LRCH3_HUMAN - dbPTM
LRCH3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRCH3_HUMAN
UniProt AC Q96II8
Protein Name Leucine-rich repeat and calponin homology domain-containing protein 3
Gene Name LRCH3
Organism Homo sapiens (Human).
Sequence Length 777
Subcellular Localization Secreted .
Protein Description
Protein Sequence MAAAGLVAVAAAAEYSGTVASGGNLPGVHCGPSSGAGPGFGPGSWSRSLDRALEEAAVTGVLSLSGRKLREFPRGAANHDLTDTTRADLSRNRLSEIPIEACHFVSLENLNLYQNCIRYIPEAILNLQALTFLNISRNQLSTLPVHLCNLPLKVLIASNNKLVSLPEEIGHLRHLMELDVSCNEIQTIPSQIGNLEALRDLNVRRNHLVHLPEELAELPLIRLDFSCNKITTIPVCYRNLRHLQTITLDNNPLQSPPAQICIKGKVHIFKYLNIQACKIAPDLPDYDRRPLGFGSCHEELYSSRPYGALDSGFNSVDSGDKRWSGNEPTDEFSDLPLRVAEITKEQRLRRESQYQENRGSLVVTNGGVEHDLDQIDYIDSCTAEEEEAEVRQPKGPDPDSLSSQFMAYIEQRRISHEGSPVKPVAIREFQKTEDMRRYLHQNRVPAEPSSLLSLSASHNQLSHTDLELHQRREQLVERTRREAQLAALQYEEEKIRTKQIQRDAVLDFVKQKASQSPQKQHPLLDGVDGECPFPSRRSQHTDDSALCMSLSGLNQVGCAATLPHSSAFTPLKSDDRPNALLSSPATETVHHSPAYSFPAAIQRNQPQRPESFLFRAGVRAETNKGHASPLPPSAAPTTDSTDSITGQNSRQREEELELIDQLRKHIEYRLKVSLPCDLGAALTDGVVLCHLANHVRPRSVPSIHVPSPAVPKLTMAKCRRNVENFLEACRKIGVPQEQLCLPLHILEEKGLSQVAVTVQALLELAPPKQQQHQLSAV
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
15PhosphorylationAVAAAAEYSGTVASG
HHHHHHHHCCCCCCC		13.9925867546
16PhosphorylationVAAAAEYSGTVASGG
HHHHHHHCCCCCCCC		21.3525867546
18PhosphorylationAAAEYSGTVASGGNL
HHHHHCCCCCCCCCC		13.6325867546
21PhosphorylationEYSGTVASGGNLPGV
HHCCCCCCCCCCCCC		42.7825867546
33PhosphorylationPGVHCGPSSGAGPGF
CCCCCCCCCCCCCCC		27.0425867546
34PhosphorylationGVHCGPSSGAGPGFG
CCCCCCCCCCCCCCC		35.4825867546
44PhosphorylationGPGFGPGSWSRSLDR
CCCCCCCHHHHHHHH		25.6325867546
46PhosphorylationGFGPGSWSRSLDRAL
CCCCCHHHHHHHHHH		17.4325867546
95PhosphorylationDLSRNRLSEIPIEAC
HHHCCCHHCCCHHHC		30.1828348404
95 (in isoform 3)Phosphorylation-30.1827251275
153UbiquitinationHLCNLPLKVLIASNN
HHCCCCCEEEECCCC		32.81-
153UbiquitinationHLCNLPLKVLIASNN
HHCCCCCEEEECCCC		32.81-
161UbiquitinationVLIASNNKLVSLPEE
EEECCCCCEECCCHH		55.29-
161UbiquitinationVLIASNNKLVSLPEE
EEECCCCCEECCCHH		55.29-
205DimethylationLRDLNVRRNHLVHLP
HHHCCCCCCCCCCCC		30.55-
205MethylationLRDLNVRRNHLVHLP
HHHCCCCCCCCCCCC		30.5524379977
222DimethylationLAELPLIRLDFSCNK
HHHCCCEEEECCCCC		35.57-
222MethylationLAELPLIRLDFSCNK
HHHCCCEEEECCCCC		35.5724379985
229UbiquitinationRLDFSCNKITTIPVC
EEECCCCCCCCHHHH		45.84-
229 (in isoform 2)Ubiquitination-45.84-
255PhosphorylationLDNNPLQSPPAQICI
ECCCCCCCCCCEEEE		40.3021712546
295PhosphorylationRRPLGFGSCHEELYS
CCCCCCCCHHHHHHH		15.2723312004
301PhosphorylationGSCHEELYSSRPYGA
CCHHHHHHHCCCCCC		14.1023312004
302PhosphorylationSCHEELYSSRPYGAL
CHHHHHHHCCCCCCC		32.28-
306PhosphorylationELYSSRPYGALDSGF
HHHHCCCCCCCCCCC		17.58-
311PhosphorylationRPYGALDSGFNSVDS
CCCCCCCCCCCCCCC		46.2423312004
315PhosphorylationALDSGFNSVDSGDKR
CCCCCCCCCCCCCCC		25.6625627689
318PhosphorylationSGFNSVDSGDKRWSG
CCCCCCCCCCCCCCC		46.8925159151
324PhosphorylationDSGDKRWSGNEPTDE
CCCCCCCCCCCCCCC		35.4622167270
