| UniProt ID | LAR_CAEEL | |
|---|---|---|
| UniProt AC | Q9BMN8 | |
| Protein Name | Tyrosine-protein phosphatase Lar-like | |
| Gene Name | ptp-3 | |
| Organism | Caenorhabditis elegans. | |
| Sequence Length | 2200 | |
| Subcellular Localization |
Cell junction, adherens junction. Cell membrane Single-pass type I membrane protein. |
|
| Protein Description | Has a role in early neural and epidermal development; neuroblast movements during closure of the gastrulation cleft and epidermal morphogenesis. Vab-1 and ptp-3 may function redundantly within the same sets of neuronal precursors.. | |
| Protein Sequence | MIQFRNKNNSMNRIARHLRNVARRKGSSLLLFLMLSTVLVAAKEDDPARLVVRPDSSTVVDESKISFFCRADGNPLPSVIWRVNGKSITDHNRISIKSLATGLSTLRFERVSLDDNATVVSCSADNGVANPVVAEASLTVVPRDKVPIGFPQIELHPSLKSVEQGKTAYVSCRVRGDPRAKVLWLRDLIPLDIRADGRYSVSTIGNPGALMIQHAREEDQGKYECIARNTLGVAHSKAANLYVKVRRVPPYFSYKLERQYVVGVGGNINLTCVAVGYPMPRVFWKKTDLMVLDDPSTAPIGKNVLTLTHVESTENFTCVAVSALGNIEATTTVIAKELPPPPVNIVVSSVTSESVVITWKPPKYNEAINKYVVNYRLKYSEGRSSRGKTMETLENSLVIDGLVAFQTYEFTVRSAGPVGVGLESLPVEAQTKPSKPATAPVSPQARSLNRDSILVKWGPCEQPNGLITGYKVYYTNDLVTTPIREWKQHDAKSDEFMTTINGLEPDSRYFVRVIAQNSEGDSPLSTLVTVATRQGIPGQPPMLTVKALDSRRMQLTWDKPLYSSPVVGYTVRYNTSDGEKELTLTSPHEKHVVTGLHPDKYYYFRVAAYSDRGQGEFTEPMISKTIASIPLSSPTIVSAAATSSKSVEIRWKGPEQKKLNGVLTAYRINYFRLEDSKTANLESVEYDEDMDDSSSFLDRMSVVVPSDATSYVLSDLLPYSSYEITVAASTMDGYGPESSIRVVKTLEDVPSAPRNFNAELTSATSVKLTWDAPAAANGALLGYYVYLDRMVNGEPVVEKGSKKRIVMIRDSSKRYFELDSLDPNTEYSFRLNAFNRNGDGEFSERKSIITQGIPPEAPEIVSVSLDRDEPPVVARIEWKMPKMKPNETPIEKYNLWLRAQGYPDSYVKAKTVDGTDLSTTISGLWMGVVYDVLLAAENREGRSQNATETIATPVGSPDGEPIDVQYEVMKGKIVVSWRPPSEEKRNGNITSYKAILSAMDATADRYEQPVPAPSTSSTFEVNVRRAYLFKVAAATMKGIGPYSPVLTINPDPAALVGPPTNVRVEATSNSTAVVQWDFESQKADSFVVKYMHEPGNRMDTEKWKQLPVVSIDKENPKRFAVVSDLNAHKPYAFCVLAVKNNLTLNEQFNKVRVTNYMTNFQRQGPCSDPPTVLESVTPTYMVQNLRVLWKTSNSVQLTWEYNGPRNVGFYVNHTGRKDYVNHELQEKTMSTPGFGQDVDEKHREYLWTNLRPHMMYTIHVGVRTLPPGARKYWPQEVVTITDPTGPPFVDVPKLVDSSGTQPGQQMIRLTPATEEYGPISHYWIILVPANYSTEDVVNLDPIELEKATAEKRAQLARSLSVSPSKKLKRKASEVGDDSQSASYHPKEKRARRATVPGAYVTARLSADRVKQQYRNNQPFIVGDSQLYDGFTNYPLEHNLHYRLMMRAFAKNDVRTKDSFEQRAPMSEKLSRMYSDSVLTEPFTIKSALRGASQKSSPWVGACIAFLVLFSIVGMLICWWLRCNKKSAGRHPRHGSITKVALTGNIMNGGGGIPGETSKLLSTSNEYGRQIMNPYEQMNGNHHMESSMDLYPLPTSHSRSNGYAPVPVAIPSLPNNGNNMTTVSHPAVPIAELANHIERLRMNNNAGFQSEFESIETGQHFTWEHSSADMNKHKNRYANVAAYDHSRVVLSNVEGYPGMDYINANYVDGYDKPRSYIATQGPLPETFSDFWRMVWEEQSVTIVMLTNLEERSRVKCDQYWPSRGTATYGDIEVTLLESVHLAHYTMRTMRLKMVGEPEVREIKHLQYTAWPDHGVPDHPTPFLIFLKRVKTLNPNDAGPIISHCSAGIGRTGAFIVIDCMLERLRYDNTVDIYGCVTALRAQRSYMVQTEEQYIFIHDAVLDAVNSGSTEVPASRLHQHLHILSQPSADQLSGIDMEFRHLTTLKWTSNRCTVANLPVNRPKNRMLSAVPYDSNRVIMRLLPGADGSDYINASWIDGYKERGAYIATQAPTNETAADFWRAIWEHNSPIIAMLVRTNERGQEQCSDYWPLETGVQVGMLVVEPMAEYDMKHYHLREFRISDINTREVRTVRQFHFMEWPDVGKPHTADHFLDFVTQVHNTYAQFGCTGPITVHCCSGAGRTAVFIALSIILDRMRAEHVVDVFTTVKLLRTERQNMIQEPEQYHFLYLAAYEYLAAYDNFS | |
| 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 |
|---|---|---|---|---|---|
| 8 | N-linked_Glycosylation | MIQFRNKNNSMNRIA CCCCCCCCHHHHHHH | 49.73 | - | |
| 116 | N-linked_Glycosylation | ERVSLDDNATVVSCS EEEECCCCCEEEECC | 36.86 | - | |
| 269 | N-linked_Glycosylation | VGVGGNINLTCVAVG EEECCCEEEEEEEEC | 33.04 | - | |
| 315 | N-linked_Glycosylation | THVESTENFTCVAVS EEEEECCCEEEEEEE | 37.30 | - | |
| 574 | N-linked_Glycosylation | VGYTVRYNTSDGEKE CEEEEEEECCCCCEE | 23.65 | 17761667 | |
| 945 | N-linked_Glycosylation | NREGRSQNATETIAT CCCCCCCCCCEEEEC | 50.50 | - | |
| 988 | N-linked_Glycosylation | SEEKRNGNITSYKAI CHHHCCCCCCCHHHH | 37.60 | - | |
| 1069 | N-linked_Glycosylation | VRVEATSNSTAVVQW EEEEEECCCEEEEEE | 38.74 | - | |
| 1141 | N-linked_Glycosylation | CVLAVKNNLTLNEQF EEEEEECCCCHHHHH | 28.78 | - | |
| 1212 | N-linked_Glycosylation | RNVGFYVNHTGRKDY CEEEEEECCCCCCCC | 18.67 | 17761667 | |
| 1330 | N-linked_Glycosylation | WIILVPANYSTEDVV EEEEEECCCCCCCCC | 25.81 | - | |
| 1676 | Phosphorylation | MNKHKNRYANVAAYD CHHHCCCCCCEEEEC | 16.36 | 27067626 |
| 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 LAR_CAEEL !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LAR_CAEEL !! | ||||||
* 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 LAR_CAEEL !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditiselegans and suggests an atypical translocation mechanism for integralmembrane proteins."; Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,Taoka M., Takahashi N., Isobe T.; Mol. Cell. Proteomics 6:2100-2109(2007). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-574 AND ASN-1212, AND MASSSPECTROMETRY. | |