LRC47_HUMAN - dbPTM
LRC47_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LRC47_HUMAN
UniProt AC Q8N1G4
Protein Name Leucine-rich repeat-containing protein 47
Gene Name LRRC47
Organism Homo sapiens (Human).
Sequence Length 583
Subcellular Localization
Protein Description
Protein Sequence MAAAAVSESWPELELAERERRRELLLTGPGLEERVRAAGGQLPPRLFTLPLLHYLEVSGCGSLRAPGPGLAQGLPQLHSLVLRRNALGPGLSPELGPLPALRVLDLSGNALEALPPGQGLGPAEPPGLPQLQSLNLSGNRLRELPADLARCAPRLQSLNLTGNCLDSFPAELFRPGALPLLSELAAADNCLRELSPDIAHLASLKTLDLSNNQLSEIPAELADCPKLKEINFRGNKLRDKRLEKMVSGCQTRSILEYLRVGGRGGGKGKGRAEGSEKEESRRKRRERKQRREGGDGEEQDVGDAGRLLLRVLHVSENPVPLTVRVSPEVRDVRPYIVGAVVRGMDLQPGNALKRFLTSQTKLHEDLCEKRTAATLATHELRAVKGPLLYCARPPQDLKIVPLGRKEAKAKELVRQLQLEAEEQRKQKKRQSVSGLHRYLHLLDGNENYPCLVDADGDVISFPPITNSEKTKVKKTTSDLFLEVTSATSLQICKDVMDALILKMAEMKKYTLENKEEGSLSDTEADAVSGQLPDPTTNPSAGKDGPSLLVVEQVRVVDLEGSLKVVYPSKADLATAPPHVTVVR
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
2Acetylation------MAAAAVSES
------CCCHHHCCC		13.0522223895
7Phosphorylation-MAAAAVSESWPELE
-CCCHHHCCCCHHHH		22.6128348404
9PhosphorylationAAAAVSESWPELELA
CCHHHCCCCHHHHHH		40.1928348404
27PhosphorylationRRRELLLTGPGLEER
HHHHHHHHCCCHHHH		41.1024043423
54PhosphorylationFTLPLLHYLEVSGCG
HHHCCHHEEECCCCC		12.4322817900
92PhosphorylationNALGPGLSPELGPLP
CCCCCCCCCCCCCCC		23.4222199227
195PhosphorylationDNCLRELSPDIAHLA
HHHHHHHCHHHHHHH		18.7728674419
215O-linked_GlycosylationDLSNNQLSEIPAELA
CCCCCCHHHCCHHHC		24.5823301498
224GlutathionylationIPAELADCPKLKEIN
CCHHHCCCCCCEECC		2.3922555962
226UbiquitinationAELADCPKLKEINFR
HHHCCCCCCEECCCC		77.7629967540
226AcetylationAELADCPKLKEINFR
HHHCCCCCCEECCCC		77.7625953088
228MalonylationLADCPKLKEINFRGN
HCCCCCCEECCCCCC		63.7826320211
228UbiquitinationLADCPKLKEINFRGN
HCCCCCCEECCCCCC		63.7829967540
228AcetylationLADCPKLKEINFRGN
HCCCCCCEECCCCCC		63.7826051181
244MalonylationLRDKRLEKMVSGCQT
HHHHHHHHHHCCHHH		49.5532601280
244AcetylationLRDKRLEKMVSGCQT
HHHHHHHHHHCCHHH		49.5525953088
244UbiquitinationLRDKRLEKMVSGCQT
HHHHHHHHHHCCHHH		49.5524816145
257PhosphorylationQTRSILEYLRVGGRG
HHHHHHHHHCCCCCC		9.07-
275PhosphorylationGKGRAEGSEKEESRR
CCCCCCCCHHHHHHH		36.6826091039
315PhosphorylationLLRVLHVSENPVPLT
HHEEEECCCCCCCEE		22.4028857561
333DimethylationSPEVRDVRPYIVGAV
CCHHHCCCHHEEEEE		23.69-
333MethylationSPEVRDVRPYIVGAV
CCHHHCCCHHEEEEE		23.6930762557
335PhosphorylationEVRDVRPYIVGAVVR
HHHCCCHHEEEEEEC		9.5528152594
3532-HydroxyisobutyrylationLQPGNALKRFLTSQT
CCCCHHHHHHHHHCC		38.40-
353AcetylationLQPGNALKRFLTSQT
CCCCHHHHHHHHHCC		38.4025953088
353UbiquitinationLQPGNALKRFLTSQT
CCCCHHHHHHHHHCC		38.4024816145
353MalonylationLQPGNALKRFLTSQT
CCCCHHHHHHHHHCC		38.4032601280
357PhosphorylationNALKRFLTSQTKLHE
HHHHHHHHHCCHHCH		18.9726852163
357O-linked_GlycosylationNALKRFLTSQTKLHE
HHHHHHHHHCCHHCH		18.97OGP
358PhosphorylationALKRFLTSQTKLHED
HHHHHHHHCCHHCHH		37.6926852163
358O-linked_GlycosylationALKRFLTSQTKLHED
HHHHHHHHCCHHCHH		37.69OGP
360O-linked_GlycosylationKRFLTSQTKLHEDLC
HHHHHHCCHHCHHHH		35.03OGP
361UbiquitinationRFLTSQTKLHEDLCE
HHHHHCCHHCHHHHH		39.9629967540
361AcetylationRFLTSQTKLHEDLCE
HHHHHCCHHCHHHHH		39.9625953088
369AcetylationLHEDLCEKRTAATLA
HCHHHHHHHHHHHHH		54.7925953088
369UbiquitinationLHEDLCEKRTAATLA
HCHHHHHHHHHHHHH		54.7929967540
371PhosphorylationEDLCEKRTAATLATH
HHHHHHHHHHHHHHH		31.5423403867
374PhosphorylationCEKRTAATLATHELR
HHHHHHHHHHHHHHH		17.9228857561
377PhosphorylationRTAATLATHELRAVK
HHHHHHHHHHHHHCC		20.9928509920
398UbiquitinationARPPQDLKIVPLGRK
CCCCCCCCEEECCCH		50.3629967540
410UbiquitinationGRKEAKAKELVRQLQ
CCHHHHHHHHHHHHH		51.3724816145
431PhosphorylationRKQKKRQSVSGLHRY
HHHHHHHCHHHHHHH		23.4525159151
433O-linked_GlycosylationQKKRQSVSGLHRYLH
HHHHHCHHHHHHHHH		40.6723301498
433PhosphorylationQKKRQSVSGLHRYLH
HHHHHCHHHHHHHHH		40.6730266825
502UbiquitinationVMDALILKMAEMKKY
HHHHHHHHHHHHHHC		29.1329967540
509PhosphorylationKMAEMKKYTLENKEE
HHHHHHHCCCCCCCC		15.8430278072
510PhosphorylationMAEMKKYTLENKEEG
HHHHHHCCCCCCCCC		36.1523401153
518PhosphorylationLENKEEGSLSDTEAD
CCCCCCCCCCCCHHH		28.1629255136
520PhosphorylationNKEEGSLSDTEADAV
CCCCCCCCCCHHHHH		44.1529255136
522PhosphorylationEEGSLSDTEADAVSG
CCCCCCCCHHHHHCC		29.6923927012
528PhosphorylationDTEADAVSGQLPDPT
CCHHHHHCCCCCCCC		23.6530278072
535PhosphorylationSGQLPDPTTNPSAGK
CCCCCCCCCCCCCCC		46.7323927012
536PhosphorylationGQLPDPTTNPSAGKD
CCCCCCCCCCCCCCC		50.9823927012
539PhosphorylationPDPTTNPSAGKDGPS
CCCCCCCCCCCCCCE		52.2923927012
546PhosphorylationSAGKDGPSLLVVEQV
CCCCCCCEEEEEEEE		39.6026074081
561PhosphorylationRVVDLEGSLKVVYPS
EEEECCCCEEEEECC		18.6825850435
566PhosphorylationEGSLKVVYPSKADLA
CCCEEEEECCHHHHC		12.5523312004
568PhosphorylationSLKVVYPSKADLATA
CEEEEECCHHHHCCC		23.8423312004
569MalonylationLKVVYPSKADLATAP
EEEEECCHHHHCCCC		41.2226320211
569UbiquitinationLKVVYPSKADLATAP
EEEEECCHHHHCCCC		41.2229967540
569AcetylationLKVVYPSKADLATAP
EEEEECCHHHHCCCC		41.2225953088
574PhosphorylationPSKADLATAPPHVTV
CCHHHHCCCCCCEEE		47.1723312004
580PhosphorylationATAPPHVTVVR----
CCCCCCEEECC----		15.3923312004
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 LRC47_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LRC47_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 LRC47_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TOPK_HUMANPBKphysical
22939629
RHG19_HUMANARHGAP19physical
22939629
TCPG_HUMANCCT3physical
22863883
SYEP_HUMANEPRSphysical
22863883
GAPD1_HUMANGAPVD1physical
22863883
IQGA1_HUMANIQGAP1physical
22863883
PP4R2_HUMANPPP4R2physical
22863883
KPRB_HUMANPRPSAP2physical
22863883
EIF2A_HUMANEIF2Aphysical
26344197
PNCB_HUMANNAPRTphysical
26344197
PSB6_HUMANPSMB6physical
26344197
EXOS4_HUMANEXOSC4physical
27173435
EXOS2_HUMANEXOSC2physical
27173435
EXOS7_HUMANEXOSC7physical
27173435
EXOS9_HUMANEXOSC9physical
27173435
LUM_HUMANLUMphysical
27173435
RSRC1_HUMANRSRC1physical
27173435
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 LRC47_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-518; SER-520 AND THR-522, AND MASSSPECTROMETRY.
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 TYR-509 AND SER-520, ANDMASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-518; SER-520 AND THR-522, 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-520, AND MASSSPECTROMETRY.
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-431, 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 THR-522, AND MASSSPECTROMETRY.

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