (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000094541 | 1-1745 | Tight junction protein ZO-1 | |||
Sequence: MSARAAAAKSTAMEETAIWEQHTVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSHPDPEPVSDNEDDSYDEEVHDPRAGRGALANRRSEKSWARDRSASRERSLSPRSDRRSVASSQPAKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSGRSHDRPPRRSQSRSPDQRSEPSDHSTQSPQQPSNGSLRSREEERMSKPGAISTPVKHVDDHPPKAVEEVTVEKNEKQTPTLPEPKPVYAQVGQPDVDLPVSPSDGALPNSAHEDGILRPSMKLVKFRKGDSVGLRLAGGNDVGIFVAGVLEDSPAAKEGLEEGDQILRVNNVDFTNIIREEAVLFLLDLPKGEEVTILAQKKKDVYRRIVESDVGDSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNKNRAEQLASVQYTLPKTAGGDRADFWRFRGLRSSKRNLRKSREDLSAQPVQTKFPAYERVVLREAGFLRPVTIFGPIADVAREKLAREEPDIYQIAKSEPRDAGTDHRSSGIIRLHTIKQIIDQDKHALLDVTPNAVDRLNYAQWYPIVVFLNPDSKQGVKTMRMRLCPESRKSARKLYERSHKLRKNNHHLFTTTINLNSMNDGWYGALKEAIQQQQNQLVWVSEGKADGATSDDLDLHDDRLSYLSAPGSEYSMYSTDSRHTSDYEDTDTEGGAYTDQELDETLNDEVGTPPESAITRSSEPVREDSSGMHHENQTYPPYSPQAQPQAIHRIDSPGLKPASQQKAEASSPVPYLSPETTPASSASAVNHNVSVTNVSLEEPAPAPPTSHASQPGCLGAPSAEAAHVVLRGEGPPLPPHADPAKVYRKEPYSEEMMRQNHILKQPALGHPGQRPDKEPNLAYEPQLPYIEKQASRDLEQPSYRYEVSSYTDQFSRNYDHRLRFEDRIPTYEDQWSYYDDKQPYQPRPFENQHPRDLDSRQHPEEASERGYFQRFEEPAPLSYDSRTRYEQLPRTSTLRHEEQPAPAYEVHNRYRPEAQPYSSTGPKSSEPKQYFDQYPRSYEQVPPPGFTSKTGHYEPLHGAAVVPPLIPSSQQKPEVLPSATKPQPPPPTLTEEEEDPAMKPQSVLTRVKMFENKRSASLENKKDVNDTASFKPPEVASKPPGASLAGPKPVPQSQFSEHDKTLYRLPEPQKPQVKPPEDIVRSNHYDPEEDEEYYRKQLSYFDRRSFESKPSAHLPAGHHSEPAKPVHSQSQPNFSSYSSKGKPETDAVDRSFSEKRYDPAQATPPPPPLPSQYSQPAPPLSSSSLHIHSKGAQGEGNSVSLDFQNSYMSKPDPPPSQSKPATFRPPTREDPPQTFYPQKSFPDKAPVNGAEQTQKTITPVYNRFTPKPYTSSARPFERKFESPKFNHNLLPSETVHKPELSSKTPTSPKTLMKAHSSTQPPEFDSGVETFSVHTDKPKYQMNNISTMPKAVPVSPSAVEEDEDEDGHTVVATARGIFNSNGGVLSSIETGVSIIIPQGAIPEGIEQEIYFKVCRDNSILPPLDKEKGETLLSPLVMCGPHGLKFLKPVELRLPHCDPKTWQNKCLPGDPNYLVGANCVSVLIDHF | ||||||
Modified residue | 125 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 132 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 175 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 178 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 179 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 185 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 212 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 241 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 267 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 275 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 277 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 280 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 284 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 290 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 294 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 297 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 300 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 323 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 329 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 334 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 337 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 353 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 354 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 617 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 622 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 809 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 810 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 821 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 822 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 824 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 828 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 837 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 846 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 848 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 854 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 861 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 868 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 912 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1071 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1138 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1139 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1164 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1353 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 1365 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1411 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1542 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 1614 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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).
This response is dependent on an intact actin microfilament system (By similarity).
Dephosphorylated by PTPRJ (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Homodimer (By similarity).
Forms heterodimers TJP3 (By similarity).
Forms a heterodimer (via PDZ2 domain) with TJP2/ZO2 (via PDZ2 domain) (PubMed:10026224).
Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJD3 and UBN1 (PubMed:10601346).
Interacts (via ZU5 domain) with CDC42BPB (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) (PubMed:16188940).
Interacts with GJA12 and KIRREL1 (PubMed:12424224, PubMed:15183511).