324 (in isoform 3)Phosphorylation-35.4624719451
329PhosphorylationRWSGNEPTDEFSDLP
CCCCCCCCCCCCCCC		41.8222167270
333PhosphorylationNEPTDEFSDLPLRVA
CCCCCCCCCCCHHHH		35.8723663014
344UbiquitinationLRVAEITKEQRLRRE
HHHHHHCHHHHHHHH		58.47-
344AcetylationLRVAEITKEQRLRRE
HHHHHHCHHHHHHHH		58.4725953088
344UbiquitinationLRVAEITKEQRLRRE
HHHHHHCHHHHHHHH		58.47-
352PhosphorylationEQRLRRESQYQENRG
HHHHHHHHHHHHHCC		32.1725159151
352 (in isoform 3)Phosphorylation-32.1727251275
354PhosphorylationRLRRESQYQENRGSL
HHHHHHHHHHHCCCE		27.3728796482
360PhosphorylationQYQENRGSLVVTNGG
HHHHHCCCEEEECCC		18.1129978859
364PhosphorylationNRGSLVVTNGGVEHD
HCCCEEEECCCEECC		22.2229978859
377PhosphorylationHDLDQIDYIDSCTAE
CCHHHCCEECCCCCC		14.3029978859
377 (in isoform 2)Phosphorylation-14.3027642862
380PhosphorylationDQIDYIDSCTAEEEE
HHCCEECCCCCCHHH		12.1029978859
382PhosphorylationIDYIDSCTAEEEEAE
CCEECCCCCCHHHHH		40.8429978859
403UbiquitinationPDPDSLSSQFMAYIE
CCCCCCHHHHHHHHH		32.50-
406SulfoxidationDSLSSQFMAYIEQRR
CCCHHHHHHHHHHCC		1.8330846556
408PhosphorylationLSSQFMAYIEQRRIS
CHHHHHHHHHHCCCC		8.00-
408 (in isoform 2)Phosphorylation-8.0027642862
415PhosphorylationYIEQRRISHEGSPVK
HHHHCCCCCCCCCCC		17.4229255136
415 (in isoform 3)Phosphorylation-17.4224719451
419PhosphorylationRRISHEGSPVKPVAI
CCCCCCCCCCCCCEE		24.4429255136
419 (in isoform 3)Phosphorylation-24.4424719451
431UbiquitinationVAIREFQKTEDMRRY
CEEEEEECCHHHHHH		60.24-
453PhosphorylationAEPSSLLSLSASHNQ
CCCCHHHHHHCCCCC		26.1027080861
455PhosphorylationPSSLLSLSASHNQLS
CCHHHHHHCCCCCCC		25.0927080861
455 (in isoform 3)Phosphorylation-25.0927251275
457PhosphorylationSLLSLSASHNQLSHT
HHHHHHCCCCCCCCC		21.4227080861
462PhosphorylationSASHNQLSHTDLELH
HCCCCCCCCCHHHHH		17.9926657352
464PhosphorylationSHNQLSHTDLELHQR
CCCCCCCCHHHHHHH		38.6127080861
466UbiquitinationNQLSHTDLELHQRRE
CCCCCCHHHHHHHHH		8.7321890473
490PhosphorylationAQLAALQYEEEKIRT
HHHHHHHHHHHHHHC		26.5921945579
490 (in isoform 2)Phosphorylation-26.5927642862
494UbiquitinationALQYEEEKIRTKQIQ
HHHHHHHHHHCHHHH		40.54-
494 (in isoform 1)Ubiquitination-40.5421890473
494 (in isoform 2)Ubiquitination-40.5421890473
494 (in isoform 3)Ubiquitination-40.5421890473
510AcetylationDAVLDFVKQKASQSP
HHHHHHHHHHHCCCC		46.187933079
510 (in isoform 4)Phosphorylation-46.1822210691
512AcetylationVLDFVKQKASQSPQK
HHHHHHHHHCCCCCC		44.267933089
514PhosphorylationDFVKQKASQSPQKQH
HHHHHHHCCCCCCCC		37.9223401153
514 (in isoform 3)Phosphorylation-37.9224719451
516PhosphorylationVKQKASQSPQKQHPL
HHHHHCCCCCCCCCC		27.1423401153
521 (in isoform 4)Phosphorylation-23.2422210691
530 (in isoform 4)Phosphorylation-34.2622210691
535PhosphorylationDGECPFPSRRSQHTD
CCCCCCCCCCCCCCC		40.4824732914
582PhosphorylationDRPNALLSSPATETV
CCCCCCCCCCCHHCC		34.8229978859
582 (in isoform 2)Phosphorylation-34.8227642862
583PhosphorylationRPNALLSSPATETVH
CCCCCCCCCCHHCCC		20.6529978859
586PhosphorylationALLSSPATETVHHSP
CCCCCCCHHCCCCCC		35.2629978859
