LSP1_HUMAN - dbPTM
LSP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LSP1_HUMAN
UniProt AC P33241
Protein Name Lymphocyte-specific protein 1
Gene Name LSP1
Organism Homo sapiens (Human).
Sequence Length 339
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side.
Protein Description May play a role in mediating neutrophil activation and chemotaxis..
Protein Sequence MAEASSDPGAEEREELLGPTAQWSVEDEEEAVHEQCQHERDRQLQAQDEEGGGHVPERPKQEMLLSLKPSEAPELDEDEGFGDWSQRPEQRQQHEGAQGALDSGEPPQCRSPEGEQEDRPGLHAYEKEDSDEVHLEELSLSKEGPGPEDTVQDNLGAAGAEEEQEEHQKCQQPRTPSPLVLEGTIEQSSPPLSPTTKLIDRTESLNRSIEKSNSVKKSQPDLPISKIDQWLEQYTQAIETAGRTPKLARQASIELPSMAVASTKSRWETGEVQAQSAAKTPSCKDIVAGDMSKKSLWEQKGGSKTSSTIKSTPSGKRYKFVATGHGKYEKVLVEGGPAP
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
5Phosphorylation---MAEASSDPGAEE
---CCCCCCCCCHHH		27.1223401153
6Phosphorylation--MAEASSDPGAEER
--CCCCCCCCCHHHH		55.6728450419
20PhosphorylationREELLGPTAQWSVED
HHHHHCCCCCCCCCC		29.6823401153
24PhosphorylationLGPTAQWSVEDEEEA
HCCCCCCCCCCHHHH		11.9828348404
60UbiquitinationGHVPERPKQEMLLSL
CCCCCCCCHHHHHCC		66.18-
66PhosphorylationPKQEMLLSLKPSEAP
CCHHHHHCCCCCCCC		30.3124719451
68UbiquitinationQEMLLSLKPSEAPEL
HHHHHCCCCCCCCCC		43.02-
103PhosphorylationGAQGALDSGEPPQCR
CCCCCHHCCCCCCCC		46.0030108239
111PhosphorylationGEPPQCRSPEGEQED
CCCCCCCCCCCCCCC		34.6223401153
125PhosphorylationDRPGLHAYEKEDSDE
CCCCCCCEECCCCCC		19.4528348404
130PhosphorylationHAYEKEDSDEVHLEE
CCEECCCCCCEEHHH		36.4420164059
139PhosphorylationEVHLEELSLSKEGPG
CEEHHHHHCCCCCCC		33.6022115753
141PhosphorylationHLEELSLSKEGPGPE
EHHHHHCCCCCCCCH		25.8628192239
175PhosphorylationQKCQQPRTPSPLVLE
HHCCCCCCCCCEEEE		34.5023401153
177PhosphorylationCQQPRTPSPLVLEGT
CCCCCCCCCEEEEEE		30.1923401153
184PhosphorylationSPLVLEGTIEQSSPP
CCEEEEEEECCCCCC		16.3820058876
188PhosphorylationLEGTIEQSSPPLSPT
EEEEECCCCCCCCCC		31.8323401153
189PhosphorylationEGTIEQSSPPLSPTT
EEEECCCCCCCCCCH		30.1723401153
193PhosphorylationEQSSPPLSPTTKLID
CCCCCCCCCCHHHHH		26.4423401153
194PhosphorylationQSSPPLSPTTKLIDR
CCCCCCCCCHHHHHC		52.3427251275
195PhosphorylationSSPPLSPTTKLIDRT
CCCCCCCCHHHHHCH		32.9428674151
196PhosphorylationSPPLSPTTKLIDRTE
CCCCCCCHHHHHCHH		27.5128674151
202PhosphorylationTTKLIDRTESLNRSI
CHHHHHCHHHHHHHH		26.6123911959
204PhosphorylationKLIDRTESLNRSIEK
HHHHCHHHHHHHHHH		30.2617001009
208PhosphorylationRTESLNRSIEKSNSV
CHHHHHHHHHHHHCC		33.7423401153
212PhosphorylationLNRSIEKSNSVKKSQ
HHHHHHHHHCCCCCC		22.8829978859
214PhosphorylationRSIEKSNSVKKSQPD
HHHHHHHCCCCCCCC		42.2629978859
218PhosphorylationKSNSVKKSQPDLPIS
HHHCCCCCCCCCCHH		41.0226657352
218O-linked_GlycosylationKSNSVKKSQPDLPIS
HHHCCCCCCCCCCHH		41.0230379171
226UbiquitinationQPDLPISKIDQWLEQ
CCCCCHHHHHHHHHH		51.53-
234PhosphorylationIDQWLEQYTQAIETA
HHHHHHHHHHHHHHC		7.4628450419
235PhosphorylationDQWLEQYTQAIETAG
HHHHHHHHHHHHHCC		15.9528450419
239PhosphorylationEQYTQAIETAGRTPK
HHHHHHHHHCCCCHH		35.3027251275
240PhosphorylationQYTQAIETAGRTPKL
HHHHHHHHCCCCHHH		28.4428450419
244PhosphorylationAIETAGRTPKLARQA
HHHHCCCCHHHHHHH		24.6928450419
252PhosphorylationPKLARQASIELPSMA
HHHHHHHCCCCCCCE		14.3017001009
257PhosphorylationQASIELPSMAVASTK
HHCCCCCCCEEECCC		31.8122115753
258PhosphorylationASIELPSMAVASTKS
HCCCCCCCEEECCCC		3.0827251275
262PhosphorylationLPSMAVASTKSRWET
CCCCEEECCCCHHHC		29.7522115753
263PhosphorylationPSMAVASTKSRWETG
CCCEEECCCCHHHCC		24.2530108239
265AcetylationMAVASTKSRWETGEV
CEEECCCCHHHCCCC		42.5919608861
265PhosphorylationMAVASTKSRWETGEV
CEEECCCCHHHCCCC		42.5919608861
267PhosphorylationVASTKSRWETGEVQA
EECCCCHHHCCCCCC		18.0027251275
269PhosphorylationSTKSRWETGEVQAQS
CCCCHHHCCCCCCCC		31.5127251275
276PhosphorylationTGEVQAQSAAKTPSC
CCCCCCCCCCCCCCH		32.9628450419
280PhosphorylationQAQSAAKTPSCKDIV
CCCCCCCCCCHHHHH		18.7328450419
282PhosphorylationQSAAKTPSCKDIVAG
CCCCCCCCHHHHHCC		38.7426657352
292PhosphorylationDIVAGDMSKKSLWEQ
HHHCCCCCHHHHHHC		41.4930108239
303O-linked_GlycosylationLWEQKGGSKTSSTIK
HHHCCCCCCCCCEEE		41.2430379171
303PhosphorylationLWEQKGGSKTSSTIK
HHHCCCCCCCCCEEE		41.2423403867
305PhosphorylationEQKGGSKTSSTIKST
HCCCCCCCCCEEEEC		29.6127251275
306PhosphorylationQKGGSKTSSTIKSTP
CCCCCCCCCEEEECC		29.2623403867
307PhosphorylationKGGSKTSSTIKSTPS
CCCCCCCCEEEECCC		39.1130576142
312PhosphorylationTSSTIKSTPSGKRYK
CCCEEEECCCCCEEE		19.2430576142
316PhosphorylationIKSTPSGKRYKFVAT
EEECCCCCEEEEEEE		57.8227251275
317PhosphorylationKSTPSGKRYKFVATG
EECCCCCEEEEEEEC		43.3227251275
318PhosphorylationSTPSGKRYKFVATGH
ECCCCCEEEEEEECC		16.5627155012
321PhosphorylationSGKRYKFVATGHGKY
CCCEEEEEEECCCCE		4.0027251275
323PhosphorylationKRYKFVATGHGKYEK
CEEEEEEECCCCEEE		25.14-
327AcetylationFVATGHGKYEKVLVE
EEEECCCCEEEEEEE		44.5619608861
328PhosphorylationVATGHGKYEKVLVEG
EEECCCCEEEEEEEC		26.1029978859
330PhosphorylationTGHGKYEKVLVEGGP
ECCCCEEEEEEECCC		37.4727251275
332PhosphorylationHGKYEKVLVEGGPAP
CCCEEEEEEECCCCC		4.2627251275
336PhosphorylationEKVLVEGGPAP----
EEEEEECCCCC----		11.1627251275
346PhosphorylationP--------------
C--------------		27251275
372Phosphorylation----------------------------------------
----------------------------------------		27251275
380Phosphorylation------------------------------------------------
------------------------------------------------		27251275
390Phosphorylation----------------------------------------------------------
----------------------------------------------------------		27251275
397Phosphorylation-----------------------------------------------------------------
-----------------------------------------------------------------		27251275
410Phosphorylation------------------------------------------------------------------------------
------------------------------------------------------------------------------		27251275
420Phosphorylation----------------------------------------------------------------------------------------
----------------------------------------------------------------------------------------		27251275
455Acetylation---------------------------------------------------------------------------------------------------------------------------
---------------------------------------------------------------------------------------------------------------------------		19608861
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
204SPhosphorylationKinaseMAPKAPK2P49137
GPS
252SPhosphorylationKinaseMAPK2P49137
PhosphoELM
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LSP1_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 LSP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GREB1_HUMANGREB1physical
25640309
IL24_HUMANIL24physical
25640309
KLK6_HUMANKLK6physical
25640309
LYPD3_HUMANLYPD3physical
25640309
SG2A2_HUMANSCGB2A2physical
25640309
SNAI1_HUMANSNAI1physical
25640309
THRSP_HUMANTHRSPphysical
25640309
FBW1A_HUMANBTRCphysical
28514442
ADSV_HUMANSCINphysical
28514442
ZMYM6_HUMANZMYM6physical
28514442
GELS_HUMANGSNphysical
28514442
FBW1B_HUMANFBXW11physical
28514442
TMOD2_HUMANTMOD2physical
28514442
CAN2_HUMANCAPN2physical
28514442
ACTBL_HUMANACTBL2physical
28514442
LIMA1_HUMANLIMA1physical
28514442
MYO1B_HUMANMYO1Bphysical
28514442
ACTB_HUMANACTBphysical
28514442
PKHG3_HUMANPLEKHG3physical
28514442
TMOD1_HUMANTMOD1physical
28514442
MYO1D_HUMANMYO1Dphysical
28514442
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 LSP1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND MASS SPECTROMETRY.
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-189, AND MASSSPECTROMETRY.
"Phosphorylation analysis of primary human T lymphocytes usingsequential IMAC and titanium oxide enrichment.";
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
J. Proteome Res. 7:5167-5176(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-252, AND MASSSPECTROMETRY.
"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-252 BY MAPKAPK2.

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