Interacts with HSPA4 (By similarity).
Interacts (via ZU5 domain) with MYZAP (PubMed:20093627).
Interacts with DLL1 (PubMed:24715457).
Interacts with USP53 (via the C-terminal region) (PubMed:26609154).
Interacts with DNMBP (via C-terminal domain); required for the apical cell-cell junction localization of DNMBP (By similarity).
Interacts with SPEF1 (By similarity).
Interacts (via N-terminus) with CTNNA1 (PubMed:10026224).
Interacts with CLDN18 (PubMed:29400695).
Interacts with CLDN16 (via TRV motif); this is a prerequisite for anchoring of CLDN16 at the tight junction
Forms heterodimers TJP3 (By similarity).
Forms a heterodimer (via PDZ2 domain) with TJP2/ZO2 (via PDZ2 domain) (PubMed:10026224).
Interacts with OCLN, CALM, claudins, CGN/cingulin, CXADR, GJD3 and UBN1 (PubMed:10601346).
Interacts (via ZU5 domain) with CDC42BPB (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) (PubMed:16188940).
Interacts with GJA12 and KIRREL1 (PubMed:12424224, PubMed:15183511).
Interacts with HSPA4 (By similarity).
Interacts (via ZU5 domain) with MYZAP (PubMed:20093627).
Interacts with DLL1 (PubMed:24715457).
Interacts with USP53 (via the C-terminal region) (PubMed:26609154).
Interacts with DNMBP (via C-terminal domain); required for the apical cell-cell junction localization of DNMBP (By similarity).
Interacts with SPEF1 (By similarity).
Interacts (via N-terminus) with CTNNA1 (PubMed:10026224).
Interacts with CLDN18 (PubMed:29400695).
Interacts with CLDN16 (via TRV motif); this is a prerequisite for anchoring of CLDN16 at the tight junction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P39447 | Actn4 P57780 | 6 | EBI-79508, EBI-445071 | |
BINARY | P39447 | Gja1 P23242 | 4 | EBI-79508, EBI-298630 | |
BINARY | P39447 | Gjb6 P70689 | 3 | EBI-79508, EBI-2615416 | |
BINARY | P39447 | Vcl Q64727 | 8 | EBI-79508, EBI-432047 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 23-110 | PDZ 1 | ||||
Sequence: TVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKK | ||||||
Region | 102-189 | Disordered | ||||
Sequence: AKITIRRKKKVQIPVSHPDPEPVSDNEDDSYDEEVHDPRAGRGALANRRSEKSWARDRSASRERSLSPRSDRRSVASSQPAKPTKVTL | ||||||
Compositional bias | 134-171 | Basic and acidic residues | ||||
Sequence: EEVHDPRAGRGALANRRSEKSWARDRSASRERSLSPRS | ||||||
Compositional bias | 172-186 | Polar residues | ||||
Sequence: DRRSVASSQPAKPTK | ||||||
Domain | 186-264 | PDZ 2 | ||||
Sequence: KVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDE | ||||||
Region | 296-364 | Disordered | ||||
Sequence: ASDHSGRSHDRPPRRSQSRSPDQRSEPSDHSTQSPQQPSNGSLRSREEERMSKPGAISTPVKHVDDHPP | ||||||
Compositional bias | 298-321 | Basic and acidic residues | ||||
Sequence: DHSGRSHDRPPRRSQSRSPDQRSE | ||||||
Compositional bias | 322-337 | Polar residues | ||||
Sequence: PSDHSTQSPQQPSNGS | ||||||
Domain | 421-502 | PDZ 3 | ||||
Sequence: SMKLVKFRKGDSVGLRLAGGNDVGIFVAGVLEDSPAAKEGLEEGDQILRVNNVDFTNIIREEAVLFLLDLPKGEEVTILAQK | ||||||
Domain | 516-584 | SH3 | ||||
Sequence: GDSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNKNRAEQLA | ||||||
Domain | 610-791 | Guanylate kinase-like | ||||
