IF2B2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF2B2_MOUSE
• UniProt AC: Q5SF07
• Protein Name: Insulin-like growth factor 2 mRNA-binding protein 2
• Gene Name: Igf2bp2
• Organism: Mus musculus (Mouse).
• Sequence Length: 592
• Subcellular Localization: Nucleus. Cytoplasm. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Localizes at the connecting piece and the tail of the spermatozoa. In response to cellular stress, such as oxidative stress, recruited to stress granules (By si
• Protein Description: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from endonuclease attacks or microRNA-mediated degradation (By similarity). Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs. Binding is isoform-specific. Binds to beta-actin/ACTB and MYC transcripts (By similarity)..
• Protein Sequence: MMNKLYIGNLSPAVTADDLRQLFGDRKLPLAGQVLLKSGYAFVDYPDQNWAIRAIETLSGKVELHGKIMEVDYSVSKKLRSRRIQIRNIPPHLQWEVLDGLLAEYGTVENVEQVNTDTETAVVNVTYMTREEAKLAIEKLSGHQFEDYSFKISYIPDEEVSSPSPPHRAREQGHGPGSSSQARQIDFPLRILVPTQFVGAIIGKEGLTIKNITKQTQSRVDIHRKENSGAAEKPVTIHATPEGTSEACRMILEIMQKEADETKLAEEVPLKILAHNGFVGRLIGKEGRNLKKIEHETGTKITISSLQDLSIYNPERTITVRGTIEACANAEIEIMKKLREAFENDMLAVNQQANLIPGLNLSALGIFSTGLSVLPPPAGPRGVPPSPPYHPFATHSGYFSSLYPHHHFGPFPHHHSYPEQETVSLFIPTQAVGAIIGKKGAHIKQLARFAGASIKIAPAEGPDVSERMVIITGPPEAQFKAQGRIFGKLKEENFFNPKEEVKLEAHIRVPSSTAGRVIGKGGKTVNELQNLTSAEVIVPRDQTPDENEEVIVRIIGHFFASQTAQRKIREIVQQVKQQEQRYPQGVAPQRSK

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
6	Phosphorylation	--MMNKLYIGNLSPA --CCCCEEECCCCCC	14.37	-
11	Phosphorylation	KLYIGNLSPAVTADD CEEECCCCCCCCHHH	18.14	26239621
15	Phosphorylation	GNLSPAVTADDLRQL CCCCCCCCHHHHHHH	26.86	26370283
40	Phosphorylation	QVLLKSGYAFVDYPD EEEEECCEEEEECCC	12.17	22817900
76	Phosphorylation	MEVDYSVSKKLRSRR EEEEHHHHHHHHHCC	20.38	29514104
149	Phosphorylation	GHQFEDYSFKISYIP CCCCCCEEEEEEECC	32.17	29514104
153	Phosphorylation	EDYSFKISYIPDEEV CCEEEEEEECCCHHC	20.01	25619855
154	Phosphorylation	DYSFKISYIPDEEVS CEEEEEEECCCHHCC	21.68	25619855
161	Phosphorylation	YIPDEEVSSPSPPHR ECCCHHCCCCCCCCC	39.55	26824392
162	Phosphorylation	IPDEEVSSPSPPHRA CCCHHCCCCCCCCCH	34.27	27087446
164	Phosphorylation	DEEVSSPSPPHRARE CHHCCCCCCCCCHHH	53.67	27087446
178	Phosphorylation	EQGHGPGSSSQARQI HCCCCCCCHHHHHCC	29.92	23684622
180	Phosphorylation	GHGPGSSSQARQIDF CCCCCCHHHHHCCCC	29.56	23684622
214	Ubiquitination	LTIKNITKQTQSRVD EEEECCCHHHHCCEE	47.77	-
218	Phosphorylation	NITKQTQSRVDIHRK CCCHHHHCCEECCCC	37.34	29514104
225	Ubiquitination	SRVDIHRKENSGAAE CCEECCCCCCCCCCC	47.27	-
263	Ubiquitination	QKEADETKLAEEVPL HHHCCCCCCHHHCCH	43.59	-
304	Phosphorylation	TGTKITISSLQDLSI CCCEEEEEECCCCCC	19.15	29514104
305	Phosphorylation	GTKITISSLQDLSIY CCEEEEEECCCCCCC	26.63	29514104
453	Phosphorylation	LARFAGASIKIAPAE HHHHHCCEEEEECCC	24.40	25338131
455	Ubiquitination	RFAGASIKIAPAEGP HHHCCEEEEECCCCC	30.25	-
533	Phosphorylation	NELQNLTSAEVIVPR HHHCCCCCCEEEECC	26.12	29514104
543	Phosphorylation	VIVPRDQTPDENEEV EEECCCCCCCCCHHH	36.68	16141072
591	Phosphorylation	QGVAPQRSK------ CCCCCCCCC------	37.15	29514104

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of IF2B2_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IF2B2_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IF2B2_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of IF2B2_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"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-162 AND SER-164, ANDMASS SPECTROMETRY.
PubMed: 19131326