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P22692

- IBP4_HUMAN

UniProt

P22692 - IBP4_HUMAN

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Protein

Insulin-like growth factor-binding protein 4

Gene

IGFBP4

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.

GO - Biological processi

  1. cell proliferation Source: ProtInc
  2. cellular protein metabolic process Source: Reactome
  3. DNA metabolic process Source: ProtInc
  4. inflammatory response Source: Ensembl
  5. positive regulation of insulin-like growth factor receptor signaling pathway Source: Ensembl
  6. positive regulation of MAPK cascade Source: Ensembl
  7. regulation of cell growth Source: Ensembl
  8. regulation of glucose metabolic process Source: Ensembl
  9. signal transduction Source: ProtInc
  10. skeletal system development Source: ProtInc
  11. type B pancreatic cell proliferation Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

Growth factor binding

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000141753-MONOMER.
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 4
Short name:
IBP-4
Short name:
IGF-binding protein 4
Short name:
IGFBP-4
Gene namesi
Name:IGFBP4
Synonyms:IBP4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:5473. IGFBP4.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29706.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21213 PublicationsAdd
BLAST
Chaini22 – 258237Insulin-like growth factor-binding protein 4PRO_0000014382Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 53
Disulfide bondi30 ↔ 55
Disulfide bondi38 ↔ 59
Disulfide bondi44 ↔ 56
Disulfide bondi67 ↔ 80
Disulfide bondi74 ↔ 100
Glycosylationi125 – 1251N-linked (GlcNAc...)1 PublicationSequence Analysis
Disulfide bondi131 ↔ 138PROSITE-ProRule annotation
Disulfide bondi174 ↔ 204
Disulfide bondi215 ↔ 226
Disulfide bondi228 ↔ 249

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP22692.
PaxDbiP22692.
PeptideAtlasiP22692.
PRIDEiP22692.

PTM databases

PhosphoSiteiP22692.

Miscellaneous databases

PMAP-CutDBP22692.

Expressioni

Inductioni

By forskolin and N6,O2'dibutyryl adenosine 3',5'-cyclic monophosphate, but not by 1,9 dideoxyforskolin.1 Publication

Gene expression databases

BgeeiP22692.
CleanExiHS_IGFBP4.
ExpressionAtlasiP22692. baseline and differential.
GenevestigatoriP22692.

Interactioni

Subunit structurei

Binds IGF2 more than IGF1.2 Publications

Protein-protein interaction databases

BioGridi109708. 6 interactions.
DIPiDIP-48432N.
IntActiP22692. 3 interactions.
MINTiMINT-6630380.
STRINGi9606.ENSP00000269593.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi32 – 365Combined sources
Beta strandi45 – 495Combined sources
Beta strandi56 – 594Combined sources
Beta strandi69 – 713Combined sources
Beta strandi78 – 814Combined sources
Helixi89 – 946Combined sources
Beta strandi98 – 1025Combined sources
Helixi103 – 1108Combined sources
Helixi173 – 18614Combined sources
Helixi195 – 1984Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi212 – 2154Combined sources
Beta strandi226 – 2294Combined sources
Turni231 – 2333Combined sources
Helixi244 – 2463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WQJX-ray1.60B24-103[»]
2DSPX-ray2.50B22-113[»]
2DSQX-ray2.80A/B22-113[»]
2DSRX-ray2.10B24-103[»]
G172-253[»]
ProteinModelPortaliP22692.
SMRiP22692. Positions 24-103, 172-250.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22692.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 10381IGFBP N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini171 – 24979Thyroglobulin 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

eggNOGiNOG46496.
GeneTreeiENSGT00550000074457.
HOGENOMiHOG000253012.
HOVERGENiHBG002631.
InParanoidiP22692.
OMAiKGMPCGV.
OrthoDBiEOG74N5HG.
PhylomeDBiP22692.
TreeFamiTF331211.

Family and domain databases

Gene3Di4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProiIPR009030. Growth_fac_rcpt_N_dom.
IPR022327. IGFBP-4.
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.
PfamiPF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view]
PRINTSiPR01976. IGFBPFAMILY.
PR01980. IGFBPFAMILY4.
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: P22692-1) [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

        10         20         30         40         50
MLPLCLVAAL LLAAGPGPSL GDEAIHCPPC SEEKLARCRP PVGCEELVRE
60 70 80 90 100
PGCGCCATCA LGLGMPCGVY TPRCGSGLRC YPPRGVEKPL HTLMHGQGVC
110 120 130 140 150
MELAEIEAIQ ESLQPSDKDE GDHPNNSFSP CSAHDRRCLQ KHFAKIRDRS
160 170 180 190 200
TSGGKMKVNG APREDARPVP QGSCQSELHR ALERLAASQS RTHEDLYIIP
210 220 230 240 250
IPNCDRNGNF HPKQCHPALD GQRGKCWCVD RKTGVKLPGG LEPKGELDCH

QLADSFRE
Length:258
Mass (Da):27,934
Last modified:March 1, 1992 - v2
Checksum:i5E8F4638D99F0A94
GO
Isoform 2 (identifier: P22692-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Note: No experimental confirmation available

Show »
Length:158
Mass (Da):17,635
Checksum:iF31375031D835A1E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 511P → A in M38177. (PubMed:1707125)Curated
Sequence conflicti51 – 511P → A in AAA62670. (PubMed:9048882)Curated
Sequence conflicti51 – 511P → A AA sequence (PubMed:1709585)Curated
Sequence conflicti160 – 1601G → E in AAV38694. 1 PublicationCurated
Sequence conflicti198 – 1981I → F in M38177. (PubMed:1707125)Curated
Sequence conflicti198 – 1981I → F in AAA62670. (PubMed:9048882)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti42 – 421V → G.
Corresponds to variant rs599199 [ dbSNP | Ensembl ].
VAR_011906

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_057034Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38177 mRNA. No translation available.
M62403 mRNA. Translation: AAB06189.1.
U20982 Genomic DNA. Translation: AAA62670.1.
Y12508 Genomic DNA. Translation: CAA73110.1.
AK304572 mRNA. Translation: BAG65363.1.
BT019891 mRNA. Translation: AAV38694.1.
BT019892 mRNA. Translation: AAV38695.1.
AY442346 Genomic DNA. Translation: AAR05443.1.
AC018629 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60664.1.
BC016041 mRNA. Translation: AAH16041.1.
CCDSiCCDS11367.1.
PIRiG01662. B37252.
RefSeqiNP_001543.2. NM_001552.2.
UniGeneiHs.462998.

Genome annotation databases

EnsembliENST00000269593; ENSP00000269593; ENSG00000141753. [P22692-1]
GeneIDi3487.
KEGGihsa:3487.
UCSCiuc002hus.3. human. [P22692-1]

Polymorphism databases

DMDMi124065.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M38177 mRNA. No translation available.
M62403 mRNA. Translation: AAB06189.1 .
U20982 Genomic DNA. Translation: AAA62670.1 .
Y12508 Genomic DNA. Translation: CAA73110.1 .
AK304572 mRNA. Translation: BAG65363.1 .
BT019891 mRNA. Translation: AAV38694.1 .
BT019892 mRNA. Translation: AAV38695.1 .
AY442346 Genomic DNA. Translation: AAR05443.1 .
AC018629 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60664.1 .
BC016041 mRNA. Translation: AAH16041.1 .
CCDSi CCDS11367.1.
PIRi G01662. B37252.
RefSeqi NP_001543.2. NM_001552.2.
UniGenei Hs.462998.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WQJ X-ray 1.60 B 24-103 [» ]
2DSP X-ray 2.50 B 22-113 [» ]
2DSQ X-ray 2.80 A/B 22-113 [» ]
2DSR X-ray 2.10 B 24-103 [» ]
G 172-253 [» ]
ProteinModelPortali P22692.
SMRi P22692. Positions 24-103, 172-250.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109708. 6 interactions.
DIPi DIP-48432N.
IntActi P22692. 3 interactions.
MINTi MINT-6630380.
STRINGi 9606.ENSP00000269593.

Chemistry

BindingDBi P22692.
ChEMBLi CHEMBL2310.

Protein family/group databases

MEROPSi I31.952.

PTM databases

PhosphoSitei P22692.

Polymorphism databases

DMDMi 124065.

Proteomic databases

MaxQBi P22692.
PaxDbi P22692.
PeptideAtlasi P22692.
PRIDEi P22692.

Protocols and materials databases

DNASUi 3487.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000269593 ; ENSP00000269593 ; ENSG00000141753 . [P22692-1 ]
GeneIDi 3487.
KEGGi hsa:3487.
UCSCi uc002hus.3. human. [P22692-1 ]

Organism-specific databases

CTDi 3487.
GeneCardsi GC17P038599.
HGNCi HGNC:5473. IGFBP4.
MIMi 146733. gene.
neXtProti NX_P22692.
PharmGKBi PA29706.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46496.
GeneTreei ENSGT00550000074457.
HOGENOMi HOG000253012.
HOVERGENi HBG002631.
InParanoidi P22692.
OMAi KGMPCGV.
OrthoDBi EOG74N5HG.
PhylomeDBi P22692.
TreeFami TF331211.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000141753-MONOMER.
Reactomei REACT_15428. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

ChiTaRSi IGFBP4. human.
EvolutionaryTracei P22692.
GeneWikii IGFBP4.
GenomeRNAii 3487.
NextBioi 13714.
PMAP-CutDB P22692.
PROi P22692.
SOURCEi Search...

Gene expression databases

Bgeei P22692.
CleanExi HS_IGFBP4.
ExpressionAtlasi P22692. baseline and differential.
Genevestigatori P22692.

Family and domain databases

Gene3Di 4.10.40.20. 1 hit.
4.10.800.10. 1 hit.
InterProi IPR009030. Growth_fac_rcpt_N_dom.
IPR022327. IGFBP-4.
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.
Pfami PF00219. IGFBP. 1 hit.
PF00086. Thyroglobulin_1. 1 hit.
[Graphical view ]
PRINTSi PR01976. IGFBPFAMILY.
PR01980. IGFBPFAMILY4.
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. "Molecular cloning of the cDNAs encoding a novel insulin-like growth factor-binding protein from rat and human."
    Shimasaki S., Uchiyama F., Shimonaka M., Ling N.
    Mol. Endocrinol. 4:1451-1458(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Inhibitory insulin-like growth factor-binding protein: cloning, complete sequence, and physiological regulation."
    Latour D., Mohan S., Linkhart T.A., Baylink D.J., Strong D.D.
    Mol. Endocrinol. 4:1806-1814(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "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] (ISOFORM 1), PROTEIN SEQUENCE OF 22-41.
    Tissue: Osteosarcoma.
  4. "Structural and functional analysis of the 5'-flanking region of the human insulin-like growth factor binding protein (IGFBP)-4 gene."
    Qin X., Morales S., Lee K.-W., Boonyaratanakornkit V., Baylink D.J., Mohan S., Strong D.D.
    Biochim. Biophys. Acta 1350:136-140(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  5. "Structure and transcription regulation of the human insulin-like growth factor binding protein 4 gene (IGFBP4)."
    Zazzi H., Nikoshkov A., Hall K., Luthman H.
    Genomics 49:401-410(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Uterus.
  7. "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] (ISOFORM 1).
  8. NIEHS SNPs program
    Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  9. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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: Colon.
  12. "Purification of a colon cancer cell growth inhibitor and its identification as an insulin-like growth factor binding protein."
    Culouscou J.-M., Shoyab M.
    Cancer Res. 51:2813-2819(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-53.
    Tissue: Colon.
  13. "Evidence that the inhibition of TE85 human bone cell proliferation by agents which stimulate cAMP production may in part be mediated by changes in the IGF-II regulatory system."
    Mohan S., Baylink D.J.
    Growth Regul. 1:110-118(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 22-42, INDUCTION.
    Tissue: Osteosarcoma.
  14. "Structural basis for the regulation of insulin-like growth factors by IGF binding proteins."
    Siwanowicz I., Popowicz G.M., Wisniewska M., Huber R., Kuenkele K.-P., Lang K., Engh R.A., Holak T.A.
    Structure 13:155-167(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 24-103 IN COMPLEX WITH IGF1, DISULFIDE BONDS.
  15. "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 (2.1 ANGSTROMS) OF 22-253 IN COMPLEX WITH IGF1, DISULFIDE BONDS.

Entry informationi

Entry nameiIBP4_HUMAN
AccessioniPrimary (citable) accession number: P22692
Secondary accession number(s): A0N9W2
, B4E351, Q5U012, Q9UCL6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: March 1, 1992
Last modified: November 26, 2014
This is version 153 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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