PTPRK_MOUSE - dbPTM
PTPRK_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
100N-linked_GlycosylationQLPTMKENDTHCIDF
CCCCCCCCCCEEEEH
54.70-
139N-linked_GlycosylationPLANPIWNVTGFTGR
CCCCCEEEECCCCCH
23.3819349973
210N-linked_GlycosylationVEVNAGQNATFQCIA
EEECCCCCCEEEEEE
39.78-
332PhosphorylationKEVEYRMTSGSWTET
EEEEEEECCCCCCEE
22.42-
333PhosphorylationEVEYRMTSGSWTETH
EEEEEECCCCCCEEE
22.83-
415N-linked_GlycosylationDWESLGYNITRCHTF
CHHHHCCEEEECEEE
27.6219349973
423N-linked_GlycosylationITRCHTFNVTICYHY
EEECEEEEEEEEEEH
31.04-
435N-linked_GlycosylationYHYFRGHNESRADCL
EEHHCCCCCCHHHHC
52.33-
461N-linked_GlycosylationNHLPPYTNVSLKMIL
HCCCCCCCEEEEEEE
18.6119349973
551N-linked_GlycosylationQTVSNLWNSTHHVFM
CCHHHHHHCCCEEEE
39.95-
585N-linked_GlycosylationFGPATAINVTTNISA
CCCCEEEEEECCCCC
23.71-
589N-linked_GlycosylationTAINVTTNISAPSLP
EEEEEECCCCCCCCC
19.49-
606N-linked_GlycosylationEGVDASLNETATTIT
CCCCCCCCCCCCEEE
41.92-
689N-linked_GlycosylationAPFTVGDNRTYKGFW
CCCCCCCCCCCCCCC
32.06-
790PhosphorylationRKDAMGNTRQEMTHM
HHHCCCCHHHHHHHH
28.1828059163
810PhosphorylationRSYADQSTLHAEDPL
CHHCCCCCCCCCCCC
19.5525338131
820PhosphorylationAEDPLSLTFMDQHNF
CCCCCCCEEECCCCC
17.3421082442
828PhosphorylationFMDQHNFSPRLPNDP
EECCCCCCCCCCCCC
17.9019060867
847PhosphorylationAVLDENHSATAESSR
EEECCCCCCCHHHHH
38.6125338131
861PhosphorylationRLLDVPRYLCEGTES
HHHCCCCHHCCCCCC
15.0525619855
866PhosphorylationPRYLCEGTESPYQTG
CCHHCCCCCCCCCCC
15.8225619855
868PhosphorylationYLCEGTESPYQTGQL
HHCCCCCCCCCCCCC
28.8427087446
870PhosphorylationCEGTESPYQTGQLHP
CCCCCCCCCCCCCCH
28.1725619855
872PhosphorylationGTESPYQTGQLHPAI
CCCCCCCCCCCCHHH
22.5027087446
893PhosphorylationQHINLMKTSDSYGFK
HHHHCCCCCCCCCCH
24.65-
928PhosphorylationQNRAKNRYGNIIAYD
HHHHHHCCCCEEEEC
24.7422499769
934PhosphorylationRYGNIIAYDHSRVIL
CCCCEEEECCCEEEE
12.0929514104
1080PhosphorylationYHATGLLSFIRRVKL
CCHHHHHHHHHHHCC
24.54-
1378UbiquitinationKLILQVEKWQEECEE
HHHHHHHHHHHHHHC
56.1522790023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PTPRK_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of PTPRK_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTPRK_MOUSE

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"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.

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