Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ribonuclease P protein subunit p38  

UniProtKB / Swiss-Prot ID :  RPP38_HUMAN

Gene Name (Synonyms) : 
RPP38  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus, nucleolus (Potential). 

Protein Function :  Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus. 

Protein Sequence MAAAPQAPGRGSLRKTRPLVVKTSLNNPYIIRWSALESEDMHFILQTLEDRLKAIGLQKIEDKKKKNKTP...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCEEEEEECCCCEEEEEECCCHHHHHHHHHHHHHHHHHHCHHHHHHHHHHHCCC...
Protein Variant
LocationDescription
86I -> V (in dbSNP:rs3814171). VAR_051811
88E -> D (in dbSNP:rs1052157). VAR_023960
114A -> V (in dbSNP:rs1132078). VAR_023961
181A -> G (in dbSNP:rs15772). VAR_023962
202S -> R (in dbSNP:rs12249258). VAR_051812
212I -> T (in dbSNP:rs10242). VAR_029298
250R -> G (in dbSNP:rs34040166). VAR_051813
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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
12PhosphoserinePGRGSLRKT
CCCCCCCCC
24.52HPRD
Link-
12PhosphoserinePGRGSLRKT
CCCCCCCCC
24.52Phosphositeplus
Link-
221PhosphothreonineENLETEPLE
CCCCCCCCH
46.17HPRD
Link-
221PhosphothreonineENLETEPLE
CCCCCCCCH
46.17PhosphoELM
Link-
226PhosphoserineEPLESQDRE
CCCHHHHHH
45.09HPRD
Link-
226PhosphoserineEPLESQDRE
CCCHHHHHH
45.09PhosphoELM
Link-
226PhosphoserineEPLESQDRE
CCCHHHHHH
45.09Phosphositeplus
Link-
234PhosphothreonineELLDTSFED
HHHHCCHHH
34.97HPRD
Link-
234PhosphothreonineELLDTSFED
HHHHCCHHH
34.97PhosphoELM
Link-
234PhosphothreonineELLDTSFED
HHHHCCHHH
34.97Phosphositeplus
Link-
235PhosphoserineLLDTSFEDL
HHHCCHHHH
26.72HPRD
Link-
235PhosphoserineLLDTSFEDL
HHHCCHHHH
26.72PhosphoELM
Link-
235PhosphoserineLLDTSFEDL
HHHCCHHHH
26.72Phosphositeplus
Link-
235PhosphoserineLLDTSFEDL
HHHCCHHHH
26.72SysPTM
Link-
235Phosphoserine.LLDTSFEDL
HHHCCHHHH
26.72UniProtKB
Link-
240PhosphoserineFEDLSKPKR
HHHHHHHHH
60.27HPRD
Link-
240PhosphoserineFEDLSKPKR
HHHHHHHHH
60.27PhosphoELM
Link-
255PhosphothreonineQASVTLQPL
CCCEEEECE
19.72Phosphositeplus
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
POP1_HUMANphysical interactionEBI-366502
intact15096576
RPP29_HUMANphysical interaction
physical interaction
EBI-366535
EBI-366610
intact15096576
15096576
POP1_HUMANyeast 2-hybridHPRD:09360HPRD11455963
POP7_HUMANin vivoHPRD:09360HPRD9630247
RPP29_HUMANyeast 2-hybridHPRD:09360HPRD11455963
RPP30_HUMANin vivoHPRD:09360HPRD9630247
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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
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-235, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures