TRA2B_MOUSE - dbPTM
TRA2B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRA2B_MOUSE
UniProt AC P62996
Protein Name Transformer-2 protein homolog beta
Gene Name Tra2b
Organism Mus musculus (Mouse).
Sequence Length 288
Subcellular Localization Nucleus.
Protein Description Sequence-specific RNA-binding protein which participates in the control of pre-mRNA splicing. Can either activate or suppress exon inclusion. Acts additively with RBMX to promote exon 7 inclusion of the survival motor neuron SMN2. Activates the splicing of MAPT/Tau exon 10. Alters pre-mRNA splicing patterns by antagonizing the effects of splicing regulators, like RBMX. Binds to the AG-rich SE2 domain in the SMN exon 7 RNA. Binds to pre-mRNA (By similarity)..
Protein Sequence MSDSGEQNYGERESRSASRSGSAHGSGKSARHTPARSRSKEDSRRSRSKSRSRSESRSRSRRSSRRHYTRSRSRSRSHRRSRSRSYSRDYRRRHSHSHSPMSTRRRHVGNRANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHTPTPGIYMGRPTYGSSRRRDYYDRGYDRGYDDRDYYSRSYRGGGGGGGGWRAAQDRDQIYRRRSPSPYYSRGGYRSRSRSRSYSPRRY
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------MSDSGEQNY
------CCCCCCCCC		40.25-
2Phosphorylation------MSDSGEQNY
------CCCCCCCCC		40.2523527152
4Phosphorylation----MSDSGEQNYGE
----CCCCCCCCCCC		36.6027742792
9PhosphorylationSDSGEQNYGERESRS
CCCCCCCCCCCCCCC		21.7623429704
14 (in isoform 2)Phosphorylation-37.4430352176
14PhosphorylationQNYGERESRSASRSG
CCCCCCCCCCCCCCC		37.4423527152
16PhosphorylationYGERESRSASRSGSA
CCCCCCCCCCCCCCC		39.6223429704
18PhosphorylationERESRSASRSGSAHG
CCCCCCCCCCCCCCC		28.3823429704
20PhosphorylationESRSASRSGSAHGSG
CCCCCCCCCCCCCCC		34.3123375375
22PhosphorylationRSASRSGSAHGSGKS
CCCCCCCCCCCCCCC		20.5225159016
26PhosphorylationRSGSAHGSGKSARHT
CCCCCCCCCCCCCCC		32.9329472430
29PhosphorylationSAHGSGKSARHTPAR
CCCCCCCCCCCCCCC		33.7823684622
33PhosphorylationSGKSARHTPARSRSK
CCCCCCCCCCCCCCH		17.0623684622
37PhosphorylationARHTPARSRSKEDSR
CCCCCCCCCCHHHHH		42.9123684622
39PhosphorylationHTPARSRSKEDSRRS
CCCCCCCCHHHHHHH		41.4629472430
43PhosphorylationRSRSKEDSRRSRSKS
CCCCHHHHHHHHHHH		30.5929472430
50PhosphorylationSRRSRSKSRSRSESR
HHHHHHHHHHHHHHH		36.4122817900
52PhosphorylationRSRSKSRSRSESRSR
HHHHHHHHHHHHHHH		47.4522817900
54PhosphorylationRSKSRSRSESRSRSR
HHHHHHHHHHHHHHH		40.9622817900
56PhosphorylationKSRSRSESRSRSRRS
HHHHHHHHHHHHHHH		36.4822817900
58PhosphorylationRSRSESRSRSRRSSR
HHHHHHHHHHHHHHH		43.8419367708
60PhosphorylationRSESRSRSRRSSRRH
HHHHHHHHHHHHHHH		33.0419367708
63PhosphorylationSRSRSRRSSRRHYTR
HHHHHHHHHHHHHHH		27.3819367708
64PhosphorylationRSRSRRSSRRHYTRS
HHHHHHHHHHHHHHH		31.3619367708
68PhosphorylationRRSSRRHYTRSRSRS
HHHHHHHHHHHHHHC		11.3123737553
69PhosphorylationRSSRRHYTRSRSRSR
HHHHHHHHHHHHHCH		18.9523737553
71PhosphorylationSRRHYTRSRSRSRSH
HHHHHHHHHHHCHHH		27.1423737553
73PhosphorylationRHYTRSRSRSRSHRR
HHHHHHHHHCHHHHH		35.5427681418
81PhosphorylationRSRSHRRSRSRSYSR
HCHHHHHHHCHHCCH		34.2722817900
83PhosphorylationRSHRRSRSRSYSRDY
HHHHHHHCHHCCHHH		27.1623684622
85PhosphorylationHRRSRSRSYSRDYRR
HHHHHCHHCCHHHHH		28.8023684622
86PhosphorylationRRSRSRSYSRDYRRR
HHHHCHHCCHHHHHH		13.4520469934
87PhosphorylationRSRSRSYSRDYRRRH
HHHCHHCCHHHHHHH		21.6628973931
90PhosphorylationSRSYSRDYRRRHSHS
CHHCCHHHHHHHCCC		12.6225159016
95PhosphorylationRDYRRRHSHSHSPMS
HHHHHHHCCCCCCCC		25.5218388127
97PhosphorylationYRRRHSHSHSPMSTR
HHHHHCCCCCCCCHH		28.7718388127
99PhosphorylationRRHSHSHSPMSTRRR
HHHCCCCCCCCHHCC		25.8818388127
102PhosphorylationSHSHSPMSTRRRHVG
CCCCCCCCHHCCCCC		23.3426824392
103PhosphorylationHSHSPMSTRRRHVGN
CCCCCCCHHCCCCCC		23.1823684622
140UbiquitinationDLREVFSKYGPIADV
HHHHHHHHHCCCCEE		42.64-
140AcetylationDLREVFSKYGPIADV
HHHHHHHHHCCCCEE		42.6423954790
197AcetylationRVDFSITKRPHTPTP
EEEEEEECCCCCCCC		63.3622826441
201PhosphorylationSITKRPHTPTPGIYM
EEECCCCCCCCCEEC		31.3824925903
203PhosphorylationTKRPHTPTPGIYMGR
ECCCCCCCCCEECCC		34.9924925903
207PhosphorylationHTPTPGIYMGRPTYG
CCCCCCEECCCCCCC		10.2225619855
212PhosphorylationGIYMGRPTYGSSRRR
CEECCCCCCCCCCCC		38.8725619855
213PhosphorylationIYMGRPTYGSSRRRD
EECCCCCCCCCCCCC		20.0725619855
215PhosphorylationMGRPTYGSSRRRDYY
CCCCCCCCCCCCCCH		15.4025619855
216PhosphorylationGRPTYGSSRRRDYYD
CCCCCCCCCCCCCHH		25.9925619855
217MethylationRPTYGSSRRRDYYDR
CCCCCCCCCCCCHHC		39.07-
235PhosphorylationRGYDDRDYYSRSYRG
CCCCCCCCCCCCCCC		12.3025367039
236PhosphorylationGYDDRDYYSRSYRGG
CCCCCCCCCCCCCCC		11.25-
237PhosphorylationYDDRDYYSRSYRGGG
CCCCCCCCCCCCCCC		14.44-
239PhosphorylationDRDYYSRSYRGGGGG
CCCCCCCCCCCCCCC		17.1627899381
241Asymmetric dimethylarginineDYYSRSYRGGGGGGG
CCCCCCCCCCCCCCC		38.23-
241MethylationDYYSRSYRGGGGGGG
CCCCCCCCCCCCCCC		38.2324129315
260PhosphorylationAQDRDQIYRRRSPSP
CCCHHHHHHCCCCCC		7.7625159016
264PhosphorylationDQIYRRRSPSPYYSR
HHHHHCCCCCCCCCC		28.1118388127
266PhosphorylationIYRRRSPSPYYSRGG
HHHCCCCCCCCCCCC		27.1218388127
268PhosphorylationRRRSPSPYYSRGGYR
HCCCCCCCCCCCCCC		20.5725521595
269PhosphorylationRRSPSPYYSRGGYRS
CCCCCCCCCCCCCCC		8.6927742792
270PhosphorylationRSPSPYYSRGGYRSR
CCCCCCCCCCCCCCC		20.7127742792
276PhosphorylationYSRGGYRSRSRSRSY
CCCCCCCCCCCCCCC		26.5623737553
278PhosphorylationRGGYRSRSRSRSYSP
CCCCCCCCCCCCCCC		35.5423684622
280PhosphorylationGYRSRSRSRSYSPRR
CCCCCCCCCCCCCCC		27.1623684622
282PhosphorylationRSRSRSRSYSPRRY-
CCCCCCCCCCCCCC-		31.0723684622
283PhosphorylationSRSRSRSYSPRRY--
CCCCCCCCCCCCC--		22.9122802335
284PhosphorylationRSRSRSYSPRRY---
CCCCCCCCCCCC---		17.1223684622
288PhosphorylationRSYSPRRY-------
CCCCCCCC-------		24.9620531401
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 TRA2B_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TRA2B_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 TRA2B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of TRA2B_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRA2B_MOUSE

loading...

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-264 AND SER-266, ANDMASS 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-2; SER-4; SER-14;SER-50; SER-52; SER-54; SER-56; SER-83; SER-85; SER-264; SER-266 ANDSER-284, AND MASS 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-201; SER-264 ANDSER-266, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-264 AND SER-266, ANDMASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory