LIPA2_MOUSE - dbPTM
LIPA2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIPA2_MOUSE
UniProt AC Q8BSS9
Protein Name Liprin-alpha-2
Gene Name Ppfia2
Organism Mus musculus (Mouse).
Sequence Length 1257
Subcellular Localization Cytoplasm. Cell surface. Colocalizes with PTPRF at the cell surface..
Protein Description Alters PTPRF cellular localization and induces PTPRF clustering. May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates (By similarity)..
Protein Sequence MMCEVMPTINEDTPMSQRGSQSSGSDSDSHFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGGLTGSKGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMVSSEGSTESEHLEGMEAGQKVHEKRLSNGSIDSTDDTSQIVELQELLEKQNYEMAQMKERLTALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESENFRKNLEESLHDKVSLAEEIEKLRSELDQMKMRTGSLIEPTISRTHIDTSTELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLGSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNLARVHPGTSITASVTASSLASSSPPSGHSTPKLTPRSPAREMDRMGVMTLPSDLRKHRRKIAVVEEDGREDKATIKCETSPPPTPRAVRMTHTLPSSYHNDARSSLSASLEPDSLGLGSANSSQDSLHKAPKKKGIKSSIGRLFGKKEKARLGQLRGFMETEAAAQESLGLGKLGTQAEKDRRLKKKHELLEEARRKGLPFAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPPTSRTPSGNVWVTHEEMENLTAPAKTKESEEGSWAQCPVFLQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELERRREASQHEIKDVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLLALGTERRLDESDDKNFRRGSTWRRQFPPREVHGISMMPGSSETLPAGFRLTTTSGQSRKMTTDVASSRLQRLDNSTVRTYSC
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
155PhosphorylationHERSLRMTVVKRQAQ
CHHHHHEEEEEHHCC		18.73-
163PhosphorylationVVKRQAQSPSGVSSE
EEEHHCCCCCCCCHH		24.8525521595
165PhosphorylationKRQAQSPSGVSSEVE
EHHCCCCCCCCHHHH		58.0122324799
168PhosphorylationAQSPSGVSSEVEVLK
CCCCCCCCHHHHHHH		25.0620415495
169PhosphorylationQSPSGVSSEVEVLKA
CCCCCCCHHHHHHHH		43.1620415495
232PhosphorylationHIQRKMVSSEGSTES
HHHHHHCCCCCCCHH		21.1229899451
233PhosphorylationIQRKMVSSEGSTESE
HHHHHCCCCCCCHHH		34.2721183079
236PhosphorylationKMVSSEGSTESEHLE
HHCCCCCCCHHHHHC		25.5819060867
237PhosphorylationMVSSEGSTESEHLEG
HCCCCCCCHHHHHCH		55.1525521595
239PhosphorylationSSEGSTESEHLEGME
CCCCCCHHHHHCHHH		30.3325521595
257PhosphorylationKVHEKRLSNGSIDST
HHHHHHCCCCCCCCC		43.0819060867
260PhosphorylationEKRLSNGSIDSTDDT
HHHCCCCCCCCCCCH		27.7219060867
263PhosphorylationLSNGSIDSTDDTSQI
CCCCCCCCCCCHHHH		31.8719060867
264PhosphorylationSNGSIDSTDDTSQIV
CCCCCCCCCCHHHHH		33.8619060867
267PhosphorylationSIDSTDDTSQIVELQ
CCCCCCCHHHHHHHH		25.9119060867
268PhosphorylationIDSTDDTSQIVELQE
CCCCCCHHHHHHHHH		25.5519060867
466PhosphorylationEEHNKRLSDTVDRLL
HHHHHHHHHHHHHHH		34.9629899451
485UbiquitinationERLQLHLKERMAALE
HHHHHHHHHHHHHHH		32.31-
536PhosphorylationLDQMKMRTGSLIEPT
HHHHHHHHCCCCCCC		27.8528066266
538PhosphorylationQMKMRTGSLIEPTIS
HHHHHHCCCCCCCCC		26.0919060867
545PhosphorylationSLIEPTISRTHIDTS
CCCCCCCCCCCCCCC		33.34-
545O-linked_GlycosylationSLIEPTISRTHIDTS
CCCCCCCCCCCCCCC		33.3455412463
552PhosphorylationSRTHIDTSTELRYSV
CCCCCCCCCCCEEEH		19.0129899451
558O-linked_GlycosylationTSTELRYSVGSLVDS
CCCCCEEEHHHHCCC		17.364099243
558PhosphorylationTSTELRYSVGSLVDS
CCCCCEEEHHHHCCC		17.3618056256
594PhosphorylationRDEPKVKSLGDHEWN
CCCCCCCCCCCCCCC		40.3428066266
673PhosphorylationLIQEEKESTELRAEE
HHHHHHHCCHHHHHH		37.9428066266
674PhosphorylationIQEEKESTELRAEEI
HHHHHHCCHHHHHHH		39.8828066266
687PhosphorylationEIENRVASVSLEGLN
HHHHHHHHEEECCCC		14.9122324799
689PhosphorylationENRVASVSLEGLNLA
HHHHHHEEECCCCCC		20.4325521595
712PhosphorylationTASVTASSLASSSPP
EEEEEHHHHHCCCCC		26.03-
716PhosphorylationTASSLASSSPPSGHS
EHHHHHCCCCCCCCC		41.0621183079
717PhosphorylationASSLASSSPPSGHST
HHHHHCCCCCCCCCC		38.0319060867
720PhosphorylationLASSSPPSGHSTPKL
HHCCCCCCCCCCCCC		53.1519060867
723PhosphorylationSSPPSGHSTPKLTPR
CCCCCCCCCCCCCCC		50.3521183079
724PhosphorylationSPPSGHSTPKLTPRS
CCCCCCCCCCCCCCC		20.8319060867
728PhosphorylationGHSTPKLTPRSPARE
CCCCCCCCCCCCCCC		23.8429899451
731PhosphorylationTPKLTPRSPAREMDR
CCCCCCCCCCCCCHH		24.9029899451
768PhosphorylationDGREDKATIKCETSP
CCCCCCCEEEECCCC		27.0616452087
773PhosphorylationKATIKCETSPPPTPR
CCEEEECCCCCCCCC		56.8825521595
774PhosphorylationATIKCETSPPPTPRA
CEEEECCCCCCCCCC		17.0825521595
778PhosphorylationCETSPPPTPRAVRMT
ECCCCCCCCCCEEEE		31.0522324799
787PhosphorylationRAVRMTHTLPSSYHN
CCEEEEEECCCCCCC		31.06-
813PhosphorylationPDSLGLGSANSSQDS
CCCCCCCCCCCCHHH		29.3529899451
816PhosphorylationLGLGSANSSQDSLHK
CCCCCCCCCHHHHHC		29.1519060867
817PhosphorylationGLGSANSSQDSLHKA
CCCCCCCCHHHHHCC		37.5019060867
820PhosphorylationSANSSQDSLHKAPKK
CCCCCHHHHHCCCHH		25.4119060867
862PhosphorylationTEAAAQESLGLGKLG
HHHHHHHHCCCCHHH		18.6923737553
965PhosphorylationIQEMVSLTSPSAPPT
HHHHHHCCCCCCCCC		30.9620415495
966PhosphorylationQEMVSLTSPSAPPTS
HHHHHCCCCCCCCCC		23.3523527152
968PhosphorylationMVSLTSPSAPPTSRT
HHHCCCCCCCCCCCC		53.8520415495
1086PhosphorylationMCLKRLNYDRKELER
HHHHHCCCCHHHHHH		23.01-
1216PhosphorylationISMMPGSSETLPAGF
EEECCCCCCCCCCCE		40.28-
1218PhosphorylationMMPGSSETLPAGFRL
ECCCCCCCCCCCEEE		39.73-
1228PhosphorylationAGFRLTTTSGQSRKM
CCEEEECCCCCCCCC		26.1428066266
1229PhosphorylationGFRLTTTSGQSRKMT
CEEEECCCCCCCCCC		32.5128066266
1232PhosphorylationLTTTSGQSRKMTTDV
EECCCCCCCCCCCHH		37.0829899451
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 LIPA2_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIPA2_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 LIPA2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LIPA2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIPA2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538 AND SER-689, ANDMASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774, AND MASSSPECTROMETRY.

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