| UniProt ID | PTPRK_MOUSE | |
|---|---|---|
| UniProt AC | P35822 | |
| Protein Name | Receptor-type tyrosine-protein phosphatase kappa | |
| Gene Name | Ptprk | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 1457 | |
| Subcellular Localization |
Membrane Single-pass type I membrane protein. |
|
| Protein Description | Regulation of processes involving cell contact and adhesion such as growth control, tumor invasion, and metastasis. Negative regulator of EGFR signaling pathway. Forms complexes with beta-catenin and gamma-catenin/plakoglobin. Beta-catenin may be a substrate for the catalytic activity of PTPRK/PTP-kappa.. | |
| Protein Sequence | MDVAAAALPAFVALWLLYPWPLLGSALGQFSAGGCTFDDGPGACDYHQDLYDDFEWVHVSAQEPHYLPPEMPQGSYMVVDSSNHDPGEKARLQLPTMKENDTHCIDFSYLLYSQKGLNPGTLNILVRVNKGPLANPIWNVTGFTGRDWLRAELAVSTFWPNEYQVIFEAEVSGGRSGYIAIDDIQVLSYPCDKSPHFLRLGDVEVNAGQNATFQCIATGRDAVHNKLWLQRRNGEDIPVAQTKNINHRRFAASFRLQEVTKTDQDLYRCVTQSERGSGVSNFAQLIVREPPRPIAPPQLLGVGPTYLLIQLNANSIIGDGPIILKEVEYRMTSGSWTETHAVNAPTYKLWHLDPDTEYEIRVLLTRPGEGGTGLPGPPLITRTKCAEPMRTPKTLKIAEIQARRIAVDWESLGYNITRCHTFNVTICYHYFRGHNESRADCLDMDPKAPQHVVNHLPPYTNVSLKMILTNPEGRKESEETIIQTDEDVPGPVPVKSLQGTSFENKIFLNWKEPLEPNGIITQYEVSYSSIRSFDPAVPVAGPPQTVSNLWNSTHHVFMHLHPGTTYQFFIRASTVKGFGPATAINVTTNISAPSLPDYEGVDASLNETATTITVLLRPAQAKGAPISAYQIVVEQLHPHRTKREAGAMECYQVPVTYQNALSGGAPYYFAAELPPGNLPEPAPFTVGDNRTYKGFWNPPLAPRKGYNIYFQAMSSVEKETKTQCVRIATKAAATEEPEVIPDPAKQTDRVVKIAGISAGILVFILLLLVVIVIVKKSKLAKKRKDAMGNTRQEMTHMVNAMDRSYADQSTLHAEDPLSLTFMDQHNFSPRLPNDPLVPTAVLDENHSATAESSRLLDVPRYLCEGTESPYQTGQLHPAIRVADLLQHINLMKTSDSYGFKEEYESFFEGQSASWDVAKKDQNRAKNRYGNIIAYDHSRVILQPVEDDPSSDYINANYIDIWLYRDGYQRPSHYIATQGPVHETVYDFWRMVWQEQSACIVMVTNLVEVGRVKCYKYWPDDTEVYGDFKVTCVEMEPLAEYVVRTFTLERRGYNEIREVKQFHFTGWPDHGVPYHATGLLSFIRRVKLSNPPSAGPIVVHCSAGAGRTGCYIVIDIMLDMAEREGVVDIYNCVKALRSRRINMVQTEEQYIFIHDAILEACLCGETAIPVCEFKAAYFDMIRIDSQTNSSHLKDEFQTLNSVTPRLQAEDCSIACLPRNHDKNRFMDMLPPDRCLPFLITIDGESSNYINAALMDSYRQPAAFIVTQYPLPNTVKDFWRLVYDYGCTSIVMLNEVDLSQGCPQYWPEEGMLRYGPIQVECMSCSMDCDVINRIFRICNLTRPQEGYLMVQQFQYLGWASHREVPGSKRSFLKLILQVEKWQEECEEGEGRTIIHCLNGGGRSGMFCAIGIVVEMVKRQNVVDVFHAVKTLRNSKPNMVEAPEQYRFCYDVALEYLESS | |
| 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 |
|---|---|---|---|---|---|
| 100 | N-linked_Glycosylation | QLPTMKENDTHCIDF CCCCCCCCCCEEEEH | 54.70 | - | |
| 139 | N-linked_Glycosylation | PLANPIWNVTGFTGR CCCCCEEEECCCCCH | 23.38 | 19349973 | |
| 210 | N-linked_Glycosylation | VEVNAGQNATFQCIA EEECCCCCCEEEEEE | 39.78 | - | |
| 332 | Phosphorylation | KEVEYRMTSGSWTET EEEEEEECCCCCCEE | 22.42 | - | |
| 333 | Phosphorylation | EVEYRMTSGSWTETH EEEEEECCCCCCEEE | 22.83 | - | |
| 415 | N-linked_Glycosylation | DWESLGYNITRCHTF CHHHHCCEEEECEEE | 27.62 | 19349973 | |
| 423 | N-linked_Glycosylation | ITRCHTFNVTICYHY EEECEEEEEEEEEEH | 31.04 | - | |
| 435 | N-linked_Glycosylation | YHYFRGHNESRADCL EEHHCCCCCCHHHHC | 52.33 | - | |
| 461 | N-linked_Glycosylation | NHLPPYTNVSLKMIL HCCCCCCCEEEEEEE | 18.61 | 19349973 | |
| 551 | N-linked_Glycosylation | QTVSNLWNSTHHVFM CCHHHHHHCCCEEEE | 39.95 | - | |
| 585 | N-linked_Glycosylation | FGPATAINVTTNISA CCCCEEEEEECCCCC | 23.71 | - | |
| 589 | N-linked_Glycosylation | TAINVTTNISAPSLP EEEEEECCCCCCCCC | 19.49 | - | |
| 606 | N-linked_Glycosylation | EGVDASLNETATTIT CCCCCCCCCCCCEEE | 41.92 | - | |
| 689 | N-linked_Glycosylation | APFTVGDNRTYKGFW CCCCCCCCCCCCCCC | 32.06 | - | |
| 790 | Phosphorylation | RKDAMGNTRQEMTHM HHHCCCCHHHHHHHH | 28.18 | 28059163 | |
| 810 | Phosphorylation | RSYADQSTLHAEDPL CHHCCCCCCCCCCCC | 19.55 | 25338131 | |
| 820 | Phosphorylation | AEDPLSLTFMDQHNF CCCCCCCEEECCCCC | 17.34 | 21082442 | |
| 828 | Phosphorylation | FMDQHNFSPRLPNDP EECCCCCCCCCCCCC | 17.90 | 19060867 | |
| 847 | Phosphorylation | AVLDENHSATAESSR EEECCCCCCCHHHHH | 38.61 | 25338131 | |
| 861 | Phosphorylation | RLLDVPRYLCEGTES HHHCCCCHHCCCCCC | 15.05 | 25619855 | |
| 866 | Phosphorylation | PRYLCEGTESPYQTG CCHHCCCCCCCCCCC | 15.82 | 25619855 | |
| 868 | Phosphorylation | YLCEGTESPYQTGQL HHCCCCCCCCCCCCC | 28.84 | 27087446 | |
| 870 | Phosphorylation | CEGTESPYQTGQLHP CCCCCCCCCCCCCCH | 28.17 | 25619855 | |
| 872 | Phosphorylation | GTESPYQTGQLHPAI CCCCCCCCCCCCHHH | 22.50 | 27087446 | |
| 893 | Phosphorylation | QHINLMKTSDSYGFK HHHHCCCCCCCCCCH | 24.65 | - | |
| 928 | Phosphorylation | QNRAKNRYGNIIAYD HHHHHHCCCCEEEEC | 24.74 | 22499769 | |
| 934 | Phosphorylation | RYGNIIAYDHSRVIL CCCCEEEECCCEEEE | 12.09 | 29514104 | |
| 1080 | Phosphorylation | YHATGLLSFIRRVKL CCHHHHHHHHHHHCC | 24.54 | - | |
| 1378 | Ubiquitination | KLILQVEKWQEECEE HHHHHHHHHHHHHHC | 56.15 | 22790023 |
| 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 PTPRK_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTPRK_MOUSE !! | ||||||
* 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 PTPRK_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of PTPRK_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| N-linked Glycosylation | |
| Reference | PubMed |
| "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139; ASN-415 AND ASN-461,AND MASS SPECTROMETRY. | |