IGF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IGF2_HUMAN
• UniProt AC: P01344
• Protein Name: Insulin-like growth factor II
• Gene Name: IGF2
• Organism: Homo sapiens (Human).
• Sequence Length: 180
• Subcellular Localization: Secreted .
• Protein Description: The insulin-like growth factors possess growth-promoting activity. Major fetal growth hormone in mammals. Plays a key role in regulating fetoplacental development. IGF-II is influenced by placental lactogen. Also involved in tissue differentiation. Positively regulates myogenic transcription factor MYOD1 function by facilitating the recruitment of transcriptional coactivators, thereby controlling muscle terminal differentiation (By similarity). In adults, involved in glucose metabolism in adipose tissue, skeletal muscle and liver (Probable). Acts as a ligand for integrin which is required for IGF2 signaling. [PubMed: 28873464; Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.]
• Protein Sequence: MGIPMGKSMLVLLTFLAFASCCIAAYRPSETLCGGELVDTLQFVCGDRGFYFSRPASRVSRRSRGIVEECCFRSCDLALLETYCATPAKSERDVSTPPTVLPDNFPRYPVGKFFQYDTWKQSTQRLRRGLPALLRARRGHVLAKELEAFREAKRHRPLIALPTQDPAHGGAPPEMASNRK

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
57	O-linked_Glycosylation	FYFSRPASRVSRRSR EECCCCHHHCCHHHC	35.58	31492838
60	O-linked_Glycosylation	SRPASRVSRRSRGIV CCCHHHCCHHHCCHH	22.36	31492838
83	Phosphorylation	DLALLETYCATPAKS CHHHHHHHCCCCCCC	3.18	19060867
86	O-linked_Glycosylation	LLETYCATPAKSERD HHHHHCCCCCCCCCC	21.88	OGP
90	Phosphorylation	YCATPAKSERDVSTP HCCCCCCCCCCCCCC	39.71	24505115
95	O-linked_Glycosylation	AKSERDVSTPPTVLP CCCCCCCCCCCCCCC	39.21	7685912
96	O-linked_Glycosylation	KSERDVSTPPTVLPD CCCCCCCCCCCCCCC	32.89	22171320
99	O-linked_Glycosylation	RDVSTPPTVLPDNFP CCCCCCCCCCCCCCC	35.56	22171320
116	Phosphorylation	PVGKFFQYDTWKQST CCCCHHCCCHHHHHH	15.35	-
163	O-linked_Glycosylation	RPLIALPTQDPAHGG CCEEECCCCCCCCCC	46.59	22171320

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

Oops, there are no upstream regulatory protein records of IGF2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
96	T	Glycosylation	Thr-96 is a minor glycosylation site compared to Thr-99.	22171320
99	T	Glycosylation	Thr-96 is a minor glycosylation site compared to Thr-99.	1569071

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IGF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IBP1_HUMAN	IGFBP1	physical	10810289
TRFE_HUMAN	TF	physical	11749962
IBP3_HUMAN	IGFBP3	physical	11749962
IBP6_HUMAN	IGFBP6	physical	7683646
IBP3_HUMAN	IGFBP3	physical	9497324
IBP5_HUMAN	IGFBP5	physical	9497324
BAG6_HUMAN	BAG6	physical	21900206
NRK2_HUMAN	NMRK2	physical	21900206
FAF1_HUMAN	FAF1	physical	21900206
RBPMS_HUMAN	RBPMS	physical	25416956

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 180860: Silver-Russell syndrome (SRS)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

O-linked Glycosylation

"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT THR-96; THR-99 AND THR-163, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
PubMed: 22171320

"Enrichment of glycopeptides for glycan structure and attachment siteidentification.";
Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E.,Brinkmalm G., Larson G.;
Nat. Methods 6:809-811(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-163, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
PubMed: 19838169

"The identification of O-glycosylated precursors of insulin-likegrowth factor II.";
Hudgins W.R., Hampton B., Burgess W.H., Perdue J.F.;
J. Biol. Chem. 267:8153-8160(1992).
Cited for: GLYCOSYLATION AT THR-99.
PubMed: 1569071