IBP6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IBP6_HUMAN
• UniProt AC: P24592
• Protein Name: Insulin-like growth factor-binding protein 6
• Gene Name: IGFBP6
• Organism: Homo sapiens (Human).
• Sequence Length: 240
• 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..
• Protein Sequence: MTPHRLLPPLLLLLALLLAASPGGALARCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPARAPAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEMGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSCPTGSSG

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
120	O-linked_Glycosylation	AEENPKESKPQAGTA HCCCCCCCCCCCCCC	56.62	55825225
126	O-linked_Glycosylation	ESKPQAGTARPQDVN CCCCCCCCCCCCCCC	23.62	9572875
126	O-linked_Glycosylation	ESKPQAGTARPQDVN CCCCCCCCCCCCCCC	23.62	9572875
143	O-linked_Glycosylation	DQQRNPGTSTTPSQP HHHCCCCCCCCCCCC	24.94	OGP
144	O-linked_Glycosylation	QQRNPGTSTTPSQPN HHCCCCCCCCCCCCC	35.88	-
144	O-linked_Glycosylation	QQRNPGTSTTPSQPN HHCCCCCCCCCCCCC	35.88	9572875
145	O-linked_Glycosylation	QRNPGTSTTPSQPNS HCCCCCCCCCCCCCC	42.43	9572875
145	O-linked_Glycosylation	QRNPGTSTTPSQPNS HCCCCCCCCCCCCCC	42.43	9572875
146	O-linked_Glycosylation	RNPGTSTTPSQPNSA CCCCCCCCCCCCCCC	22.25	9572875
146	O-linked_Glycosylation	RNPGTSTTPSQPNSA CCCCCCCCCCCCCCC	22.25	9572875
148	Phosphorylation	PGTSTTPSQPNSAGV CCCCCCCCCCCCCCC	57.06	27251275
148	O-linked_Glycosylation	PGTSTTPSQPNSAGV CCCCCCCCCCCCCCC	57.06	OGP
152	Phosphorylation	TTPSQPNSAGVQDTE CCCCCCCCCCCCCCC	32.84	24505115
152	O-linked_Glycosylation	TTPSQPNSAGVQDTE CCCCCCCCCCCCCCC	32.84	-
152	O-linked_Glycosylation	TTPSQPNSAGVQDTE CCCCCCCCCCCCCCC	32.84	9572875
176	O-linked_Glycosylation	SVLQQLQTEVYRGAQ HHHHHHHHHHHCCCC	35.69	55834601
184	Phosphorylation	EVYRGAQTLYVPNCD HHHCCCCEEECCCCC	21.37	24732914
184	O-linked_Glycosylation	EVYRGAQTLYVPNCD HHHCCCCEEECCCCC	21.37	55825363
186	Phosphorylation	YRGAQTLYVPNCDHR HCCCCEEECCCCCCC	19.76	24732914
204	Phosphorylation	RKRQCRSSQGQRRGP CCCCCCCCCCCCCCC	20.98	-
204	O-linked_Glycosylation	RKRQCRSSQGQRRGP CCCCCCCCCCCCCCC	20.98	56220401
231	Phosphorylation	GSPDGNGSSSCPTGS CCCCCCCCCCCCCCC	24.07	-
233	Phosphorylation	PDGNGSSSCPTGSSG CCCCCCCCCCCCCCC	26.30	30576142
236	Phosphorylation	NGSSSCPTGSSG--- CCCCCCCCCCCC---	54.76	30576142
238	Phosphorylation	SSSCPTGSSG----- CCCCCCCCCC-----	34.07	30576142

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

Oops, there are no upstream regulatory protein records of IBP6_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IBP6_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IBP6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TCAF2_HUMAN	FAM115C	physical	28514442
PP2BC_HUMAN	PPP3CC	physical	28514442
CANB1_HUMAN	PPP3R1	physical	28514442
CDK19_HUMAN	CDK19	physical	28514442
PSMG3_HUMAN	PSMG3	physical	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.

Related Literatures of Post-Translational Modification

O-linked Glycosylation

"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-126, STRUCTURE OFCARBOHYDRATES, AND MASS SPECTROMETRY.
PubMed: 19838169

"Identification of O-glycosylation sites and partial characterizationof carbohydrate structure and disulfide linkages of human insulin-likegrowth factor binding protein 6.";
Neumann G.M., Marinaro J.A., Bach L.A.;
Biochemistry 37:6572-6585(1998).
Cited for: GLYCOSYLATION AT THR-126; SER-144; THR-145; THR-146 AND SER-152.
PubMed: 9572875