RBM5_MOUSE - dbPTM
RBM5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RBM5_MOUSE
UniProt AC Q91YE7
Protein Name RNA-binding protein 5
Gene Name Rbm5
Organism Mus musculus (Mouse).
Sequence Length 815
Subcellular Localization Nucleus.
Protein Description Component of the spliceosome A complex. Regulates alternative splicing of a number of mRNAs. May modulate splice site pairing after recruitment of the U1 and U2 snRNPs to the 5' and 3' splice sites of the intron. May both positively and negatively regulate apoptosis by regulating the alternative splicing of several genes involved in this process, including FAS and CASP2/caspase-2. In the case of FAS, promotes production of a soluble form of FAS that inhibits apoptosis. In the case of CASP2/caspase-2, promotes production of a catalytically active form of CASP2/Caspase-2 that induces apoptosis (By similarity)..
Protein Sequence MGSDKRVSRTERSGRYGSIIDRDDRDERESRSRRRDSDYKRSSDDRRGDRYDDYRDYDSPERERERRNSDRSEDGYHSDGDYGEHDYRHDISDERESKTIMLRGLPITITESDIREMMESFEGPQPADVRLMKRKTGVSRGFAFVEFYHLQDATSWMEANQKKLVIQGKHIAMHYSNPRPKFEDWLCNKCCLNNFRKRLKCFRCGADKFDSEQEVPPGTTESAQSVDYYCDTIILRNIAPHTVVDSIMTALSPYASLAVNNIRLIKDKQTQQNRGFAFVQLSSAMDASQLLQILQSLHPPLKIDGKTIGVDFAKSARKDLVLPDGNRVSAFSVASTAIAAAQWSSTQSQSGEGGSVDYSYMQPGQDGYTQYTQYSQDYQQFYQQQAGGLESDTSATSGTTVTTTSAAVVSQSPQLYNQTSNPPGSPTEEAQPSTSTSTQAPAASPTGVVPGTKYAVPDTSTYQYDESSGYYYDPTTGLYYDPNSQYYYNSLTQQYLYWDGEKETYVPAAEASSNQQTGLPSTKEGKEKKEKPKSKTAQQIAKDMERWAKSLNKQKENFKNSFQPVNSLREEERRESAAADAGFALFEKKGALAERQQLLPELVRNGDEENPLKRGLVAAYSGDSDNEEELVERLESEEEKLADWKKMACLLCRRQFPNRDALVRHQQLSDLHKQNMDIYRRSRLSEQELEALELREREMKYRDRAAERREKYGIPEPPEPKRKKQFDAGTVNYEQPTKDGIDHSNIGNKMLQAMGWREGSGLGRKCQGITAPIEAQVRLKGAGLGAKGSAYGLSGADSYKDAVRKAMFARFTEME
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
18PhosphorylationERSGRYGSIIDRDDR
CCCCCCCCCCCCCCC
13.8727600695
37PhosphorylationSRSRRRDSDYKRSSD
HHHHHCCHHCCCCCC
40.8229899451
51PhosphorylationDDRRGDRYDDYRDYD
CCCCCCCCCCCCCCC
20.2225777480
54PhosphorylationRGDRYDDYRDYDSPE
CCCCCCCCCCCCCHH
11.5025159016
57PhosphorylationRYDDYRDYDSPERER
CCCCCCCCCCHHHHH
14.8825159016
59PhosphorylationDDYRDYDSPERERER
CCCCCCCCHHHHHHH
23.5625521595
69PhosphorylationRERERRNSDRSEDGY
HHHHHHCCCCCCCCC
32.3727087446
72PhosphorylationERRNSDRSEDGYHSD
HHHCCCCCCCCCCCC
45.0627087446
76PhosphorylationSDRSEDGYHSDGDYG
CCCCCCCCCCCCCCC
15.5225619855
78PhosphorylationRSEDGYHSDGDYGEH
CCCCCCCCCCCCCCC
34.5025521595
82PhosphorylationGYHSDGDYGEHDYRH
CCCCCCCCCCCCCCC
29.9125619855
87PhosphorylationGDYGEHDYRHDISDE
CCCCCCCCCCCCCCH
16.2621149613
92PhosphorylationHDYRHDISDERESKT
CCCCCCCCCHHHCCE
39.2023684622
249PhosphorylationTVVDSIMTALSPYAS
HHHHHHHHHHHHHHH
23.8322802335
252PhosphorylationDSIMTALSPYASLAV
HHHHHHHHHHHHHHH
17.2522802335
444PhosphorylationSTQAPAASPTGVVPG
CCCCCCCCCCCCCCC
25.71-
528AcetylationSTKEGKEKKEKPKSK
CCCCCHHCCCCCCCH
70.497613431
531AcetylationEGKEKKEKPKSKTAQ
CCHHCCCCCCCHHHH
67.637613441
542AcetylationKTAQQIAKDMERWAK
HHHHHHHHHHHHHHH
60.2723806337
576PhosphorylationREEERRESAAADAGF
CHHHHHHHHHHHHHH
22.7728833060
620PhosphorylationKRGLVAAYSGDSDNE
CCCCEEEECCCCCCH
11.9326239621
621PhosphorylationRGLVAAYSGDSDNEE
CCCEEEECCCCCCHH
31.2525521595
623 (in isoform 2)Phosphorylation-47.0519144319
624PhosphorylationVAAYSGDSDNEEELV
EEEECCCCCCHHHHH
45.9527087446
636PhosphorylationELVERLESEEEKLAD
HHHHHHHHHHHHHHH
55.7025159016
682PhosphorylationNMDIYRRSRLSEQEL
CHHHHHHHCCCHHHH
28.6828833060
685PhosphorylationIYRRSRLSEQELEAL
HHHHHCCCHHHHHHH
35.8028833060
787AcetylationKGAGLGAKGSAYGLS
CCCCCCCCCCCCCCC
52.1522826441

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 RBM5_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RBM5_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 RBM5_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of RBM5_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RBM5_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-624, AND MASSSPECTROMETRY.
"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-78, AND MASSSPECTROMETRY.
"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-69 AND SER-621, AND MASSSPECTROMETRY.
"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-624, AND MASSSPECTROMETRY.

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