LIPA2_HUMAN - dbPTM
LIPA2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIPA2_HUMAN
UniProt AC O75334
Protein Name Liprin-alpha-2
Gene Name PPFIA2
Organism Homo sapiens (Human).
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..
Protein Sequence MMCEVMPTINEDTPMSQRGSQSSGSDSDSHFEQLMVNMLDERDRLLDTLRETQESLSLAQQRLQDVIYDRDSLQRQLNSALPQDIESLTGGLAGSKGADPPEFAALTKELNACREQLLEKEEEISELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPSGVSSEVEVLKALKSLFEHHKALDEKVRERLRVSLERVSALEEELAAANQEIVALREQNVHIQRKMASSEGSTESEHLEGMEPGQKVHEKRLSNGSIDSTDETSQIVELQELLEKQNYEMAQMKERLAALSSRVGEVEQEAETARKDLIKTEEMNTKYQRDIREAMAQKEDMEERITTLEKRYLSAQRESTSIHDMNDKLENELANKEAILRQMEEKNRQLQERLELAEQKLQQTMRKAETLPEVEAELAQRIAALTKAEERHGNIEERMRHLEGQLEEKNQELQRARQREKMNEEHNKRLSDTVDRLLTESNERLQLHLKERMAALEEKNVLIQESETFRKNLEESLHDKERLAEEIEKLRSELDQLKMRTGSLIEPTIPRTHLDTSAELRYSVGSLVDSQSDYRTTKVIRRPRRGRMGVRRDEPKVKSLGDHEWNRTQQIGVLSSHPFESDTEMSDIDDDDRETIFSSMDLLSPSGHSDAQTLAMMLQEQLDAINKEIRLIQEEKESTELRAEEIENRVASVSLEGLNLARVHPGTSITASVTASSLASSSPPSGHSTPKLTPRSPAREMDRMGVMTLPSDLRKHRRKIAVVEEDGREDKATIKCETSPPPTPRALRMTHTLPSSYHNDARSSLSVSLEPESLGLGSANSSQDSLHKAPKKKGIKSSIGRLFGKKEKARLGQLRGFMETEAAAQESLGLGKLGTQAEKDRRLKKKHELLEEARRKGLPFAQWDGPTVVAWLELWLGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPPTSRTPSGNVWVTHEEMENLAAPAKTKESEEGSWAQCPVFLQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRVHLKMVDSFHRTSLQYGIMCLKRLNYDRKELERRREASQHEIKDVLVWSNDRVIRWIQAIGLREYANNILESGVHGSLIALDENFDYSSLALLLQIPTQNTQARQILEREYNNLLALGTERRLDESDDKNFRRGSTWRRQFPPREVHGISMMPGSSETLPAGFRLTTTSGQSRKMTTDVASSRLQRLDNSTVRTYSC
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
79 (in isoform 2)Phosphorylation-39.5130631047
79PhosphorylationSLQRQLNSALPQDIE
HHHHHHHHCCCHHHH
39.5128122231
87PhosphorylationALPQDIESLTGGLAG
CCCHHHHHHHCCCCC
31.4028122231
89PhosphorylationPQDIESLTGGLAGSK
CHHHHHHHCCCCCCC
38.1828122231
95PhosphorylationLTGGLAGSKGADPPE
HHCCCCCCCCCCCHH
23.4728122231
151PhosphorylationLVSRHERSLRMTVVK
HHHHCHHHHHEEEEE
19.83-
163PhosphorylationVVKRQAQSPSGVSSE
EEEHHCCCCCCCCHH
24.8524076635
165PhosphorylationKRQAQSPSGVSSEVE
EHHCCCCCCCCHHHH
58.0124076635
168PhosphorylationAQSPSGVSSEVEVLK
CCCCCCCCHHHHHHH
25.06-
198PhosphorylationVRERLRVSLERVSAL
HHHHHHHHHHHHHHH
20.3424719451
229UbiquitinationQNVHIQRKMASSEGS
CCHHHHHHHHCCCCC
23.5721906983
233PhosphorylationIQRKMASSEGSTESE
HHHHHHCCCCCCCHH
36.1226434552
236PhosphorylationKMASSEGSTESEHLE
HHHCCCCCCCHHHHC
25.58-
237PhosphorylationMASSEGSTESEHLEG
HHCCCCCCCHHHHCC
55.15-
239PhosphorylationSSEGSTESEHLEGME
CCCCCCCHHHHCCCC
30.3326434552
257PhosphorylationKVHEKRLSNGSIDST
CCCHHHCCCCCCCCC
43.0829514088
260PhosphorylationEKRLSNGSIDSTDET
HHHCCCCCCCCCCHH
27.7223403867
263PhosphorylationLSNGSIDSTDETSQI
CCCCCCCCCCHHHHH
35.7729514088
264PhosphorylationSNGSIDSTDETSQIV
CCCCCCCCCHHHHHH
33.8229514088
267PhosphorylationSIDSTDETSQIVELQ
CCCCCCHHHHHHHHH
28.8329514088
268PhosphorylationIDSTDETSQIVELQE
CCCCCHHHHHHHHHH
18.8329514088
315O-linked_GlycosylationARKDLIKTEEMNTKY
HHHHHHHHHHHHHHH
30.1330379171
347PhosphorylationITTLEKRYLSAQRES
HHHHHHHHHHHHHHC
18.9723663014
349PhosphorylationTLEKRYLSAQRESTS
HHHHHHHHHHHHCCC
17.2723663014
354PhosphorylationYLSAQRESTSIHDMN
