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P17936

- IBP3_HUMAN

UniProt

P17936 - IBP3_HUMAN

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Protein
Insulin-like growth factor-binding protein 3
Gene
IGFBP3, IBP3
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. 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 I binding Source: BHF-UCL
  2. insulin-like growth factor binding Source: UniProtKB
  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 MAPK cascade Source: Ensembl
  9. positive regulation of apoptotic process Source: UniProtKB
  10. positive regulation of catalytic activity Source: GOC
  11. positive regulation of insulin-like growth factor receptor signaling pathway 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29705.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 27273 Publications
Add
BLAST
Chaini28 – 291264Insulin-like growth factor-binding protein 3
PRO_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 ↔ 240 By similarity
Disulfide bondi251 ↔ 262 By similarity
Disulfide bondi264 ↔ 285 By similarity

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 TMEM219.3 Publications

Protein-protein interaction databases

BioGridi109707. 17 interactions.
DIPiDIP-40786N.
IntActiP17936. 4 interactions.
MINTiMINT-142445.
STRINGi9606.ENSP00000370473.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 11782IGFBP N-terminal
Add
BLAST
Domaini210 – 28576Thyroglobulin type-1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 134107IGF-binding Reviewed prediction
Add
BLAST

Compositional bias

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

Domaini

The thyroglobulin type-1 domain mediates interaction with HN.

Sequence similaritiesi

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.
VSP_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. 4 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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 172 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

Similar proteinsi