LIPA3_HUMAN - dbPTM
LIPA3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LIPA3_HUMAN
UniProt AC O75145
Protein Name Liprin-alpha-3
Gene Name PPFIA3
Organism Homo sapiens (Human).
Sequence Length 1194
Subcellular Localization Cytoplasm . Cytoplasmic vesicle, secretory vesicle, acrosome . Also detected in epididymosome.
Protein Description 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 MMCEVMPTISEDGRRGSALGPDEAGGELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSLPGSALELRYSQAPTLPSGAHLDPYVAGSGRAGKRGRWSGVKEEPSKDWERSAPAGSIPPPFPGELDGSDEEEAEGMFGAELLSPSGQADVQTLAIMLQEQLEAINKEIKLIQEEKETTEQRAEELESRVSSSGLDSLGRYRSSCSLPPSLTTSTLASPSPPSSGHSTPRLAPPSPAREGTDKANHVPKEEAGAPRGEGPAIPGDTPPPTPRSARLERMTQALALQAGSLEDGGPPRGSEGTPDSLHKAPKKKSIKSSIGRLFGKKEKGRMGPPGRDSSSLAGTPSDETLATDPLGLAKLTGPGDKDRRNKRKHELLEEACRQGLPFAAWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPASSRTSTGNVWMTHEEMESLTATTKPETKEISWEQILAYGDMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLKRLNYDRKDLERRREESQTQIRDVMVWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSNLISLGTDRRLDEDSAKSFSRSPSWRKMFREKDLRGVTPDSAEMLPPNFRSAAAGALGSPGLPLRKLQPEGQTSGSSRADGVSVRTYSC
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
17PhosphorylationSEDGRRGSALGPDEA
CCCCCCCCCCCCCCC
20.6430266825
55PhosphorylationEAQDGLATAQLRLRE
HHHHHHHHHHHHHHH
21.70-
75PhosphorylationDSLQRQLSIALPQEF
HHHHHHHHHHCHHHH
9.4722817900
130PhosphorylationLVSRHERSLRMTVVK
HHHHCHHHHHEEEEE
19.83-
142PhosphorylationVVKRQAQSPGGVSSE
EEEHHCCCCCCCCHH
28.6430576142
147PhosphorylationAQSPGGVSSEVEVLK
CCCCCCCCHHHHHHH
24.8527732954
148PhosphorylationQSPGGVSSEVEVLKA
CCCCCCCHHHHHHHH
43.1627732954
164UbiquitinationKSLFEHHKALDEKVR
HHHHHHHHHHHHHHH
53.1822505724
195PhosphorylationLELSNQETLNLREQL
HHHCCHHHHHHHHHH
15.9320886841
207PhosphorylationEQLSRRRSGLEEPGK
HHHHHHHCCCCCCCC
46.0130266825
220PhosphorylationGKDGDGQTLANGLGP
CCCCCCCCCCCCCCC
33.1130266825
231PhosphorylationGLGPGGDSNRRTAEL
CCCCCCCCCHHHHHH
35.2024719451
264PhosphorylationAVLCRQMSQLEEELG
HHHHHHHHHHHHHHH
24.23-
272PhosphorylationQLEEELGTAHRELGK
HHHHHHHHHHHHHHH
31.73-
286UbiquitinationKAEEANSKLQRDLKE
HHHHHHHHHHHHHHH
48.7424816145
292UbiquitinationSKLQRDLKEALAQRE
HHHHHHHHHHHHCCH
45.2724816145
340PhosphorylationLASKESLYRQSEEKS
HHCHHHHHHHCHHHH
18.8423403867
343PhosphorylationKESLYRQSEEKSRQL
HHHHHHHCHHHHHHH
38.4323403867
387UbiquitinationQRVAALNKAEERHGN
HHHHHHHHHHHHCCC
59.0124816145