Sequence: SKRNLRKSREDLSAQPVQTKFPAYERVVLREAGFLRPVTIFGPIADVAREKLAREEPDIYQIAKSEPRDAGTDHRSSGIIRLHTIKQIIDQDKHALLDVTPNAVDRLNYAQWYPIVVFLNPDSKQGVKTMRMRLCPESRKSARKLYERSHKLRKNNHHLFTTTINLNSMNDGWYGALKEAIQ | ||||||
Region | 633-876 | Occludin (OCLN)-binding region | ||||
Sequence: YERVVLREAGFLRPVTIFGPIADVAREKLAREEPDIYQIAKSEPRDAGTDHRSSGIIRLHTIKQIIDQDKHALLDVTPNAVDRLNYAQWYPIVVFLNPDSKQGVKTMRMRLCPESRKSARKLYERSHKLRKNNHHLFTTTINLNSMNDGWYGALKEAIQQQQNQLVWVSEGKADGATSDDLDLHDDRLSYLSAPGSEYSMYSTDSRHTSDYEDTDTEGGAYTDQELDETLNDEVGTPPESAITR | ||||||
Region | 825-944 | Disordered | ||||
Sequence: APGSEYSMYSTDSRHTSDYEDTDTEGGAYTDQELDETLNDEVGTPPESAITRSSEPVREDSSGMHHENQTYPPYSPQAQPQAIHRIDSPGLKPASQQKAEASSPVPYLSPETTPASSASA | ||||||
Compositional bias | 848-864 | Acidic residues | ||||
Sequence: TEGGAYTDQELDETLND | ||||||
Compositional bias | 919-944 | Polar residues | ||||
Sequence: SQQKAEASSPVPYLSPETTPASSASA | ||||||
Region | 956-1042 | Disordered | ||||
Sequence: LEEPAPAPPTSHASQPGCLGAPSAEAAHVVLRGEGPPLPPHADPAKVYRKEPYSEEMMRQNHILKQPALGHPGQRPDKEPNLAYEPQ | ||||||
Compositional bias | 999-1013 | Basic and acidic residues | ||||
Sequence: PAKVYRKEPYSEEMM | ||||||
Region | 1090-1586 | Disordered | ||||
Sequence: QWSYYDDKQPYQPRPFENQHPRDLDSRQHPEEASERGYFQRFEEPAPLSYDSRTRYEQLPRTSTLRHEEQPAPAYEVHNRYRPEAQPYSSTGPKSSEPKQYFDQYPRSYEQVPPPGFTSKTGHYEPLHGAAVVPPLIPSSQQKPEVLPSATKPQPPPPTLTEEEEDPAMKPQSVLTRVKMFENKRSASLENKKDVNDTASFKPPEVASKPPGASLAGPKPVPQSQFSEHDKTLYRLPEPQKPQVKPPEDIVRSNHYDPEEDEEYYRKQLSYFDRRSFESKPSAHLPAGHHSEPAKPVHSQSQPNFSSYSSKGKPETDAVDRSFSEKRYDPAQATPPPPPLPSQYSQPAPPLSSSSLHIHSKGAQGEGNSVSLDFQNSYMSKPDPPPSQSKPATFRPPTREDPPQTFYPQKSFPDKAPVNGAEQTQKTITPVYNRFTPKPYTSSARPFERKFESPKFNHNLLPSETVHKPELSSKTPTSPKTLMKAHSSTQPPEFDSG | ||||||
Compositional bias | 1107-1128 | Basic and acidic residues | ||||
Sequence: NQHPRDLDSRQHPEEASERGYF | ||||||
Region | 1150-1370 | Actin-binding region (ABR) | ||||
Sequence: RTSTLRHEEQPAPAYEVHNRYRPEAQPYSSTGPKSSEPKQYFDQYPRSYEQVPPPGFTSKTGHYEPLHGAAVVPPLIPSSQQKPEVLPSATKPQPPPPTLTEEEEDPAMKPQSVLTRVKMFENKRSASLENKKDVNDTASFKPPEVASKPPGASLAGPKPVPQSQFSEHDKTLYRLPEPQKPQVKPPEDIVRSNHYDPEEDEEYYRKQLSYFDRRSFESKP | ||||||
Compositional bias | 1173-1191 | Polar residues | ||||
Sequence: EAQPYSSTGPKSSEPKQYF | ||||||
Compositional bias | 1272-1288 | Basic and acidic residues | ||||
Sequence: NKRSASLENKKDVNDTA | ||||||
Compositional bias | 1337-1369 | Basic and acidic residues | ||||
Sequence: EDIVRSNHYDPEEDEEYYRKQLSYFDRRSFESK | ||||||
Compositional bias | 1384-1402 | Polar residues | ||||
Sequence: KPVHSQSQPNFSSYSSKGK | ||||||
Compositional bias | 1420-1435 | Pro residues | ||||
Sequence: AQATPPPPPLPSQYSQ | ||||||
Compositional bias | 1436-1472 | Polar residues | ||||
Sequence: PAPPLSSSSLHIHSKGAQGEGNSVSLDFQNSYMSKPD | ||||||
Compositional bias | 1473-1492 | Pro residues | ||||
Sequence: PPPSQSKPATFRPPTREDPP | ||||||
Compositional bias | 1507-1529 | Polar residues | ||||
Sequence: VNGAEQTQKTITPVYNRFTPKPY | ||||||
Compositional bias | 1555-1585 | Polar residues | ||||
Sequence: VHKPELSSKTPTSPKTLMKAHSSTQPPEFDS | ||||||
Domain | 1631-1745 | ZU5 | ||||
Sequence: ATARGIFNSNGGVLSSIETGVSIIIPQGAIPEGIEQEIYFKVCRDNSILPPLDKEKGETLLSPLVMCGPHGLKFLKPVELRLPHCDPKTWQNKCLPGDPNYLVGANCVSVLIDHF |
Domain
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).
