P24592 · IBP6_HUMAN

  • Protein
    Insulin-like growth factor-binding protein 6
  • Gene
    IGFBP6
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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 annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Cellular Componentextracellular space
Cellular Componentinsulin-like growth factor binary complex
Molecular Functionfibronectin binding
Molecular Functionidentical protein binding
Molecular Functioninsulin-like growth factor I binding
Molecular Functioninsulin-like growth factor II binding
Molecular Functionsignaling receptor binding
Biological Processcell migration
Biological Processnegative regulation of canonical Wnt signaling pathway
Biological Processnegative regulation of cell population proliferation
Biological Processpositive regulation of MAPK cascade
Biological Processpositive regulation of stress-activated MAPK cascade
Biological Processregulation of insulin-like growth factor receptor signaling pathway
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Insulin-like growth factor-binding protein 6
  • Short names
    IBP-6; IGF-binding protein 6; IGFBP-6

Gene names

    • Name
      IGFBP6
    • Synonyms
      IBP6

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    P24592
  • Secondary accessions
    • Q14492

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_018932128in dbSNP:rs9658616
Natural variantVAR_049565134in dbSNP:rs34995393
Natural variantVAR_018933217in dbSNP:rs6413498
Natural variantVAR_011907236in dbSNP:rs1053134

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.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation.

TypeIDPosition(s)Description
Signal1-27
ChainPRO_000001438928-240Insulin-like growth factor-binding protein 6
Disulfide bond29↔32
Disulfide bond40↔44
Disulfide bond57↔63
Disulfide bond71↔84
Disulfide bond78↔104
Glycosylation126O-linked (HexNAc...) threonine
Glycosylation144O-linked (HexNAc...) serine
Glycosylation145O-linked (HexNAc...) threonine
Glycosylation146O-linked (HexNAc...) threonine
Glycosylation152O-linked (HexNAc...) serine
Disulfide bond163↔190
Disulfide bond201↔212
Disulfide bond214↔234

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

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts (via C-terminal domain) with PHB2.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P24592ALPP P051873EBI-947015, EBI-1211484
BINARY P24592ANKRD11 X5D7783EBI-947015, EBI-17183751
BINARY P24592AQP1 P299723EBI-947015, EBI-745213
BINARY P24592C1orf74 Q96LT63EBI-947015, EBI-12049899
BINARY P24592CCDC116 Q8IYX33EBI-947015, EBI-744311
BINARY P24592CCDC28A Q7Z6N93EBI-947015, EBI-10258115
BINARY P24592CDIPT O147353EBI-947015, EBI-358858
BINARY P24592CREB5 Q02930-33EBI-947015, EBI-10192698
BINARY P24592EFEMP1 Q128053EBI-947015, EBI-536772
BINARY P24592EFEMP2 O959673EBI-947015, EBI-743414
BINARY P24592ENKD1 Q9H0I23EBI-947015, EBI-744099
BINARY P24592EPDR1 Q9UM223EBI-947015, EBI-946972
BINARY P24592GAS8 O959953EBI-947015, EBI-1052570
BINARY P24592GET3 O436813EBI-947015, EBI-2515857
BINARY P24592IGFBP6 P245923EBI-947015, EBI-947015
BINARY P24592KRTAP10-8 P604103EBI-947015, EBI-10171774
BINARY P24592KRTAP5-7 Q6L8G83EBI-947015, EBI-11987425
BINARY P24592KRTAP5-9 P263713EBI-947015, EBI-3958099
BINARY P24592MBD3 O95983-23EBI-947015, EBI-11978579
BINARY P24592MEIS2 O14770-43EBI-947015, EBI-8025850
BINARY P24592MSGN1 A6NI153EBI-947015, EBI-11991020
BINARY P24592NCALD P616013EBI-947015, EBI-749635
BINARY P24592PLEKHA7 Q6IQ23-23EBI-947015, EBI-12069346
BINARY P24592POU4F2 Q128373EBI-947015, EBI-17236143
BINARY P24592RABGGTB P536113EBI-947015, EBI-536715
BINARY P24592RANBP10 Q6VN203EBI-947015, EBI-310569
BINARY P24592SDCBP O005603EBI-947015, EBI-727004
BINARY P24592SGTA O437653EBI-947015, EBI-347996
BINARY P24592SMCP P499013EBI-947015, EBI-750494
BINARY P24592UBAC1 Q9BSL13EBI-947015, EBI-749370
BINARY P24592UBQLN1 Q9UMX03EBI-947015, EBI-741480
BINARY P24592UBQLN2 Q9UHD93EBI-947015, EBI-947187
BINARY P24592ZNF417 Q8TAU35EBI-947015, EBI-740727
BINARY P24592ZNF587 Q96SQ53EBI-947015, EBI-6427977

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain28-107IGFBP N-terminal
Region109-160Disordered
Compositional bias126-156Polar residues
Domain160-234Thyroglobulin type-1
Region217-240Disordered
Compositional bias225-240Polar residues

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    240
  • Mass (Da)
    25,322
  • Last updated
    1992-03-01 v1
  • Checksum
    285308231C025009
MTPHRLLPPLLLLLALLLAASPGGALARCPGCGQGVQAGCPGGCVEEEDGGSPAEGCAEAEGCLRREGQECGVYTPNCAPGLQCHPPKDDEAPLRALLLGRGRCLPARAPAVAEENPKESKPQAGTARPQDVNRRDQQRNPGTSTTPSQPNSAGVQDTEMGPCRRHLDSVLQQLQTEVYRGAQTLYVPNCDHRGFYRKRQCRSSQGQRRGPCWCVDRMGKSLPGSPDGNGSSSCPTGSSG

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F8VYK9F8VYK9_HUMANIGFBP6238
F8VVA5F8VVA5_HUMANIGFBP6136
A0A3B3IUE0A0A3B3IUE0_HUMANIGFBP681

Features

Showing features for sequence conflict, compositional bias.

TypeIDPosition(s)Description
Sequence conflict2in Ref. 5; AAA88070
Sequence conflict28-29in Ref. 6; AA sequence
Sequence conflict28-29in Ref. 8; AA sequence
Sequence conflict32in Ref. 6; AA sequence
Sequence conflict55-57in Ref. 6; AA sequence
Compositional bias126-156Polar residues
Compositional bias225-240Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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