| UniProt ID | ZO1_CANLF | |
|---|---|---|
| UniProt AC | O97758 | |
| Protein Name | Tight junction protein ZO-1 {ECO:0000250|UniProtKB:Q07157} | |
| Gene Name | TJP1 | |
| Organism | Canis lupus familiaris (Dog) (Canis familiaris). | |
| Sequence Length | 1769 | |
| Subcellular Localization |
Cell membrane Peripheral membrane protein Cytoplasmic side . Cell junction, tight junction . Cell junction . Cell junction, gap junction . Moves from the cytoplasm to the cell membrane concurrently with cell-cell contact (PubMed:9792688). Distrib |
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| Protein Description | 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] | |
| Protein Sequence | MSARAAAAKNTAMEETAIWEQHTVTLHRAPGFGFGIAISGGRDNPHFQSGETSIVISDVLKGGPAEGQLQENDRVAMVNGVSMDNVEHAFAVQQLRKSGKNAKITIRRKKKVQIPVSRPDPEPVSENEDSYDEEVHDPRSSRGGLVSRRSEKSWARDRSASRERSLSPRSDRRSVASSQPPKPTKVTLVKSRKNEEYGLRLASHIFVKEISQDSLAARDGNIQEGDVVLKINGTVTENMSLTDAKTLIERSKGKLKMVVQRDERATLLNVPDLSDSIHSANASERDDISEIQSLASDHSGRSHDRPPRHSRSRSPDQRSEPSDHSRHSPQQPSSGSLRSREEERISKPGAVSTPVKHADDHTHKTVEEVVVERNEKQAPSLPEPKPVYAQVGQPDVDLPVSPSDGVLPNSTHEDGILRPSMKLVKFRKGDSVGLRLAGGNDVGIFVAGVLEDSPAAKEGLEEGDQILRVNNVDFTNIIREEAVLFLLDLPKGEEVTILAQKKKDVYRRIVESDVGDSFYIRTHFEYEKESPYGLSFNKGEVFRVVDTLYNGKLGSWLAIRIGKNHKEVERGIIPNKNRAEQLASVQYTLPKTAGGDRADFWRFRGLRSSKRNLRKSREDLSAQPVQTKFPAYERVVLREAGFLRPVTIFGPIADVAREKLAREEPDIYQIAKSEPRDAGTDQRSSGIIRLHTIKQIIDQDKHALLDVTPNAVDRLNYAQWYPIVVFLNPDSKQGVKTMRMRLCPESRKSARKLYERSHKLRKNNHHLFTTTINLNSMNDGWYGALKEAIQQQQNQLVWVSEGKADGATSDDLDLHDDRLSYLSAPGSEYSMYSTDSRHTSDYEDTDTEGGAYTDQELDETLNDEVGTPPESAITRSSEPVREDSSGMHHENQTYPPYSPQAQPQPIHRIDSPGFKTASQQKAEASSPVPYLSPETNPASSTSAVNHNVTLTNVRLEGPTPAPSTSYSPQADSLRTPSTEAAHIMLRDQEPSLPSHVEPAKVYRKDPYPEEMMRQNHVLKQPAVGHPGQRPDKEPNLSYESQPPYVEKQANRDLEQPTYRYDSSSYTDQFSRNYDHRLRYEERIPTYEEQWSYYDDKQPYQPRPSLDNQHPRDLDSRQHPEESSERGSYPRFEEPAPLSYDSRPRYDQPPRTSTLRHEEQPTPGYDMHNRYRPEAQSYSSAGPKASEPKQYFDQYPRSYEQVPSQGFSSKAGHYEPLHGAAVVPPLIPASQHKPEVLPSNTKPLPPPPTLTEEEEDPAMKPQSVLTRVKMFENKRSASLENKKDENHTAGFKPPEVASKPPGAPIIGPKPTPQNQFSEHDKTLYRIPEPQKPQMKPPEDIVRSNHYDPEEDEEYYRKQLSYFDRRSFENKPSTHIPAGHLSEPAKPVHSQNQTNFSSYSSKGKSPEADAPDRSFGEKRYEPVQATPPPPPLPSQYAQPSQPGTSSSLALHTHAKGAHGEGNSISLDFQNSLVSKPDPPPSQNKPATFRPPNREDTVQSTFYPQKSFPDKAPVNGAEQTQKTVTPAYNRFTPKPYTSSARPFERKFESPKFNHNLLPSETAHKPDLSSKAPASPKTLAKAHSRAQPPEFDSGVETFSIHADKPKYQMNNLSTVPKAIPVSPSAVEEDEDEDGHTVVATARGVFNNNGGVLSSIETGVSIIIPQGAIPEGVEQEIYFKVCRDNSILPPLDKEKGETLLSPLVMCGPHGLKFLKPVELRLPHCASMTPDGWSFALKSSDSSSGDPKTWQNKCLPGDPNYLVGANCVSVLIDHF | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 125 | Phosphorylation | RPDPEPVSENEDSYD CCCCCCCCCCCCCCC | - | ||
| 131 | Phosphorylation | VSENEDSYDEEVHDP CCCCCCCCCCCCCCC | - | ||
| 174 | Phosphorylation | SPRSDRRSVASSQPP CCHHHCCHHHCCCCC | - | ||
| 177 | Phosphorylation | SDRRSVASSQPPKPT HHCCHHHCCCCCCCC | - | ||
| 178 | Phosphorylation | DRRSVASSQPPKPTK HCCHHHCCCCCCCCE | - | ||
| 184 | Phosphorylation | SSQPPKPTKVTLVKS CCCCCCCCEEEEEEC | - | ||
| 211 | Phosphorylation | HIFVKEISQDSLAAR EEEEEECCCCCHHHC | - | ||
| 240 | Phosphorylation | GTVTENMSLTDAKTL CEEECCCCCHHHHHH | - | ||
| 266 | Phosphorylation | VQRDERATLLNVPDL EEHHHCCEECCCCCC | - | ||
| 274 | Phosphorylation | LLNVPDLSDSIHSAN ECCCCCCHHHHHHCC | - | ||
| 276 | Phosphorylation | NVPDLSDSIHSANAS CCCCCHHHHHHCCHH | - | ||
| 279 | Phosphorylation | DLSDSIHSANASERD CCHHHHHHCCHHHCC | - | ||
| 283 | Phosphorylation | SIHSANASERDDISE HHHHCCHHHCCCHHH | - | ||
| 289 | Phosphorylation | ASERDDISEIQSLAS HHHCCCHHHHHHHHH | - | ||
| 293 | Phosphorylation | DDISEIQSLASDHSG CCHHHHHHHHHCCCC | - | ||
| 296 | Phosphorylation | SEIQSLASDHSGRSH HHHHHHHHCCCCCCC | - | ||
| 299 | Phosphorylation | QSLASDHSGRSHDRP HHHHHCCCCCCCCCC | - | ||
| 322 | Phosphorylation | PDQRSEPSDHSRHSP CCCCCCCCCCCCCCC | - | ||
| 328 | Phosphorylation | PSDHSRHSPQQPSSG CCCCCCCCCCCCCCC | - | ||
| 333 | Phosphorylation | RHSPQQPSSGSLRSR CCCCCCCCCCCCCCH | - | ||
| 336 | Phosphorylation | PQQPSSGSLRSREEE CCCCCCCCCCCHHHH | - | ||
| 352 | Phosphorylation | ISKPGAVSTPVKHAD CCCCCCCCCCCCCCC | - | ||
| 353 | Phosphorylation | SKPGAVSTPVKHADD CCCCCCCCCCCCCCC | - | ||
| 616 | Phosphorylation | SKRNLRKSREDLSAQ HHHHHHHCHHHHHCC | - | ||
| 621 | Phosphorylation | RKSREDLSAQPVQTK HHCHHHHHCCCCCCC | - | ||
| 808 | Phosphorylation | EGKADGATSDDLDLH ECCCCCCCCCCCCCC | - | ||
| 809 | Phosphorylation | GKADGATSDDLDLHD CCCCCCCCCCCCCCC | - | ||
| 820 | Phosphorylation | DLHDDRLSYLSAPGS CCCCCHHHHEECCCC | - | ||
| 821 | Phosphorylation | LHDDRLSYLSAPGSE CCCCHHHHEECCCCC | - | ||
| 823 | Phosphorylation | DDRLSYLSAPGSEYS CCHHHHEECCCCCCE | - | ||
| 827 | Phosphorylation | SYLSAPGSEYSMYST HHEECCCCCCEEEEC | - | ||
| 836 | Phosphorylation | YSMYSTDSRHTSDYE CEEEECCCCCCCCCC | - | ||
| 845 | Phosphorylation | HTSDYEDTDTEGGAY CCCCCCCCCCCCCCC | - | ||
| 847 | Phosphorylation | SDYEDTDTEGGAYTD CCCCCCCCCCCCCCH | - | ||
| 853 | Phosphorylation | DTEGGAYTDQELDET CCCCCCCCHHHHHHH | - | ||
| 860 | Phosphorylation | TDQELDETLNDEVGT CHHHHHHHHCCCCCC | - | ||
| 867 | Phosphorylation | TLNDEVGTPPESAIT HHCCCCCCCCHHHCC | - | ||
| 911 | Phosphorylation | QPIHRIDSPGFKTAS CCCCCCCCCCCCCHH | - | ||
| 967 | Phosphorylation | PAPSTSYSPQADSLR CCCCCCCCCCCCCCC | - | ||
| 1070 | Phosphorylation | SSYTDQFSRNYDHRL CCCCCCCCCCCHHCC | - | ||
| 1138 | Phosphorylation | FEEPAPLSYDSRPRY CCCCCCCCCCCCCCC | - | ||
| 1139 | Phosphorylation | EEPAPLSYDSRPRYD CCCCCCCCCCCCCCC | - | ||
| 1164 | Phosphorylation | EEQPTPGYDMHNRYR CCCCCCCCCCCCCCC | - | ||
| 1353 | Phosphorylation | DPEEDEEYYRKQLSY CHHHCHHHHHHHHHH | - | ||
| 1365 | Phosphorylation | LSYFDRRSFENKPST HHHHCHHHHCCCCCC | - | ||
| 1412 | Phosphorylation | EADAPDRSFGEKRYE CCCCCCCCCCCCCCC | - | ||
| 1546 | Phosphorylation | PFERKFESPKFNHNL CCCCCCCCCCCCCCC | - | ||
| 1618 | Phosphorylation | VPKAIPVSPSAVEED CCCEEECCHHHCCCC | - |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of ZO1_CANLF !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZO1_CANLF !! | ||||||
* Distance = the distance between SAP position and PTM sites.
| Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
|---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of ZO1_CANLF !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ZO1_CANLF !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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