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P08833 (IBP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 168. 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 1

Short name=IBP-1
Short name=IGF-binding protein 1
Short name=IGFBP-1
Alternative name(s):
Placental protein 12
Short name=PP12
Gene names
Name:IGFBP1
Synonyms:IBP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length259 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. Promotes cell migration. Ref.20

Subunit structure

Binds equally well IGF1 and IGF2.

Subcellular location

Secreted.

Post-translational modification

Phosphorylated; probably by casein kinase II. Phosphorylation alters the affinity of the protein for IGFs. In amniotic fluid, the unmodified protein is the most abundant form, while mono-, bi-, tri- and tetraphosphorylated forms are present in decreasing amounts. The phosphorylation state may influence the propensity to proteolysis. Ref.14 Ref.18 Ref.20

Sequence similarities

Contains 1 IGFBP N-terminal domain.

Contains 1 thyroglobulin type-1 domain.

Sequence caution

The sequence AAA52540.1 differs from that shown. Reason: Frameshift at positions 55 and 71.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Ref.14 Ref.15 Ref.16
Chain26 – 259234Insulin-like growth factor-binding protein 1
PRO_0000014365

Regions

Domain26 – 10782IGFBP N-terminal
Domain173 – 25179Thyroglobulin type-1
Motif246 – 2483Cell attachment site

Amino acid modifications

Modified residue1201Phosphoserine Ref.14
Modified residue1231Phosphoserine Ref.14
Modified residue1261Phosphoserine Ref.14 Ref.18
Modified residue1441Phosphoserine Ref.14 Ref.18
Modified residue1941Phosphoserine Ref.14 Ref.18
Disulfide bond71 ↔ 84 Ref.19 Ref.20 Ref.21
Disulfide bond78 ↔ 104 Ref.19 Ref.20 Ref.21
Disulfide bond176 ↔ 206 Ref.19 Ref.20 Ref.21
Disulfide bond217 ↔ 228 Ref.19 Ref.20 Ref.21
Disulfide bond230 ↔ 251 Ref.19 Ref.20 Ref.21

Natural variations

Natural variant1141H → D.
Corresponds to variant rs41258845 [ dbSNP | Ensembl ].
VAR_049564
Natural variant1831V → I. Ref.10
Corresponds to variant rs1065782 [ dbSNP | Ensembl ].
VAR_011905
Natural variant2531I → M. Ref.10 Ref.13
Corresponds to variant rs4619 [ dbSNP | Ensembl ].
VAR_003821

Experimental info

Sequence conflict2131H → Q in AAA52540. Ref.2

Secondary structure

................. 259
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08833 [UniParc].

Last modified November 1, 1988. Version 1.
Checksum: 8AA75AF7DC966012

FASTA25927,904
        10         20         30         40         50         60 
MSEVPVARVW LVLLLLTVQV GVTAGAPWQC APCSAEKLAL CPPVSASCSE VTRSAGCGCC 

        70         80         90        100        110        120 
PMCALPLGAA CGVATARCAR GLSCRALPGE QQPLHALTRG QGACVQESDA SAPHAAEAGS 

       130        140        150        160        170        180 
PESPESTEIT EEELLDNFHL MAPSEEDHSI LWDAISTYDG SKALHVTNIK KWKEPCRIEL 

       190        200        210        220        230        240 
YRVVESLAKA QETSGEEISK FYLPNCNKNG FYHSRQCETS MDGEAGLCWC VYPWNGKRIP 

       250 
GSPEIRGDPN CQIYFNVQN 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of a cDNA encoding the low molecular weight insulin-like growth factor binding protein (IBP-1)."
Brinkman A., Groffen C., Kortleve D.J., Geurts A., Drop S.L.S.
EMBO J. 7:2417-2423(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[2]"Cloning, characterization, and expression of a human insulin-like growth factor binding protein."
Brewer M.T., Stetler G.L., Squires C.H., Thompson R.C., Busby W.H. Jr., Clemmons D.R.
Biochem. Biophys. Res. Commun. 152:1289-1297(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Decidua.
[3]"Cloning of cDNA encoding human placental protein 12 (PP12): binding protein for IGF I and somatomedin."
Grundmann U., Nerlich C., Bohn H., Rein T.
Nucleic Acids Res. 16:8711-8711(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[4]"Primary structure of human insulin-like growth factor-binding protein/placental protein 12 and tissue-specific expression of its mRNA."
Julkunen M., Koistinen R., Aalto-Setala K., Seppala M., Janne O.A., Kontula K.
FEBS Lett. 236:295-302(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Decidua.
[5]"Insulin-like growth factor (IGF) binding protein complementary deoxyribonucleic acid from human HEP G2 hepatoma cells: predicted protein sequence suggests an IGF binding domain different from those of the IGF-I and IGF-II receptors."
Lee Y.-L., Hintz R.L., James P.M., Lee P.D.K., Shively J.E., Powell D.R.
Mol. Endocrinol. 2:404-411(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]"Structure of the human chromosomal gene for the 25 kilodalton insulin-like growth factor binding protein."
Cubbage M.L., Suwanichkul A., Powell D.R.
Mol. Endocrinol. 3:846-851(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Organization of the gene encoding the insulin-like growth factor binding protein IBP-1."
Brinkman A., Groffen C.A., Kortleve D.J., Drop S.L.
Biochem. Biophys. Res. Commun. 157:898-907(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]"Contiguous localization of the genes encoding human insulin-like growth factor binding proteins 1 (IGBP1) and 3 (IGBP3) on chromosome 7."
Ehrenborg E., Larsson C., Stern I., Janson M., Powell D.R., Luthman H.
Genomics 12:497-502(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Liver.
[9]"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].
[10]NIEHS SNPs program
Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-183 AND MET-253.
[11]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]"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], VARIANT MET-253.
Tissue: Skin.
[14]"Identification of the amniotic fluid insulin-like growth factor binding protein-1 phosphorylation sites and propensity to proteolysis of the isoforms."
Dolcini L., Sala A., Campagnoli M., Labo S., Valli M., Visai L., Minchiotti L., Monaco H.L., Galliano M.
FEBS J. 276:6033-6046(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-53; 95-152 AND 182-208, CLEAVAGE OF INITIATOR METHIONINE, PHOSPHORYLATION AT SER-120; SER-123; SER-126; SER-144 AND SER-194, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Amniotic fluid.
[15]"Human insulin-like growth-factor-binding protein. Low-molecular-mass form: protein sequence and cDNA cloning."
Luthman H., Soederling-Barros J., Persson B., Engberg C., Stern I., Lake M., Franzen S.A., Israelsson M., Raden B., Lindgren B., Hjelmqvist L., Enerbaeck S., Carlsson P., Bjursell G., Povoa G., Hall K., Joernvall H.
Eur. J. Biochem. 180:259-265(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 141-259, PROTEIN SEQUENCE OF 26-259.
Tissue: Amniotic fluid.
[16]"Purification of a 31,000-dalton insulin-like growth factor binding protein from human amniotic fluid. Isolation of two forms with different biologic actions."
Busby W.H. Jr., Klapper D.G., Clemmons D.R.
J. Biol. Chem. 263:14203-14210(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 26-53.
[17]"Site-directed mutagenesis of the N-terminal region of IGF binding protein 1; analysis of IGF binding capability."
Brinkman A., Kortlrve D.J., Schuller A.G.P., Zwarthoff E.C., Drop S.L.S.
FEBS Lett. 291:264-268(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS.
[18]"Identification of the sites of phosphorylation in insulin-like growth factor binding protein-1. Regulation of its affinity by phosphorylation of serine 101."
Jones J.I., Busby W.H. Jr., Wright G., Smith C.E., Kimack N.M., Clemmons D.R.
J. Biol. Chem. 268:1125-1131(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-126; SER-144 AND SER-194, PARTIAL PROTEIN SEQUENCE.
[19]"The N-terminal disulfide linkages of human insulin-like growth factor-binding protein-6 (hIGFBP-6) and hIGFBP-1 are different as determined by mass spectrometry."
Neumann G.M., Bach L.A.
J. Biol. Chem. 274:14587-14594(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.
[20]"Structure and properties of the C-terminal domain of insulin-like growth factor-binding protein-1 isolated from human amniotic fluid."
Sala A., Capaldi S., Campagnoli M., Faggion B., Labo S., Perduca M., Romano A., Carrizo M.E., Valli M., Visai L., Minchiotti L., Galliano M., Monaco H.L.
J. Biol. Chem. 280:29812-29819(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 172-251, PARTIAL PROTEIN SEQUENCE, FUNCTION, PHOSPHORYLATION, DISULFIDE BONDS.
[21]"Structural basis for the inhibition of insulin-like growth factors by insulin-like growth factor-binding proteins."
Sitar T., Popowicz G.M., Siwanowicz I., Huber R., Holak T.A.
Proc. Natl. Acad. Sci. U.S.A. 103:13028-13033(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 166-259 IN COMPLEX WITH IGFBP4 AND IGF1, DISULFIDE BONDS.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y00856 mRNA. Translation: CAA68770.1.
M20841 mRNA. Translation: AAA52540.1. Frameshift.
X12385 mRNA. Translation: CAA30942.1.
X13405 mRNA. Translation: CAA31771.1.
M31145 mRNA. Translation: AAA52542.1.
M59316 Genomic DNA. Translation: AAA52783.1.
M23595 expand/collapse EMBL AC list , M23592, M23593, M23594 Genomic DNA. Translation: AAA52785.1.
M74587 Genomic DNA. Translation: AAA52784.1.
BT019685 mRNA. Translation: AAV38491.1.
AY434089 Genomic DNA. Translation: AAQ96599.1.
CH236958 Genomic DNA. Translation: EAL23800.1.
CH471128 Genomic DNA. Translation: EAW61030.1.
CH471128 Genomic DNA. Translation: EAW61031.1.
BC035263 mRNA. Translation: AAH35263.2.
X15002 mRNA. Translation: CAA33110.1.
CCDSCCDS5504.1.
PIRIOHU1. A31867.
RefSeqNP_000587.1. NM_000596.2.
UniGeneHs.642938.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZT3X-ray1.80A172-251[»]
1ZT5X-ray1.82A172-251[»]
2DSQX-ray2.80G/H166-259[»]
ProteinModelPortalP08833.
SMRP08833. Positions 29-106, 172-251.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109705. 1 interaction.
DIPDIP-59846N.
STRING9606.ENSP00000275525.

Chemistry

BindingDBP08833.
ChEMBLCHEMBL4178.

Protein family/group databases

MEROPSI31.951.

PTM databases

PhosphoSiteP08833.

Polymorphism databases

DMDM124055.

Proteomic databases

MaxQBP08833.
PaxDbP08833.
PeptideAtlasP08833.
PRIDEP08833.

Protocols and materials databases

DNASU3484.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275525; ENSP00000275525; ENSG00000146678.
GeneID3484.
KEGGhsa:3484.
UCSCuc003tnp.3. human.

Organism-specific databases

CTD3484.
GeneCardsGC07P045927.
HGNCHGNC:5469. IGFBP1.
HPACAB004445.
HPA046972.
HPA050640.
MIM146730. gene.
neXtProtNX_P08833.
PharmGKBPA29703.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG44381.
HOGENOMHOG000253012.
HOVERGENHBG002631.
InParanoidP08833.
OMAMCALPLG.
OrthoDBEOG74N5HG.
PhylomeDBP08833.
TreeFamTF331211.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
SignaLinkP08833.

Gene expression databases

ArrayExpressP08833.
BgeeP08833.
CleanExHS_IGFBP1.
GenevestigatorP08833.

Family and domain databases

Gene3D4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProIPR009030. Growth_fac_rcpt_N_dom.
IPR000867. IGFBP-like.
IPR022322. IGFBP1.
IPR009168. IGFBP1-6.
IPR022321. IGFBP_1-6_chordata.
IPR017891. Insulin_GF-bd_Cys-rich_CS.
IPR000716. Thyroglobulin_1.
[Graphical view]
PANTHERPTHR11551. PTHR11551. 1 hit.
PfamPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSPR01976. IGFBPFAMILY.
PR01977. IGFBPFAMILY1.
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

EvolutionaryTraceP08833.
GeneWikiIGFBP1.
GenomeRNAi3484.
NextBio13700.
PMAP-CutDBP08833.
PROP08833.
SOURCESearch...

Entry information

Entry nameIBP1_HUMAN
AccessionPrimary (citable) accession number: P08833
Secondary accession number(s): A4D2F4, D3DVL9, Q8IYP5
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: July 9, 2014
This is version 168 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 7

Human chromosome 7: entries, gene names and cross-references to MIM