LPP_MOUSE - dbPTM
LPP_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LPP_MOUSE
UniProt AC Q8BFW7
Protein Name Lipoma-preferred partner homolog
Gene Name Lpp
Organism Mus musculus (Mouse).
Sequence Length 613
Subcellular Localization Nucleus. Cytoplasm. Cell junction. Found in the nucleus, in the cytoplasm and at cell adhesion sites..
Protein Description May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus (By similarity)..
Protein Sequence MSHPSWLPPKSTGEPLGHVPARMETTHSFGNPSISVSTQQPPKKYAPVVAPKPKYNPYKQPGGEGDLLPPPPPPLEDPGTIPPGPGHFPPPPPLDEGAFKVQQGNPGGKTLEERRSSLDAEIDSLTSILADLECSSPYKPRPPQGSASSIASPPVSTPVTGHKRMVIPQQPPLTATKKSATKPQPAPQAAPIPVTPIGTLKPQPQPVPASYTTASTSSRPTFNVQVKSAQPSPHYMAGPSSGQIYGPGPRGYNNQPVPVSGQCPPPPTCVGTDYAYIPPSGHPPESGYGYTSNQGRYYEPYYAAGPSYGGRSEGDTAYGQQVQPNTWKREAAYAPPASGNQNHPGMYPVSGPKKTYITDPVSAPCAPPLQPKGGYPGPMGPPSIPPSFRPEDELEHLTKKMLYDMENPPADDYFGRCARCGENVVGEGTGCTAMDQVFHVDCFTCIVCDVKLRGQPFYAVEKKAYCEPCYINTLEQCSVCSKPIMERILRATGKAYHPHCFTCVMCHRSLDGIPFTVDACGLIHCIEDFHKKFAPRCSVCKEPIMPAPGQEETVRIVALDRDFHVHCYRCEDCGGLLSEGDNQGCYPLDGHILCKTCNSARIRVLTAKASTDL
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
11PhosphorylationPSWLPPKSTGEPLGH
CCCCCCCCCCCCCCC		47.6322345495
11O-linked_GlycosylationPSWLPPKSTGEPLGH
CCCCCCCCCCCCCCC		47.6321540332
12PhosphorylationSWLPPKSTGEPLGHV
CCCCCCCCCCCCCCC		52.2522345495
25PhosphorylationHVPARMETTHSFGNP
CCCCEEEEECCCCCC		22.0722345495
26PhosphorylationVPARMETTHSFGNPS
CCCEEEEECCCCCCC		11.3822345495
28PhosphorylationARMETTHSFGNPSIS
CEEEEECCCCCCCEE		32.5322345495
33PhosphorylationTHSFGNPSISVSTQQ
ECCCCCCCEEEECCC		31.3422345495
35PhosphorylationSFGNPSISVSTQQPP
CCCCCCEEEECCCCC		17.8522345495
37PhosphorylationGNPSISVSTQQPPKK
CCCCEEEECCCCCCC		17.4422345495
38PhosphorylationNPSISVSTQQPPKKY
CCCEEEECCCCCCCC		29.1222345495
44MalonylationSTQQPPKKYAPVVAP
ECCCCCCCCCCCCCC		53.0426320211
45PhosphorylationTQQPPKKYAPVVAPK
CCCCCCCCCCCCCCC		23.4326824392
54MalonylationPVVAPKPKYNPYKQP
CCCCCCCCCCCCCCC		64.8826320211
108UbiquitinationVQQGNPGGKTLEERR
ECCCCCCCCCHHHHH		22.4927667366
109UbiquitinationQQGNPGGKTLEERRS
CCCCCCCCCHHHHHH		56.7122790023
109AcetylationQQGNPGGKTLEERRS
CCCCCCCCCHHHHHH		56.7123806337
110PhosphorylationQGNPGGKTLEERRSS
CCCCCCCCHHHHHHH		42.5526824392
116PhosphorylationKTLEERRSSLDAEID
CCHHHHHHHHHHHHH		41.2826643407
117PhosphorylationTLEERRSSLDAEIDS
CHHHHHHHHHHHHHH		28.5826643407
124PhosphorylationSLDAEIDSLTSILAD
HHHHHHHHHHHHHHH		38.9326643407
126PhosphorylationDAEIDSLTSILADLE
HHHHHHHHHHHHHHC		20.0626643407
127PhosphorylationAEIDSLTSILADLEC
HHHHHHHHHHHHHCC		22.3926643407
146PhosphorylationKPRPPQGSASSIASP
CCCCCCCCCCCCCCC		21.5223375375
148PhosphorylationRPPQGSASSIASPPV
CCCCCCCCCCCCCCC		24.7929472430
149PhosphorylationPPQGSASSIASPPVS
CCCCCCCCCCCCCCC		23.1423375375
152PhosphorylationGSASSIASPPVSTPV
CCCCCCCCCCCCCCC		28.2426824392
156PhosphorylationSIASPPVSTPVTGHK
CCCCCCCCCCCCCCC		32.5426643407