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 (By similarity).
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).
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).
The second PDZ domain (PDZ2) mediates homodimerization and heterodimerization with Tjp2 and Tjp3 (By similarity).
PDZ2 domain also mediates interaction with Gja12 (PubMed:15183511).
PDZ2 domain also mediates interaction with Gja12 (PubMed:15183511).
Sequence similarities
Belongs to the MAGUK family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,745
- Mass (Da)194,742
- Last updated2011-07-27 v2
- Checksum002B96F5A998B5CD
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0U1RPW2 | A0A0U1RPW2_MOUSE | Tjp1 | 1128 | ||
A0A0U1RPB2 | A0A0U1RPB2_MOUSE | Tjp1 | 171 | ||
B9EHJ3 | B9EHJ3_MOUSE | Tjp1 | 1685 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 134-171 | Basic and acidic residues | ||||
Sequence: EEVHDPRAGRGALANRRSEKSWARDRSASRERSLSPRS | ||||||
Compositional bias | 172-186 | Polar residues | ||||
Sequence: DRRSVASSQPAKPTK | ||||||
Sequence conflict | 202 | in Ref. 1; BAA03274 | ||||
Sequence: L → P | ||||||
Sequence conflict | 222 | in Ref. 1; BAA03274 | ||||
Sequence: N → D | ||||||
Compositional bias | 298-321 | Basic and acidic residues | ||||
Sequence: DHSGRSHDRPPRRSQSRSPDQRSE | ||||||
Compositional bias | 322-337 | Polar residues | ||||
Sequence: PSDHSTQSPQQPSNGS | ||||||
Sequence conflict | 676 | in Ref. 1; BAA03274 | ||||
Sequence: P → L | ||||||
Compositional bias | 848-864 | Acidic residues | ||||
Sequence: TEGGAYTDQELDETLND | ||||||
Compositional bias | 919-944 | Polar residues | ||||
Sequence: SQQKAEASSPVPYLSPETTPASSASA | ||||||
Sequence conflict | 985 | in Ref. 1; BAA03274 | ||||
Sequence: V → G | ||||||
Compositional bias | 999-1013 | Basic and acidic residues | ||||
Sequence: PAKVYRKEPYSEEMM | ||||||
Compositional bias | 1107-1128 | Basic and acidic residues | ||||
Sequence: NQHPRDLDSRQHPEEASERGYF | ||||||
Compositional bias | 1173-1191 | Polar residues | ||||
Sequence: EAQPYSSTGPKSSEPKQYF | ||||||
Sequence conflict | 1237 | in Ref. 1; BAA03274 | ||||
Sequence: P → R | ||||||
Compositional bias | 1272-1288 | Basic and acidic residues | ||||
Sequence: NKRSASLENKKDVNDTA | ||||||
Compositional bias | 1337-1369 | Basic and acidic residues | ||||
Sequence: EDIVRSNHYDPEEDEEYYRKQLSYFDRRSFESK | ||||||
Compositional bias | 1384-1402 | Polar residues | ||||
Sequence: KPVHSQSQPNFSSYSSKGK | ||||||
Sequence conflict | 1395 | in Ref. 1; BAA03274 | ||||
Sequence: S → P | ||||||
Compositional bias | 1420-1435 | Pro residues | ||||
Sequence: AQATPPPPPLPSQYSQ | ||||||
Compositional bias | 1436-1472 | Polar residues | ||||
Sequence: PAPPLSSSSLHIHSKGAQGEGNSVSLDFQNSYMSKPD | ||||||
Compositional bias | 1473-1492 | Pro residues | ||||
Sequence: PPPSQSKPATFRPPTREDPP | ||||||
Compositional bias | 1507-1529 | Polar residues | ||||
Sequence: VNGAEQTQKTITPVYNRFTPKPY | ||||||
Compositional bias | 1555-1585 | Polar residues | ||||
Sequence: VHKPELSSKTPTSPKTLMKAHSSTQPPEFDS | ||||||
Sequence conflict | 1584 | in Ref. 1; BAA03274 | ||||
Sequence: D → G |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
D14340 EMBL· GenBank· DDBJ | BAA03274.1 EMBL· GenBank· DDBJ | mRNA | ||
AC122222 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC131741 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |