P17936 · IBP3_HUMAN
- ProteinInsulin-like growth factor-binding protein 3
- GeneIGFBP3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids291 (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. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. Inhibits the positive effect of humanin on insulin sensitivity (PubMed:19623253).
Promotes testicular germ cell apoptosis (PubMed:19952275).
Promotes testicular germ cell apoptosis (PubMed:19952275).
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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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameInsulin-like growth factor-binding protein 3
- Short namesIBP-3; IGF-binding protein 3; IGFBP-3
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP17936
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_036279 | 7 | in a colorectal cancer sample; somatic mutation; dbSNP:rs754430221 | |||
Sequence: T → M | ||||||
Natural variant | VAR_025262 | 32 | in dbSNP:rs2854746 | |||
Sequence: A → G | ||||||
Natural variant | VAR_025263 | 56 | in dbSNP:rs34257987 | |||
Sequence: A → T | ||||||
Natural variant | VAR_021974 | 158 | in dbSNP:rs9282734 | |||
Sequence: H → P | ||||||
Natural variant | VAR_025264 | 234 | in dbSNP:rs35712717 | |||
Sequence: G → S | ||||||
Natural variant | VAR_036280 | 252 | in a colorectal cancer sample; somatic mutation; dbSNP:rs538312081 | |||
Sequence: R → C |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 364 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, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-27 | UniProt | |||||
Sequence: MQRARPTLWAAALTLLVLLRGPPVARA | |||||||
Chain | PRO_0000014378 | 28-291 | UniProt | Insulin-like growth factor-binding protein 3 | |||
Sequence: GASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAPGNASESEEDRSAGSVESPSVSSTHRVSDPKFHPLHSKIIIIKKGHAKDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHCYSMQSK | |||||||
Disulfide bond | 40↔67 | UniProt | |||||
Sequence: CEPCDARALAQCAPPPAVCAELVREPGC | |||||||
Disulfide bond | 43↔69 | UniProt | |||||
Sequence: CDARALAQCAPPPAVCAELVREPGCGC | |||||||
Disulfide bond | 51↔70 | UniProt | |||||
Sequence: CAPPPAVCAELVREPGCGCC | |||||||
Disulfide bond | 58↔73 | UniProt | |||||
Sequence: CAELVREPGCGCCLTC | |||||||
Disulfide bond | 81↔94 | UniProt | |||||
Sequence: CGIYTERCGSGLRC | |||||||
Disulfide bond | 88↔114 | UniProt | |||||
Sequence: CGSGLRCQPSPDEARPLQALLDGRGLC | |||||||
Glycosylation | 116 | UniProt | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 136 | UniProt | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 145 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 148 | UniProt | Phosphoserine; by FAM20C | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 148 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 151 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Glycosylation | 199 | UniProt | N-linked (GlcNAc...) (complex) asparagine | ||||
Sequence: N | |||||||
Modified residue | 201 | UniProt | Phosphoserine; by FAM20C | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 213↔240 | UniProt | |||||
Sequence: CRREMEDTLNHLKFLNVLSPRGVHIPNC | |||||||
Disulfide bond | 251↔262 | UniProt | |||||
Sequence: CRPSKGRKRGFC | |||||||
Disulfide bond | 264↔285 | UniProt | |||||
Sequence: CVDKYGQPLPGYTTKGKEDVHC |
Post-translational modification
Phosphorylated by FAM20C in the extracellular medium.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed by most tissues. Present in plasma.
Induction
Up-regulated in the presence of IGF1, insulin and other growth-stimulating factors such as growth hormone, EGF and phorbol esters.
Developmental stage
IGFBP3 levels are higher during extrauterine life and peak during puberty.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with XLKD1 (By similarity).
Binds IGF2 more than IGF1. Forms a ternary complex of about 140 to 150 kDa with IGF1 or IGF2 and a 85 kDa glycoprotein (ALS). Interacts with humanin; humanin competes with importin KPNB1 for binding to IGFBP3, blocking IGFBP3 nuclear import and IGFBP3-mediated apoptosis (PubMed:14561895, PubMed:19623253, PubMed:26216267).
Interacts with TMEM219
Binds IGF2 more than IGF1. Forms a ternary complex of about 140 to 150 kDa with IGF1 or IGF2 and a 85 kDa glycoprotein (ALS). Interacts with humanin; humanin competes with importin KPNB1 for binding to IGFBP3, blocking IGFBP3 nuclear import and IGFBP3-mediated apoptosis (PubMed:14561895, PubMed:19623253, PubMed:26216267).
Interacts with TMEM219
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P17936 | EGFR P00533 | 3 | EBI-715709, EBI-297353 | |
BINARY | P17936 | KAT5 Q92993 | 3 | EBI-715709, EBI-399080 | |
BINARY | P17936 | LMO3 Q8TAP4-4 | 3 | EBI-715709, EBI-11742507 | |
BINARY | P17936 | MT-RNR2 Q8IVG9 | 7 | EBI-715709, EBI-8643752 | |
BINARY | P17936 | PRKCA P17252 | 3 | EBI-715709, EBI-1383528 | |
BINARY | P17936 | SETDB1 Q15047-2 | 3 | EBI-715709, EBI-9090795 | |
BINARY | P17936 | TMEM219 Q86XT9 | 8 | EBI-715709, EBI-20264080 | |
BINARY | P17936 | YWHAG P61981 | 3 | EBI-715709, EBI-359832 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 28-134 | IGF-binding | ||||
Sequence: GASSAGLGPVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNASAVSRLRAYLLPAPPAP | ||||||
Domain | 36-117 | IGFBP N-terminal | ||||
Sequence: PVVRCEPCDARALAQCAPPPAVCAELVREPGCGCCLTCALSEGQPCGIYTERCGSGLRCQPSPDEARPLQALLDGRGLCVNA | ||||||
Region | 130-162 | Disordered | ||||
Sequence: APPAPGNASESEEDRSAGSVESPSVSSTHRVSD | ||||||
Region | 189-211 | Disordered | ||||
Sequence: DYESQSTDTQNFSSESKRETEYG | ||||||
Compositional bias | 190-206 | Polar residues | ||||
Sequence: YESQSTDTQNFSSESKR | ||||||
Domain | 210-285 | Thyroglobulin type-1 | ||||
Sequence: YGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYTTKGKEDVHC |
Domain
The thyroglobulin type-1 domain mediates interaction with HN.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P17936-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length291
- Mass (Da)31,674
- Last updated2007-03-06 v2
- ChecksumA9682065AB266586
P17936-2
- Name2
- Differences from canonical
- 135-135: G → GEPPAPG
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047293 | 135 | in isoform 2 | |||
Sequence: G → GEPPAPG | ||||||
Compositional bias | 190-206 | Polar residues | ||||
Sequence: YESQSTDTQNFSSESKR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M31159 EMBL· GenBank· DDBJ | AAA52541.1 EMBL· GenBank· DDBJ | mRNA | ||
M35878 EMBL· GenBank· DDBJ | AAA52706.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X64875 EMBL· GenBank· DDBJ | CAA46087.1 EMBL· GenBank· DDBJ | mRNA | ||
DQ301819 EMBL· GenBank· DDBJ | ABB96247.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC091524 EMBL· GenBank· DDBJ | AAS07554.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH236958 EMBL· GenBank· DDBJ | EAL23801.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471128 EMBL· GenBank· DDBJ | EAW61028.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471128 EMBL· GenBank· DDBJ | EAW61029.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC000013 EMBL· GenBank· DDBJ | AAH00013.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018962 EMBL· GenBank· DDBJ | AAH18962.1 EMBL· GenBank· DDBJ | mRNA | ||
BC064987 EMBL· GenBank· DDBJ | AAH64987.1 EMBL· GenBank· DDBJ | mRNA |