Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Ribonucleoprotein PTB-binding 2  

UniProtKB / Swiss-Prot ID :  RAVR2_HUMAN

Gene Name (Synonyms) : 
RAVER2, KIAA1579  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). Cytoplasm (By similarity). Note=May shuttle between the nucleus and the cytoplasm (By similarity). 

Protein Function :  May bind single stranded nucleic acids (Potential). 

Protein Sequence MAAAAGDGGGEGGAGLGSAAGLGPGPGLRGQGPSAEAHEGAPDPMPAALHPEEVAARLQRMQRELSNRRK...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCHHHHHHHHHHCCCCCCCCCE...
Protein Variant -
- top -

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
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAAAAG
---CCCCCC
13.05UniProtKB
Link-
18PhosphoserineAGLGSAAGL
CCCCCCCCC
21.71HPRD
Link-
18PhosphoserineAGLGSAAGL
CCCCCCCCC
21.71Phosphositeplus
Link-
190PhosphotyrosineGFVEYMKKD
EEEEECCHH
14.66Phosphositeplus
Link-
253PhosphoserineLQIFSSVHK
HHHHHHCCC
32.83HPRD
Link-
598PhosphoserineVCLSSPASK
HHHCCCCCC
16.13PhosphoELM
Link-
601PhosphoserineSSPASKTTL
CCCCCCCCC
33.64PhosphoELM
Link-
619PhosphoserineLDAISQGSE
HHHHCCCCH
30.15PhosphoELM
Link-
619PhosphoserineLDAISQGSE
HHHHCCCCH
30.15Phosphositeplus
Link-
619Phosphoserine.LDAISQGSE
HHHHCCCCH
30.15UniProtKB
Link-
624PhosphoserineQGSESQHAL
CCCHHHHHH
29.03Phosphositeplus
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
PTBP1_HUMANyeast 2-hybridHPRD:11154HPRD16051233
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
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.
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures