IF2B3_HUMAN - dbPTM
IF2B3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF2B3_HUMAN
UniProt AC O00425
Protein Name Insulin-like growth factor 2 mRNA-binding protein 3
Gene Name IGF2BP3
Organism Homo sapiens (Human).
Sequence Length 579
Subcellular Localization Nucleus. Cytoplasm. Found in lamellipodia of the leading edge, in the perinuclear region, and beneath the plasma membrane. The subcytoplasmic localization is cell specific and regulated by cell contact and growth. Localized at the connecting piece an
Protein Description RNA-binding factor that may recruit 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. Binds to the 3'-UTR of CD44 mRNA and stabilizes it, hence promotes cell adhesion and invadopodia formation in cancer cells. Binds to beta-actin/ACTB and MYC transcripts. Binds to the 5'-UTR of the insulin-like growth factor 2 (IGF2) mRNAs..
Protein Sequence MNKLYIGNLSENAAPSDLESIFKDAKIPVSGPFLVKTGYAFVDCPDESWALKAIEALSGKIELHGKPIEVEHSVPKRQRIRKLQIRNIPPHLQWEVLDSLLVQYGVVESCEQVNTDSETAVVNVTYSSKDQARQALDKLNGFQLENFTLKVAYIPDEMAAQQNPLQQPRGRRGLGQRGSSRQGSPGSVSKQKPCDLPLRLLVPTQFVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKSITILSTPEGTSAACKSILEIMHKEAQDIKFTEEIPLKILAHNNFVGRLIGKEGRNLKKIEQDTDTKITISPLQELTLYNPERTITVKGNVETCAKAEEEIMKKIRESYENDIASMNLQAHLIPGLNLNALGLFPPTSGMPPPTSGPPSAMTPPYPQFEQSETETVHLFIPALSVGAIIGKQGQHIKQLSRFAGASIKIAPAEAPDAKVRMVIITGPPEAQFKAQGRIYGKIKEENFVSPKEEVKLEAHIRVPSFAAGRVIGKGGKTVNELQNLSSAEVVVPRDQTPDENDQVVVKITGHFYACQVAQRKIQEILTQVKQHQQQKALQSGPPQSRRK
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
5Phosphorylation---MNKLYIGNLSEN
---CCCEEECCCCCC
14.3720873877
10PhosphorylationKLYIGNLSENAAPSD
CEEECCCCCCCCCCH
32.5720873877
16PhosphorylationLSENAAPSDLESIFK
CCCCCCCCHHHHHHH
50.5320873877
20PhosphorylationAAPSDLESIFKDAKI
CCCCHHHHHHHCCCC
40.3924719451
23UbiquitinationSDLESIFKDAKIPVS
CHHHHHHHCCCCCCC
55.9221906983
23 (in isoform 1)Ubiquitination-55.9221906983
26UbiquitinationESIFKDAKIPVSGPF
HHHHHCCCCCCCCCE
58.6427667366
30PhosphorylationKDAKIPVSGPFLVKT
HCCCCCCCCCEEEEE
35.0821406692
33UbiquitinationKIPVSGPFLVKTGYA
CCCCCCCEEEEECEE
16.2827667366
36UbiquitinationVSGPFLVKTGYAFVD
CCCCEEEEECEEEEE
38.0832015554
39PhosphorylationPFLVKTGYAFVDCPD
CEEEEECEEEEECCC
11.3323822953
44GlutathionylationTGYAFVDCPDESWAL
ECEEEEECCCHHHHH
3.7322555962
45UbiquitinationGYAFVDCPDESWALK
CEEEEECCCHHHHHH
43.8921890473
52UbiquitinationPDESWALKAIEALSG
CCHHHHHHHHHHHCC
39.3032015554
56UbiquitinationWALKAIEALSGKIEL
HHHHHHHHHCCCEEE
10.8321890473
59 (in isoform 2)Ubiquitination-35.4921906983
66AcetylationGKIELHGKPIEVEHS
CCEEECCCEEEEECC
31.8826051181
66UbiquitinationGKIELHGKPIEVEHS
CCEEECCCEEEEECC
31.8822053931
69 (in isoform 2)Ubiquitination-50.8321906983
71UbiquitinationHGKPIEVEHSVPKRQ
CCCEEEEECCCCHHH
20.0422817900
73PhosphorylationKPIEVEHSVPKRQRI
CEEEEECCCCHHHHH
26.9820873877
76UbiquitinationEVEHSVPKRQRIRKL
EEECCCCHHHHHHHC
60.0329967540
82UbiquitinationPKRQRIRKLQIRNIP
CHHHHHHHCCCCCCC
42.2327667366
84 (in isoform 2)Ubiquitination-35.3121906983
97UbiquitinationPHLQWEVLDSLLVQY
HHHCHHHHHHHHHHH
2.2227667366
105UbiquitinationDSLLVQYGVVESCEQ
HHHHHHHCCEECEEE
10.4121890473
109UbiquitinationVQYGVVESCEQVNTD
HHHCCEECEEECCCC
16.0223503661
115UbiquitinationESCEQVNTDSETAVV
ECEEECCCCCCEEEE
41.8827667366
120UbiquitinationVNTDSETAVVNVTYS
CCCCCCEEEEEEEEC
10.1421890473
123UbiquitinationDSETAVVNVTYSSKD
CCCEEEEEEEECCHH
17.5121890473
129AcetylationVNVTYSSKDQARQAL
EEEEECCHHHHHHHH
48.1730589459
130UbiquitinationNVTYSSKDQARQALD
EEEECCHHHHHHHHH
49.6922053931
135UbiquitinationSKDQARQALDKLNGF
CHHHHHHHHHHHCCC
16.5122817900
138UbiquitinationQARQALDKLNGFQLE
HHHHHHHHHCCCEEE
44.7122817900
143UbiquitinationLDKLNGFQLENFTLK
HHHHCCCEEECEEEE
49.6321890473
158SulfoxidationVAYIPDEMAAQQNPL
EEECCHHHHHHHCCC
4.9621406390
158UbiquitinationVAYIPDEMAAQQNPL
EEECCHHHHHHHCCC
4.9623503661
164UbiquitinationEMAAQQNPLQQPRGR
HHHHHHCCCCCCCCC
27.4927667366
172UbiquitinationLQQPRGRRGLGQRGS
CCCCCCCCCCCCCCC
47.7321890473
173UbiquitinationQQPRGRRGLGQRGSS
CCCCCCCCCCCCCCC
32.5723503661
179PhosphorylationRGLGQRGSSRQGSPG
CCCCCCCCCCCCCCC
25.2429396449
179UbiquitinationRGLGQRGSSRQGSPG
CCCCCCCCCCCCCCC
25.2427667366
180PhosphorylationGLGQRGSSRQGSPGS
CCCCCCCCCCCCCCC
31.2926055452
184PhosphorylationRGSSRQGSPGSVSKQ
CCCCCCCCCCCCCCC
20.1121955146
186 (in isoform 2)Ubiquitination-42.2321906983
187PhosphorylationSRQGSPGSVSKQKPC
CCCCCCCCCCCCCCC
26.9728176443
187UbiquitinationSRQGSPGSVSKQKPC
CCCCCCCCCCCCCCC
26.9721890473
189PhosphorylationQGSPGSVSKQKPCDL
CCCCCCCCCCCCCCC
30.9428176443
190AcetylationGSPGSVSKQKPCDLP
CCCCCCCCCCCCCCC
61.2525953088
190UbiquitinationGSPGSVSKQKPCDLP
CCCCCCCCCCCCCCC
61.2532015554
192UbiquitinationPGSVSKQKPCDLPLR
CCCCCCCCCCCCCEE
51.8832015554
195UbiquitinationVSKQKPCDLPLRLLV
CCCCCCCCCCEEEEE
60.9027667366
213UbiquitinationFVGAIIGKEGATIRN
HHHHHHCCCCCCHHH
42.4322817900
213 (in isoform 1)Ubiquitination-42.4321906983
218UbiquitinationIGKEGATIRNITKQT
HCCCCCCHHHHHHHH
2.9221890473
223NeddylationATIRNITKQTQSKID
CCHHHHHHHHHCCEE
47.7732015554
223UbiquitinationATIRNITKQTQSKID
CCHHHHHHHHHCCEE
47.7721906983
223 (in isoform 1)Ubiquitination-47.7721906983
225PhosphorylationIRNITKQTQSKIDVH
HHHHHHHHHCCEEHH
36.0420860994
228UbiquitinationITKQTQSKIDVHRKE
HHHHHHCCEEHHHHH
32.8622817900
233UbiquitinationQSKIDVHRKENAGAA
HCCEEHHHHHCCCCC
48.0822817900
234UbiquitinationSKIDVHRKENAGAAE
CCEEHHHHHCCCCCC
40.20-
242UbiquitinationENAGAAEKSITILST
HCCCCCCCEEEEEEC
42.2929967540
243PhosphorylationNAGAAEKSITILSTP
CCCCCCCEEEEEECC
19.2322199227
245PhosphorylationGAAEKSITILSTPEG
CCCCCEEEEEECCCC
23.9822199227
248PhosphorylationEKSITILSTPEGTSA
CCEEEEEECCCCHHH
37.7620068231
249PhosphorylationKSITILSTPEGTSAA
CEEEEEECCCCHHHH
23.1621815630
253PhosphorylationILSTPEGTSAACKSI
EEECCCCHHHHHHHH
17.3320068231
254PhosphorylationLSTPEGTSAACKSIL
EECCCCHHHHHHHHH
25.4020068231
257GlutathionylationPEGTSAACKSILEIM
CCCHHHHHHHHHHHH
3.3922555962
257S-nitrosylationPEGTSAACKSILEIM
CCCHHHHHHHHHHHH
3.392212679
258UbiquitinationEGTSAACKSILEIMH
CCHHHHHHHHHHHHH
35.4929967540
259PhosphorylationGTSAACKSILEIMHK
CHHHHHHHHHHHHHH
32.0828555341
266UbiquitinationSILEIMHKEAQDIKF
HHHHHHHHHHHCCCC
37.0532015554
271UbiquitinationMHKEAQDIKFTEEIP
HHHHHHCCCCCCCCC
2.3523503661
272UbiquitinationHKEAQDIKFTEEIPL
HHHHHCCCCCCCCCC
55.3027667366
272 (in isoform 1)Ubiquitination-55.3021906983
277UbiquitinationDIKFTEEIPLKILAH
CCCCCCCCCCCHHHC
3.8427667366
280AcetylationFTEEIPLKILAHNNF
CCCCCCCCHHHCCCH
30.2526051181
280UbiquitinationFTEEIPLKILAHNNF
CCCCCCCCHHHCCCH
30.2522817900
280 (in isoform 1)Ubiquitination-30.2521906983
283UbiquitinationEIPLKILAHNNFVGR
CCCCCHHHCCCHHHH
13.5621890473
285UbiquitinationPLKILAHNNFVGRLI
CCCHHHCCCHHHHHH
37.7221890473
293UbiquitinationNFVGRLIGKEGRNLK
CHHHHHHCCCCCCCH
26.9327667366
294UbiquitinationFVGRLIGKEGRNLKK
HHHHHHCCCCCCCHH
50.42-
300UbiquitinationGKEGRNLKKIEQDTD
CCCCCCCHHCCCCCC
56.08-
301UbiquitinationKEGRNLKKIEQDTDT
CCCCCCHHCCCCCCC
55.4229967540
308UbiquitinationKIEQDTDTKITISPL
HCCCCCCCCEEECCC
26.8321890473
309UbiquitinationIEQDTDTKITISPLQ
CCCCCCCCEEECCCC
40.4329967540
311PhosphorylationQDTDTKITISPLQEL
CCCCCCEEECCCCEE
19.5628122231
313PhosphorylationTDTKITISPLQELTL
CCCCEEECCCCEEEE
15.7728122231
318UbiquitinationTISPLQELTLYNPER
EECCCCEEEECCCCC
2.2927667366
321UbiquitinationPLQELTLYNPERTIT
CCCEEEECCCCCEEE
24.3627667366
330UbiquitinationPERTITVKGNVETCA
CCCEEEEECCHHHHH
35.8032015554
332UbiquitinationRTITVKGNVETCAKA
CEEEEECCHHHHHHH
23.8021890473
336UbiquitinationVKGNVETCAKAEEEI
EECCHHHHHHHHHHH
2.0127667366
338UbiquitinationGNVETCAKAEEEIMK
CCHHHHHHHHHHHHH
59.4829967540
342UbiquitinationTCAKAEEEIMKKIRE
HHHHHHHHHHHHHHH
39.6327667366
347UbiquitinationEEEIMKKIRESYEND
HHHHHHHHHHHHHHC
5.0121890473
348UbiquitinationEEIMKKIRESYENDI
HHHHHHHHHHHHHCH
35.3724816145
351UbiquitinationMKKIRESYENDIASM
HHHHHHHHHHCHHHH
17.6323503661
357UbiquitinationSYENDIASMNLQAHL
HHHHCHHHHHHHHHC
14.4527667366
367UbiquitinationLQAHLIPGLNLNALG
HHHHCCCCCCCCCCC
21.8727667366
372UbiquitinationIPGLNLNALGLFPPT
CCCCCCCCCCCCCCC
13.2321890473
382UbiquitinationLFPPTSGMPPPTSGP
CCCCCCCCCCCCCCC
4.5127667366
397UbiquitinationPSAMTPPYPQFEQSE
CCCCCCCCCCCCCCC
15.7424816145
400UbiquitinationMTPPYPQFEQSETET
CCCCCCCCCCCCCCE
8.7923503661
404UbiquitinationYPQFEQSETETVHLF
CCCCCCCCCCEEEEE
50.8123503661
410UbiquitinationSETETVHLFIPALSV
CCCCEEEEEEEHHHH
3.4622817900
412UbiquitinationTETVHLFIPALSVGA
CCEEEEEEEHHHHHH
2.1624816145
415UbiquitinationVHLFIPALSVGAIIG
EEEEEEHHHHHHHHC
3.4123503661
429AcetylationGKQGQHIKQLSRFAG
CCCCHHHHHHHHHCC
42.9627452117
429UbiquitinationGKQGQHIKQLSRFAG
CCCCHHHHHHHHHCC
42.9627667366
434UbiquitinationHIKQLSRFAGASIKI
HHHHHHHHCCCCEEE
7.0827667366
438PhosphorylationLSRFAGASIKIAPAE
HHHHCCCCEEEECCC
24.4028355574
440UbiquitinationRFAGASIKIAPAEAP
HHCCCCEEEECCCCC
30.2522817900
440 (in isoform 1)Ubiquitination-30.2521906983
445UbiquitinationSIKIAPAEAPDAKVR
CEEEECCCCCCCEEE
60.7321890473
4502-HydroxyisobutyrylationPAEAPDAKVRMVIIT
CCCCCCCEEEEEEEE
37.44-
450NeddylationPAEAPDAKVRMVIIT
CCCCCCCEEEEEEEE
37.4432015554
450SumoylationPAEAPDAKVRMVIIT
CCCCCCCEEEEEEEE
37.4428112733
450UbiquitinationPAEAPDAKVRMVIIT
CCCCCCCEEEEEEEE
37.4427667366
450 (in isoform 1)Ubiquitination-37.4421906983
453SulfoxidationAPDAKVRMVIITGPP
CCCCEEEEEEEECCC
2.5821406390
453UbiquitinationAPDAKVRMVIITGPP
CCCCEEEEEEEECCC
2.5823503661
455UbiquitinationDAKVRMVIITGPPEA
CCEEEEEEEECCCHH
1.3827667366
459UbiquitinationRMVIITGPPEAQFKA
EEEEEECCCHHHHHH
18.2122817900
465MethylationGPPEAQFKAQGRIYG
CCCHHHHHHCCCEEE
27.9324711551
465UbiquitinationGPPEAQFKAQGRIYG
CCCHHHHHHCCCEEE
27.9322817900
465 (in isoform 1)Ubiquitination-27.9321906983
468UbiquitinationEAQFKAQGRIYGKIK
HHHHHHCCCEEEEEC
23.8623503661
470UbiquitinationQFKAQGRIYGKIKEE
HHHHCCCEEEEECHH
7.3221890473
473UbiquitinationAQGRIYGKIKEENFV
HCCCEEEEECHHCCC
33.36-
474UbiquitinationQGRIYGKIKEENFVS
CCCEEEEECHHCCCC
6.1922817900
475SumoylationGRIYGKIKEENFVSP
CCEEEEECHHCCCCC
63.56-
475AcetylationGRIYGKIKEENFVSP
CCEEEEECHHCCCCC
63.5626051181
475SumoylationGRIYGKIKEENFVSP
CCEEEEECHHCCCCC
63.5628112733
475UbiquitinationGRIYGKIKEENFVSP
CCEEEEECHHCCCCC
63.5627667366
480UbiquitinationKIKEENFVSPKEEVK
EECHHCCCCCHHHEE
16.8427667366
481PhosphorylationIKEENFVSPKEEVKL
ECHHCCCCCHHHEEE
26.5621815630
483UbiquitinationEENFVSPKEEVKLEA
HHCCCCCHHHEEEEE
60.0333845483
487UbiquitinationVSPKEEVKLEAHIRV
CCCHHHEEEEEEEEC
43.8429967540
496PhosphorylationEAHIRVPSFAAGRVI
EEEEECCCHHHCCEE
25.3527273156
505AcetylationAAGRVIGKGGKTVNE
HHCCEECCCCCCHHH
54.0619828211
505UbiquitinationAAGRVIGKGGKTVNE
HHCCEECCCCCCHHH
54.0624816145
508AcetylationRVIGKGGKTVNELQN
CEECCCCCCHHHHCC
58.9526051181
508UbiquitinationRVIGKGGKTVNELQN
CEECCCCCCHHHHCC
58.9532015554
510UbiquitinationIGKGGKTVNELQNLS
ECCCCCCHHHHCCCC
6.2924816145
513UbiquitinationGGKTVNELQNLSSAE
CCCCHHHHCCCCCCE
3.2723503661
528PhosphorylationVVVPRDQTPDENDQV
EEECCCCCCCCCCCE
36.6829255136
540PhosphorylationDQVVVKITGHFYACQ
CCEEEEEECCHHHHH
20.9123663014
544PhosphorylationVKITGHFYACQVAQR
EEEECCHHHHHHHHH
10.7823663014
552UbiquitinationACQVAQRKIQEILTQ
HHHHHHHHHHHHHHH
36.3429967540
558PhosphorylationRKIQEILTQVKQHQQ
HHHHHHHHHHHHHHH
36.6629514088
561UbiquitinationQEILTQVKQHQQQKA
HHHHHHHHHHHHHHH
32.0432015554
566UbiquitinationQVKQHQQQKALQSGP
HHHHHHHHHHHHCCC
26.8123503661
567UbiquitinationVKQHQQQKALQSGPP
HHHHHHHHHHHCCCC
46.8827667366
567 (in isoform 1)Ubiquitination-46.8821906983
571PhosphorylationQQQKALQSGPPQSRR
HHHHHHHCCCCCCCC
54.8620068231
572UbiquitinationQQKALQSGPPQSRRK
HHHHHHCCCCCCCCC
25.5822817900
576PhosphorylationLQSGPPQSRRK----
HHCCCCCCCCC----
39.5725159151

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 IF2B3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IF2B3_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 IF2B3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAP4A_HUMANLAPTM4Aphysical
22939629
LGMN_HUMANLGMNphysical
22939629
UBP16_HUMANUSP16physical
22939629
NDUF4_HUMANNDUFAF4physical
22939629
QOR_HUMANCRYZphysical
22863883
ROA2_HUMANHNRNPA2B1physical
22863883
HNRPM_HUMANHNRNPMphysical
22863883
HNRPU_HUMANHNRNPUphysical
22863883
SYIC_HUMANIARSphysical
22863883
K1C17_HUMANKRT17physical
22863883
MRE11_HUMANMRE11Aphysical
22863883
PA2G4_HUMANPA2G4physical
22863883
RL23A_HUMANRPL23Aphysical
22863883
PIHD2_HUMANPIH1D2physical
25416956
G3BP2_HUMANG3BP2physical
26344197
RAB2A_HUMANRAB2Aphysical
26344197
RL37A_HUMANRPL37Aphysical
26344197
SH3BG_HUMANSH3BGRphysical
28514442

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 IF2B3_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 THR-528, AND MASSSPECTROMETRY.
"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 THR-528, AND MASSSPECTROMETRY.

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