RAVR1_MOUSE - dbPTM
RAVR1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RAVR1_MOUSE
UniProt AC Q9CW46
Protein Name Ribonucleoprotein PTB-binding 1
Gene Name Raver1
Organism Mus musculus (Mouse).
Sequence Length 748
Subcellular Localization Nucleus . Cytoplasm . Nuclear, in perinucleolar structures. Shuttles between nucleus and cytoplasm. Cytoplasm, at focal contacts and cell-cell contacts. Associated with myotubes during muscle differentiation.
Protein Description 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..
Protein Sequence MAADVSVTHRPPLSPEAEAEAETPETVDRRAPEQELPPLDPEEIRKRLEHTERQFRNRRKILIRGLPGDVTNQEVHDLLSDYELKYCFVDKYKGTAFVTLLNGEQAEAAINTFHQSRLRERELSVQLQPTDALLCVANLPPSLTQAQFEELVRPFGSLERCFLVYSERTGHSKGYGFAEYMKKDSAARAKSDLLGKPLGPRTLYVHWTDAGQLTPALLHSRCLCVDHLPPGFSDVDALRRALSVVYTPTFCQLACGQDGQLKGFAVLEYETAEMAEAAQERADGQALGDSHLRVSFCAPGPPGRSMLAALIAAQATALNRGKGLLPEPNLLQLLNNLGPSASLQLLLNPLLHGGASGKQGLLGAPPAMPLLSGPALSTALLQLALQSQSQNQSQGQKKPGILGDSPLGTLQAGAQPSNSLLGELSAGGGLAPELPPRRGKPQPLLPPLLGPSGGDREPMGLGPPATQLTPPPAPVGLRGSNHRGLPKDSGPLPTPPGVSLLGEPPKDYRIPLNPYLNLHSLLPSSNLAGKETRGWGGSGRGRRPAEPPLPSPAVPGGGSGSNNGNKAFQMKSRLLSPIASNRLPPEPGLPDSYGFDYPTDVGPRRLFSHPREPTLGAHGPSRHKMSPPPSSFNEPRSGGGSGGPLSHFYSGSPTSYFTSGLQAGLKQSHLNKAVGSSPMGSSEGLLGLGPGPNGHSHLLKTPLGGQKRSFSHLLPSPEPSPEGSYVGQHSQGLGGHYADSYLKRKRIF
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAADVSVTH
------CCCCCEECC		16.6319131326
6Phosphorylation--MAADVSVTHRPPL
--CCCCCEECCCCCC		23.1127742792
8PhosphorylationMAADVSVTHRPPLSP
CCCCCEECCCCCCCH		12.5027742792
14PhosphorylationVTHRPPLSPEAEAEA
ECCCCCCCHHHHHHC		26.8523527152
23PhosphorylationEAEAEAETPETVDRR
HHHHHCCCCCCCCCC		33.2126824392
26PhosphorylationAEAETPETVDRRAPE
HHCCCCCCCCCCCCC		28.9825168779
91AcetylationLKYCFVDKYKGTAFV
EEEEEEECCCCEEEE		43.4922826441
185PhosphorylationAEYMKKDSAARAKSD
HHHHHHHHHHHHHHH		32.4822817900
222S-nitrosylationPALLHSRCLCVDHLP
HHHHHCCEEECCCCC		3.7620925432
222S-nitrosocysteinePALLHSRCLCVDHLP
HHHHHCCEEECCCCC		3.76-
247PhosphorylationRALSVVYTPTFCQLA
HHHHHHCCCCCHHHH		12.30-
249PhosphorylationLSVVYTPTFCQLACG
HHHHCCCCCHHHHCC		29.28-
255GlutathionylationPTFCQLACGQDGQLK
CCCHHHHCCCCCCEE		7.3724333276
316PhosphorylationALIAAQATALNRGKG
HHHHHHHHHHHCCCC		21.4326026062
405PhosphorylationKPGILGDSPLGTLQA
CCCCCCCCCCCCCCC		21.8926643407
409PhosphorylationLGDSPLGTLQAGAQP
CCCCCCCCCCCCCCC		24.3126643407
452PhosphorylationLPPLLGPSGGDREPM
CCCCCCCCCCCCCCC		54.3225159016
466PhosphorylationMGLGPPATQLTPPPA
CCCCCCCCCCCCCCC		29.8625159016
469PhosphorylationGPPATQLTPPPAPVG
CCCCCCCCCCCCCCC		24.7526824392
480PhosphorylationAPVGLRGSNHRGLPK
CCCCCCCCCCCCCCC		24.03-
489PhosphorylationHRGLPKDSGPLPTPP
CCCCCCCCCCCCCCC		48.7321149613
494PhosphorylationKDSGPLPTPPGVSLL
CCCCCCCCCCCCCCC		50.2026824392
499PhosphorylationLPTPPGVSLLGEPPK
CCCCCCCCCCCCCCC		24.6421149613
508PhosphorylationLGEPPKDYRIPLNPY
CCCCCCCCCCCCCCC		19.3025777480
525PhosphorylationLHSLLPSSNLAGKET
HHHCCCCCCCCCCCC		33.64-
538PhosphorylationETRGWGGSGRGRRPA
CCCCCCCCCCCCCCC		22.7527149854
551PhosphorylationPAEPPLPSPAVPGGG
CCCCCCCCCCCCCCC		32.9227087446
559PhosphorylationPAVPGGGSGSNNGNK
CCCCCCCCCCCCCCH		42.1818846507
561PhosphorylationVPGGGSGSNNGNKAF
CCCCCCCCCCCCHHH		28.9018846507
572PhosphorylationNKAFQMKSRLLSPIA
CHHHHHHHHHHCHHH		23.8726239621
576PhosphorylationQMKSRLLSPIASNRL
HHHHHHHCHHHHCCC		20.8927087446
580PhosphorylationRLLSPIASNRLPPEP
HHHCHHHHCCCCCCC		24.1726239621
592PhosphorylationPEPGLPDSYGFDYPT
CCCCCCCCCCCCCCC		25.8024759943
593PhosphorylationEPGLPDSYGFDYPTD
CCCCCCCCCCCCCCC		29.2325777480
597PhosphorylationPDSYGFDYPTDVGPR
CCCCCCCCCCCCCCC		13.0325777480
614PhosphorylationFSHPREPTLGAHGPS
CCCCCCCCCCCCCCC		32.8329176673
621PhosphorylationTLGAHGPSRHKMSPP
CCCCCCCCCCCCCCC		52.1627149854
625OxidationHGPSRHKMSPPPSSF
CCCCCCCCCCCCHHC		6.2517242355
626PhosphorylationGPSRHKMSPPPSSFN
CCCCCCCCCCCHHCC		38.7727087446
630PhosphorylationHKMSPPPSSFNEPRS
CCCCCCCHHCCCCCC		54.0227742792
631PhosphorylationKMSPPPSSFNEPRSG
CCCCCCHHCCCCCCC		37.5527742792
637PhosphorylationSSFNEPRSGGGSGGP
HHCCCCCCCCCCCCC		53.1326160508
641PhosphorylationEPRSGGGSGGPLSHF
CCCCCCCCCCCCHHC		43.8026160508
646PhosphorylationGGSGGPLSHFYSGSP
CCCCCCCHHCCCCCC		18.0626160508
649PhosphorylationGGPLSHFYSGSPTSY
CCCCHHCCCCCCCHH		13.4926745281
650PhosphorylationGPLSHFYSGSPTSYF
CCCHHCCCCCCCHHH		31.6726239621
652PhosphorylationLSHFYSGSPTSYFTS
CHHCCCCCCCHHHHH		21.0426239621
654PhosphorylationHFYSGSPTSYFTSGL
HCCCCCCCHHHHHHH		37.4426239621
655PhosphorylationFYSGSPTSYFTSGLQ
CCCCCCCHHHHHHHH		22.9526745281
656PhosphorylationYSGSPTSYFTSGLQA
CCCCCCHHHHHHHHH		17.2226160508
658PhosphorylationGSPTSYFTSGLQAGL
CCCCHHHHHHHHHHH		17.4125293948
659PhosphorylationSPTSYFTSGLQAGLK
CCCHHHHHHHHHHHC		27.8326643407
676PhosphorylationHLNKAVGSSPMGSSE
HHHHHHCCCCCCCCC		25.3523984901
677PhosphorylationLNKAVGSSPMGSSEG
HHHHHCCCCCCCCCC		16.9923984901
681PhosphorylationVGSSPMGSSEGLLGL
HCCCCCCCCCCCCCC		20.9723984901
682PhosphorylationGSSPMGSSEGLLGLG
CCCCCCCCCCCCCCC		29.9223984901
709PhosphorylationPLGGQKRSFSHLLPS
CCCCCCCCHHHCCCC		37.8325777480
711PhosphorylationGGQKRSFSHLLPSPE
CCCCCCHHHCCCCCC		17.9325777480
716PhosphorylationSFSHLLPSPEPSPEG
CHHHCCCCCCCCCCC		41.6926824392
720PhosphorylationLLPSPEPSPEGSYVG
CCCCCCCCCCCCCCC		33.6416141072
724PhosphorylationPEPSPEGSYVGQHSQ
CCCCCCCCCCCCCCC		18.2525777480
725PhosphorylationEPSPEGSYVGQHSQG
CCCCCCCCCCCCCCC		21.3226643407
730PhosphorylationGSYVGQHSQGLGGHY
CCCCCCCCCCCCCCC		20.3225777480
737PhosphorylationSQGLGGHYADSYLKR
CCCCCCCCCHHHHHH		18.5125777480
740PhosphorylationLGGHYADSYLKRKRI
CCCCCCHHHHHHCCC		24.9625777480
741PhosphorylationGGHYADSYLKRKRIF
CCCCCHHHHHHCCCC		19.4525777480
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of RAVR1_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RAVR1_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RAVR1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTN4_MOUSEActn4physical
11724819
ACTN2_MOUSEActn2physical
11724819
PTBP3_MOUSEPtbp3physical
11724819
VINC_MOUSEVclphysical
11724819
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RAVR1_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND THR-469, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-576 AND SER-626, ANDMASS SPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, AND MASSSPECTROMETRY.

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