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Protein

Insulin-like growth factor-binding protein 5

Gene

IGFBP5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. fibronectin binding Source: GO_Central
  2. insulin-like growth factor I binding Source: BHF-UCL
  3. insulin-like growth factor II binding Source: GO_Central

GO - Biological processi

  1. cellular protein metabolic process Source: Reactome
  2. cellular response to cAMP Source: UniProtKB
  3. cellular response to organic cyclic compound Source: UniProtKB
  4. glucose homeostasis Source: Ensembl
  5. glucose metabolic process Source: Ensembl
  6. hair follicle morphogenesis Source: Ensembl
  7. intracellular signal transduction Source: Ensembl
  8. mammary gland involution Source: Ensembl
  9. negative regulation of cell migration Source: BHF-UCL
  10. negative regulation of insulin-like growth factor receptor signaling pathway Source: BHF-UCL
  11. negative regulation of osteoblast differentiation Source: Ensembl
  12. negative regulation of smooth muscle cell migration Source: BHF-UCL
  13. negative regulation of smooth muscle cell proliferation Source: BHF-UCL
  14. negative regulation of translation Source: BHF-UCL
  15. osteoblast differentiation Source: Ensembl
  16. positive regulation of insulin-like growth factor receptor signaling pathway Source: Ensembl
  17. positive regulation of protein kinase B signaling Source: Ensembl
  18. regulation of cell growth Source: Ensembl
  19. regulation of glucose metabolic process Source: Ensembl
  20. signal transduction Source: ProtInc
  21. skeletal muscle tissue growth Source: Ensembl
  22. striated muscle cell differentiation Source: Ensembl
  23. type B pancreatic cell proliferation Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Growth factor binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000115461-MONOMER.
ReactomeiREACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Protein family/group databases

MEROPSiI31.952.

Names & Taxonomyi

Protein namesi
Recommended name:
Insulin-like growth factor-binding protein 5
Short name:
IBP-5
Short name:
IGF-binding protein 5
Short name:
IGFBP-5
Gene namesi
Name:IGFBP5
Synonyms:IBP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:5474. IGFBP5.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
  2. extracellular space Source: GO_Central
  3. insulin-like growth factor binding protein complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29707.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Chaini21 – 272252Insulin-like growth factor-binding protein 5PRO_0000014385Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 ↔ 591 PublicationPROSITE-ProRule annotation
Disulfide bondi67 ↔ 801 PublicationPROSITE-ProRule annotation
Glycosylationi172 – 1721O-linked (HexNAc...)1 Publication
Disulfide bondi192 ↔ 2191 PublicationPROSITE-ProRule annotation
Disulfide bondi230 ↔ 2411 PublicationPROSITE-ProRule annotation
Disulfide bondi243 ↔ 2631 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP24593.
PeptideAtlasiP24593.
PRIDEiP24593.

PTM databases

PhosphoSiteiP24593.

Miscellaneous databases

PMAP-CutDBP24593.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP24593.
CleanExiHS_IGFBP5.
ExpressionAtlasiP24593. baseline and differential.
GenevestigatoriP24593.

Organism-specific databases

HPAiCAB009216.

Interactioni

Protein-protein interaction databases

BioGridi109709. 10 interactions.
DIPiDIP-48433N.
IntActiP24593. 3 interactions.
MINTiMINT-1378863.
STRINGi9606.ENSP00000233813.

Structurei

Secondary structure

1
272
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi79 – 813Combined sources
Turni84 – 863Combined sources
Helixi89 – 946Combined sources
Beta strandi98 – 1014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOENMR-A60-106[»]
1H59X-ray2.10B60-112[»]
ProteinModelPortaliP24593.
SMRiP24593. Positions 25-105, 190-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP24593.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 10381IGFBP N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini189 – 26375Thyroglobulin type-1PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 IGFBP N-terminal domain.PROSITE-ProRule annotation
Contains 1 thyroglobulin type-1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG42882.
GeneTreeiENSGT00550000074457.
HOGENOMiHOG000253012.
HOVERGENiHBG002631.
InParanoidiP24593.
OMAiYREQAKI.
OrthoDBiEOG74N5HG.
PhylomeDBiP24593.
TreeFamiTF331211.

Family and domain databases

Gene3Di4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProiIPR009030. 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]
PANTHERiPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF4. PTHR11551:SF4. 1 hit.
PfamiPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSiPR01976. IGFBPFAMILY.
PR01981. IGFBPFAMILY5.
SMARTiSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEiPS00222. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P24593-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLLTAVLLL LAAYAGPAQS LGSFVHCEPC DEKALSMCPP SPLGCELVKE
60 70 80 90 100
PGCGCCMTCA LAEGQSCGVY TERCAQGLRC LPRQDEEKPL HALLHGRGVC
110 120 130 140 150
LNEKSYREQV KIERDSREHE EPTTSEMAEE TYSPKIFRPK HTRISELKAE
160 170 180 190 200
AVKKDRRKKL TQSKFVGGAE NTAHPRIISA PEMRQESEQG PCRRHMEASL
210 220 230 240 250
QELKASPRMV PRAVYLPNCD RKGFYKRKQC KPSRGRKRGI CWCVDKYGMK
260 270
LPGMEYVDGD FQCHTFDSSN VE
Length:272
Mass (Da):30,570
Last modified:March 1, 1992 - v1
Checksum:i0A7AD37C6EEA3A81
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti138 – 1381R → W.1 Publication
Corresponds to variant rs11575194 [ dbSNP | Ensembl ].
VAR_019284

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65062 mRNA. Translation: AAD04730.1.
M62782 mRNA. Translation: AAA53505.1.
L27559
, 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.
CCDSiCCDS2405.1.
PIRiA53748.
RefSeqiNP_000590.1. NM_000599.3.
UniGeneiHs.607212.

Genome annotation databases

EnsembliENST00000233813; ENSP00000233813; ENSG00000115461.
GeneIDi3488.
KEGGihsa:3488.
UCSCiuc002vgj.4. human.

Polymorphism databases

DMDMi124069.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M65062 mRNA. Translation: AAD04730.1.
M62782 mRNA. Translation: AAA53505.1.
L27559
, 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.
CCDSiCCDS2405.1.
PIRiA53748.
RefSeqiNP_000590.1. NM_000599.3.
UniGeneiHs.607212.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BOENMR-A60-106[»]
1H59X-ray2.10B60-112[»]
ProteinModelPortaliP24593.
SMRiP24593. Positions 25-105, 190-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109709. 10 interactions.
DIPiDIP-48433N.
IntActiP24593. 3 interactions.
MINTiMINT-1378863.
STRINGi9606.ENSP00000233813.

Chemistry

BindingDBiP24593.
ChEMBLiCHEMBL2665.

Protein family/group databases

MEROPSiI31.952.

PTM databases

PhosphoSiteiP24593.

Polymorphism databases

DMDMi124069.

Proteomic databases

PaxDbiP24593.
PeptideAtlasiP24593.
PRIDEiP24593.

Protocols and materials databases

DNASUi3488.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000233813; ENSP00000233813; ENSG00000115461.
GeneIDi3488.
KEGGihsa:3488.
UCSCiuc002vgj.4. human.

Organism-specific databases

CTDi3488.
GeneCardsiGC02M217504.
HGNCiHGNC:5474. IGFBP5.
HPAiCAB009216.
MIMi146734. gene.
neXtProtiNX_P24593.
PharmGKBiPA29707.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG42882.
GeneTreeiENSGT00550000074457.
HOGENOMiHOG000253012.
HOVERGENiHBG002631.
InParanoidiP24593.
OMAiYREQAKI.
OrthoDBiEOG74N5HG.
PhylomeDBiP24593.
TreeFamiTF331211.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000115461-MONOMER.
ReactomeiREACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

ChiTaRSiIGFBP5. human.
EvolutionaryTraceiP24593.
GeneWikiiIGFBP5.
GenomeRNAii3488.
NextBioi13718.
PMAP-CutDBP24593.
PROiP24593.
SOURCEiSearch...

Gene expression databases

BgeeiP24593.
CleanExiHS_IGFBP5.
ExpressionAtlasiP24593. baseline and differential.
GenevestigatoriP24593.

Family and domain databases

Gene3Di4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProiIPR009030. 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]
PANTHERiPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF4. PTHR11551:SF4. 1 hit.
PfamiPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSiPR01976. IGFBPFAMILY.
PR01981. IGFBPFAMILY5.
SMARTiSM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
SSF57610. SSF57610. 1 hit.
PROSITEiPS00222. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiIBP5_HUMAN
AccessioniPrimary (citable) accession number: P24593
Secondary accession number(s): Q5U0A3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: February 4, 2015
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.