IBP3_HUMAN - dbPTM
IBP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IBP3_HUMAN
UniProt AC P17936
Protein Name Insulin-like growth factor-binding protein 3
Gene Name IGFBP3
Organism Homo sapiens (Human).
Sequence Length 291
Subcellular Localization Secreted .
Protein Description IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R..
Protein Sequence MQRARPTLWAAALTLLVLLRGPPVARAGASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPLHSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHCYSMQSK
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
7Phosphorylation-MQRARPTLWAAALT
-CCCCHHHHHHHHHH		29.4024043423
14PhosphorylationTLWAAALTLLVLLRG
HHHHHHHHHHHHHHC		17.2024043423
116N-linked_GlycosylationDGRGLCVNASAVSRL
CCCCEECCHHHHHHH		27.4718638581
116N-linked_GlycosylationDGRGLCVNASAVSRL
CCCCEECCHHHHHHH		27.4710076184
126PhosphorylationAVSRLRAYLLPAPPA
HHHHHHHHHCCCCCC		11.4430242111
136N-linked_GlycosylationPAPPAPGNASESEED
CCCCCCCCCCCCCCH		38.9519139490
138PhosphorylationPPAPGNASESEEDRS
CCCCCCCCCCCCHHC		45.7326657352
140PhosphorylationAPGNASESEEDRSAG
CCCCCCCCCCHHCCC		43.737530253
144 (in isoform 2)Phosphorylation-31.5210650937
145PhosphorylationSESEEDRSAGSVESP
CCCCCHHCCCCCCCC		49.6729759185
146 (in isoform 2)Phosphorylation-18.3810650937
148PhosphorylationEEDRSAGSVESPSVS
CCHHCCCCCCCCCCC		23.5623911959
148O-linked_GlycosylationEEDRSAGSVESPSVS
CCHHCCCCCCCCCCC		23.5655818115
151O-linked_GlycosylationRSAGSVESPSVSSTH
HCCCCCCCCCCCCCC		21.9655828039
151PhosphorylationRSAGSVESPSVSSTH
HCCCCCCCCCCCCCC		21.9628857561
153O-linked_GlycosylationAGSVESPSVSSTHRV
CCCCCCCCCCCCCCC		43.8655828045
153PhosphorylationAGSVESPSVSSTHRV
CCCCCCCCCCCCCCC		43.8628857561
154PhosphorylationGSVESPSVSSTHRVS
CCCCCCCCCCCCCCC		6.2624719451
155O-linked_GlycosylationSVESPSVSSTHRVSD
CCCCCCCCCCCCCCC		33.5855828049
155PhosphorylationSVESPSVSSTHRVSD
CCCCCCCCCCCCCCC		33.5823312004
156PhosphorylationVESPSVSSTHRVSDP
CCCCCCCCCCCCCCC		26.5223312004
156O-linked_GlycosylationVESPSVSSTHRVSDP
CCCCCCCCCCCCCCC		26.5255828053
157O-linked_GlycosylationESPSVSSTHRVSDPK
CCCCCCCCCCCCCCC		13.2455828059
157PhosphorylationESPSVSSTHRVSDPK
CCCCCCCCCCCCCCC		13.2420071362
161O-linked_GlycosylationVSSTHRVSDPKFHPL
CCCCCCCCCCCCCCC		48.4255828065
161PhosphorylationVSSTHRVSDPKFHPL
CCCCCCCCCCCCCCC		48.42-
170PhosphorylationPKFHPLHSKIIIIKK
CCCCCCCCEEEEEEC		32.98-
183PhosphorylationKKGHAKDSQRYKVDY
ECCCCCCCCCEEECC		18.8217108124
186PhosphorylationHAKDSQRYKVDYESQ
CCCCCCCEEECCCCC		14.0227130503
190PhosphorylationSQRYKVDYESQSTDT
CCCEEECCCCCCCCC		22.0728270605
192PhosphorylationRYKVDYESQSTDTQN
CEEECCCCCCCCCCC		24.1728270605
192O-linked_GlycosylationRYKVDYESQSTDTQN
CEEECCCCCCCCCCC		24.1755826341
194PhosphorylationKVDYESQSTDTQNFS
EECCCCCCCCCCCCC		37.2119556345
195O-linked_GlycosylationVDYESQSTDTQNFSS
ECCCCCCCCCCCCCC		35.1155826347
195PhosphorylationVDYESQSTDTQNFSS
ECCCCCCCCCCCCCC		35.1126657352
197PhosphorylationYESQSTDTQNFSSES
CCCCCCCCCCCCCCH		26.0426657352
