Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Protein RRP5 homolog  

UniProtKB / Swiss-Prot ID :  RRP5_HUMAN

Gene Name (Synonyms) : 
PDCD11, KIAA0185  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nucleolus. 

Protein Function :  Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA. Involved in the biogenesis of rRNA (By similarity). 

Protein Sequence MANLEESFPRGGTRKIHKPEKAFQQSVEQDNLFDISTEEGSTKRKKSQKGPAKTKKLKIEKRESSKSARE...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCEECCCHHCCHHHHH...
Protein Variant
LocationDescription
397S -> N (in dbSNP:rs7074814). VAR_054485
623A -> S (in dbSNP:rs11598673). VAR_031669
780A -> S (in dbSNP:rs11591914). VAR_054486
1216L -> F (in dbSNP:rs2986014). VAR_031670
1453P -> S (in dbSNP:rs2274289). VAR_054487
1871D -> A (in dbSNP:rs7831). VAR_014930
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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.---MANLEE
---CCCCCC
40.39UniProtKB
Link-
7PhosphoserineNLEESFPRG
CCCCCCCCC
31.04HPRD
Link-
7PhosphoserineNLEESFPRG
CCCCCCCCC
31.04Phosphositeplus
Link-
7Phosphoserine.NLEESFPRG
CCCCCCCCC
31.04UniProtKB
Link-
13PhosphothreoninePRGGTRKIH
CCCCCCCCC
31.45Phosphositeplus
Link-
36PhosphoserineLFDISTEEG
HCCCCCCCC
31.45HPRD
Link-
36PhosphoserineLFDISTEEG
HCCCCCCCC
31.45PhosphoELM
Link-
37PhosphothreonineFDISTEEGS
CCCCCCCCC
38.09HPRD
Link-
37PhosphothreonineFDISTEEGS
CCCCCCCCC
38.09PhosphoELM
Link-
89S-nitrosocysteineRILGCVKEV
EEEEEEEEE
3.37dbSNO
Link-
219Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LPLLKAQEY
ECCCHHHHH
56.56Phosphositeplus
Link
437PhosphothreonineLSLRTSIIE
EEHHHHHHH
29.57HPRD
Link-
437Phosphothreonine.LSLRTSIIE
EEHHHHHHH
29.57UniProtKB
Link-
438PhosphoserineSLRTSIIEA
EHHHHHHHH
18.35HPRD
Link-
438PhosphoserineSLRTSIIEA
EHHHHHHHH
18.35PhosphoELM
Link-
438PhosphoserineSLRTSIIEA
EHHHHHHHH
18.35Phosphositeplus
Link-
438Phosphoserine.SLRTSIIEA
EHHHHHHHH
18.35UniProtKB
Link-
459PhosphothreonineVVKGTVLTI
EEEEEEEEE
13.46HPRD
Link-
520PhosphothreonineKLMMTLKKT
EEEEEHHHH
22.81HPRD
Link-
1206PhosphothreonineALRATVVGP
EEEEEEEEC
14.86Phosphositeplus
Link-
1346PhosphoserineRLGPSVVGL
EECCCCEEE
27.86HPRD
Link-
1346PhosphoserineRLGPSVVGL
EECCCCEEE
27.86Phosphositeplus
Link-
1360PhosphoserineVSQHSPSKK
EEECCCCCC
24.19HPRD
Link-
1360PhosphoserineVSQHSPSKK
EEECCCCCC
24.19PhosphoELM
Link-
1360PhosphoserineVSQHSPSKK
EEECCCCCC
24.19Phosphositeplus
Link-
1360PhosphoserineVSQHSPSKK
EEECCCCCC
24.19SysPTM
Link-
1360Phosphoserine.VSQHSPSKK
EEECCCCCC
24.19UniProtKB
Link-
1362PhosphoserineQHSPSKKAL
ECCCCCCCC
50.21Phosphositeplus
Link-
1454PhosphoserineVEMPSKEKQ
CCCCCCCCC
52.73HPRD
Link-
1454PhosphoserineVEMPSKEKQ
CCCCCCCCC
52.73Phosphositeplus
Link-
1454Phosphoserine.VEMPSKEKQ
CCCCCCCCC
52.73UniProtKB
Link-
1493PhosphoserineKAGLSEEDD
HCCCCCCCC
37.71HPRD
Link-
1493PhosphoserineKAGLSEEDD
HCCCCCCCC
37.71PhosphoELM
Link-
1493PhosphoserineKAGLSEEDD
HCCCCCCCC
37.71Phosphositeplus
Link-
1493PhosphoserineKAGLSEEDD
HCCCCCCCC
37.71SysPTM
Link-
1493Phosphoserine.KAGLSEEDD
HCCCCCCCC
37.71UniProtKB
Link-
1498PhosphoserineEEDDSLVDV
CCCCCCCCC
42.48HPRD
Link-
1498PhosphoserineEEDDSLVDV
CCCCCCCCC
42.48PhosphoELM
Link-
1498PhosphoserineEEDDSLVDV
CCCCCCCCC
42.48Phosphositeplus
Link-
1498PhosphoserineEEDDSLVDV
CCCCCCCCC
42.48SysPTM
Link-
1498Phosphoserine.EEDDSLVDV
CCCCCCCCC
42.48UniProtKB
Link-
1781Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AERAKAIFE
HHHHHHHHH
48.51Phosphositeplus
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, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-437; SER-438 ANDSER-1454, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1498, 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-1493 AND SER-1498, ANDMASS SPECTROMETRY.
"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-1360, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-437; SER-438 ANDSER-1454, ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures