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P08833

- IBP1_HUMAN

UniProt

P08833 - IBP1_HUMAN

Protein

Insulin-like growth factor-binding protein 1

Gene

IGFBP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 170 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    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. Promotes cell migration.1 Publication

    GO - Molecular functioni

    1. insulin-like growth factor binding Source: ProtInc

    GO - Biological processi

    1. activation of signaling protein activity involved in unfolded protein response Source: Reactome
    2. cellular protein metabolic process Source: Reactome
    3. endoplasmic reticulum unfolded protein response Source: Reactome
    4. insulin receptor signaling pathway Source: Ensembl
    5. positive regulation of cell growth Source: Ensembl
    6. signal transduction Source: ProtInc
    7. tissue regeneration Source: Ensembl

    Keywords - Ligandi

    Growth factor binding

    Enzyme and pathway databases

    ReactomeiREACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    REACT_18355. ATF4 activates genes.
    SignaLinkiP08833.

    Protein family/group databases

    MEROPSiI31.951.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:IGFBP1
    Synonyms:IBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:5469. IGFBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: ProtInc

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29703.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 25253 PublicationsAdd
    BLAST
    Chaini26 – 259234Insulin-like growth factor-binding protein 1PRO_0000014365Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi71 ↔ 84
    Disulfide bondi78 ↔ 104
    Modified residuei120 – 1201Phosphoserine2 Publications
    Modified residuei123 – 1231Phosphoserine2 Publications
    Modified residuei126 – 1261Phosphoserine3 Publications
    Modified residuei144 – 1441Phosphoserine3 Publications
    Disulfide bondi176 ↔ 206
    Modified residuei194 – 1941Phosphoserine3 Publications
    Disulfide bondi217 ↔ 228
    Disulfide bondi230 ↔ 251

    Post-translational modificationi

    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.3 Publications

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP08833.
    PaxDbiP08833.
    PeptideAtlasiP08833.
    PRIDEiP08833.

    PTM databases

    PhosphoSiteiP08833.

    Miscellaneous databases

    PMAP-CutDBP08833.

    Expressioni

    Gene expression databases

    ArrayExpressiP08833.
    BgeeiP08833.
    CleanExiHS_IGFBP1.
    GenevestigatoriP08833.

    Organism-specific databases

    HPAiCAB004445.
    HPA046972.
    HPA050640.

    Interactioni

    Subunit structurei

    Binds equally well IGF1 and IGF2.1 Publication

    Protein-protein interaction databases

    BioGridi109705. 1 interaction.
    DIPiDIP-59846N.
    STRINGi9606.ENSP00000275525.

    Structurei

    Secondary structure

    1
    259
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi175 – 19319
    Beta strandi199 – 2013
    Beta strandi210 – 2123
    Beta strandi214 – 2174
    Beta strandi222 – 2243
    Beta strandi228 – 2314
    Turni233 – 2353
    Beta strandi245 – 2473

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZT3X-ray1.80A172-251[»]
    1ZT5X-ray1.82A172-251[»]
    2DSQX-ray2.80G/H166-259[»]
    ProteinModelPortaliP08833.
    SMRiP08833. Positions 29-106, 172-251.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08833.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini26 – 10782IGFBP N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini173 – 25179Thyroglobulin type-1PROSITE-ProRule annotationAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi246 – 2483Cell attachment site

    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

    eggNOGiNOG44381.
    HOGENOMiHOG000253012.
    HOVERGENiHBG002631.
    InParanoidiP08833.
    OMAiMCALPLG.
    OrthoDBiEOG74N5HG.
    PhylomeDBiP08833.
    TreeFamiTF331211.

    Family and domain databases

    Gene3Di4.10.40.20. 1 hit.
    4.10.800.10. 1 hit.
    InterProiIPR009030. 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]
    PANTHERiPTHR11551. PTHR11551. 1 hit.
    PfamiPF00219. IGFBP. 1 hit.
    PF00086. Thyroglobulin_1. 1 hit.
    [Graphical view]
    PRINTSiPR01976. IGFBPFAMILY.
    PR01977. IGFBPFAMILY1.
    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.

