dbPTM

PURB_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PURB_MOUSE
UniProt AC	O35295
Protein Name	Transcriptional activator protein Pur-beta
Gene Name	Purb
Organism	Mus musculus (Mouse).
Sequence Length	324
Subcellular Localization	Nucleus.
Protein Description	Has capacity to bind repeated elements in single-stranded DNA such as the purine-rich single strand of the PUR element located upstream of the MYC gene. Participates in transcriptional and translational regulation of alpha-MHC expression in cardiac myocytes by binding to the purine-rich negative regulatory (PNR) element. Modulates constitutive liver galectin-3 gene transcription by binding to its promoter. May play a role in the dendritic transport of a subset of mRNAs (By similarity). Plays a role in the control of vascular smooth muscle (VSM) alpha-actin gene transcription as repressor in myoblasts and fibroblasts..
Protein Sequence	MADGDSGSERGGGGGGGGGPGGFQPAPRGGGGGGGGPGGEQETQELASKRLDIQNKRFYLDVKQNAKGRFLKIAEVGAGGSKSRLTLSMAVAAEFRDSLGDFIEHYAQLGPSSPEQLAAGAEEGGGPRRALKSEFLVRENRKYYLDLKENQRGRFLRIRQTVNRGGGGFGGGPGPGGLQSGQTIALPAQGLIEFRDALAKLIDDYGGDEDELAGGPGGGAGGPGGGLYGELPEGTSITVDSKRFFFDVGCNKYGVFLRVSEVKPSYRNAITVPFKAWGKFGGAFCRYADEMKEIQERQRDKLYERRGGGSGGGDESEGEEVDED

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADGDSGSE ------CCCCCCCCC	29.50	19131326
6	Phosphorylation	--MADGDSGSERGGG --CCCCCCCCCCCCC	50.15	26824392
8	Phosphorylation	MADGDSGSERGGGGG CCCCCCCCCCCCCCC	28.24	26824392
28	Methylation	GGFQPAPRGGGGGGG CCCCCCCCCCCCCCC	59.50	24129315
43	Phosphorylation	GPGGEQETQELASKR CCCCHHHHHHHHHHH	27.34	17525332
63	Ubiquitination	KRFYLDVKQNAKGRF CEEEEECHHHCCCCE	37.19	-
63	Malonylation	KRFYLDVKQNAKGRF CEEEEECHHHCCCCE	37.19	26320211
72	Ubiquitination	NAKGRFLKIAEVGAG HCCCCEEEEEEECCC	36.84	27667366
72	Malonylation	NAKGRFLKIAEVGAG HCCCCEEEEEEECCC	36.84	26320211
72	Acetylation	NAKGRFLKIAEVGAG HCCCCEEEEEEECCC	36.84	22826441
82	Malonylation	EVGAGGSKSRLTLSM EECCCCCHHHHHHHH	42.76	26320211
82	Ubiquitination	EVGAGGSKSRLTLSM EECCCCCHHHHHHHH	42.76	27667366
98	Phosphorylation	VAAEFRDSLGDFIEH HHHHHHHHHHHHHHH	29.96	25619855
106	Phosphorylation	LGDFIEHYAQLGPSS HHHHHHHHHHHCCCC	5.35	25619855
112	Phosphorylation	HYAQLGPSSPEQLAA HHHHHCCCCHHHHHH	57.64	25521595
113	Phosphorylation	YAQLGPSSPEQLAAG HHHHCCCCHHHHHHH	35.27	25521595
132	Ubiquitination	GGPRRALKSEFLVRE CCHHHHHHHHEEEEC	47.13	27667366
148	Malonylation	RKYYLDLKENQRGRF CEEEEECCCCCCCCE	55.04	26320211
148	Ubiquitination	RKYYLDLKENQRGRF CEEEEECCCCCCCCE	55.04	-
148	Acetylation	RKYYLDLKENQRGRF CEEEEECCCCCCCCE	55.04	23954790
164	Methylation	RIRQTVNRGGGGFGG EEEEEECCCCCCCCC	40.57	24129315
242	Acetylation	TSITVDSKRFFFDVG CEEEECCEEEEEECC	49.08	15608907
250	S-nitrosylation	RFFFDVGCNKYGVFL EEEEECCCCEEEEEE	3.89	21278135
250	S-nitrosocysteine	RFFFDVGCNKYGVFL EEEEECCCCEEEEEE	3.89	-
265	Phosphorylation	RVSEVKPSYRNAITV EEEECCCCHHCCEEE	30.89	29176673
279	Malonylation	VPFKAWGKFGGAFCR ECCCHHHHCCHHHHH	30.09	26320211
279	Ubiquitination	VPFKAWGKFGGAFCR ECCCHHHHCCHHHHH	30.09	-
279	Acetylation	VPFKAWGKFGGAFCR ECCCHHHHCCHHHHH	30.09	23806337
292	Acetylation	CRYADEMKEIQERQR HHHHHHHHHHHHHHH	50.01	23954790
303	Phosphorylation	ERQRDKLYERRGGGS HHHHHHHHHCCCCCC	17.09	25367039
306	Methylation	RDKLYERRGGGSGGG HHHHHHCCCCCCCCC	35.85	24129315
310	Phosphorylation	YERRGGGSGGGDESE HHCCCCCCCCCCHHC	37.22	25521595
316	Phosphorylation	GSGGGDESEGEEVDE CCCCCCHHCCCCCCC	56.49	27087446

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 PURB_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of PURB_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 PURB_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PURB_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PURB_MOUSE

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-6;SER-8 AND SER-316, AND MASS SPECTROMETRY.	16452087 [Abstract]
Phosphorylation
Reference	PubMed
"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-6; SER-8 AND SER-316,AND MASS SPECTROMETRY.	19131326 [Abstract]
"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-316, AND MASSSPECTROMETRY.	19367708 [Abstract]
"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-316, AND MASSSPECTROMETRY.	18630941 [Abstract]
"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-316, AND MASSSPECTROMETRY.	17242355 [Abstract]
"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-316, AND MASSSPECTROMETRY.	17203969 [Abstract]
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION AT SER-6;SER-8 AND SER-316, AND MASS SPECTROMETRY.	16452087 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-43, AND MASSSPECTROMETRY.	17525332 [Abstract]