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insulin-like growth factor-binding protein 6; IBP-6; IGF-binding protein 6; IGFBP-6 (IGFBP6 IBP6)

Function: - IGF-binding proteins prolong the half-life of the IGFs - they 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 Structure: - O-glycosylated - O-linked glycans consist of hexose (probably gal), N-acetylhexosamine (probably galNAc) & sialic acid residues - O-glycosylated with core 1 glycan or possibly core 8 glycan - O-glycosylated on one site only in the region AA 143-168 in cerebrospinal fluid - contains 1 IGFBP N-terminal domain - contains 1 thyroglobulin type-1 domain Compartment: secreted

General

glycoprotein insulin-like growth factor [IGF]-binding protein

Properties

SIZE: entity length = 240 aa MW = 25 kD COMPARTMENT: extracellular compartment MOTIF: signal sequence {1-27} IGFBP N-terminal {28-107} MOTIF: cysteine residue {C29} MODIFICATION: cysteine residue {C32} cysteine residue {C32} MODIFICATION: cysteine residue {C29} cysteine residue {C40} MODIFICATION: cysteine residue {C44} cysteine residue {C44} MODIFICATION: cysteine residue {C40} cysteine residue {C57} MODIFICATION: cysteine residue {C63} cysteine residue {C63} MODIFICATION: cysteine residue {C57} cysteine residue {C71} MODIFICATION: cysteine residue {C84} cysteine residue {C78} MODIFICATION: cysteine residue {C104} cysteine residue {C84} MODIFICATION: cysteine residue {C71} cysteine residue {C104} MODIFICATION: cysteine residue {C78} Thr glycosylation site {T126} Ser glycosylation site {S144} Thr glycosylation site {T145} Thr glycosylation site {T146} Ser glycosylation site {S152} Thyroglobulin type-1 {160-234} MOTIF: cysteine residue {C163} MODIFICATION: cysteine residue {C190} cysteine residue {C190} MODIFICATION: cysteine residue {C163} cysteine residue {C201} MODIFICATION: cysteine residue {C212} cysteine residue {C212} MODIFICATION: cysteine residue {C201} cysteine residue {C214} MODIFICATION: cysteine residue {C234} cysteine residue {C234} MODIFICATION: cysteine residue {C214} SECRETED-BY: hepatocyte smooth muscle

Database Correlations

OMIM 146735 UniProt P24592 PFAM correlations Entrez Gene 3489 Kegg hsa:3489

References

  1. UniProt :accession P24592
  2. NIEHS-SNPs http://egp.gs.washington.edu/data/igfbp6/
  3. Entrez Gene :accession 3489