588PhosphorylationLSSPATETVHHSPAY
CCCCCHHCCCCCCCC		22.3029978859
592PhosphorylationATETVHHSPAYSFPA
CHHCCCCCCCCCCCH		9.0628796482
592 (in isoform 2)Phosphorylation-9.0627642862
595PhosphorylationTVHHSPAYSFPAAIQ
CCCCCCCCCCCHHHH		17.7728796482
595 (in isoform 2)Phosphorylation-17.7727642862
596PhosphorylationVHHSPAYSFPAAIQR
CCCCCCCCCCHHHHH		27.1928796482
611PhosphorylationNQPQRPESFLFRAGV
CCCCCCCCCEEECCC		29.9020873877
611 (in isoform 3)Phosphorylation-29.9024719451
628PhosphorylationETNKGHASPLPPSAA
CCCCCCCCCCCCCCC		22.6923401153
628 (in isoform 3)Phosphorylation-22.6927251275
633PhosphorylationHASPLPPSAAPTTDS
CCCCCCCCCCCCCCC		34.8129255136
637PhosphorylationLPPSAAPTTDSTDSI
CCCCCCCCCCCCCCC		38.2129255136
638PhosphorylationPPSAAPTTDSTDSIT
CCCCCCCCCCCCCCC		27.2229255136
640PhosphorylationSAAPTTDSTDSITGQ
CCCCCCCCCCCCCCC		31.8320873877
641PhosphorylationAAPTTDSTDSITGQN
CCCCCCCCCCCCCCC		36.2520873877
643PhosphorylationPTTDSTDSITGQNSR
CCCCCCCCCCCCCHH		23.3420873877
645PhosphorylationTDSTDSITGQNSRQR
CCCCCCCCCCCHHHH		36.3520873877
649PhosphorylationDSITGQNSRQREEEL
CCCCCCCHHHHHHHH		23.1520873877
679UbiquitinationVSLPCDLGAALTDGV
CCCCCCHHHHHCCCC		8.78-
699PhosphorylationANHVRPRSVPSIHVP
CCCCCCCCCCCCCCC		40.8526055452
702PhosphorylationVRPRSVPSIHVPSPA
CCCCCCCCCCCCCCC		24.1426425664
707PhosphorylationVPSIHVPSPAVPKLT
CCCCCCCCCCCCCHH		25.1322199227
714PhosphorylationSPAVPKLTMAKCRRN
CCCCCCHHHHHHHHH		22.6224719451
731UbiquitinationNFLEACRKIGVPQEQ
HHHHHHHHHCCCHHH		43.63-
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
419SPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRCH3_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 LRCH3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTS_HUMANACTA1physical
24255178
BASP1_HUMANBASP1physical
24255178
CALD1_HUMANCALD1physical
24255178
COR1C_HUMANCORO1Cphysical
24255178
CRLF3_HUMANCRLF3physical
24255178
DREB_HUMANDBN1physical
24255178
DOCK6_HUMANDOCK6physical
24255178
DOCK7_HUMANDOCK7physical
24255178
LIMA1_HUMANLIMA1physical
24255178
LRCH1_HUMANLRCH1physical
24255178
LRCH2_HUMANLRCH2physical
24255178
RSU1_HUMANRSU1physical
24255178
SGT1_HUMANSUGT1physical
24255178
TPM1_HUMANTPM1physical
24255178
DOCK8_HUMANDOCK8physical
28514442
DOCK6_HUMANDOCK6physical
28514442
DOCK7_HUMANDOCK7physical
28514442
LRCH1_HUMANLRCH1physical
28514442
PIHD1_HUMANPIH1D1physical
28514442
LRCH2_HUMANLRCH2physical
28514442
VCIP1_HUMANVCPIP1physical
28514442
TMOD3_HUMANTMOD3physical
28514442
LRCH4_HUMANLRCH4physical
28514442
DYR1A_HUMANDYRK1Aphysical
28514442
CBX5_HUMANCBX5physical
28514442
SGT1_HUMANSUGT1physical
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 LRCH3_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-324, AND MASSSPECTROMETRY.
"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-324; SER-415 ANDSER-419, AND MASS SPECTROMETRY.
"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-415, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory