LRCH4_HUMAN - dbPTM
LRCH4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRCH4_HUMAN
UniProt AC O75427
Protein Name Leucine-rich repeat and calponin homology domain-containing protein 4
Gene Name LRCH4
Organism Homo sapiens (Human).
Sequence Length 683
Subcellular Localization
Protein Description
Protein Sequence MAAAVAAPLAAGGEEAAATTSVPGSPGLPGRRSAERALEEAVATGTLNLSNRRLKHFPRGAARSYDLSDITQADLSRNRFPEVPEAACQLVSLEGLSLYHNCLRCLNPALGNLTALTYLNLSRNQLSLLPPYICQLPLRVLIVSNNKLGALPPDIGTLGSLRQLDVSSNELQSLPSELCGLSSLRDLNVRRNQLSTLPEELGDLPLVRLDFSCNRVSRIPVSFCRLRHLQVILLDSNPLQSPPAQVCLKGKLHIFKYLSTEAGQRGSALGDLAPSRPPSFSPCPAEDLFPGHRYDGGLDSGFHSVDSGSKRWSGNESTDEFSELSFRISELAREPRGPRERKEDGSADGDPVQIDFIDSHVPGEDEERGTVEEQRPPELSPGAGDRERAPSSRREEPAGEERRRPDTLQLWQERERRQQQQSGAWGAPRKDSLLKPGLRAVVGGAAAVSTQAMHNGSPKSSASQAGAAAGQGAPAPAPASQEPLPIAGPATAPAPRPLGSIQRPNSFLFRSSSQSGSGPSSPDSVLRPRRYPQVPDEKDLMTQLRQVLESRLQRPLPEDLAEALASGVILCQLANQLRPRSVPFIHVPSPAVPKLSALKARKNVESFLEACRKMGVPEADLCSPSDLLQGTARGLRTALEAVKRVGGKALPPLWPPSGLGGFVVFYVVLMLLLYVTYTRLLGS
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
19PhosphorylationGGEEAAATTSVPGSP
CCCCCCCCCCCCCCC		18.1929255136
20PhosphorylationGEEAAATTSVPGSPG
CCCCCCCCCCCCCCC		24.0129255136
21PhosphorylationEEAAATTSVPGSPGL
CCCCCCCCCCCCCCC		23.2029255136
25PhosphorylationATTSVPGSPGLPGRR
CCCCCCCCCCCCCHH		15.1029255136
33PhosphorylationPGLPGRRSAERALEE
CCCCCHHHHHHHHHH		32.8726074081
64PhosphorylationFPRGAARSYDLSDIT
CCCCCCCCCCHHHCC		20.4828796482
65PhosphorylationPRGAARSYDLSDITQ
CCCCCCCCCHHHCCH		18.4928796482
68O-linked_GlycosylationAARSYDLSDITQADL
CCCCCCHHHCCHHHH		24.8629351928
71O-linked_GlycosylationSYDLSDITQADLSRN
CCCHHHCCHHHHHCC		23.7729351928
97PhosphorylationLVSLEGLSLYHNCLR
HHCCCHHHHHHHHHH		37.43-
99PhosphorylationSLEGLSLYHNCLRCL
CCCHHHHHHHHHHHH		6.39-
147UbiquitinationVLIVSNNKLGALPPD
EEEEECCCCCCCCCC		53.18-
160PhosphorylationPDIGTLGSLRQLDVS
CCCCCHHHHHEECCC		24.4024719451
168PhosphorylationLRQLDVSSNELQSLP
HHEECCCHHHHHHCC		33.8822210691
182PhosphorylationPSELCGLSSLRDLNV
CHHHHCCHHHHHHHC		16.7719060867
183PhosphorylationSELCGLSSLRDLNVR
HHHHCCHHHHHHHCC		32.2525954137
236PhosphorylationLQVILLDSNPLQSPP
EEEEEECCCCCCCCC		40.0728348404
241PhosphorylationLDSNPLQSPPAQVCL
ECCCCCCCCCHHHHH		40.3030108239
249UbiquitinationPPAQVCLKGKLHIFK
CCHHHHHCCCEEHHH		49.20-
251UbiquitinationAQVCLKGKLHIFKYL
HHHHHCCCEEHHHHH		34.99-
251AcetylationAQVCLKGKLHIFKYL
HHHHHCCCEEHHHHH		34.9925953088
256UbiquitinationKGKLHIFKYLSTEAG
CCCEEHHHHHCCCCH		44.6829967540
267PhosphorylationTEAGQRGSALGDLAP
CCCHHCCCCCCCCCC		23.6229496963
275PhosphorylationALGDLAPSRPPSFSP
CCCCCCCCCCCCCCC		52.3823401153
279PhosphorylationLAPSRPPSFSPCPAE
CCCCCCCCCCCCCHH		40.8329255136
281PhosphorylationPSRPPSFSPCPAEDL
CCCCCCCCCCCHHHC		29.9029255136
294PhosphorylationDLFPGHRYDGGLDSG
HCCCCCCCCCCCCCC		17.1726434776
300PhosphorylationRYDGGLDSGFHSVDS
CCCCCCCCCCEECCC		48.6923684312
304PhosphorylationGLDSGFHSVDSGSKR
CCCCCCEECCCCCCC		25.9223401153
307PhosphorylationSGFHSVDSGSKRWSG
CCCEECCCCCCCCCC		42.6923401153
309PhosphorylationFHSVDSGSKRWSGNE
CEECCCCCCCCCCCC		24.0125849741
310UbiquitinationHSVDSGSKRWSGNES
EECCCCCCCCCCCCC		62.5029967540
313PhosphorylationDSGSKRWSGNESTDE
CCCCCCCCCCCCCHH		35.4630266825
317PhosphorylationKRWSGNESTDEFSEL
CCCCCCCCCHHHHHH		45.2030266825
318PhosphorylationRWSGNESTDEFSELS
CCCCCCCCHHHHHHH		33.1128464451
322PhosphorylationNESTDEFSELSFRIS
