P24592 · IBP6_HUMAN
- ProteinInsulin-like growth factor-binding protein 6
- GeneIGFBP6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids240 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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. Activates the MAPK signaling pathway and induces cell migration (PubMed:24003225).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | extracellular space | |
Cellular Component | insulin-like growth factor binary complex | |
Molecular Function | fibronectin binding | |
Molecular Function | identical protein binding | |
Molecular Function | insulin-like growth factor I binding | |
Molecular Function | insulin-like growth factor II binding | |
Molecular Function | signaling receptor binding | |
Biological Process | cell migration | |
Biological Process | negative regulation of canonical Wnt signaling pathway | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | positive regulation of MAPK cascade | |
Biological Process | positive regulation of stress-activated MAPK cascade | |
Biological Process | regulation of insulin-like growth factor receptor signaling pathway | |
Biological Process | signal transduction |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameInsulin-like growth factor-binding protein 6
- Short namesIBP-6; IGF-binding protein 6; IGFBP-6
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP24592
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_018932 | 128 | in dbSNP:rs9658616 | |||
Sequence: R → G | ||||||
Natural variant | VAR_049565 | 134 | in dbSNP:rs34995393 | |||
Sequence: R → L | ||||||
Natural variant | VAR_018933 | 217 | in dbSNP:rs6413498 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_011907 | 236 | in dbSNP:rs1053134 | |||
Sequence: T → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 294 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-27 | |||||
Sequence: MTPHRLLPPLLLLLALLLAASPGGALA | ||||||
Chain | PRO_0000014389 | 28-240 | Insulin-like growth factor-binding protein 6 | |||
Sequence: RCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPARAPAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEMGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSCPTGSSG | ||||||
Disulfide bond | 29↔32 | |||||
Sequence: CPGC | ||||||
Disulfide bond | 40↔44 | |||||
Sequence: CPGGC | ||||||
Disulfide bond | 57↔63 | |||||
Sequence: CAEAEGC | ||||||
Disulfide bond | 71↔84 | |||||
Sequence: CGVYTPNCAPGLQC | ||||||
Disulfide bond | 78↔104 | |||||
Sequence: CAPGLQCHPPKDDEAPLRALLLGRGRC | ||||||
Glycosylation | 126 | O-linked (HexNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 144 | O-linked (HexNAc...) serine | ||||
Sequence: S | ||||||
Glycosylation | 145 | O-linked (HexNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 146 | O-linked (HexNAc...) threonine | ||||
Sequence: T | ||||||
Glycosylation | 152 | O-linked (HexNAc...) serine | ||||
Sequence: S | ||||||
Disulfide bond | 163↔190 | |||||
Sequence: CRRHLDSVLQQLQTEVYRGAQTLYVPNC | ||||||
Disulfide bond | 201↔212 | |||||
Sequence: CRSSQGQRRGPC | ||||||
Disulfide bond | 214↔234 | |||||
Sequence: CVDRMGKSLPGSPDGNGSSSC |
Post-translational modification
O-linked glycans consist of hexose (probably Gal), N-acetylhexosamine (probably GalNAc) and sialic acid residues. O-glycosylated with core 1 or possibly core 8 glycans. O-glycosylated on one site only in the region AA 143-168 in cerebrospinal fluid.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts (via C-terminal domain) with PHB2.
Binary interactions
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 28-107 | IGFBP N-terminal | ||||
Sequence: RCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPA | ||||||
Region | 109-160 | Disordered | ||||
Sequence: APAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEM | ||||||
Compositional bias | 126-156 | Polar residues | ||||
Sequence: TARPQDVNRRDQQRNPGTSTTPSQPNSAGVQ | ||||||
Domain | 160-234 | Thyroglobulin type-1 | ||||
Sequence: MGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSC | ||||||
Region | 217-240 | Disordered | ||||
Sequence: RMGKSLPGSPDGNGSSSCPTGSSG | ||||||
Compositional bias | 225-240 | Polar residues | ||||
Sequence: SPDGNGSSSCPTGSSG |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length240
- Mass (Da)25,322
- Last updated1992-03-01 v1
- Checksum285308231C025009
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8VYK9 | F8VYK9_HUMAN | IGFBP6 | 238 | ||
F8VVA5 | F8VVA5_HUMAN | IGFBP6 | 136 | ||
A0A3B3IUE0 | A0A3B3IUE0_HUMAN | IGFBP6 | 81 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 2 | in Ref. 5; AAA88070 | ||||
Sequence: T → C | ||||||
Sequence conflict | 28-29 | in Ref. 6; AA sequence | ||||
Sequence: RC → AA | ||||||
Sequence conflict | 28-29 | in Ref. 8; AA sequence | ||||
Sequence: RC → LA | ||||||
Sequence conflict | 32 | in Ref. 6; AA sequence | ||||
Sequence: C → H | ||||||
Sequence conflict | 55-57 | in Ref. 6; AA sequence | ||||
Sequence: EGC → QGG | ||||||
Compositional bias | 126-156 | Polar residues | ||||
Sequence: TARPQDVNRRDQQRNPGTSTTPSQPNSAGVQ | ||||||
Compositional bias | 225-240 | Polar residues | ||||
Sequence: SPDGNGSSSCPTGSSG |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M62402 EMBL· GenBank· DDBJ | AAB06187.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ006952 EMBL· GenBank· DDBJ | CAA07346.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY443494 EMBL· GenBank· DDBJ | AAR05445.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003507 EMBL· GenBank· DDBJ | AAH03507.1 EMBL· GenBank· DDBJ | mRNA | ||
BC005007 EMBL· GenBank· DDBJ | AAH05007.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010162 EMBL· GenBank· DDBJ | AAH10162.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011708 EMBL· GenBank· DDBJ | AAH11708.1 EMBL· GenBank· DDBJ | mRNA | ||
M69054 EMBL· GenBank· DDBJ | AAA88070.1 EMBL· GenBank· DDBJ | mRNA |