Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Leucine-rich repeat-containing protein 47  

UniProtKB / Swiss-Prot ID :  LRC47_HUMAN

Gene Name (Synonyms) : 
LRRC47, KIAA1185  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :   

Protein Sequence MAAAAVSESWPELELAERERRRELLLTGPGLEERVRAAGGQLPPRLFTLPLLHYLEVSGCGSLRAPGPGL...
Predicted Secondary Structure CCCHHHHHHCCCCHHHHCCCCCEEEECCCCCCEECCCCCCCCCHHHHCCCCCEEEEECCCCCCCCCCCHH...
Protein Variant
LocationDescription
193E -> D (in a colorectal cancer sample;somatic mutation).
545P -> L (in dbSNP:rs11547614). VAR_051118
581V -> I (in dbSNP:rs11547615). VAR_051119
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAV
---CCCHHH
13.05UniProtKB
Link-
54PhosphotyrosinePLLHYLEVS
CCCEEEEEC
12.43Phosphositeplus
Link-
431PhosphoserineKKRQSVSGL
CCCCCCCCC
23.45HPRD
Link-
431PhosphoserineKKRQSVSGL
CCCCCCCCC
23.45Phosphositeplus
Link-
431Phosphoserine.KKRQSVSGL
CCCCCCCCC
23.45UniProtKB
Link-
433PhosphoserineRQSVSGLHR
CCCCCCCHH
40.67Phosphositeplus
Link-
509PhosphotyrosineEMKKYTLEN
HCCCCEEEE
15.84HPRD
Link-
509PhosphotyrosineEMKKYTLEN
HCCCCEEEE
15.84PhosphoELM
Link-
509PhosphotyrosineEMKKYTLEN
HCCCCEEEE
15.84Phosphositeplus
Link-
509Phosphotyrosine.EMKKYTLEN
HCCCCEEEE
15.84UniProtKB
Link-
510PhosphothreonineMKKYTLENK
CCCCEEEEE
36.15HPRD
Link-
510PhosphothreonineMKKYTLENK
CCCCEEEEE
36.15PhosphoELM
Link-
518PhosphoserineKEEGSLSDT
EECCCCCCC
28.16HPRD
Link-
518PhosphoserineKEEGSLSDT
EECCCCCCC
28.16PhosphoELM
Link-
518PhosphoserineKEEGSLSDT
EECCCCCCC
28.16Phosphositeplus
Link-
518Phosphoserine.KEEGSLSDT
EECCCCCCC
28.16UniProtKB
Link-
520PhosphoserineEGSLSDTEA
CCCCCCCCC
44.15HPRD
Link-
520PhosphoserineEGSLSDTEA
CCCCCCCCC
44.15PhosphoELM
Link-
520PhosphoserineEGSLSDTEA
CCCCCCCCC
44.15Phosphositeplus
Link-
520PhosphoserineEGSLSDTEA
CCCCCCCCC
44.15SysPTM
Link-
520Phosphoserine.EGSLSDTEA
CCCCCCCCC
44.15UniProtKB
Link-
522PhosphothreonineSLSDTEADA
CCCCCCCCC
29.69HPRD
Link-
522PhosphothreonineSLSDTEADA
CCCCCCCCC
29.69PhosphoELM
Link-
522PhosphothreonineSLSDTEADA
CCCCCCCCC
29.69Phosphositeplus
Link-
522PhosphothreonineSLSDTEADA
CCCCCCCCC
29.69SysPTM
Link-
522Phosphothreonine.SLSDTEADA
CCCCCCCCC
29.69UniProtKB
Link-
525Caspase cleavage aspartic acidDTEADAVSG
CCCCCCCCC
41.07Phosphositeplus
Link-
528PhosphoserineADAVSGQLP
CCCCCCCCC
23.65Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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
"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.
"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.
"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.
"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.
"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.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures