P24593 (IBP5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	272 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Ligand	Growth factor binding
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular protein metabolic process Traceable author statement. Source: Reactome cellular response to cAMP Inferred from direct assay PubMed 7559606. Source: UniProtKB glucose homeostasis Inferred from electronic annotation. Source: Compara glucose metabolic process Inferred from electronic annotation. Source: Compara hair follicle morphogenesis Inferred from electronic annotation. Source: Compara intracellular signal transduction Inferred from electronic annotation. Source: Compara mammary gland involution Inferred from electronic annotation. Source: Compara 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: Compara 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: Compara positive regulation of insulin-like growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of protein kinase B signaling cascade Inferred from electronic annotation. Source: Compara regulation of cell growth Inferred from electronic annotation. Source: Compara regulation of glucose metabolic process Inferred from electronic annotation. Source: Compara signal transduction Non-traceable author statement PubMed 7525452. Source: ProtInc skeletal muscle tissue growth Inferred from electronic annotation. Source: Compara striated muscle cell differentiation Inferred from electronic annotation. Source: Compara type B pancreatic cell proliferation Inferred from electronic annotation. Source: Compara
Cellular_component	insulin-like growth factor binding protein complex Inferred by curator PubMed 10766744. Source: BHF-UCL
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 272

252

Insulin-like growth factor-binding protein 5

PRO_0000014385

Regions

Domain

23 – 103

81

IGFBP N-terminal

Domain

189 – 263

75

Thyroglobulin type-1

Amino acid modifications

Glycosylation

172

1

O-linked (HexNAc...) Ref.9

Disulfide bond

45 ↔ 59

Ref.10

Disulfide bond

67 ↔ 80

Ref.10

Disulfide bond

192 ↔ 219

Ref.10

Disulfide bond

230 ↔ 241

Ref.10

Disulfide bond

243 ↔ 263

Ref.10

Natural variations

Natural variant

138

1

R → W. Ref.6
Corresponds to variant rs11575194 [ dbSNP | Ensembl ].

VAR_019284

Secondary structure

1

.

.

.

.

.

.

.

.

.

272

Helix Strand Turn

Details...

Beta strand

79 – 81

3

Turn

84 – 86

3

Helix

89 – 94

6

Beta strand

98 – 101

4

Sequences

	Sequence		Length	Mass (Da)
	P24593 [UniParc]. Last modified March 1, 1992. Version 1. Checksum: 0A7AD37C6EEA3A81	FASTA	272	30,570
	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

References

	« Hide 'large scale' referencesShow '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, 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

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00029236.

PIR

A53748.

RefSeq

NP_000590.1. NM_000599.3.

UniGene

Hs.607212.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BOE	NMR	-	A	60-106	[»]
1H59	X-ray	2.10	B	60-112	[»]

ProteinModelPortal

P24593.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-48433N.

IntAct

P24593. 3 interactions.

MINT

MINT-1378863.

STRING

9606.ENSP00000233813.

Protein family/group databases

MEROPS

I31.952.

PTM databases

PhosphoSite

P24593.

Polymorphism databases

DMDM

124069.

Proteomic databases

PaxDb

P24593.

PeptideAtlas

P24593.

PRIDE

P24593.

Protocols and materials databases

DNASU

3488.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000233813; ENSP00000233813; ENSG00000115461.

GeneID

3488.

KEGG

hsa:3488.

UCSC

uc002vgj.4. human.

Organism-specific databases

CTD

3488.

GeneCards

GC02M217504.

HGNC

HGNC:5474. IGFBP5.

HPA

CAB009216.

MIM

146734. gene.

neXtProt

NX_P24593.

PharmGKB

PA29707.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG42882.

HOGENOM

HOG000253012.

HOVERGEN

HBG002631.

InParanoid

P24593.

OMA

HEPEFGP.

OrthoDB

EOG4RV2RZ.

PhylomeDB

P24593.

Enzyme and pathway databases

BioCyc

MetaCyc:ENSG00000115461-MONOMER.

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

P24593.

Bgee

P24593.

CleanEx

HS_IGFBP5.

Genevestigator

P24593.

GermOnline

ENSG00000115461. Homo sapiens.

Family and domain databases

Gene3D

4.10.40.20. 1 hit.
4.10.800.10. 1 hit.

InterPro

IPR009030. 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]

PANTHER

PTHR11551. PTHR11551. 1 hit.
PTHR11551:SF4. PTHR11551:SF4. 1 hit.

Pfam

PF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]

PRINTS

PR01976. IGFBPFAMILY.
PR01981. IGFBPFAMILY5.

SMART

SM00121. IB. 1 hit.
SM00211. TY. 1 hit.
[Graphical view]

SUPFAM

SSF57184. Grow_fac_recept. 1 hit.
SSF57610. Thyroglobulin_1. 1 hit.

PROSITE

PS00222. 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]

ProtoNet

Search...

Other

BindingDB

P24593.

ChEMBL

CHEMBL2665.

ChiTaRS

IGFBP5. human.

EvolutionaryTrace

P24593.

GenomeRNAi

3488.

NextBio

13718.

PMAP-CutDB

P24593.

SOURCE

Search...

Entry information

Entry name

IBP5_HUMAN

Accession

Primary (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:	May 29, 2013
This is version 147 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.