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P17936

- IBP3_HUMAN

UniProt

P17936 - IBP3_HUMAN

Protein

Insulin-like growth factor-binding protein 3

Gene

IGFBP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 2 (06 Mar 2007)
      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. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R.1 Publication

    GO - Molecular functioni

    1. insulin-like growth factor binding Source: UniProtKB
    2. insulin-like growth factor I binding Source: BHF-UCL
    3. metal ion binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein tyrosine phosphatase activator activity Source: UniProtKB

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cellular protein metabolic process Source: Reactome
    3. negative regulation of cell proliferation Source: MGI
    4. negative regulation of protein phosphorylation Source: MGI
    5. negative regulation of signal transduction Source: UniProtKB
    6. negative regulation of smooth muscle cell migration Source: BHF-UCL
    7. negative regulation of smooth muscle cell proliferation Source: BHF-UCL
    8. positive regulation of apoptotic process Source: UniProtKB
    9. positive regulation of catalytic activity Source: GOC
    10. positive regulation of insulin-like growth factor receptor signaling pathway Source: Ensembl
    11. positive regulation of MAPK cascade Source: Ensembl
    12. positive regulation of myoblast differentiation Source: UniProtKB
    13. protein phosphorylation Source: MGI
    14. regulation of cell growth Source: Ensembl
    15. regulation of glucose metabolic process Source: Ensembl
    16. type B pancreatic cell proliferation Source: Ensembl

    Keywords - Biological processi

    Apoptosis

    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).

    Protein family/group databases

    MEROPSiI31.952.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Insulin-like growth factor-binding protein 3
    Short name:
    IBP-3
    Short name:
    IGF-binding protein 3
    Short name:
    IGFBP-3
    Gene namesi
    Name:IGFBP3
    Synonyms:IBP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:5472. IGFBP3.

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. insulin-like growth factor binding protein complex Source: BHF-UCL
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29705.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27273 PublicationsAdd
    BLAST
    Chaini28 – 291264Insulin-like growth factor-binding protein 3PRO_0000014378Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi116 – 1161N-linked (GlcNAc...) (complex)1 Publication
    Glycosylationi136 – 1361N-linked (GlcNAc...) (complex)4 Publications
    Glycosylationi199 – 1991N-linked (GlcNAc...) (complex)2 Publications
    Disulfide bondi213 ↔ 240PROSITE-ProRule annotation
    Disulfide bondi251 ↔ 262PROSITE-ProRule annotation
    Disulfide bondi264 ↔ 285PROSITE-ProRule annotation

    Post-translational modificationi

    Phosphorylation sites are present in the extracellular medium.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP17936.
    PaxDbiP17936.
    PeptideAtlasiP17936.
    PRIDEiP17936.

    PTM databases

    PhosphoSiteiP17936.

    Miscellaneous databases

    PMAP-CutDBP17936.

    Expressioni

    Tissue specificityi

    Expressed by most tissues. Present in plasma.

    Developmental stagei

    IGFBP3 levels are higher during extrauterine life and peak during puberty.

    Inductioni

    Up-regulated in the presence of IGF1, insulin and other growth-stimulating factors such as growth hormone, EGF and phorbol esters.

    Gene expression databases

    ArrayExpressiP17936.
    BgeeiP17936.
    CleanExiHS_IGFBP3.
    GenevestigatoriP17936.

    Organism-specific databases

    HPAiCAB010360.
    HPA013357.

    Interactioni

    Subunit structurei

    Interacts with XLKD1 By similarity. Binds IGF2 more than IGF1. Forms a ternary complex of about 140 to 150 kDa with IGF1 or IGF2 and a 85 kDa glycoprotein (ALS). Interacts with HN. Interacts with TMEM219.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EGFRP005333EBI-715709,EBI-297353
    PRKDCP785272EBI-715709,EBI-352053

    Protein-protein interaction databases

    BioGridi109707. 17 interactions.
    DIPiDIP-40786N.
    IntActiP17936. 6 interactions.
    MINTiMINT-142445.
    STRINGi9606.ENSP00000370473.

    Structurei

    3D structure databases

    ProteinModelPortaliP17936.
    SMRiP17936. Positions 38-116, 211-274.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini36 – 11782IGFBP N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini210 – 28576Thyroglobulin type-1PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni28 – 134107IGF-bindingSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi138 – 16124Ser/Thr-richAdd
    BLAST
    Compositional biasi192 – 20817Ser/Thr-richAdd
    BLAST

    Domaini

    The thyroglobulin type-1 domain mediates interaction with HN.

    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

    eggNOGiNOG38980.
    HOGENOMiHOG000253012.
    HOVERGENiHBG002631.
    KOiK10138.
    OMAiYTERCGA.
    PhylomeDBiP17936.
    TreeFamiTF331211.

    Family and domain databases

    Gene3Di4.10.40.20. 1 hit.
    4.10.800.10. 1 hit.
    InterProiIPR009030. Growth_fac_rcpt_N_dom.
    IPR012211. IGFBP-3.
    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:SF3. PTHR11551:SF3. 1 hit.
    PfamiPF00219. IGFBP. 1 hit.
    PF00086. Thyroglobulin_1. 1 hit.
    [Graphical view]
    PRINTSiPR01976. IGFBPFAMILY.
    PR01979. IGFBPFAMILY3.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P17936-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQRARPTLWA AALTLLVLLR GPPVARAGAS SAGLGPVVRC EPCDARALAQ    50
    CAPPPAVCAE LVREPGCGCC LTCALSEGQP CGIYTERCGS GLRCQPSPDE 100
    ARPLQALLDG RGLCVNASAV SRLRAYLLPA PPAPGNASES EEDRSAGSVE 150
    SPSVSSTHRV SDPKFHPLHS KIIIIKKGHA KDSQRYKVDY ESQSTDTQNF 200
    SSESKRETEY GPCRREMEDT LNHLKFLNVL SPRGVHIPNC DKKGFYKKKQ 250
    CRPSKGRKRG FCWCVDKYGQ PLPGYTTKGK EDVHCYSMQS K 291
    Length:291
    Mass (Da):31,674
    Last modified:March 6, 2007 - v2
    Checksum:iA9682065AB266586
    GO
    Isoform 2 (identifier: P17936-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         135-135: G → GEPPAPG

    Note: Gene prediction based on EST data.

    Show »
    Length:297
    Mass (Da):32,223
    Checksum:i8CCFAD16904D0DF4
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71T → M in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036279
    Natural varianti32 – 321A → G.4 Publications
    Corresponds to variant rs2854746 [ dbSNP | Ensembl ].
    VAR_025262
    Natural varianti56 – 561A → T.1 Publication
    Corresponds to variant rs34257987 [ dbSNP | Ensembl ].
    VAR_025263
    Natural varianti158 – 1581H → P.
    Corresponds to variant rs9282734 [ dbSNP | Ensembl ].
    VAR_021974
    Natural varianti234 – 2341G → S.1 Publication
    Corresponds to variant rs35712717 [ dbSNP | Ensembl ].
    VAR_025264
    Natural varianti252 – 2521R → C in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036280

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei135 – 1351G → GEPPAPG in isoform 2. CuratedVSP_047293

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31159 mRNA. Translation: AAA52541.1.
    M35878 Genomic DNA. Translation: AAA52706.1.
    X64875 mRNA. Translation: CAA46087.1.
    DQ301819 Genomic DNA. Translation: ABB96247.1.
    AC091524 Genomic DNA. Translation: AAS07554.1.
    CH236958 Genomic DNA. Translation: EAL23801.1.
    CH471128 Genomic DNA. Translation: EAW61028.1.
    CH471128 Genomic DNA. Translation: EAW61029.1.
    BC000013 mRNA. Translation: AAH00013.1.
    BC018962 mRNA. Translation: AAH18962.1.
    BC064987 mRNA. Translation: AAH64987.1.
    CCDSiCCDS34632.1. [P17936-2]
    CCDS5505.1. [P17936-1]
    PIRiA36578. IOHU3.
    RefSeqiNP_000589.2. NM_000598.4. [P17936-1]
    NP_001013416.1. NM_001013398.1. [P17936-2]
    UniGeneiHs.450230.

    Genome annotation databases

    EnsembliENST00000275521; ENSP00000275521; ENSG00000146674. [P17936-1]
    ENST00000381083; ENSP00000370473; ENSG00000146674. [P17936-2]
    GeneIDi3486.
    KEGGihsa:3486.
    UCSCiuc003tnr.3. human. [P17936-1]

    Polymorphism databases

    DMDMi146327827.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs
    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31159 mRNA. Translation: AAA52541.1 .
    M35878 Genomic DNA. Translation: AAA52706.1 .
    X64875 mRNA. Translation: CAA46087.1 .
    DQ301819 Genomic DNA. Translation: ABB96247.1 .
    AC091524 Genomic DNA. Translation: AAS07554.1 .
    CH236958 Genomic DNA. Translation: EAL23801.1 .
    CH471128 Genomic DNA. Translation: EAW61028.1 .
    CH471128 Genomic DNA. Translation: EAW61029.1 .
    BC000013 mRNA. Translation: AAH00013.1 .
    BC018962 mRNA. Translation: AAH18962.1 .
    BC064987 mRNA. Translation: AAH64987.1 .
    CCDSi CCDS34632.1. [P17936-2 ]
    CCDS5505.1. [P17936-1 ]
    PIRi A36578. IOHU3.
    RefSeqi NP_000589.2. NM_000598.4. [P17936-1 ]
    NP_001013416.1. NM_001013398.1. [P17936-2 ]
    UniGenei Hs.450230.

    3D structure databases

    ProteinModelPortali P17936.
    SMRi P17936. Positions 38-116, 211-274.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109707. 17 interactions.
    DIPi DIP-40786N.
    IntActi P17936. 6 interactions.
    MINTi MINT-142445.
    STRINGi 9606.ENSP00000370473.

    Chemistry

    BindingDBi P17936.
    ChEMBLi CHEMBL3997.
    DrugBanki DB01277. Mecasermin.

    Protein family/group databases

    MEROPSi I31.952.

    PTM databases

    PhosphoSitei P17936.

    Polymorphism databases

    DMDMi 146327827.

    Proteomic databases

    MaxQBi P17936.
    PaxDbi P17936.
    PeptideAtlasi P17936.
    PRIDEi P17936.

    Protocols and materials databases

    DNASUi 3486.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000275521 ; ENSP00000275521 ; ENSG00000146674 . [P17936-1 ]
    ENST00000381083 ; ENSP00000370473 ; ENSG00000146674 . [P17936-2 ]
    GeneIDi 3486.
    KEGGi hsa:3486.
    UCSCi uc003tnr.3. human. [P17936-1 ]

    Organism-specific databases

    CTDi 3486.
    GeneCardsi GC07M045918.
    HGNCi HGNC:5472. IGFBP3.
    HPAi CAB010360.
    HPA013357.
    MIMi 146732. gene.
    neXtProti NX_P17936.
    PharmGKBi PA29705.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG38980.
    HOGENOMi HOG000253012.
    HOVERGENi HBG002631.
    KOi K10138.
    OMAi YTERCGA.
    PhylomeDBi P17936.
    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).

    Miscellaneous databases

    ChiTaRSi IGFBP3. human.
    GeneWikii IGFBP3.
    GenomeRNAii 3486.
    NextBioi 13708.
    PMAP-CutDB P17936.
    PROi P17936.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P17936.
    Bgeei P17936.
    CleanExi HS_IGFBP3.
    Genevestigatori P17936.

    Family and domain databases

    Gene3Di 4.10.40.20. 1 hit.
    4.10.800.10. 1 hit.
    InterProi IPR009030. Growth_fac_rcpt_N_dom.
    IPR012211. IGFBP-3.
    IPR000867. IGFBP-like.
    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.
    PTHR11551:SF3. PTHR11551:SF3. 1 hit.
    Pfami PF00219. IGFBP. 1 hit.
    PF00086. Thyroglobulin_1. 1 hit.
    [Graphical view ]
    PRINTSi PR01976. IGFBPFAMILY.
    PR01979. IGFBPFAMILY3.
    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. "Cloning and expression of the growth hormone-dependent insulin-like growth factor-binding protein."
      Wood W.I., Cachianes G., Henzel W.J., Winslow G.A., Spencer S.A., Hellmiss R., Martin J.L., Baxter R.C.
      Mol. Endocrinol. 2:1176-1185(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-32.
    2. "Insulin-like growth factor binding protein-3. Organization of the human chromosomal gene and demonstration of promoter activity."
      Cubbage M.L., Suwanichkul A., Powell D.R.
      J. Biol. Chem. 265:12642-12649(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), VARIANT GLY-32.
    3. "Analysis of the primary structure of insulin-like growth factor binding protein-3 cDNA from Werner syndrome fibroblasts."
      Thweatt R., Fleischmann R., Goldstein S.
      DNA Seq. 4:43-46(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-32.
      Tissue: Skin.
    4. NIEHS SNPs program
      Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), VARIANTS THR-56 AND SER-234.
    5. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORM 1).
      Tissue: Kidney and Spleen.
    9. "Isolation from adult human serum of four insulin-like growth factor (IGF) binding proteins and molecular cloning of one of them that is increased by IGF I administration and in extrapancreatic tumor hypoglycemia."
      Zapf J., Kiefer M., Merryweather J., Musiarz F., Bauer D., Born W., Fischer J.A., Froesch E.R.
      J. Biol. Chem. 265:14892-14898(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-65.
    10. "Purification from human cerebrospinal fluid of insulin-like growth factor binding proteins (IGFBPs). Isolation of IGFBP-2, an altered form of IGFBP-3 and a new IGFBP species."
      Roghani M., Segovia B., Whitechurch O., Binoux M.
      Growth Regul. 1:125-130(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-45, INTERACTION WITH IGF2, VARIANT GLY-32.
      Tissue: Cerebrospinal fluid.
    11. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-42.
    12. "Interaction between the Alzheimer's survival peptide humanin and insulin-like growth factor-binding protein 3 regulates cell survival and apoptosis."
      Ikonen M., Liu B., Hashimoto Y., Ma L., Lee K.W., Niikura T., Nishimoto I., Cohen P.
      Proc. Natl. Acad. Sci. U.S.A. 100:13042-13047(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HN.
    13. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136.
      Tissue: Plasma.
    14. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136 AND ASN-199.
      Tissue: Plasma.
    15. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-136.
      Tissue: Liver.
    16. Cited for: GLYCOSYLATION AT ASN-116; ASN-136 AND ASN-199.
    17. "Identification of a novel cell death receptor mediating IGFBP-3-induced anti-tumor effects in breast and prostate cancer."
      Ingermann A.R., Yang Y.F., Han J., Mikami A., Garza A.E., Mohanraj L., Fan L., Idowu M., Ware J.L., Kim H.S., Lee D.Y., Oh Y.
      J. Biol. Chem. 285:30233-30246(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TMEM219.
    18. Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-7 AND CYS-252.

    Entry informationi

    Entry nameiIBP3_HUMAN
    AccessioniPrimary (citable) accession number: P17936
    Secondary accession number(s): A4D2F5
    , D3DVM0, Q2V509, Q6P1M6, Q9UCL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 173 of the entry and version 2 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

    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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3