IF2B2_HUMAN - dbPTM
IF2B2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF2B2_HUMAN
UniProt AC Q9Y6M1
Protein Name Insulin-like growth factor 2 mRNA-binding protein 2
Gene Name IGF2BP2
Organism Homo sapiens (Human).
Sequence Length 599
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.
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..
Protein Sequence MMNKLYIGNLSPAVTADDLRQLFGDRKLPLAGQVLLKSGYAFVDYPDQNWAIRAIETLSGKVELHGKIMEVDYSVSKKLRSRKIQIRNIPPHLQWEVLDGLLAQYGTVENVEQVNTDTETAVVNVTYATREEAKIAMEKLSGHQFENYSFKISYIPDEEVSSPSPPQRAQRGDHSSREQGHAPGGTSQARQIDFPLRILVPTQFVGAIIGKEGLTIKNITKQTQSRVDIHRKENSGAAEKPVTIHATPEGTSEACRMILEIMQKEADETKLAEEIPLKILAHNGLVGRLIGKEGRNLKKIEHETGTKITISSLQDLSIYNPERTITVKGTVEACASAEIEIMKKLREAFENDMLAVNQQANLIPGLNLSALGIFSTGLSVLSPPAGPRGAPPAAPYHPFTTHSGYFSSLYPHHQFGPFPHHHSYPEQEIVNLFIPTQAVGAIIGKKGAHIKQLARFAGASIKIAPAEGPDVSERMVIITGPPEAQFKAQGRIFGKLKEENFFNPKEEVKLEAHIRVPSSTAGRVIGKGGKTVNELQNLTSAEVIVPRDQTPDENEEVIVRIIGHFFASQTAQRKIREIVQQVKQQEQKYPQGVASQRSK
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
1 (in isoform 6)Acetylation-6.3622223895
6Phosphorylation--MMNKLYIGNLSPA
--CCCCEEECCCCCC		14.3720068231
11PhosphorylationKLYIGNLSPAVTADD
CEEECCCCCCCCHHH		18.1428355574
15PhosphorylationGNLSPAVTADDLRQL
CCCCCCCCHHHHHHH		26.8622199227
38PhosphorylationAGQVLLKSGYAFVDY
CCEEEEECCEEEEEC		36.6928442448
40PhosphorylationQVLLKSGYAFVDYPD
EEEEECCEEEEECCC		12.1728152594
45PhosphorylationSGYAFVDYPDQNWAI
CCEEEEECCCCCEEH		11.92-
73PhosphorylationGKIMEVDYSVSKKLR
EEEEEEEHHHHHHHH		19.0221406692
74PhosphorylationKIMEVDYSVSKKLRS
EEEEEEHHHHHHHHH		18.5621406692
76PhosphorylationMEVDYSVSKKLRSRK
EEEEHHHHHHHHHCC		20.3821406692
76 (in isoform 3)Ubiquitination-20.3821890473
77UbiquitinationEVDYSVSKKLRSRKI
EEEHHHHHHHHHCCC		54.3821906983
77 (in isoform 1)Ubiquitination-54.3821890473
77 (in isoform 2)Ubiquitination-54.3821890473
77MethylationEVDYSVSKKLRSRKI
EEEHHHHHHHHHCCC		54.38-
78MethylationVDYSVSKKLRSRKIQ
EEHHHHHHHHHCCCC		41.44-
148PhosphorylationSGHQFENYSFKISYI
HCCCCCCEEEEEEEC		14.3228450419
149PhosphorylationGHQFENYSFKISYIP
CCCCCCEEEEEEECC		31.4828450419
153PhosphorylationENYSFKISYIPDEEV
CCEEEEEEECCCCCC		20.0123927012
154PhosphorylationNYSFKISYIPDEEVS
CEEEEEEECCCCCCC		21.6823927012
158 (in isoform 5)Ubiquitination-55.7521890473
161PhosphorylationYIPDEEVSSPSPPQR
ECCCCCCCCCCCCHH		39.5529255136
162PhosphorylationIPDEEVSSPSPPQRA
CCCCCCCCCCCCHHH		34.2719664994
164 (in isoform 4)Ubiquitination-51.6821890473
164PhosphorylationDEEVSSPSPPQRAQR
CCCCCCCCCCHHHCC		51.6819664994
175PhosphorylationRAQRGDHSSREQGHA
HHCCCCCCCCCCCCC		35.5129449344
176PhosphorylationAQRGDHSSREQGHAP
HCCCCCCCCCCCCCC		36.1029449344
186PhosphorylationQGHAPGGTSQARQID
CCCCCCCCCHHHCCC		24.47-
187PhosphorylationGHAPGGTSQARQIDF
CCCCCCCCHHHCCCC		25.72-
207 (in isoform 5)Ubiquitination-5.7321890473
213 (in isoform 4)Ubiquitination-31.4421890473
215 (in isoform 5)Ubiquitination-40.5421890473
220 (in isoform 3)Ubiquitination-26.8821890473
221 (in isoform 2)Ubiquitination-47.7721890473
221 (in isoform 1)Ubiquitination-47.7721890473
221 (in isoform 4)Ubiquitination-47.7721890473
221UbiquitinationLTIKNITKQTQSRVD
EEEECCCHHHHCCEE		47.7721906983
223PhosphorylationIKNITKQTQSRVDIH
EECCCHHHHCCEECC		30.02-
240UbiquitinationENSGAAEKPVTIHAT
CCCCCCCCCEEEEEC		39.81-
240MalonylationENSGAAEKPVTIHAT
CCCCCCCCCEEEEEC		39.8126320211
240AcetylationENSGAAEKPVTIHAT
CCCCCCCCCEEEEEC		39.8126051181
269PhosphorylationMQKEADETKLAEEIP
HHHHCCCCCHHHHCC		31.7218452278
269 (in isoform 3)Ubiquitination-31.7221890473
270 (in isoform 1)Ubiquitination-43.5921890473
270 (in isoform 2)Ubiquitination-43.5921890473
270UbiquitinationQKEADETKLAEEIPL
HHHCCCCCHHHHCCH		43.5921906983
277 (in isoform 3)Ubiquitination-7.0921890473
278UbiquitinationLAEEIPLKILAHNGL
HHHHCCHHHHHHCCH		30.2521890473
278 (in isoform 2)Ubiquitination-30.2521890473
278 (in isoform 1)Ubiquitination-30.2521890473
292UbiquitinationLVGRLIGKEGRNLKK
HHHHHHCCCCCCCEE		50.42-
311PhosphorylationTGTKITISSLQDLSI
CCCEEEEEECCCCCC		19.1524247654
312PhosphorylationGTKITISSLQDLSIY
CCEEEEEECCCCCCC		26.6329507054
324PhosphorylationSIYNPERTITVKGTV
CCCCCCCEEEEEEEH		21.24-
326PhosphorylationYNPERTITVKGTVEA
CCCCCEEEEEEEHHH		18.62-
330PhosphorylationRTITVKGTVEACASA
CEEEEEEEHHHHHHH		14.95-
336PhosphorylationGTVEACASAEIEIMK
EEHHHHHHHHHHHHH		26.73-
356 (in isoform 5)Ubiquitination-6.1421890473
381 (in isoform 5)Ubiquitination-5.9721890473
391 (in isoform 5)Ubiquitination-23.1421890473
405 (in isoform 4)Ubiquitination-11.8721890473
419 (in isoform 1)Ubiquitination-29.0921890473
430 (in isoform 4)Ubiquitination-5.1121890473
440 (in isoform 4)Ubiquitination-17.6721890473
444 (in isoform 1)Ubiquitination-21.3621890473
454 (in isoform 1)Ubiquitination-11.3121890473
460PhosphorylationLARFAGASIKIAPAE
HHHHHCCEEEEECCC		24.4028355574
461 (in isoform 3)Ubiquitination-3.5721890473
462 (in isoform 2)Ubiquitination-30.2521890473
462UbiquitinationRFAGASIKIAPAEGP
HHHCCEEEEECCCCC		30.2521890473
472PhosphorylationPAEGPDVSERMVIIT
CCCCCCCCCCEEEEE		27.1926714015
482 (in isoform 5)Ubiquitination-51.4021890473
486 (in isoform 3)Ubiquitination-10.2421890473
487 (in isoform 2)Ubiquitination-27.9321890473
487MethylationGPPEAQFKAQGRIFG
CCCHHHHHHHCCCCH		27.9324712139
487UbiquitinationGPPEAQFKAQGRIFG
CCCHHHHHHHCCCCH		27.9321890473
487 (in isoform 1)Ubiquitination-27.93-
496 (in isoform 3)Ubiquitination-9.6221890473
497UbiquitinationGRIFGKLKEENFFNP
CCCCHHCCCCCCCCC		67.4821906983
497 (in isoform 2)Ubiquitination-67.4821890473
518PhosphorylationEAHIRVPSSTAGRVI
EEEEECCCCCCCCEE		37.15-
530UbiquitinationRVIGKGGKTVNELQN
CEECCCCCCHHHHCC		58.95-
531 (in isoform 4)Ubiquitination-31.6621890473
545 (in isoform 1)Ubiquitination-3.7221890473
550PhosphorylationVIVPRDQTPDENEEV
EEECCCCCCCCCHHH		36.6829255136
583UbiquitinationREIVQQVKQQEQKYP
HHHHHHHHHHHHHCC		41.76-
587 (in isoform 3)Ubiquitination-46.3621890473
588UbiquitinationQVKQQEQKYPQGVAS
HHHHHHHHCCCCCHH		59.132190698
588 (in isoform 2)Ubiquitination-59.1321890473
589PhosphorylationVKQQEQKYPQGVASQ
HHHHHHHCCCCCHHH		10.6529083192
595PhosphorylationKYPQGVASQRSK---
HCCCCCHHHCCC---		24.5824245541
598PhosphorylationQGVASQRSK------
CCCHHHCCC------		34.7729083192
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 IF2B2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF2B2_HUMAN !!
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 IF2B2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HNRPD_HUMANHNRNPDphysical
12674497
RAB5A_HUMANRAB5Aphysical
22939629
PLPP1_HUMANPPAP2Aphysical
22939629
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF2B2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164, AND MASSSPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162 AND SER-164, ANDMASS SPECTROMETRY.

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