RALY_MOUSE - dbPTM
RALY_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RALY_MOUSE
UniProt AC Q64012
Protein Name RNA-binding protein Raly
Gene Name Raly
Organism Mus musculus (Mouse).
Sequence Length 312
Subcellular Localization Nucleus .
Protein Description RNA-binding protein that acts as a transcriptional cofactor for cholesterol biosynthetic genes in the liver. [PubMed: 27251289 Binds the lipid-responsive non-coding RNA LeXis and is required for LeXis-mediated effect on cholesterogenesis]
Protein Sequence MSLKIQTSNVTNKNDPKSINSRVFIGNLNTAVVKKSDVETIFSKYGRVAGCSVHKGYAFVQYANERHARAAVLGENGRVLAGQTLDINMAGEPKPNRPKGLKRAATAIYSGYSFDYDYYQDYFCARLFDYRGRLSPVPVPRAVPVKRPRVTVPLVRRVKTTIPVKLFARSTAVTTGSAKIKLKSSELQTIKTELTQIKSNIDALLGRLEQIAEEQKANPDGKKKGDSSSGGGGGSSGGGGSSNVGGGSSGGSGSCSSSSRLPAPQEDTASEAGTPQGEVQTRDDGDEEGLLTHSEEELEHSQDTDAEDGALQ
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
2Phosphorylation------MSLKIQTSN
------CCCEEECCC		38.0724719451
2Acetylation------MSLKIQTSN
------CCCEEECCC		38.07-
36PhosphorylationNTAVVKKSDVETIFS
CEEEEEHHHHHHHHH		40.97-
44AcetylationDVETIFSKYGRVAGC
HHHHHHHHHCCCCCC		40.7623806337
52PhosphorylationYGRVAGCSVHKGYAF
HCCCCCCEEECCCEE		26.7529514104
55AcetylationVAGCSVHKGYAFVQY
CCCCEEECCCEEEEE		52.0022826441
57PhosphorylationGCSVHKGYAFVQYAN
CCEEECCCEEEEECC		11.1528066266
106 (in isoform 2)Phosphorylation-16.7724453211
109 (in isoform 2)Phosphorylation-8.1229514104
119 (in isoform 2)Phosphorylation-7.6327818261
135PhosphorylationFDYRGRLSPVPVPRA
CCCCCCCCCCCCCCC		23.6124925903
151PhosphorylationPVKRPRVTVPLVRRV
CCCCCCEECEEEEEE		20.0622807455
160PhosphorylationPLVRRVKTTIPVKLF
EEEEEECCCCCEEEE		27.4029176673
161PhosphorylationLVRRVKTTIPVKLFA
EEEEECCCCCEEEEE		19.9829176673
165AcetylationVKTTIPVKLFARSTA
ECCCCCEEEEEECEE		32.3123806337
165UbiquitinationVKTTIPVKLFARSTA
ECCCCCEEEEEECEE		32.3122790023
171PhosphorylationVKLFARSTAVTTGSA
EEEEEECEEEEECCE		21.4228285833
174PhosphorylationFARSTAVTTGSAKIK
EEECEEEEECCEEEE		23.9929550500
175PhosphorylationARSTAVTTGSAKIKL
EECEEEEECCEEEEE		23.6529550500
177PhosphorylationSTAVTTGSAKIKLKS
CEEEEECCEEEEECH		25.0526824392
179SuccinylationAVTTGSAKIKLKSSE
EEEECCEEEEECHHH		41.9123806337
179AcetylationAVTTGSAKIKLKSSE
EEEECCEEEEECHHH		41.9123806337
179UbiquitinationAVTTGSAKIKLKSSE
EEEECCEEEEECHHH		41.91-
183UbiquitinationGSAKIKLKSSELQTI
CCEEEEECHHHHHHH		47.1122790023
185PhosphorylationAKIKLKSSELQTIKT
EEEEECHHHHHHHHH		40.5128285833
191AcetylationSSELQTIKTELTQIK
HHHHHHHHHHHHHHH		39.0622826441
216UbiquitinationEQIAEEQKANPDGKK
HHHHHHHHCCCCCCC		54.1022790023
222AcetylationQKANPDGKKKGDSSS
HHCCCCCCCCCCCCC		59.7119852105
223AcetylationKANPDGKKKGDSSSG
HCCCCCCCCCCCCCC		68.477609989
227PhosphorylationDGKKKGDSSSGGGGG
CCCCCCCCCCCCCCC		34.7630635358
228PhosphorylationGKKKGDSSSGGGGGS
CCCCCCCCCCCCCCC		37.4330635358
229PhosphorylationKKKGDSSSGGGGGSS
CCCCCCCCCCCCCCC		45.4630635358
235PhosphorylationSSGGGGGSSGGGGSS
CCCCCCCCCCCCCCC		29.1430635358
236PhosphorylationSGGGGGSSGGGGSSN
CCCCCCCCCCCCCCC		44.7430635358
241PhosphorylationGSSGGGGSSNVGGGS
CCCCCCCCCCCCCCC		23.2430635358
242PhosphorylationSSGGGGSSNVGGGSS
CCCCCCCCCCCCCCC		38.5230635358
248PhosphorylationSSNVGGGSSGGSGSC
CCCCCCCCCCCCCCC		29.1430635358
249PhosphorylationSNVGGGSSGGSGSCS
CCCCCCCCCCCCCCC		50.9125195567
252PhosphorylationGGGSSGGSGSCSSSS
CCCCCCCCCCCCCCC		30.9322802335
254PhosphorylationGSSGGSGSCSSSSRL
CCCCCCCCCCCCCCC		16.7229899451
256PhosphorylationSGGSGSCSSSSRLPA
CCCCCCCCCCCCCCC		34.6530635358
257PhosphorylationGGSGSCSSSSRLPAP
CCCCCCCCCCCCCCC		36.3430635358
258PhosphorylationGSGSCSSSSRLPAPQ
CCCCCCCCCCCCCCC		11.8130635358
259PhosphorylationSGSCSSSSRLPAPQE
CCCCCCCCCCCCCCC		39.5230635358
268PhosphorylationLPAPQEDTASEAGTP
CCCCCCCCCCCCCCC		31.1924925903
270PhosphorylationAPQEDTASEAGTPQG
CCCCCCCCCCCCCCC		30.0324925903
274PhosphorylationDTASEAGTPQGEVQT
CCCCCCCCCCCCEEE		21.3424925903
281PhosphorylationTPQGEVQTRDDGDEE
CCCCCEEECCCCCCC		41.0424925903
292PhosphorylationGDEEGLLTHSEEELE
CCCCCEECCCHHHHH		28.5325521595
294PhosphorylationEEGLLTHSEEELEHS
CCCEECCCHHHHHHC		41.2825521595
301PhosphorylationSEEELEHSQDTDAED
CHHHHHHCCCCCCCC		22.0025521595
304PhosphorylationELEHSQDTDAEDGAL
HHHHCCCCCCCCCCC		29.4925521595
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 RALY_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RALY_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 RALY_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RALY_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RALY_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-135, 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-135; THR-268; SER-270AND THR-274, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, AND MASSSPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND THR-274, 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 THR-268; SER-270; THR-274;THR-292 AND THR-304, AND MASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-270 AND THR-274, ANDMASS SPECTROMETRY.

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