409AcetylationLEAQLEEKNQELQRA
HHHHHHHHHHHHHHH
55.3326051181
431PhosphorylationDDHNKRLSETVDKLL
HHHHHHHHHHHHHHH
34.94-
439PhosphorylationETVDKLLSESNERLQ
HHHHHHHHHCHHHHH
49.7928348404
441PhosphorylationVDKLLSESNERLQLH
HHHHHHHCHHHHHHH
40.3828348404
450UbiquitinationERLQLHLKERMGALE
HHHHHHHHHHHHHHH
32.31-
505PhosphorylationRGRPPSSYSRSLPGS
CCCCCCCCCCCCCCC
16.67-
508PhosphorylationPPSSYSRSLPGSALE
CCCCCCCCCCCCCEE
32.7330266825
512PhosphorylationYSRSLPGSALELRYS
CCCCCCCCCEEEECC
27.9530266825
518PhosphorylationGSALELRYSQAPTLP
CCCEEEECCCCCCCC
20.1228796482
519PhosphorylationSALELRYSQAPTLPS
CCEEEECCCCCCCCC
17.2728796482
526PhosphorylationSQAPTLPSGAHLDPY
CCCCCCCCCCCCCCC
52.2928796482
533PhosphorylationSGAHLDPYVAGSGRA
CCCCCCCCCCCCCCC
11.5528796482
537PhosphorylationLDPYVAGSGRAGKRG
CCCCCCCCCCCCCCC
18.5028796482
639PhosphorylationEELESRVSSSGLDSL
HHHHHHHHHCCCHHH
20.0628555341
640PhosphorylationELESRVSSSGLDSLG
HHHHHHHHCCCHHHH
26.1029449344
641PhosphorylationLESRVSSSGLDSLGR
HHHHHHHCCCHHHHC
35.5529449344
645PhosphorylationVSSSGLDSLGRYRSS
HHHCCCHHHHCCCCC
37.4525849741
651PhosphorylationDSLGRYRSSCSLPPS
HHHHCCCCCCCCCCC
27.1127732954
652PhosphorylationSLGRYRSSCSLPPSL
HHHCCCCCCCCCCCC
9.9527732954
654PhosphorylationGRYRSSCSLPPSLTT
HCCCCCCCCCCCCCC
45.9527732954
658PhosphorylationSSCSLPPSLTTSTLA
CCCCCCCCCCCCCCC
36.0927732954
660PhosphorylationCSLPPSLTTSTLASP
CCCCCCCCCCCCCCC
24.0427732954
661PhosphorylationSLPPSLTTSTLASPS
CCCCCCCCCCCCCCC
25.6327732954
662PhosphorylationLPPSLTTSTLASPSP
CCCCCCCCCCCCCCC
19.0527732954
663PhosphorylationPPSLTTSTLASPSPP
CCCCCCCCCCCCCCC
25.0127732954
666PhosphorylationLTTSTLASPSPPSSG
CCCCCCCCCCCCCCC
29.0827732954
668PhosphorylationTSTLASPSPPSSGHS
CCCCCCCCCCCCCCC
47.1227732954
671PhosphorylationLASPSPPSSGHSTPR
CCCCCCCCCCCCCCC
52.9527732954
672PhosphorylationASPSPPSSGHSTPRL
CCCCCCCCCCCCCCC
46.4227732954
675PhosphorylationSPPSSGHSTPRLAPP
CCCCCCCCCCCCCCC
43.5627732954
676PhosphorylationPPSSGHSTPRLAPPS
CCCCCCCCCCCCCCC
13.5227732954
683PhosphorylationTPRLAPPSPAREGTD
CCCCCCCCCCCCCCC
30.0830266825
689PhosphorylationPSPAREGTDKANHVP
CCCCCCCCCCCCCCC
29.5823898821
697UbiquitinationDKANHVPKEEAGAPR
CCCCCCCHHHCCCCC
68.0724816145
714PhosphorylationGPAIPGDTPPPTPRS
CCCCCCCCCCCCCCH
43.5430266825
718PhosphorylationPGDTPPPTPRSARLE
CCCCCCCCCCHHHHH
36.7930266825
721PhosphorylationTPPPTPRSARLERMT
CCCCCCCHHHHHHHH
20.9526074081
728PhosphorylationSARLERMTQALALQA
