LSP1_MOUSE - dbPTM
LSP1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSP1_MOUSE
UniProt AC P19973
Protein Name Lymphocyte-specific protein 1
Gene Name Lsp1
Organism Mus musculus (Mouse).
Sequence Length 330
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description May play a role in mediating neutrophil activation and chemotaxis..
Protein Sequence MAEAAIDPRCEEQEELHAEDSEGLTTQWREEDEEEAAREQRQRERERQLQDQDKDKEDDGGHSLEQPGQQTLISLKSSELDEDEGFGDWSQKPEPRQQFWGNEGTAEGTEPSQSERPEEKQTEESSHQAKVHLEESNLSYREPDPEDAVGGSGEAEEHLIRHQVRTPSPLALEDTVELSSPPLSPTTKLADRTESLNRSIKKSNSVKKSQPTLPISTIDERLQQYTQATESSGRTPKLSRQPSIELPSMAVASTKTLWETGEVQSQSASKTPSCQDIVAGDMSKKSLWEQKGGSKISSTIKSTPSGKRYKFVATGHGKYEKVLVDEGSAP
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
21PhosphorylationEELHAEDSEGLTTQW
HHHHHCCCCCCCCCC		25.6830635358
25PhosphorylationAEDSEGLTTQWREED
HCCCCCCCCCCHHHH		28.0030635358
26PhosphorylationEDSEGLTTQWREEDE
CCCCCCCCCCHHHHH		31.0430635358
61PhosphorylationKDKEDDGGHSLEQPG
CCCCCCCCCCCCCCC		17.7624719451
63PhosphorylationKEDDGGHSLEQPGQQ
CCCCCCCCCCCCCCE		36.5622942356
71PhosphorylationLEQPGQQTLISLKSS
CCCCCCEEEEEEECC		20.4020531401
74PhosphorylationPGQQTLISLKSSELD
CCCEEEEEEECCCCC		32.6220531401
77PhosphorylationQTLISLKSSELDEDE
EEEEEEECCCCCCCC		34.0521082442
78PhosphorylationTLISLKSSELDEDEG
EEEEEECCCCCCCCC		40.3629472430
90PhosphorylationDEGFGDWSQKPEPRQ
CCCCCCCCCCCCCCC		32.8214729942
112PhosphorylationTAEGTEPSQSERPEE
CCCCCCCCCCCCCCH		39.8620531401
136PhosphorylationAKVHLEESNLSYREP
HHHHHHHHCCCCCCC		33.4225266776
137PhosphorylationKVHLEESNLSYREPD
HHHHHHHCCCCCCCC		35.9624719451
139PhosphorylationHLEESNLSYREPDPE
HHHHHCCCCCCCCHH		26.7930635358
140PhosphorylationLEESNLSYREPDPED
HHHHCCCCCCCCHHH		23.3526026062
150PhosphorylationPDPEDAVGGSGEAEE
CCHHHCCCCCCHHHH		26.6924719451
152PhosphorylationPEDAVGGSGEAEEHL
HHHCCCCCCHHHHHH		27.7728833060
164PhosphorylationEHLIRHQVRTPSPLA
HHHHHHCCCCCCCCC		6.3424719451
166PhosphorylationLIRHQVRTPSPLALE
HHHHCCCCCCCCCCC		29.3026824392
168PhosphorylationRHQVRTPSPLALEDT
HHCCCCCCCCCCCCC		31.7526824392
175PhosphorylationSPLALEDTVELSSPP
CCCCCCCCEECCCCC		13.4025521595
177PhosphorylationLALEDTVELSSPPLS
CCCCCCEECCCCCCC		45.0524719451
178PhosphorylationALEDTVELSSPPLSP
CCCCCEECCCCCCCC		5.5124719451
179PhosphorylationLEDTVELSSPPLSPT
CCCCEECCCCCCCCC		27.5626824392
180PhosphorylationEDTVELSSPPLSPTT
CCCEECCCCCCCCCC		43.0626824392
182PhosphorylationTVELSSPPLSPTTKL
CEECCCCCCCCCCHH		47.6324719451
184PhosphorylationELSSPPLSPTTKLAD
ECCCCCCCCCCHHHH		26.4426824392
186PhosphorylationSSPPLSPTTKLADRT
CCCCCCCCCHHHHHH		32.9421082442
187PhosphorylationSPPLSPTTKLADRTE
CCCCCCCCHHHHHHH		27.6922942356
193PhosphorylationTTKLADRTESLNRSI
CCHHHHHHHHHHHHH		30.3928833060
195PhosphorylationKLADRTESLNRSIKK
HHHHHHHHHHHHHHH		30.2626824392
197PhosphorylationADRTESLNRSIKKSN
HHHHHHHHHHHHHHC		44.9524719451
199PhosphorylationRTESLNRSIKKSNSV
HHHHHHHHHHHHCCC		37.3725266776
205PhosphorylationRSIKKSNSVKKSQPT
HHHHHHCCCCCCCCC		42.2627600695
209PhosphorylationKSNSVKKSQPTLPIS
HHCCCCCCCCCCCCC		35.3627180971
209O-linked_GlycosylationKSNSVKKSQPTLPIS
HHCCCCCCCCCCCCC		35.3627555448
212PhosphorylationSVKKSQPTLPISTID
CCCCCCCCCCCCHHH		37.2129176673
225PhosphorylationIDERLQQYTQATESS
HHHHHHHHHHHHHHC		6.4525367039
226PhosphorylationDERLQQYTQATESSG
HHHHHHHHHHHHHCC		13.8520531401
227PhosphorylationERLQQYTQATESSGR