    P08833-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSEVPVARVW LVLLLLTVQV GVTAGAPWQC APCSAEKLAL CPPVSASCSE    50
    VTRSAGCGCC PMCALPLGAA CGVATARCAR GLSCRALPGE QQPLHALTRG 100
    QGACVQESDA SAPHAAEAGS PESPESTEIT EEELLDNFHL MAPSEEDHSI 150
    LWDAISTYDG SKALHVTNIK KWKEPCRIEL YRVVESLAKA QETSGEEISK 200
    FYLPNCNKNG FYHSRQCETS MDGEAGLCWC VYPWNGKRIP GSPEIRGDPN 250
    CQIYFNVQN 259
    Length:259
    Mass (Da):27,904
    Last modified:November 1, 1988 - v1
    Checksum:i8AA75AF7DC966012
    GO

    Sequence cautioni

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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti213 – 2131H → Q in AAA52540. (PubMed:2454104)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1141H → D.
    Corresponds to variant rs41258845 [ dbSNP | Ensembl ].
    VAR_049564
    Natural varianti183 – 1831V → I.1 Publication
    Corresponds to variant rs1065782 [ dbSNP | Ensembl ].
    VAR_011905
    Natural varianti253 – 2531I → M.2 Publications
    Corresponds to variant rs4619 [ dbSNP | Ensembl ].
    VAR_003821

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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.
    CCDSiCCDS5504.1.
    PIRiA31867. IOHU1.
    RefSeqiNP_000587.1. NM_000596.2.
    UniGeneiHs.642938.

    Genome annotation databases

    EnsembliENST00000275525; ENSP00000275525; ENSG00000146678.
    GeneIDi3484.
    KEGGihsa:3484.
    UCSCiuc003tnp.3. human.

    Polymorphism databases

    DMDMi124055.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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
    , 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 .
    CCDSi CCDS5504.1.
    PIRi A31867. IOHU1.
    RefSeqi NP_000587.1. NM_000596.2.
    UniGenei Hs.642938.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZT3 X-ray 1.80 A 172-251 [» ]
    1ZT5 X-ray 1.82 A 172-251 [» ]
    2DSQ X-ray 2.80 G/H 166-259 [» ]
    ProteinModelPortali P08833.
    SMRi P08833. Positions 29-106, 172-251.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109705. 1 interaction.
    DIPi DIP-59846N.
    STRINGi 9606.ENSP00000275525.

    Chemistry

    BindingDBi P08833.
    ChEMBLi CHEMBL4178.

    Protein family/group databases

    MEROPSi I31.951.

    PTM databases

    PhosphoSitei P08833.

    Polymorphism databases

    DMDMi 124055.

    Proteomic databases

    MaxQBi P08833.
    PaxDbi P08833.
    PeptideAtlasi P08833.
    PRIDEi P08833.

    Protocols and materials databases

    DNASUi 3484.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000275525 ; ENSP00000275525 ; ENSG00000146678 .
    GeneIDi 3484.
    KEGGi hsa:3484.
    UCSCi uc003tnp.3. human.

    Organism-specific databases

    CTDi 3484.
    GeneCardsi GC07P045927.
    HGNCi HGNC:5469. IGFBP1.
    HPAi CAB004445.
    HPA046972.
    HPA050640.
    MIMi 146730. gene.
    neXtProti NX_P08833.
    PharmGKBi PA29703.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG44381.
    HOGENOMi HOG000253012.
    HOVERGENi HBG002631.
    InParanoidi P08833.
    OMAi MCALPLG.
    OrthoDBi EOG74N5HG.
    PhylomeDBi P08833.
    TreeFami TF331211.

    Enzyme and pathway databases

    Reactomei REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
    REACT_18355. ATF4 activates genes.
    SignaLinki P08833.

    Miscellaneous databases

    EvolutionaryTracei P08833.
    GeneWikii IGFBP1.
    GenomeRNAii 3484.
    NextBioi 13700.
    PMAP-CutDB P08833.
    PROi P08833.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08833.
    Bgeei P08833.
    CleanExi HS_IGFBP1.
    Genevestigatori P08833.

    Family and domain databases

    Gene3Di 4.10.40.20. 1 hit.
    4.10.800.10. 1 hit.
    InterProi IPR009030. 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 ]
    PANTHERi PTHR11551. PTHR11551. 1 hit.
    Pfami PF00219. IGFBP. 1 hit.
    PF00086. Thyroglobulin_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01976. IGFBPFAMILY.
    PR01977. IGFBPFAMILY1.
    SMARTi SM00121. IB. 1 hit.
    SM00211. TY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    SSF57610. SSF57610. 1 hit.
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiIBP1_HUMAN
    AccessioniPrimary (citable) accession number: P08833
    Secondary accession number(s): A4D2F4, D3DVL9, Q8IYP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 170 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 7
      Human chromosome 7: 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