HHHHHHHHHHHHHHH
19.5328258704
737PhosphorylationALALQAGSLEDGGPP
HHHHHHCCCCCCCCC
31.4428258704
762PhosphorylationHKAPKKKSIKSSIGR
CCCCCCCCHHHHHHH
44.0923909892
765PhosphorylationPKKKSIKSSIGRLFG
CCCCCHHHHHHHHHC
26.0521712546
766PhosphorylationKKKSIKSSIGRLFGK
CCCCHHHHHHHHHCC
24.8621712546
792PhosphorylationDSSSLAGTPSDETLA
CCCCCCCCCCCCCCC
17.6325332170
794PhosphorylationSSLAGTPSDETLATD
CCCCCCCCCCCCCCC
48.17-
807UbiquitinationTDPLGLAKLTGPGDK
CCCCCCHHHHCCCCH
52.1829967540
821UbiquitinationKDRRNKRKHELLEEA
HHHHHHHHHHHHHHH
42.94-
866UbiquitinationAACRANVKSGAIMAN
HHHHCCCCCCCEEEC
42.8730230243
989UbiquitinationRMLDHLNKKELRGQL
HHHHHCCHHHHHHHH
54.72-
1001PhosphorylationGQLKMVDSFHRVSLH
HHHCCHHCCHHHHHH
16.1328857561
1033O-linked_GlycosylationRRREESQTQIRDVMV
HHHHHHHHHHHHHHH
34.9330379171
1102UbiquitinationQARQLLEKEFSNLIS
HHHHHHHHHHHHHHH
65.1230230243
1105PhosphorylationQLLEKEFSNLISLGT
HHHHHHHHHHHHHCC
31.64-
1112PhosphorylationSNLISLGTDRRLDED
HHHHHHCCCCCCCHH
31.46-
1113UbiquitinationNLISLGTDRRLDEDS
HHHHHCCCCCCCHHH
31.7224816145
1122UbiquitinationRLDEDSAKSFSRSPS
CCCHHHHHHHCCCHH
56.8624816145
1123PhosphorylationLDEDSAKSFSRSPSW
CCHHHHHHHCCCHHH
28.3323312004
1125PhosphorylationEDSAKSFSRSPSWRK
HHHHHHHCCCHHHHH
38.6523312004
1127PhosphorylationSAKSFSRSPSWRKMF
HHHHHCCCHHHHHHH
23.3028555341
1129PhosphorylationKSFSRSPSWRKMFRE
HHHCCCHHHHHHHHH
40.5426074081
1143PhosphorylationEKDLRGVTPDSAEML
HHHHCCCCCCCHHHC
24.9727251275
1146PhosphorylationLRGVTPDSAEMLPPN
HCCCCCCCHHHCCCC
27.6027251275
1156PhosphorylationMLPPNFRSAAAGALG
HCCCCHHHHHCHHHC
20.3726074081
1162UbiquitinationRSAAAGALGSPGLPL
HHHHCHHHCCCCCCC
7.3524816145
1164PhosphorylationAAAGALGSPGLPLRK
HHCHHHCCCCCCCCC
19.3530266825
1171UbiquitinationSPGLPLRKLQPEGQT
CCCCCCCCCCCCCCC
60.1924816145

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 LIPA3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LIPA3_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 LIPA3_HUMAN !!

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

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LIPA3_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; SER-207; THR-714 ANDTHR-718, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-683; THR-714 ANDSER-1164, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17; THR-714 AND THR-718,AND MASS SPECTROMETRY.

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