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P24593 (IBP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like growth factor-binding protein 5

Short name=IBP-5
Short name=IGF-binding protein 5
Short name=IGFBP-5
Gene names
Name:IGFBP5
Synonyms:IBP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subcellular location

Secreted.

Tissue specificity

Osteosarcoma, and at lower levels in liver, kidney and brain.

Sequence similarities

Contains 1 IGFBP N-terminal domain.

Contains 1 thyroglobulin type-1 domain.

Ontologies

Keywords
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   LigandGrowth factor binding
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcellular protein metabolic process

Traceable author statement. Source: Reactome

cellular response to cAMP

Inferred from direct assay PubMed 7559606. Source: UniProtKB

cellular response to organic cyclic compound

Inferred from direct assay PubMed 7559606. Source: UniProtKB

glucose homeostasis

Inferred from electronic annotation. Source: Ensembl

glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

hair follicle morphogenesis

Inferred from electronic annotation. Source: Ensembl

intracellular signal transduction

Inferred from electronic annotation. Source: Ensembl

mammary gland involution

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell migration

Inferred from direct assay PubMed 15700281. Source: BHF-UCL

negative regulation of insulin-like growth factor receptor signaling pathway

Inferred from direct assay PubMed 10766744. Source: BHF-UCL

negative regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell migration

Inferred from direct assay PubMed 10766744. Source: BHF-UCL

negative regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 10766744. Source: BHF-UCL

negative regulation of translation

Inferred from direct assay PubMed 15700281. Source: BHF-UCL

osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

regulation of glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

signal transduction

Non-traceable author statement PubMed 7525452. Source: ProtInc

skeletal muscle tissue growth

Inferred from electronic annotation. Source: Ensembl

striated muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

type B pancreatic cell proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

insulin-like growth factor binding protein complex

Inferred by curator PubMed 10766744. Source: BHF-UCL

   Molecular_functioninsulin-like growth factor I binding

Inferred from physical interaction PubMed 10766744. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 15700281. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 272252Insulin-like growth factor-binding protein 5
PRO_0000014385

Regions

Domain23 – 10381IGFBP N-terminal
Domain189 – 26375Thyroglobulin type-1

Amino acid modifications

Glycosylation1721O-linked (HexNAc...) Ref.9
Disulfide bond45 ↔ 59 Ref.10
Disulfide bond67 ↔ 80 Ref.10
Disulfide bond192 ↔ 219 Ref.10
Disulfide bond230 ↔ 241 Ref.10
Disulfide bond243 ↔ 263 Ref.10

Natural variations

Natural variant1381R → W. Ref.6
Corresponds to variant rs11575194 [ dbSNP | Ensembl ].
VAR_019284

Secondary structure

......... 272
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P24593 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 0A7AD37C6EEA3A81

FASTA27230,570
        10         20         30         40         50         60 
MVLLTAVLLL LAAYAGPAQS LGSFVHCEPC DEKALSMCPP SPLGCELVKE PGCGCCMTCA 

        70         80         90        100        110        120 
LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC LNEKSYREQV KIERDSREHE 

       130        140        150        160        170        180 
EPTTSEMAEE TYSPKIFRPK HTRISELKAE AVKKDRRKKL TQSKFVGGAE NTAHPRIISA 

       190        200        210        220        230        240 
PEMRQESEQG PCRRHMEASL QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI 

       250        260        270 
CWCVDKYGMK LPGMEYVDGD FQCHTFDSSN VE 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of a new human insulin-like growth factor binding protein."
Kiefer M.C., Ioh R.S., Bauer D.M., Zapf J.
Biochem. Biophys. Res. Commun. 176:219-225(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Osteosarcoma.
[2]"Identification of five different insulin-like growth factor binding proteins (IGFBPs) from adult rat serum and molecular cloning of a novel IGFBP-5 in rat and human."
Shimasaki S., Shimonaka M., Zhang H.-P., Ling N.
J. Biol. Chem. 266:10646-10653(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[3]"Characterization of the chromosomal gene and promoter for human insulin-like growth factor binding protein-5."
Allander S.V., Larsson C., Ehrenborg E., Suwanichkul A., Weber G., Morris S.L., Bajalica S., Kiefer M.C., Luthman H., Powell D.R.
J. Biol. Chem. 269:10891-10898(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]Yu W., Gibbs R.A.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]NIEHS SNPs program
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT TRP-138.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[8]"A novel human insulin-like growth factor binding protein secreted by osteoblast-like cells."
Andress D.L., Birnbaum R.S.
Biochem. Biophys. Res. Commun. 176:213-218(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 24-43.
[9]"Isolation and characterization of circulating 13-kDa C-terminal fragments of human insulin-like growth factor binding protein-5."
Standker L., Wobst P., Mark S., Forssmann W.-G.
FEBS Lett. 441:281-286(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 141-178 AND 209-223, GLYCOSYLATION AT THR-172.
Tissue: Plasma.
[10]"Defining the disulfide bonds of insulin-like growth factor-binding protein-5 by tandem mass spectrometry with electron transfer dissociation and collision-induced dissociation."
Nili M., Mukherjee A., Shinde U., David L., Rotwein P.
J. Biol. Chem. 287:1510-1519(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Structure of the IGF-binding domain of the insulin-like growth factor-binding protein-5 (IGFBP-5): implications for IGF and IGF-I receptor interactions."
Kalus W., Zweckstetter M., Renner C., Sanchez Y., Georgescu J., Grol M., Demuth D., Schumacher R., Dony C., Lang K., Holak T.A.
EMBO J. 17:6558-6572(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 60-106.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M65062 mRNA. Translation: AAD04730.1.
M62782 mRNA. Translation: AAA53505.1.
L27559 expand/collapse EMBL AC list , L27556, L27557, L27558 Genomic DNA. Translation: AAA72051.1.
AF055033 mRNA. Translation: AAC09368.1.
BT019706 mRNA. Translation: AAV38512.1.
BT019707 mRNA. Translation: AAV38513.1.
AY534685 Genomic DNA. Translation: AAS16353.1.
BC011453 mRNA. Translation: AAH11453.1.
CCDSCCDS2405.1.
PIRA53748.
RefSeqNP_000590.1. NM_000599.3.
UniGeneHs.607212.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOENMR-A60-106[»]
1H59X-ray2.10B60-112[»]
ProteinModelPortalP24593.
SMRP24593. Positions 25-105, 190-268.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109709. 10 interactions.
DIPDIP-48433N.
IntActP24593. 3 interactions.
MINTMINT-1378863.
STRING9606.ENSP00000233813.

Chemistry

BindingDBP24593.
ChEMBLCHEMBL2665.

Protein family/group databases

MEROPSI31.952.

PTM databases

PhosphoSiteP24593.

Polymorphism databases

DMDM124069.

Proteomic databases

PaxDbP24593.
PeptideAtlasP24593.
PRIDEP24593.

Protocols and materials databases

DNASU3488.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000233813; ENSP00000233813; ENSG00000115461.
GeneID3488.
KEGGhsa:3488.
UCSCuc002vgj.4. human.

Organism-specific databases

CTD3488.
GeneCardsGC02M217504.
HGNCHGNC:5474. IGFBP5.
HPACAB009216.
MIM146734. gene.
neXtProtNX_P24593.
PharmGKBPA29707.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG42882.
HOGENOMHOG000253012.
HOVERGENHBG002631.
InParanoidP24593.
OMAYREQAKI.
OrthoDBEOG74N5HG.
PhylomeDBP24593.
TreeFamTF331211.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000115461-MONOMER.
ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP24593.
BgeeP24593.
CleanExHS_IGFBP5.
GenevestigatorP24593.

Family and domain databases

Gene3D4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProIPR009030. Growth_fac_rcpt_N_dom.
IPR012213. IGFBP-5.
IPR000867. IGFBP-like.
IPR009168. IGFBP1-6.
IPR022321. IGFBP_1-6_chordata.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF4. PTHR11551:SF4. 1 hit.
PfamPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSPR01976. IGFBPFAMILY.
PR01981. IGFBPFAMILY5.
SMARTSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEPS00222. IGFBP_N_1. 1 hit.
PS51323. IGFBP_N_2. 1 hit.
PS00484. THYROGLOBULIN_1_1. 1 hit.
PS51162. THYROGLOBULIN_1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIGFBP5. human.
EvolutionaryTraceP24593.
GeneWikiIGFBP5.
GenomeRNAi3488.
NextBio13718.
PMAP-CutDBP24593.
PROP24593.
SOURCESearch...

Entry information

Entry nameIBP5_HUMAN
AccessionPrimary (citable) accession number: P24593
Secondary accession number(s): Q5U0A3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: July 9, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM