UniProt ID | PTPRF_MOUSE | |
---|---|---|
UniProt AC | A2A8L5 | |
Protein Name | Receptor-type tyrosine-protein phosphatase F | |
Gene Name | Ptprf | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 1898 | |
Subcellular Localization |
Membrane Single-pass membrane protein . |
|
Protein Description | Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity (By similarity).. | |
Protein Sequence | MAPEPAPGRRMVPLVPALVMLGLMAGAHGDSKPVFVKVPEDQTGLSGGVASFVCQATGEPKPRITWMKKGKKVSSQRFEVIEFDDGAGSVLRIQPLRVQRDEAIYECTATNSLGEINTSAKLSVLEEDQLPSGFPTIDMGPQLKVVEKGRTATMLCAAGGNPDPEISWFKDFLPVDPAASNGRIKQLRSGALQIESSEESDQGKYECVATNSAGTRYSAPANLYVRVRRVAPRFSIPPSSQEVMPGGSVNLTCVAVGAPMPYVKWMMGAEELTKEDEMPVGRNVLELSNVMRSANYTCVAISSLGMIEATAQVTVKALPKPPIDLVVTETTATSVTLTWDSGNTEPVSFYGIQYRAAGTDGPFQEVDGVASTRYSIGGLSPFSEYAFRVLAVNSIGRGPPSEAVRARTGEQAPSSPPRRVQARMLSASTMLVQWEPPEEPNGLVRGYRVYYTPDSRRPLSAWHKHNTDAGLLTTVGSLLPGITYSLRVLAFTAVGDGPPSPTIQVKTQQGVPAQPADFQANAESDTRIQLSWLLPPQERIVKYELVYWAAEDEGQQHKVTFDPTSSYTLEDLKPDTLYHFQLAARSDLGVGVFTPTVEARTAQSTPSAPPQKVTCVSTGSTTVRVSWVPPPADSRNGIITQYSVAYEAVDGEDRKRHVVDGISREHSSWDLLGLEKWTEYRVWVRAHTDVGPGPESSPVLVRTDEDVPSGPPRKVEVEPLNSTAVHVSWKLPVPNKQHGQIRGYQVTYVRLENGEPRGQPIIQDVMLAEAQETTISGLTPETTYSITVAAYTTKGDGARSKPKVVTTTGAVPGRPTMMVSTTAMHTALLQWHPPKELPGELLGYRLQYRRADEARPNTIDFGKDDQHFTVTGLHKGATYVFRLAAKNRAGPGEEFEKEITTPEDVPSGFPQNLRVTGLTTSTTELTWDPPVLAERNGHITNYTVVYRDINSQLELQNVTNDTHLTLLGLKPDTTYDIKVRAHTSKGAGPLSPSIQSRTMPVEQVFAKNFRVAAAMKTSVLLSWEVPDSYKSAVPFKILYNGQSVEVDGHSMRKLIADLQPNTEYSFVLMNRGSSAGGLQHLVSIRTAPDLLPQKPLPASAFIEDGRFSLSMPQVQDPSLVRWFYIVVVPIDRVGGNLLAPRWNTPEELELDELLEAIEQGEEKQRRRRRQAERLKPYVAAQVDVLPDTFTLGDKKSYRGFYNRPLSPDLSYQCFVLASLKEPMDQKRYASSPYSDEIVVQVTPAQQQEEPEMLWVTGPVLAVILIILIVIAILLFKRKRTHSPSSKDEQSIGLKDSLLAHSSDPVEMRRLNYQTPGMRDHPPIPITDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNSEVNKPKNRYANVIAYDHSRVLLTSIDGVPGSDYINANYIDGYRKQNAYIATQGPLPETMGDFWRMVWEQRTATVVMMTRLEEKSRVKCDQYWPVRGTETYGLIQVTLVDTVELATYTMRTFALHKSGSSEKRELRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPLDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYVFIHEALLEAAMCGHTEVLARNLYAHIQKLGQVPPGESVTAMELEFKLLANSKAHTSRFVSANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFLDGYRQQKAYIATQGPLAESTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSFDHYAT | |
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 |
---|---|---|---|---|---|
117 | N-linked_Glycosylation | TNSLGEINTSAKLSV CCCCCCCCCCCEEEE | 24.55 | - | |
218 | Phosphorylation | NSAGTRYSAPANLYV CCCCCCEECCCEEEE | 25.20 | 28059163 | |
250 | N-linked_Glycosylation | VMPGGSVNLTCVAVG CCCCCCEEEEEEEEC | 31.18 | - | |
295 | N-linked_Glycosylation | SNVMRSANYTCVAIS HHHHHHCCCEEEEEE | 33.61 | - | |
298 | S-palmitoylation | MRSANYTCVAISSLG HHHCCCEEEEEECCC | 1.06 | 26165157 | |
721 | N-linked_Glycosylation | KVEVEPLNSTAVHVS EEEEEECCCCEEEEE | 48.29 | 19349973 | |
879 | Phosphorylation | GLHKGATYVFRLAAK EECCCCEEEEHHHHC | 9.32 | 22817900 | |
900 | Phosphorylation | EEFEKEITTPEDVPS HHHHCCCCCCCCCCC | 37.07 | 28576409 | |
901 | Phosphorylation | EFEKEITTPEDVPSG HHHCCCCCCCCCCCC | 30.27 | 28576409 | |
936 | N-linked_Glycosylation | PPVLAERNGHITNYT CCCHHHCCCEECEEE | 37.59 | 19349973 | |
941 | N-linked_Glycosylation | ERNGHITNYTVVYRD HCCCEECEEEEEEEC | 29.85 | 19349973 | |
957 | N-linked_Glycosylation | NSQLELQNVTNDTHL CCCEEEEECCCCCEE | 56.03 | - | |
960 | N-linked_Glycosylation | LELQNVTNDTHLTLL EEEEECCCCCEEEEE | 48.15 | 19349973 | |
1290 | Phosphorylation | PSSKDEQSIGLKDSL CCCCCHHCCCCCHHH | 19.31 | 27841257 | |
1294 | Ubiquitination | DEQSIGLKDSLLAHS CHHCCCCCHHHHHCC | 39.81 | 22790023 | |
1296 | Phosphorylation | QSIGLKDSLLAHSSD HCCCCCHHHHHCCCC | 24.56 | 19060867 | |
1301 | Phosphorylation | KDSLLAHSSDPVEMR CHHHHHCCCCHHHHH | 30.72 | 22817900 | |
1302 | Phosphorylation | DSLLAHSSDPVEMRR HHHHHCCCCHHHHHH | 35.75 | 22324799 | |
1312 | Phosphorylation | VEMRRLNYQTPGMRD HHHHHCCCCCCCCCC | 20.53 | 29514104 | |
1342 | Ubiquitination | LKANDGLKFSQEYES HHHCCCCCCCCEECC | 48.80 | 22790023 | |
1367 | Ubiquitination | NSNSEVNKPKNRYAN CCCCCCCCCCCCCCE | 63.65 | 22790023 | |
1372 | Phosphorylation | VNKPKNRYANVIAYD CCCCCCCCCEEEEEC | 16.36 | 29899451 | |
1723 | Phosphorylation | RMLWEHNSTIIVMLT HHHHHCCCEEEEEHH | 23.92 | 28576409 | |
1724 | Phosphorylation | MLWEHNSTIIVMLTK HHHHCCCEEEEEHHH | 21.75 | 28576409 | |
1730 | Phosphorylation | STIIVMLTKLREMGR CEEEEEHHHHHHHCH | 15.22 | 28576409 | |
1801 | Ubiquitination | WPEQGVPKTGEGFID CCCCCCCCCCCCHHH | 67.75 | - | |
1852 | Phosphorylation | IVLERMRYEGVVDMF HHHHHHCCCCHHHHH | 14.00 | 28059163 |
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 PTPRF_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PTPRF_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 PTPRF_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CTNB1_MOUSE | Ctnnb1 | physical | 8830779 | |
FYN_MOUSE | Fyn | physical | 18854310 |
Kegg Drug | ||||||
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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-721; ASN-936; ASN-941 ANDASN-960, AND MASS SPECTROMETRY. |