CCCCHHHHHHHHHHH		35.2628450419
342UbiquitinationPRGPRERKEDGSADG
CCCCCCCCCCCCCCC		56.2429967540
346PhosphorylationRERKEDGSADGDPVQ
CCCCCCCCCCCCCEE		35.1926657352
359PhosphorylationVQIDFIDSHVPGEDE
EEEEEECCCCCCCCC		22.9029255136
370PhosphorylationGEDEERGTVEEQRPP
CCCCCCCCCCCCCCC		30.8523186163
380PhosphorylationEQRPPELSPGAGDRE
CCCCCCCCCCCCCCC		21.4523401153
432PhosphorylationWGAPRKDSLLKPGLR
CCCCCCCCCCCCCCH		38.3423401153
435MethylationPRKDSLLKPGLRAVV
CCCCCCCCCCCHHHH		42.19115972587
435UbiquitinationPRKDSLLKPGLRAVV
CCCCCCCCCCCHHHH		42.1932142685
449PhosphorylationVGGAAAVSTQAMHNG
HCCHHHHHHHHHHCC		15.2929978859
450PhosphorylationGGAAAVSTQAMHNGS
CCHHHHHHHHHHCCC		17.4730108239
457PhosphorylationTQAMHNGSPKSSASQ
HHHHHCCCCCCHHHH		34.1830266825
460PhosphorylationMHNGSPKSSASQAGA
HHCCCCCCHHHHHHH		34.2223312004
461PhosphorylationHNGSPKSSASQAGAA
HCCCCCCHHHHHHHH		37.7623312004
463PhosphorylationGSPKSSASQAGAAAG
CCCCCHHHHHHHHCC		23.6323312004
480PhosphorylationAPAPAPASQEPLPIA
CCCCCCCCCCCCCCC		33.7323898821
491PhosphorylationLPIAGPATAPAPRPL
CCCCCCCCCCCCCCC		35.9926434776
500PhosphorylationPAPRPLGSIQRPNSF
CCCCCCCCCCCCCCE		24.1928450419
506PhosphorylationGSIQRPNSFLFRSSS
CCCCCCCCEEEECCC		26.4725159151
511PhosphorylationPNSFLFRSSSQSGSG
CCCEEEECCCCCCCC		27.3223401153
512PhosphorylationNSFLFRSSSQSGSGP
CCEEEECCCCCCCCC		28.3030266825
513PhosphorylationSFLFRSSSQSGSGPS
CEEEECCCCCCCCCC		29.6130183078
515PhosphorylationLFRSSSQSGSGPSSP
EEECCCCCCCCCCCC		36.5530266825
517PhosphorylationRSSSQSGSGPSSPDS
ECCCCCCCCCCCCCC		53.4230266825
520PhosphorylationSQSGSGPSSPDSVLR
CCCCCCCCCCCCCCC		59.0123401153
521PhosphorylationQSGSGPSSPDSVLRP
CCCCCCCCCCCCCCC		35.5430631047
524PhosphorylationSGPSSPDSVLRPRRY
CCCCCCCCCCCCCCC		26.8321712546
531PhosphorylationSVLRPRRYPQVPDEK
CCCCCCCCCCCCCHH		10.1732645325
542PhosphorylationPDEKDLMTQLRQVLE
CCHHHHHHHHHHHHH		31.5829978859
550PhosphorylationQLRQVLESRLQRPLP
HHHHHHHHHHCCCCC		33.8429978859
581PhosphorylationANQLRPRSVPFIHVP
HHHHCCCCCCEEECC		36.5029396449
589PhosphorylationVPFIHVPSPAVPKLS
CCEEECCCCCCCCHH		25.1322617229
599UbiquitinationVPKLSALKARKNVES
CCCHHHHHHHHCHHH		45.9529967540
602UbiquitinationLSALKARKNVESFLE
HHHHHHHHCHHHHHH		70.9229967540
602MalonylationLSALKARKNVESFLE
HHHHHHHHCHHHHHH		70.9226320211
623PhosphorylationVPEADLCSPSDLLQG
CCHHHCCCHHHHHHH		34.4330576142
625PhosphorylationEADLCSPSDLLQGTA
HHHCCCHHHHHHHHH		25.2927732954
631PhosphorylationPSDLLQGTARGLRTA
HHHHHHHHHHHHHHH		10.5430576142
643UbiquitinationRTALEAVKRVGGKAL
HHHHHHHHHHCCEEC		48.7132142685
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 LRCH4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRCH4_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 LRCH4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RTN4_HUMANRTN4physical
16189514
MDFI_HUMANMDFIphysical
16189514
MDFI_HUMANMDFIphysical
19060904
DOCK7_HUMANDOCK7physical
24255178
SGT1_HUMANSUGT1physical
24255178
K1C40_HUMANKRT40physical
25416956
KR107_HUMANKRTAP10-7physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
NT2NL_HUMANNOTCH2NLphysical
25416956
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 LRCH4_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-457; SER-511; SER-513;SER-515; SER-517 AND SER-521, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-183, ANDMASS SPECTROMETRY.

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