HHHHHHHCCCHHHCC
29.6423663014
355PhosphorylationLSAQRESTSIHDMND
HHHHHHCCCHHHCCH
27.2623663014
356PhosphorylationSAQRESTSIHDMNDK
HHHHHCCCHHHCCHH
27.4923663014
405PhosphorylationQTMRKAETLPEVEAE
HHHHHHCCHHHHHHH
53.0930624053
468PhosphorylationHNKRLSDTVDRLLTE
HHHHHHHHHHHHHHH
22.41-
474PhosphorylationDTVDRLLTESNERLQ
HHHHHHHHHCHHHHH
41.79-
476PhosphorylationVDRLLTESNERLQLH
HHHHHHHCHHHHHHH
38.46-
485UbiquitinationERLQLHLKERMAALE
HHHHHHHHHHHHHHH
32.31-
536PhosphorylationLDQLKMRTGSLIEPT
HHHHHHHHCCCCCCC
27.8528857561
538PhosphorylationQLKMRTGSLIEPTIP
HHHHHHCCCCCCCCC
26.0928857561
558PhosphorylationTSAELRYSVGSLVDS
CCCHHHHHHHHHCCC
17.3627499020
594PhosphorylationRDEPKVKSLGDHEWN
CCCCCCCCCCCCCCC
40.3427251275
687PhosphorylationEIENRVASVSLEGLN
HHHHHHHHEEECCCC
14.9127499020
689PhosphorylationENRVASVSLEGLNLA
HHHHHHEEECCCCCC
20.4328348404
712PhosphorylationTASVTASSLASSSPP
EEEEEHHHHHCCCCC
26.03-
715PhosphorylationVTASSLASSSPPSGH
EEHHHHHCCCCCCCC
36.32-
728PhosphorylationGHSTPKLTPRSPARE
CCCCCCCCCCCCCCC
23.84-
743PhosphorylationMDRMGVMTLPSDLRK
CHHCCCCCCCHHHHH
32.8627732954
746PhosphorylationMGVMTLPSDLRKHRR
CCCCCCCHHHHHHCC
53.0027732954
773PhosphorylationKATIKCETSPPPTPR
CCEEEECCCCCCCCC
56.8823403867
774PhosphorylationATIKCETSPPPTPRA
CEEEECCCCCCCCCH
17.0823403867
817PhosphorylationGLGSANSSQDSLHKA
CCCCCCCCHHHHHCC
37.50-
820PhosphorylationSANSSQDSLHKAPKK
CCCCCHHHHHCCCHH
25.4124076635
828AcetylationLHKAPKKKGIKSSIG
HHCCCHHHCCCHHHH
72.50130207
831AcetylationAPKKKGIKSSIGRLF
CCHHHCCCHHHHHHH
46.98130203
832PhosphorylationPKKKGIKSSIGRLFG
CHHHCCCHHHHHHHC
25.8521712546
833PhosphorylationKKKGIKSSIGRLFGK
HHHCCCHHHHHHHCH
24.8621712546
855PhosphorylationQLRGFMETEAAAQES
HHHHHHHHHHHHHHH
21.09-
891 (in isoform 5)Phosphorylation-60.2827762562
901 (in isoform 5)Phosphorylation-21.3927762562
935PhosphorylationGAIMSALSDTEIQRE
CCHHHHCCCHHHHHH
42.05-
965 (in isoform 4)Phosphorylation-30.9627762562
966PhosphorylationQEMVSLTSPSAPPTS
HHHHHCCCCCCCCCC
23.3525307156
972PhosphorylationTSPSAPPTSRTPSGN
CCCCCCCCCCCCCCC
29.76-
975PhosphorylationSAPPTSRTPSGNVWV
CCCCCCCCCCCCEEE
22.90-
1068PhosphorylationVHLKMVDSFHRTSLQ
HHHHHHHCCHHHHHH
16.1328857561
1098PhosphorylationLERRREASQHEIKDV
HHHHHHHHHHHHHHH
27.58-
1179PhosphorylationNNLLALGTERRLDES
HHHHHHCCCCCCCCC
27.4624719451
1215PhosphorylationGISMMPGSSETLPAG
EEEECCCCCCCCCCC
21.09-
1218PhosphorylationMMPGSSETLPAGFRL
ECCCCCCCCCCCEEE
39.73-
1227PhosphorylationPAGFRLTTTSGQSRK
CCCEEEECCCCCCCC
24.45-
1237PhosphorylationGQSRKMTTDVASSRL
CCCCCCCCHHHHHHH
25.61-

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_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIPA2_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GIT1_HUMANGIT1physical
12923177
ERC2_HUMANERC2physical
12923177
LIPA1_HUMANPPFIA1physical
9624153
LIPA2_HUMANPPFIA2physical
9624153
LIPA3_HUMANPPFIA3physical
9624153
LIPB1_HUMANPPFIBP1physical
9624153

Drug and Disease Associations
Kegg Disease
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIPA2_HUMAN

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Related Literatures of Post-Translational Modification

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