HHHHHHHHHHHHCCC		41.1624719451
229PhosphorylationLQQYTQATESSGRTP
HHHHHHHHHHCCCCC		26.9529472430
231PhosphorylationQYTQATESSGRTPKL
HHHHHHHHCCCCCCC		33.4630635358
232PhosphorylationYTQATESSGRTPKLS
HHHHHHHCCCCCCCC		26.5125266776
233PhosphorylationTQATESSGRTPKLSR
HHHHHHCCCCCCCCC		46.9224719451
235PhosphorylationATESSGRTPKLSRQP
HHHHCCCCCCCCCCC		28.4426824392
239PhosphorylationSGRTPKLSRQPSIEL
CCCCCCCCCCCCCCC		34.6922802335
241PhosphorylationRTPKLSRQPSIELPS
CCCCCCCCCCCCCCC		32.4924719451
243PhosphorylationPKLSRQPSIELPSMA
CCCCCCCCCCCCCCE		21.9825521595
248PhosphorylationQPSIELPSMAVASTK
CCCCCCCCCEEECCC		31.8127742792
253PhosphorylationLPSMAVASTKTLWET
CCCCEEECCCCHHHC		24.6828833060
254PhosphorylationPSMAVASTKTLWETG
CCCEEECCCCHHHCC		20.5020531401
256PhosphorylationMAVASTKTLWETGEV
CEEECCCCHHHCCCC		36.8725367039
260PhosphorylationSTKTLWETGEVQSQS
CCCCHHHCCCCCCCC		27.3626060331
265PhosphorylationWETGEVQSQSASKTP
HHCCCCCCCCCCCCC		31.1430635358
267PhosphorylationTGEVQSQSASKTPSC
CCCCCCCCCCCCCCH		39.4930635358
269PhosphorylationEVQSQSASKTPSCQD
CCCCCCCCCCCCHHH		42.1630635358
271PhosphorylationQSQSASKTPSCQDIV
CCCCCCCCCCHHHHH		20.2428833060
273PhosphorylationQSASKTPSCQDIVAG
CCCCCCCCHHHHHCC		29.6428833060
291AcetylationKKSLWEQKGGSKISS
HHHHHHHHCCCCCCC		54.4419855827
294PhosphorylationLWEQKGGSKISSTIK
HHHHHCCCCCCCEEE		35.1727600695
297PhosphorylationQKGGSKISSTIKSTP
HHCCCCCCCEEEECC		25.7629176673
298PhosphorylationKGGSKISSTIKSTPS
HCCCCCCCEEEECCC		37.3129176673
299PhosphorylationGGSKISSTIKSTPSG
CCCCCCCEEEECCCC		26.1529176673
301AcetylationSKISSTIKSTPSGKR
CCCCCEEEECCCCCE		48.6519855837
302PhosphorylationKISSTIKSTPSGKRY
CCCCEEEECCCCCEE		41.5229176673
303PhosphorylationISSTIKSTPSGKRYK
CCCEEEECCCCCEEE		19.2425266776
305PhosphorylationSTIKSTPSGKRYKFV
CEEEECCCCCEEEEE		57.9729176673
309PhosphorylationSTPSGKRYKFVATGH
ECCCCCEEEEEEECC		16.5625367039
318AcetylationFVATGHGKYEKVLVD
EEEECCCCEEEEEEE		44.56-
319PhosphorylationVATGHGKYEKVLVDE
EEECCCCEEEEEEEC		26.1029514104
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
77SPhosphorylationKinaseCK2-Uniprot
78SPhosphorylationKinaseCK2-Uniprot
195SPhosphorylationKinaseMAPKAPK2P49137
PSP
243SPhosphorylationKinaseMAPKAPK2P49137
PSP
243SPhosphorylationKinaseMAPKAPK2P49138
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSP1_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 LSP1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of LSP1_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LSP1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166; SER-168 ANDSER-243, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166 AND SER-168, ANDMASS SPECTROMETRY.
"MAPKAPK2-mediated LSP1 phosphorylation and FMLP-induced neutrophilpolarization.";
Wu Y., Zhan L., Ai Y., Hannigan M., Gaestel M., Huang C.-K.,Madri J.A.;
Biochem. Biophys. Res. Commun. 358:170-175(2007).
Cited for: PHOSPHORYLATION AT SER-243 BY MAPKAPK2, MUTAGENESIS OF SER-195 ANDSER-243, AND FUNCTION.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-166 AND SER-168, ANDMASS SPECTROMETRY.
"Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line.";
Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.;
Mol. Cell. Proteomics 3:279-286(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, AND MASSSPECTROMETRY.

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