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 1  

UniProtKB / Swiss-Prot ID :  RAVR1_HUMAN

Gene Name (Synonyms) : 
RAVER1, KIAA1978  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus (By similarity). Cytoplasm (By similarity). Note=Nuclear, in perinucleolar structures. Shuttles between nucleus and cytoplasm. Cytoplasm, at focal contacts and cell-cell contacts. Associated with myotubes during muscle differentiation (By similar 

Protein Function :  Cooperates with PTBP1 to modulate regulated alternative splicing events. Promotes exon skipping. Cooperates with PTBP1 to modulate switching between mutually exclusive exons during maturation of the TPM1 pre-mRNA (By similarity). 

Protein Sequence MAADVSVTHRPPLSPKSGAEVEAGDAAERRAPEEELPPLDPEEIRKRLEHTERQFRNRRKILIRGLPGDV...
Predicted Secondary Structure CCHHHHCCCCCCCCCCCCCCCCCHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCEEEEECCCCCC...
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.---MAADVS
---CCHHHH
16.63UniProtKB
Link-
6PhosphoserineAADVSVTHR
CHHHHCCCC
23.11SysPTM
Link-
8PhosphothreonineDVSVTHRPP
HHHCCCCCC
12.50SysPTM
Link-
14PhosphoserineRPPLSPKSG
CCCCCCCCC
35.74SysPTM
Link-
14PhosphoserineRPPLSPKSG
CCCCCCCCC
35.74SysPTM
Link-
14Phosphoserine.RPPLSPKSG
CCCCCCCCC
35.74UniProtKB
Link-
17PhosphoserineLSPKSGAEV
CCCCCCCCC
46.77SysPTM
Link-
17Phosphoserine.LSPKSGAEV
CCCCCCCCC
46.77UniProtKB
Link-
175PhosphotyrosineQSKGYGFAE
CCCCEEEEE
16.89Phosphositeplus
Link
463PhosphothreonineAAQLTPPPA
CCCCCCCCC
22.97PhosphoELM
Link-
463PhosphothreonineAAQLTPPPA
CCCCCCCCC
22.97SysPTM
Link-
463PhosphothreonineAAQLTPPPA
CCCCCCCCC
22.97SysPTM
Link-
463Phosphothreonine.AAQLTPPPA
CCCCCCCCC
22.97UniProtKB
Link-
474PhosphoserineGLRGSGLRG
CCCCCCCCC
28.37SysPTM
Link-
474Phosphoserine.GLRGSGLRG
CCCCCCCCC
28.37UniProtKB
Link-
512PhosphoserineAIGSSPLGS
HCCCCCCCC
20.94SysPTM
Link-
512Phosphoserine.AIGSSPLGS
HCCCCCCCC
20.94UniProtKB
Link-
524PhosphoserineLLGLSPGPN
CCCCCCCCC
26.47SysPTM
Link-
524Phosphoserine.LLGLSPGPN
CCCCCCCCC
26.47UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
ACTN2_HUMANin vivo
yeast 2-hybrid
HPRD:11484HPRD11724819
ACTN1_HUMANin vivoHPRD:11484HPRD11724819
VINC_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:11484HPRD11724819
PTBP1_HUMANin vivo
yeast 2-hybrid
HPRD:11484HPRD11724819
- 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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-14 AND THR-463, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, 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 SER-14, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463, AND MASSSPECTROMETRY.
"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-14; THR-463; SER-512 ANDSER-524, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567; SER-617;SER-707 AND SER-711 (ISOFORM 2), AND MASS SPECTROMETRY.
"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-17; THR-463; SER-474;SER-512 AND SER-524, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-567(ISOFORM 2), AND MASS 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-14 AND THR-463, AND MASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures