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P08833

- IBP1_HUMAN

UniProt

P08833 - IBP1_HUMAN

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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

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
Complete GO annotation...

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
Complete GO annotation...

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 – 1201Phosphoserine1 Publication
Modified residuei123 – 1231Phosphoserine1 Publication
Modified residuei126 – 1261Phosphoserine2 Publications
Modified residuei144 – 1441Phosphoserine2 Publications
Disulfide bondi176 ↔ 206
Modified residuei194 – 1941Phosphoserine2 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

BgeeiP08833.
CleanExiHS_IGFBP1.
ExpressionAtlasiP08833. baseline and differential.
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 – 19319Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi214 – 2174Combined sources
Beta strandi222 – 2243Combined sources
Beta strandi228 – 2314Combined sources
Turni233 – 2353Combined sources
Beta strandi245 – 2473Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074457.
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

        10         20         30         40         50
MSEVPVARVW LVLLLLTVQV GVTAGAPWQC APCSAEKLAL CPPVSASCSE
60 70 80 90 100
VTRSAGCGCC PMCALPLGAA CGVATARCAR GLSCRALPGE QQPLHALTRG
110 120 130 140 150
QGACVQESDA SAPHAAEAGS PESPESTEIT EEELLDNFHL MAPSEEDHSI
160 170 180 190 200
LWDAISTYDG SKALHVTNIK KWKEPCRIEL YRVVESLAKA QETSGEEISK
210 220 230 240 250
FYLPNCNKNG FYHSRQCETS MDGEAGLCWC VYPWNGKRIP GSPEIRGDPN

CQIYFNVQN
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreei ENSGT00550000074457.
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

Bgeei P08833.
CleanExi HS_IGFBP1.
ExpressionAtlasi P08833. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 172 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

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