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P24592

- IBP6_HUMAN

UniProt

P24592 - IBP6_HUMAN

Protein

Insulin-like growth factor-binding protein 6

Gene

IGFBP6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 1 (01 Mar 1992)
      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.

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. negative regulation of cell proliferation Source: ProtInc
    3. regulation of cell growth Source: InterPro
    4. signal transduction Source: ProtInc

    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).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Insulin-like growth factor-binding protein 6
    Short name:
    IBP-6
    Short name:
    IGF-binding protein 6
    Short name:
    IGFBP-6
    Gene namesi
    Name:IGFBP6
    Synonyms:IBP6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:5475. IGFBP6.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: Ensembl
    3. extracellular vesicular exosome Source: UniProt
    4. Golgi apparatus Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29708.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 27273 PublicationsAdd
    BLAST
    Chaini28 – 240213Insulin-like growth factor-binding protein 6PRO_0000014389Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 321 PublicationPROSITE-ProRule annotation
    Disulfide bondi40 ↔ 441 PublicationPROSITE-ProRule annotation
    Disulfide bondi57 ↔ 631 PublicationPROSITE-ProRule annotation
    Disulfide bondi71 ↔ 841 PublicationPROSITE-ProRule annotation
    Disulfide bondi78 ↔ 1041 PublicationPROSITE-ProRule annotation
    Glycosylationi126 – 1261O-linked (HexNAc...)2 Publications
    Glycosylationi144 – 1441O-linked (HexNAc...)By similarity
    Glycosylationi145 – 1451O-linked (HexNAc...)By similarity
    Glycosylationi146 – 1461O-linked (HexNAc...)By similarity
    Glycosylationi152 – 1521O-linked (HexNAc...)By similarity
    Disulfide bondi163 ↔ 1901 PublicationPROSITE-ProRule annotation
    Disulfide bondi201 ↔ 2121 PublicationPROSITE-ProRule annotation
    Disulfide bondi214 ↔ 2341 PublicationPROSITE-ProRule annotation

    Post-translational modificationi

    O-linked glycans consist of hexose (probably Gal), N-acetylhexosamine (probably GalNAc) and sialic acid residues. O-glycosylated with core 1 or possibly core 8 glycans. O-glycosylated on one site only in the region AA 143-168 in cerebrospinal fluid.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP24592.
    PaxDbiP24592.
    PeptideAtlasiP24592.
    PRIDEiP24592.

    Expressioni

    Gene expression databases

    ArrayExpressiP24592.
    BgeeiP24592.
    CleanExiHS_IGFBP6.
    GenevestigatoriP24592.

    Organism-specific databases

    HPAiHPA008005.

    Interactioni

    Protein-protein interaction databases

    BioGridi109710. 2 interactions.
    IntActiP24592. 1 interaction.
    MINTiMINT-2859943.
    STRINGi9606.ENSP00000301464.

    Structurei

    Secondary structure

    1
    240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi162 – 17716
    Turni179 – 1813
    Beta strandi182 – 1887
    Beta strandi198 – 20811
    Beta strandi212 – 2154
    Turni226 – 2283
    Turni231 – 2333
    Beta strandi234 – 2363

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1RMJNMR-A161-240[»]
    DisProtiDP00211.
    ProteinModelPortaliP24592.
    SMRiP24592. Positions 25-105, 161-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP24592.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 10780IGFBP N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini160 – 23475Thyroglobulin 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

    eggNOGiNOG47794.
    HOGENOMiHOG000253012.
    HOVERGENiHBG002631.
    InParanoidiP24592.
    OMAiRDQQRNP.
    PhylomeDBiP24592.
    TreeFamiTF331211.

    Family and domain databases

    Gene3Di4.10.40.20. 1 hit.
    4.10.800.10. 1 hit.
    InterProiIPR009030. Growth_fac_rcpt_N_dom.
    IPR022326. IGFBP-6.
    IPR000867. IGFBP-like.
    IPR009168. IGFBP1-6.
    IPR022321. IGFBP_1-6_chordata.
    IPR000716. Thyroglobulin_1.
    [Graphical view]
    PANTHERiPTHR11551. PTHR11551. 1 hit.
    PfamiPF00219. IGFBP. 1 hit.
    PF00086. Thyroglobulin_1. 1 hit.
    [Graphical view]
    PRINTSiPR01976. IGFBPFAMILY.
    PR01982. IGFBPFAMILY6.
    SMARTiSM00121. IB. 1 hit.
    SM00211. TY. 1 hit.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 1 hit.
    SSF57610. SSF57610. 1 hit.
    PROSITEiPS51323. 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.

    P24592-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTPHRLLPPL LLLLALLLAA SPGGALARCP GCGQGVQAGC PGGCVEEEDG    50
    GSPAEGCAEA EGCLRREGQE CGVYTPNCAP GLQCHPPKDD EAPLRALLLG 100
    RGRCLPARAP AVAEENPKES KPQAGTARPQ DVNRRDQQRN PGTSTTPSQP 150
    NSAGVQDTEM GPCRRHLDSV LQQLQTEVYR GAQTLYVPNC DHRGFYRKRQ 200
    CRSSQGQRRG PCWCVDRMGK SLPGSPDGNG SSSCPTGSSG 240
    Length:240
    Mass (Da):25,322
    Last modified:March 1, 1992 - v1
    Checksum:i285308231C025009
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21T → C in AAA88070. (PubMed:1719383)Curated
    Sequence conflicti28 – 292RC → AA AA sequence (PubMed:1697583)Curated
    Sequence conflicti28 – 292RC → LA AA sequence (PubMed:2154495)Curated
    Sequence conflicti32 – 321C → H AA sequence (PubMed:1697583)Curated
    Sequence conflicti55 – 573EGC → QGG AA sequence (PubMed:1697583)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti128 – 1281R → G.1 Publication
    Corresponds to variant rs9658616 [ dbSNP | Ensembl ].
    VAR_018932
    Natural varianti134 – 1341R → L.
    Corresponds to variant rs34995393 [ dbSNP | Ensembl ].
    VAR_049565
    Natural varianti217 – 2171R → Q.1 Publication
    Corresponds to variant rs6413498 [ dbSNP | Ensembl ].
    VAR_018933
    Natural varianti236 – 2361T → P.
    Corresponds to variant rs1053134 [ dbSNP | Ensembl ].
    VAR_011907

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62402 mRNA. Translation: AAB06187.1.
    AJ006952 Genomic DNA. Translation: CAA07346.1.
    AY443494 Genomic DNA. Translation: AAR05445.1.
    BC003507 mRNA. Translation: AAH03507.1.
    BC005007 mRNA. Translation: AAH05007.1.
    BC010162 mRNA. Translation: AAH10162.1.
    BC011708 mRNA. Translation: AAH11708.1.
    M69054 mRNA. Translation: AAA88070.1.
    CCDSiCCDS8846.1.
    PIRiA39842.
    S05699.
    RefSeqiNP_002169.1. NM_002178.2.
    UniGeneiHs.274313.

    Genome annotation databases

    EnsembliENST00000301464; ENSP00000301464; ENSG00000167779.
    GeneIDi3489.
    KEGGihsa:3489.
    UCSCiuc001sbu.1. human.

    Polymorphism databases

    DMDMi124068.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M62402 mRNA. Translation: AAB06187.1 .
    AJ006952 Genomic DNA. Translation: CAA07346.1 .
    AY443494 Genomic DNA. Translation: AAR05445.1 .
    BC003507 mRNA. Translation: AAH03507.1 .
    BC005007 mRNA. Translation: AAH05007.1 .
    BC010162 mRNA. Translation: AAH10162.1 .
    BC011708 mRNA. Translation: AAH11708.1 .
    M69054 mRNA. Translation: AAA88070.1 .
    CCDSi CCDS8846.1.
    PIRi A39842.
    S05699.
    RefSeqi NP_002169.1. NM_002178.2.
    UniGenei Hs.274313.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1RMJ NMR - A 161-240 [» ]
    DisProti DP00211.
    ProteinModelPortali P24592.
    SMRi P24592. Positions 25-105, 161-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109710. 2 interactions.
    IntActi P24592. 1 interaction.
    MINTi MINT-2859943.
    STRINGi 9606.ENSP00000301464.

    Chemistry

    BindingDBi P24592.
    ChEMBLi CHEMBL2139.

    Polymorphism databases

    DMDMi 124068.

    Proteomic databases

    MaxQBi P24592.
    PaxDbi P24592.
    PeptideAtlasi P24592.
    PRIDEi P24592.

    Protocols and materials databases

    DNASUi 3489.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301464 ; ENSP00000301464 ; ENSG00000167779 .
    GeneIDi 3489.
    KEGGi hsa:3489.
    UCSCi uc001sbu.1. human.

    Organism-specific databases

    CTDi 3489.
    GeneCardsi GC12P053491.
    HGNCi HGNC:5475. IGFBP6.
    HPAi HPA008005.
    MIMi 146735. gene.
    neXtProti NX_P24592.
    PharmGKBi PA29708.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG47794.
    HOGENOMi HOG000253012.
    HOVERGENi HBG002631.
    InParanoidi P24592.
    OMAi RDQQRNP.
    PhylomeDBi P24592.
    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

    EvolutionaryTracei P24592.
    GeneWikii IGFBP6.
    GenomeRNAii 3489.
    NextBioi 13722.
    PROi P24592.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24592.
    Bgeei P24592.
    CleanExi HS_IGFBP6.
    Genevestigatori P24592.

    Family and domain databases

    Gene3Di 4.10.40.20. 1 hit.
    4.10.800.10. 1 hit.
    InterProi IPR009030. Growth_fac_rcpt_N_dom.
    IPR022326. IGFBP-6.
    IPR000867. IGFBP-like.
    IPR009168. IGFBP1-6.
    IPR022321. IGFBP_1-6_chordata.
    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.
    PR01982. IGFBPFAMILY6.
    SMARTi SM00121. IB. 1 hit.
    SM00211. TY. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    SSF57610. SSF57610. 1 hit.
    PROSITEi PS51323. IGFBP_N_2. 1 hit.
    PS00484. THYROGLOBULIN_1_1. 1 hit.
    PS51162. THYROGLOBULIN_1_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification and molecular cloning of two new 30-kDa insulin-like growth factor binding proteins isolated from adult human serum."
      Kiefer M.C., Masiarz F.R., Bauer D.M., Zapf J.
      J. Biol. Chem. 266:9043-9049(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Osteosarcoma.
    2. "Characterization and chromosomal localization of the human insulin-like growth factor-binding protein 6 gene."
      Ehrenborg E., Zazzi H., Lagercrantz S., Granqvist M., Hillerbrand U., Allander S.V., Larsson C., Luthman H.
      Mamm. Genome 10:376-380(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. NIEHS SNPs program
      Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-128 AND GLN-217.
    4. "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: Pancreas.
    5. "Isolation and molecular cloning of insulin-like growth factor-binding protein-6."
      Shimasaki S., Gao L., Shimonaka M., Ling N.
      Mol. Endocrinol. 5:938-948(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-240.
      Tissue: Placenta.
    6. "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 28-57.
      Tissue: Serum.
    7. "Isolation from human cerebrospinal fluid of a new insulin-like growth factor-binding protein with a selective affinity for IGF-II."
      Roghani M., Hossenlopp P., Lepage P., Balland A., Binoux M.
      FEBS Lett. 255:253-258(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY PROTEIN SEQUENCE OF 28-42.
      Tissue: Cerebrospinal fluid.
    8. "Purification and properties of a novel insulin-like growth factor-II binding protein from transformed human fibroblasts."
      Martin J.L., Willetts K.E., Baxter R.C.
      J. Biol. Chem. 265:4124-4130(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 28-42.
      Tissue: Fibroblast.
    9. "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 28-42.
      Tissue: Osteosarcoma.
    10. "Identification of O-glycosylation sites and partial characterization of carbohydrate structure and disulfide linkages of human insulin-like growth factor binding protein 6."
      Neumann G.M., Marinaro J.A., Bach L.A.
      Biochemistry 37:6572-6585(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-126; SER-144; THR-145; THR-146 AND SER-152.
    11. "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.
    12. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-126, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.

    Entry informationi

    Entry nameiIBP6_HUMAN
    AccessioniPrimary (citable) accession number: P24592
    Secondary accession number(s): Q14492
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: March 1, 1992
    Last modified: October 1, 2014
    This is version 152 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 12
      Human chromosome 12: 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