LCP2_HUMAN - dbPTM
LCP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LCP2_HUMAN
UniProt AC Q13094
Protein Name Lymphocyte cytosolic protein 2
Gene Name LCP2
Organism Homo sapiens (Human).
Sequence Length 533
Subcellular Localization Cytoplasm .
Protein Description Involved in T-cell antigen receptor mediated signaling..
Protein Sequence MALRNVPFRSEVLGWDPDSLADYFKKLNYKDCEKAVKKYHIDGARFLNLTENDIQKFPKLRVPILSKLSQEINKNEERRSIFTRKPQVPRFPEETESHEEDNGGWSSFEEDDYESPNDDQDGEDDGDYESPNEEEEAPVEDDADYEPPPSNDEEALQNSILPAKPFPNSNSMYIDRPPSGKTPQQPPVPPQRPMAALPPPPAGRNHSPLPPPQTNHEEPSRSRNHKTAKLPAPSIDRSTKPPLDRSLAPFDREPFTLGKKPPFSDKPSIPAGRSLGEHLPKIQKPPLPPTTERHERSSPLPGKKPPVPKHGWGPDRRENDEDDVHQRPLPQPALLPMSSNTFPSRSTKPSPMNPLPSSHMPGAFSESNSSFPQSASLPPYFSQGPSNRPPIRAEGRNFPLPLPNKPRPPSPAEEENSLNEEWYVSYITRPEAEAALRKINQDGTFLVRDSSKKTTTNPYVLMVLYKDKVYNIQIRYQKESQVYLLGTGLRGKEDFLSVSDIIDYFRKMPLLLIDGKNRGSRYQCTLTHAAGYP
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
23PhosphorylationDPDSLADYFKKLNYK
CHHHHHHHHHHCCHH
16.2221082442
29PhosphorylationDYFKKLNYKDCEKAV
HHHHHCCHHHHHHHH
20.74-
30UbiquitinationYFKKLNYKDCEKAVK
HHHHCCHHHHHHHHH
55.62-
39PhosphorylationCEKAVKKYHIDGARF
HHHHHHHHCCCHHHH
9.78-
59UbiquitinationNDIQKFPKLRVPILS
HHHHHCCCCHHHHHH
52.6524816145
80PhosphorylationNKNEERRSIFTRKPQ
HCCHHHHHHHHCCCC
28.4230576142
106PhosphorylationEEDNGGWSSFEEDDY
CCCCCCCCCCCCCCC
28.55-
107PhosphorylationEDNGGWSSFEEDDYE
CCCCCCCCCCCCCCC
30.12-
113PhosphorylationSSFEEDDYESPNDDQ
CCCCCCCCCCCCCCC
30.5417148460
128PhosphorylationDGEDDGDYESPNEEE
CCCCCCCCCCCCCCC
24.6817148460
130PhosphorylationEDDGDYESPNEEEEA
CCCCCCCCCCCCCCC
27.1417353368
145PhosphorylationPVEDDADYEPPPSND
CCCCCCCCCCCCCCC
31.8617148460
169PhosphorylationPAKPFPNSNSMYIDR
CCCCCCCCCCCEECC
30.44-
171PhosphorylationKPFPNSNSMYIDRPP
CCCCCCCCCEECCCC
16.88-
173PhosphorylationFPNSNSMYIDRPPSG
CCCCCCCEECCCCCC
10.2516094384
207PhosphorylationPPAGRNHSPLPPPQT
CCCCCCCCCCCCCCC
31.5123401153
214PhosphorylationSPLPPPQTNHEEPSR
CCCCCCCCCCCCCCC
44.2926074081
220PhosphorylationQTNHEEPSRSRNHKT
CCCCCCCCCCCCCCC
46.2826074081
222PhosphorylationNHEEPSRSRNHKTAK
CCCCCCCCCCCCCCC
41.60-
227PhosphorylationSRSRNHKTAKLPAPS
CCCCCCCCCCCCCCC
22.82-
229AcetylationSRNHKTAKLPAPSID
CCCCCCCCCCCCCCC
61.3025953088
234PhosphorylationTAKLPAPSIDRSTKP
CCCCCCCCCCCCCCC
38.9521949786
240UbiquitinationPSIDRSTKPPLDRSL
CCCCCCCCCCCCCCC
45.9824816145
246PhosphorylationTKPPLDRSLAPFDRE
CCCCCCCCCCCCCCC
28.66-
256PhosphorylationPFDREPFTLGKKPPF
CCCCCCCCCCCCCCC
45.3728060719
260AcetylationEPFTLGKKPPFSDKP
CCCCCCCCCCCCCCC
57.0025953088
260UbiquitinationEPFTLGKKPPFSDKP
CCCCCCCCCCCCCCC
57.00-
264PhosphorylationLGKKPPFSDKPSIPA
CCCCCCCCCCCCCCC
50.96-
268PhosphorylationPPFSDKPSIPAGRSL
CCCCCCCCCCCCCCH
47.12-
273MethylationKPSIPAGRSLGEHLP
CCCCCCCCCHHHCCC
30.71115386307
274PhosphorylationPSIPAGRSLGEHLPK
CCCCCCCCHHHCCCC
39.55-
297PhosphorylationTTERHERSSPLPGKK
CCCCCCCCCCCCCCC
33.0726657352
298PhosphorylationTERHERSSPLPGKKP
CCCCCCCCCCCCCCC
36.3623401153
338PhosphorylationQPALLPMSSNTFPSR
CCCEEECCCCCCCCC
20.6330108239
339PhosphorylationPALLPMSSNTFPSRS
CCEEECCCCCCCCCC
33.3730108239
341PhosphorylationLLPMSSNTFPSRSTK
EEECCCCCCCCCCCC
38.5828787133
344PhosphorylationMSSNTFPSRSTKPSP
CCCCCCCCCCCCCCC
34.3730108239
367PhosphorylationMPGAFSESNSSFPQS
CCCCCCCCCCCCCCC
40.5926074081
369PhosphorylationGAFSESNSSFPQSAS
CCCCCCCCCCCCCCC
42.5126074081
370PhosphorylationAFSESNSSFPQSASL
CCCCCCCCCCCCCCC
45.2426074081
374PhosphorylationSNSSFPQSASLPPYF
CCCCCCCCCCCCCCC
21.7726074081
376PhosphorylationSSFPQSASLPPYFSQ
CCCCCCCCCCCCCCC
46.8126074081
380PhosphorylationQSASLPPYFSQGPSN
CCCCCCCCCCCCCCC
17.5826074081
382PhosphorylationASLPPYFSQGPSNRP
CCCCCCCCCCCCCCC
28.5226074081
386PhosphorylationPYFSQGPSNRPPIRA
CCCCCCCCCCCCCCC
52.9026074081
392MethylationPSNRPPIRAEGRNFP
CCCCCCCCCCCCCCC
32.15115386315
410PhosphorylationPNKPRPPSPAEEENS
CCCCCCCCCHHHCCC
39.1528348404
417PhosphorylationSPAEEENSLNEEWYV
CCHHHCCCCCCCEEE
35.5328464451
423PhosphorylationNSLNEEWYVSYITRP
CCCCCCEEEEEECCH
5.258702662
425PhosphorylationLNEEWYVSYITRPEA
CCCCEEEEEECCHHH
8.63-
426PhosphorylationNEEWYVSYITRPEAE
CCCEEEEEECCHHHH
9.038702662
428PhosphorylationEWYVSYITRPEAEAA
CEEEEEECCHHHHHH
31.75-
438UbiquitinationEAEAALRKINQDGTF
HHHHHHHHHCCCCCE
47.0329967540
454PhosphorylationVRDSSKKTTTNPYVL
EECCCCCCCCCCEEE
42.4625907765
455PhosphorylationRDSSKKTTTNPYVLM
ECCCCCCCCCCEEEE
33.1925907765
456PhosphorylationDSSKKTTTNPYVLMV
CCCCCCCCCCEEEEE
39.1525907765
459PhosphorylationKKTTTNPYVLMVLYK
CCCCCCCEEEEEEEC
14.3225907765
465PhosphorylationPYVLMVLYKDKVYNI
CEEEEEEECCCEEEE
13.0125907765
470PhosphorylationVLYKDKVYNIQIRYQ
EEECCCEEEEEEEEE
16.58-
476PhosphorylationVYNIQIRYQKESQVY
EEEEEEEEECCCEEE
26.09-
483PhosphorylationYQKESQVYLLGTGLR
EECCCEEEEECCCCC
6.64-
492UbiquitinationLGTGLRGKEDFLSVS
ECCCCCCCCCCCCHH
47.9129967540
507UbiquitinationDIIDYFRKMPLLLID
HHHHHHHCCCEEEEC
34.6624816145
516UbiquitinationPLLLIDGKNRGSRYQ
CEEEECCCCCCCCCE
39.4629967540
522PhosphorylationGKNRGSRYQCTLTHA
CCCCCCCCEEEEECC
15.05-
532PhosphorylationTLTHAAGYP------
EEECCCCCC------
10.8825839225

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
113YPhosphorylationKinaseSYKP43405
PSP
113YPhosphorylationKinaseLCKP06239
PSP
113YPhosphorylationKinaseSYKQ15046
PhosphoELM
113YPhosphorylationKinaseZAP70P43403
PSP
128YPhosphorylationKinaseSYKP43405
PSP
128YPhosphorylationKinaseLCKP06239
PSP
128YPhosphorylationKinaseSYKQ15046
PhosphoELM
128YPhosphorylationKinaseZAP70P43403
PSP
145YPhosphorylationKinaseLCKP06239
PSP
145YPhosphorylationKinaseTXKP42681
PhosphoELM
145YPhosphorylationKinaseZAP70P43403
PSP
173YPhosphorylationKinaseITKQ08881
PSP
376SPhosphorylationKinaseMAP4K1Q92918
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LCP2_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 LCP2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GRAP2_HUMANGRAP2physical
16189514
P85A_HUMANPIK3R1physical
15388330
ITK_HUMANITKphysical
15388330
NCK1_HUMANNCK1physical
15388330
PLCG1_HUMANPLCG1physical
11390650
LYN_HUMANLYNphysical
10026222
PHAG1_HUMANPAG1physical
10790433
TRAT1_HUMANTRAT1physical
10790433
CBL_HUMANCBLphysical
10204582
GRB2_HUMANGRB2physical
10204582
FYB1_MOUSEFybphysical
10497204
GRAP2_HUMANGRAP2physical
10021361
GRAP2_HUMANGRAP2genetic
10021361
GRAP2_HUMANGRAP2physical
10224278
GRB2_HUMANGRB2physical
10224278
CBL_HUMANCBLphysical
9716598
GRB2_HUMANGRB2physical
9716598
SHC1_HUMANSHC1physical
9716598
GRAP2_HUMANGRAP2physical
12176364
GRB2_HUMANGRB2physical
12176364
FYB1_HUMANFYBphysical
9207119
A4_HUMANAPPphysical
21832049
PLCG1_HUMANPLCG1physical
16467851
YBOX1_HUMANYBX1physical
21988832
NCK2_HUMANNCK2physical
25416956
GRAP2_HUMANGRAP2physical
25416956
FXR2_HUMANFXR2physical
25416956
STAM2_HUMANSTAM2physical
25416956
GRAP2_HUMANGRAP2physical
21516116
FXR2_HUMANFXR2physical
21516116
ACK1_HUMANTNK2physical
28188290
FYB1_HUMANFYBphysical
29127148

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 LCP2_HUMAN

loading...

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-207, AND MASSSPECTROMETRY.
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASSSPECTROMETRY.
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry.";
Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.;
Nat. Methods 2:591-598(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-173 AND SER-207, ANDMASS SPECTROMETRY.
"Robust phosphoproteomic profiling of tyrosine phosphorylation sitesfrom human T cells using immobilized metal affinity chromatography andtandem mass spectrometry.";
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,Peters E.C.;
Anal. Chem. 76:2763-2772(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASSSPECTROMETRY.

TOP