199N-linked_GlycosylationSQSTDTQNFSSESKR
CCCCCCCCCCCCHHH		40.6410076184
199N-linked_GlycosylationSQSTDTQNFSSESKR
CCCCCCCCCCCCHHH		40.6410076184
201PhosphorylationSTDTQNFSSESKRET
CCCCCCCCCCHHHCC		40.5229255136
202PhosphorylationTDTQNFSSESKRETE
CCCCCCCCCHHHCCC		41.5730206219
203PhosphorylationDTQNFSSESKRETEY
CCCCCCCCHHHCCCC		60.1127251275
204PhosphorylationTQNFSSESKRETEYG
CCCCCCCHHHCCCCC		38.6729255136
207PhosphorylationFSSESKRETEYGPCR
CCCCHHHCCCCCCCH		50.1324719451
210PhosphorylationESKRETEYGPCRREM
CHHHCCCCCCCHHHH		33.51-
231PhosphorylationLKFLNVLSPRGVHIP
HHHHHHCCCCCCCCC		14.31-
246PhosphorylationNCDKKGFYKKKQCRP
CCCCCCCCCCCCCCC		30.48-
277O-linked_GlycosylationQPLPGYTTKGKEDVH
CCCCCCCCCCCCCCE		29.3455825755
287PhosphorylationKEDVHCYSMQSK---
CCCCEEEECCCC---		18.7528348404
290PhosphorylationVHCYSMQSK------
CEEEECCCC------		31.5228348404
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
138SPhosphorylationKinaseCSNK2A1P68400
GPS
138SPhosphorylationKinaseCK2-FAMILY-GPS
138SPhosphorylationKinaseCK2_GROUP-PhosphoELM
140SPhosphorylationKinaseCSNK2A1P68400
GPS
140SPhosphorylationKinaseCK2-FAMILY-GPS
140SPhosphorylationKinaseCK2_GROUP-PhosphoELM
148SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
183SPhosphorylationKinasePRKDCP78527
GPS
194SPhosphorylationKinaseCSNK2A1P68400
GPS
201SPhosphorylationKinaseFAM20CQ8IXL6
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IBP3_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 IBP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CO1A1_HUMANCOL1A1physical
12735930
LTBP1_MOUSELtbp1physical
12962157
IGF2_MOUSEIgf2physical
12962157
DPOA2_HUMANPOLA2physical
16169070
TF3C1_HUMANGTF3C1physical
16169070
IGF1R_HUMANIGF1Rphysical
9389554
CD44_HUMANCD44physical
12127836
FINC_HUMANFN1physical
12127836
ADA12_HUMANADAM12physical
10849447
IGF1_HUMANIGF1physical
11600567
IGF2_HUMANIGF2physical
11600567
TRFE_HUMANTFphysical
11297622
FINC_HUMANFN1physical
11344214
IGF1_HUMANIGF1physical
1383255
IGF1_HUMANIGF1physical
9446566
IGF2_HUMANIGF2physical
9446566
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 IBP3_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136, AND MASSSPECTROMETRY.
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry.";
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.;
J. Proteome Res. 4:2070-2080(2005).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-199, AND MASSSPECTROMETRY.
"Screening for N-glycosylated proteins by liquid chromatography massspectrometry.";
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
Proteomics 4:454-465(2004).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"An initial characterization of the serum phosphoproteome.";
Zhou W., Ross M.M., Tessitore A., Ornstein D., Vanmeter A.,Liotta L.A., Petricoin E.F. III;
J. Proteome Res. 8:5523-5531(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-195 AND SER-201, TISSUESPECIFICITY, AND MASS SPECTROMETRY.

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