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P17936 (IBP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Insulin-like growth factor-binding protein 3

Short name=IBP-3
Short name=IGF-binding protein 3
Short name=IGFBP-3
Gene names
Name:IGFBP3
Synonyms:IBP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length291 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. Also exhibits IGF-independent antiproliferative and apoptotic effects mediated by its receptor TMEM219/IGFBP-3R. Ref.17

Subunit structure

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. Ref.10 Ref.12 Ref.17

Subcellular location

Secreted Ref.17.

Tissue specificity

Expressed by most tissues. Present in plasma.

Developmental stage

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

Induction

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

Domain

The thyroglobulin type-1 domain mediates interaction with HN.

Post-translational modification

Phosphorylation sites are present in the extracellular medium.

Sequence similarities

Contains 1 IGFBP N-terminal domain.

Contains 1 thyroglobulin type-1 domain.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentSecreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSignal
   LigandGrowth factor binding
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

cellular protein metabolic process

Traceable author statement. Source: Reactome

negative regulation of cell proliferation

Inferred from genetic interaction PubMed 19258508. Source: MGI

negative regulation of protein phosphorylation

Inferred from direct assay PubMed 17591901. Source: MGI

negative regulation of signal transduction

Non-traceable author statement PubMed 11940579. Source: UniProtKB

negative regulation of smooth muscle cell migration

Inferred from direct assay PubMed 10766744. Source: BHF-UCL

negative regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 10766744. Source: BHF-UCL

positive regulation of MAPK cascade

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 11971816. Source: UniProtKB

positive regulation of catalytic activity

Inferred from direct assay PubMed 11940579. Source: GOC

positive regulation of insulin-like growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of myoblast differentiation

Inferred from direct assay PubMed 12599210. Source: UniProtKB

protein phosphorylation

Inferred from direct assay PubMed 17434920. Source: MGI

regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

regulation of glucose metabolic process

Inferred from electronic annotation. Source: Ensembl

type B pancreatic cell proliferation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Non-traceable author statement PubMed 14718574. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 17119061. Source: BHF-UCL

insulin-like growth factor binding protein complex

Inferred by curator PubMed 10766744. Source: BHF-UCL

nucleus

Inferred from direct assay PubMed 17434920. Source: MGI

   Molecular_functioninsulin-like growth factor I binding

Inferred from physical interaction PubMed 10766744. Source: BHF-UCL

insulin-like growth factor binding

Non-traceable author statement PubMed 12599210. Source: UniProtKB

metal ion binding

Non-traceable author statement PubMed 14576163. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12PubMed 9388210. Source: UniProtKB

protein tyrosine phosphatase activator activity

Inferred from direct assay PubMed 11940579. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P17936-1)

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.
Isoform 2 (identifier: P17936-2)

The sequence of this isoform differs from the canonical sequence as follows:
     135-135: G → GEPPAPG
Note: Gene prediction based on EST data.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Ref.9 Ref.10 Ref.11
Chain28 – 291264Insulin-like growth factor-binding protein 3
PRO_0000014378

Regions

Domain36 – 11782IGFBP N-terminal
Domain210 – 28576Thyroglobulin type-1
Region28 – 134107IGF-binding Potential
Compositional bias138 – 16124Ser/Thr-rich
Compositional bias192 – 20817Ser/Thr-rich

Amino acid modifications

Glycosylation1161N-linked (GlcNAc...) (complex) Ref.16
Glycosylation1361N-linked (GlcNAc...) (complex) Ref.13 Ref.14 Ref.15 Ref.16
Glycosylation1991N-linked (GlcNAc...) (complex) Ref.14 Ref.16
Disulfide bond213 ↔ 240 By similarity
Disulfide bond251 ↔ 262 By similarity
Disulfide bond264 ↔ 285 By similarity

Natural variations

Alternative sequence1351G → GEPPAPG in isoform 2.
VSP_047293
Natural variant71T → M in a colorectal cancer sample; somatic mutation. Ref.18
VAR_036279
Natural variant321A → G. Ref.1 Ref.2 Ref.3 Ref.10
Corresponds to variant rs2854746 [ dbSNP | Ensembl ].
VAR_025262
Natural variant561A → T. Ref.4
Corresponds to variant rs34257987 [ dbSNP | Ensembl ].
VAR_025263
Natural variant1581H → P.
Corresponds to variant rs9282734 [ dbSNP | Ensembl ].
VAR_021974
Natural variant2341G → S. Ref.4
Corresponds to variant rs35712717 [ dbSNP | Ensembl ].
VAR_025264
Natural variant2521R → C in a colorectal cancer sample; somatic mutation. Ref.18
VAR_036280

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: A9682065AB266586

FASTA29131,674
        10         20         30         40         50         60 
MQRARPTLWA AALTLLVLLR GPPVARAGAS SAGLGPVVRC EPCDARALAQ CAPPPAVCAE 

        70         80         90        100        110        120 
LVREPGCGCC LTCALSEGQP CGIYTERCGS GLRCQPSPDE ARPLQALLDG RGLCVNASAV 

       130        140        150        160        170        180 
SRLRAYLLPA PPAPGNASES EEDRSAGSVE SPSVSSTHRV SDPKFHPLHS KIIIIKKGHA 

       190        200        210        220        230        240 
KDSQRYKVDY ESQSTDTQNF SSESKRETEY GPCRREMEDT LNHLKFLNVL SPRGVHIPNC 

       250        260        270        280        290 
DKKGFYKKKQ CRPSKGRKRG FCWCVDKYGQ PLPGYTTKGK EDVHCYSMQS K 

« Hide

Isoform 2 [UniParc].

Checksum: 8CCFAD16904D0DF4
Show »

FASTA29732,223

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. 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].
[7]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].
[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]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
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]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] MET-7 AND CYS-252.
+Additional computationally mapped references.

Web resources

NIEHS-SNPs
SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34632.1. [P17936-2]
CCDS5505.1. [P17936-1]
PIRIOHU3. A36578.
RefSeqNP_000589.2. NM_000598.4. [P17936-1]
NP_001013416.1. NM_001013398.1. [P17936-2]
UniGeneHs.450230.

3D structure databases

ProteinModelPortalP17936.
SMRP17936. Positions 38-116, 211-274.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109707. 17 interactions.
DIPDIP-40786N.
IntActP17936. 4 interactions.
MINTMINT-142445.
STRING9606.ENSP00000370473.

Chemistry

BindingDBP17936.
ChEMBLCHEMBL3997.
DrugBankDB01277. Mecasermin.

Protein family/group databases

MEROPSI31.952.

PTM databases

PhosphoSiteP17936.

Polymorphism databases

DMDM146327827.

Proteomic databases

MaxQBP17936.
PaxDbP17936.
PeptideAtlasP17936.
PRIDEP17936.

Protocols and materials databases

DNASU3486.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275521; ENSP00000275521; ENSG00000146674. [P17936-1]
ENST00000381083; ENSP00000370473; ENSG00000146674. [P17936-2]
GeneID3486.
KEGGhsa:3486.
UCSCuc003tnr.3. human. [P17936-1]

Organism-specific databases

CTD3486.
GeneCardsGC07M045918.
HGNCHGNC:5472. IGFBP3.
HPACAB010360.
HPA013357.
MIM146732. gene.
neXtProtNX_P17936.
PharmGKBPA29705.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG38980.
HOGENOMHOG000253012.
HOVERGENHBG002631.
KOK10138.
OMAYTERCGA.
PhylomeDBP17936.
TreeFamTF331211.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP17936.
BgeeP17936.
CleanExHS_IGFBP3.
GenevestigatorP17936.

Family and domain databases

Gene3D4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProIPR009030. 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]
PANTHERPTHR11551. PTHR11551. 1 hit.
PTHR11551:SF3. PTHR11551:SF3. 1 hit.
PfamPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSPR01976. IGFBPFAMILY.
PR01979. IGFBPFAMILY3.
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

ChiTaRSIGFBP3. human.
GeneWikiIGFBP3.
GenomeRNAi3486.
NextBio13708.
PMAP-CutDBP17936.
PROP17936.
SOURCESearch...

Entry information

Entry nameIBP3_HUMAN
AccessionPrimary (citable) accession number: P17936
Secondary accession number(s): A4D2F5 expand/collapse secondary AC list , D3DVM0, Q2V509, Q6P1M6, Q9UCL4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: March 6, 2007
Last modified: July 9, 2014
This is version 171 of the entry and version 2 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

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