dbPTM

IF2B1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF2B1_MOUSE
UniProt AC	O88477
Protein Name	Insulin-like growth factor 2 mRNA-binding protein 1
Gene Name	Igf2bp1
Organism	Mus musculus (Mouse).
Sequence Length	577
Subcellular Localization	Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Cell projection, lamellipodium. Cell projection, dendrite. Cell projection, dendritic spine. Cell projection, growth cone. Cell projection, filopodium. Cell projection, axon. In the nucleus, located
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. Regulates localized beta-actin/ACTB mRNA translation, a crucial process for cell polarity, cell migration and neurite outgrowth. Co-transcriptionally associates with the ACTB mRNA in the nucleus. This binding involves a conserved 54-nucleotide element in the ACTB mRNA 3'-UTR, known as the 'zipcode'. The RNP thus formed is exported to the cytoplasm, binds to a motor protein and is transported along the cytoskeleton to the cell periphery. During transport, prevents ACTB mRNA from being translated into protein. When the RNP complex reaches its destination near the plasma membrane, IGF2BP1 is phosphorylated. This releases the mRNA, allowing ribosomal 40S and 60S subunits to assemble and initiate ACTB protein synthesis. Monomeric ACTB then assembles into the subcortical actin cytoskeleton (By similarity). During neuronal development, key regulator of neurite outgrowth, growth cone guidance and neuronal cell migration, presumably through the spatiotemporal fine tuning of protein synthesis, such as that of ACTB (By similarity). May regulate mRNA transport to activated synapses (By similarity). Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells (By similarity). Binds to the oncofetal H19 transcript and regulates its localization (By similarity). Binds to and stabilizes BTRC/FBW1A mRNA (By similarity). Binds to the adenine-rich autoregulatory sequence (ARS) located in PABPC1 mRNA and represses its translation. PABPC1 mRNA-binding is stimulated by PABPC1 protein. Prevents BTRC/FBW1A mRNA degradation by disrupting microRNA-dependent interaction with AGO2 (By similarity). During cellular stress, such as oxidative stress or heat shock, stabilizes target mRNAs that are recruited to stress granules, including CD44, IGF2, MAPK4, MYC, PTEN, RAPGEF2 and RPS6KA5 transcripts (By similarity). Interacts with GAP43 transcript and transports it to axons. Binds to the 3'-UTR of IGF2 mRNA by a mechanism of cooperative and sequential dimerization and regulates IGF2 mRNA subcellular localization and translation. Binds to MYC mRNA, in the coding region instability determinant (CRD) of the open reading frame (ORF), hence prevents MYC cleavage by endonucleases and possibly microRNA targeting to MYC-CRD. Binds to and stabilizes ABCB1/MDR-1 mRNA. Binds to the neuron-specific TAU mRNA and regulates its localization. Plays a direct role in the transport and translation of transcripts required for axonal regeneration in adult sensory neurons. During interstinal wound repair, interacts with and stabilizes PTGS2 transcript. PTGS2 mRNA stabilization may be crucial for colonic mucosal wound healing..
Protein Sequence	MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQITQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQPVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTLYNPERTITVKGAIENCCRAEQEIMKKVREAYENDVAAMSLQSHLIPGLNLAAVGLFPASSSAVPPPPSSVTGAAPYSSFMQAPEQEMVQVFIPAQAVGAIIGKKGQHIKQLSRFASASIKIAPPETPDSKVRMVVITGPPEAQFKAQGRIYGKLKEENFFGPKEEVKLETHIRVPASAAGRVIGKGGKTVNELQNLTAAEVVVPRDQTPDENDQVIVKIIGHFYASQMAQRKIRDILAQVKQQHQKGQSNLAQARRK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
12	Phosphorylation	YIGNLNESVTPADLE EECCCCCCCCHHHHH	30.16	29514104
20	Ubiquitination	VTPADLEKVFAEHKI CCHHHHHHHHHHCCC	50.37	-
26	Ubiquitination	EKVFAEHKISYSGQF HHHHHHCCCEECCEE	25.50	-
39	Phosphorylation	QFLVKSGYAFVDCPD EEEEEECEEEEECCC	12.17	22817900
56	Phosphorylation	WAMKAIETFSGKVEL HHHHHHHHCCCEEEE	19.58	23984901
58	Phosphorylation	MKAIETFSGKVELQG HHHHHHCCCEEEECC	45.16	23984901
73	Phosphorylation	KRLEIEHSVPKKQRS EEEEEEECCCCCCCC	27.59	-
181	Phosphorylation	RGQPRQGSPVAAGAP CCCCCCCCCCCCCCC	14.09	27087446
190	Ubiquitination	VAAGAPAKQQPVDIP CCCCCCCCCCCCCCC	48.70	-
213	Ubiquitination	YVGAIIGKEGATIRN HHHHHHCCCCCCHHH	42.43	-
223	Ubiquitination	ATIRNITKQTQSKID CCHHHHCHHHHCCEE	47.77	-
272	Ubiquitination	HKEAKDTKTADEVPL HHHHCCCCCCCCCCC	52.42	-
313	Phosphorylation	TETKITISSLQDLTL CCCCEEEEECCCCCC	19.15	22006019
314	Phosphorylation	ETKITISSLQDLTLY CCCEEEEECCCCCCC	26.63	22006019
396	Phosphorylation	SVTGAAPYSSFMQAP CCCCCCCCCHHCCCC	16.54	21964071
397	Phosphorylation	VTGAAPYSSFMQAPE CCCCCCCCHHCCCCH	18.95	-
398	Phosphorylation	TGAAPYSSFMQAPEQ CCCCCCCHHCCCCHH	20.92	-
436	Phosphorylation	KQLSRFASASIKIAP HHHHHHHHCCEEECC	21.60	25338131
438	Phosphorylation	LSRFASASIKIAPPE HHHHHHCCEEECCCC	23.17	25338131
440	Ubiquitination	RFASASIKIAPPETP HHHHCCEEECCCCCC	30.25	-
446	Phosphorylation	IKIAPPETPDSKVRM EEECCCCCCCCCEEE	37.86	22006019
450	Ubiquitination	PPETPDSKVRMVVIT CCCCCCCCEEEEEEE	41.04	-
475	Ubiquitination	GRIYGKLKEENFFGP CCEEEECCCCCCCCC	67.48	-
483	Ubiquitination	EENFFGPKEEVKLET CCCCCCCHHHEEEEE	67.87	-
508	Ubiquitination	RVIGKGGKTVNELQN CEECCCCCCHHHHHH	58.95	-
528	Phosphorylation	VVVPRDQTPDENDQV EEECCCCCCCCCCCE	36.68	25619855
566	Ubiquitination	QVKQQHQKGQSNLAQ HHHHHHHHHHCHHHH	57.71	-

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
181	S	Phosphorylation	Kinase	MTOR	P42345	PSP
181	S	Phosphorylation	Kinase	MTOR	Q9JLN9	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF2B1_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 IF2B1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of IF2B1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of IF2B1_MOUSE

Related Literatures of Post-Translational Modification

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-181, AND MASSSPECTROMETRY.	19131326 [Abstract]