157PhosphorylationIASPPVSTPVTGHKR
CCCCCCCCCCCCCCC		23.2426643407
160PhosphorylationPPVSTPVTGHKRMVI
CCCCCCCCCCCCCCC		34.4726643407
203UbiquitinationPIGTLKPQPQPVPAS
CCCCCCCCCCCCCCC		47.9027667366
210O-linked_GlycosylationQPQPVPASYTTASTS
CCCCCCCCEECCCCC		19.5521540332
219MethylationTTASTSSRPTFNVQV
ECCCCCCCCEEEEEE		33.7658856209
219DimethylationTTASTSSRPTFNVQV
ECCCCCCCCEEEEEE		33.76-
228PhosphorylationTFNVQVKSAQPSPHY
EEEEEEEECCCCCCC		33.0222499769
232PhosphorylationQVKSAQPSPHYMAGP
EEEECCCCCCCCCCC		16.5422499769
235PhosphorylationSAQPSPHYMAGPSSG
ECCCCCCCCCCCCCC		7.6422499769
240PhosphorylationPHYMAGPSSGQIYGP
CCCCCCCCCCCEECC		46.3022499769
241PhosphorylationHYMAGPSSGQIYGPG
CCCCCCCCCCEECCC		37.5422499769
245PhosphorylationGPSSGQIYGPGPRGY
CCCCCCEECCCCCCC		14.9118515860
250MethylationQIYGPGPRGYNNQPV
CEECCCCCCCCCCCC		67.1724129315
268PhosphorylationGQCPPPPTCVGTDYA
CCCCCCCCEECCCEE		26.12-
274PhosphorylationPTCVGTDYAYIPPSG
CCEECCCEEECCCCC		10.9225263469
276PhosphorylationCVGTDYAYIPPSGHP
EECCCEEECCCCCCC		14.0229514104
297PhosphorylationYTSNQGRYYEPYYAA
CCCCCCCEEECEEEC		21.0022499769
298PhosphorylationTSNQGRYYEPYYAAG
CCCCCCEEECEEECC		14.7422499769
301PhosphorylationQGRYYEPYYAAGPSY
CCCEEECEEECCCCC		8.1918515860
302PhosphorylationGRYYEPYYAAGPSYG
CCEEECEEECCCCCC		10.7418515860
307PhosphorylationPYYAAGPSYGGRSEG
CEEECCCCCCCCCCC		35.1822499769
308PhosphorylationYYAAGPSYGGRSEGD
EEECCCCCCCCCCCC		27.0822499769
312PhosphorylationGPSYGGRSEGDTAYG
CCCCCCCCCCCCCCC		49.56-
316PhosphorylationGGRSEGDTAYGQQVQ
CCCCCCCCCCCCCCC		32.4122817900
318PhosphorylationRSEGDTAYGQQVQPN
CCCCCCCCCCCCCCC		19.9822817900
326PhosphorylationGQQVQPNTWKREAAY
CCCCCCCCCCCEEEC		38.7625521595
327UbiquitinationQQVQPNTWKREAAYA
CCCCCCCCCCEEECC		12.3527667366
328AcetylationQVQPNTWKREAAYAP
CCCCCCCCCEEECCC		38.027610091
328UbiquitinationQVQPNTWKREAAYAP
CCCCCCCCCEEECCC		38.0222790023
333PhosphorylationTWKREAAYAPPASGN
CCCCEEECCCCCCCC		27.0422499769
338PhosphorylationAAYAPPASGNQNHPG
EECCCCCCCCCCCCC		44.01-
347PhosphorylationNQNHPGMYPVSGPKK
CCCCCCCCCCCCCCC		13.3429514104
400UbiquitinationELEHLTKKMLYDMEN
HHHHHHHHHHHCCCC		28.9822790023
403PhosphorylationHLTKKMLYDMENPPA
HHHHHHHHCCCCCCC		15.1122817900
413PhosphorylationENPPADDYFGRCARC
CCCCCCCCCCCCCCC		14.4222817900
462UbiquitinationQPFYAVEKKAYCEPC
CEEEEEEECCCCEEC		35.7822790023
509PhosphorylationTCVMCHRSLDGIPFT
EHHEECCCCCCCCEE		13.7226824392
578PhosphorylationEDCGGLLSEGDNQGC
CCCCCCCCCCCCCCC		44.5726525534
606PhosphorylationSARIRVLTAKASTDL
CCEEEEEEEECCCCC		24.2125777480
610PhosphorylationRVLTAKASTDL----
EEEEEECCCCC----		23.0324068923
611PhosphorylationVLTAKASTDL-----
EEEEECCCCC-----		46.2924068923
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 LPP_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-245, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-302, AND MASSSPECTROMETRY.

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