Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Insulin-like growth factor-binding protein 4

Gene

Igfbp4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 - Molecular functioni

  1. insulin-like growth factor binding Source: MGI
  2. insulin-like growth factor I binding Source: GO_Central
  3. insulin-like growth factor II binding Source: GO_Central

GO - Biological processi

  1. inflammatory response Source: Ensembl
  2. positive regulation of insulin-like growth factor receptor signaling pathway Source: MGI
  3. positive regulation of MAPK cascade Source: MGI
  4. regulation of cell growth Source: MGI
  5. regulation of glucose metabolic process Source: MGI
  6. regulation of growth Source: MGI
  7. type B pancreatic cell proliferation Source: MGI
Complete GO annotation...

Keywords - Ligandi

Growth factor binding

Enzyme and pathway databases

ReactomeiREACT_235886. 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:Igfbp-4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:96439. Igfbp4.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121By similarityAdd
BLAST
Chaini22 – 254233Insulin-like growth factor-binding protein 4PRO_0000014383Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 53PROSITE-ProRule annotation
Disulfide bondi30 ↔ 55PROSITE-ProRule annotation
Disulfide bondi38 ↔ 59PROSITE-ProRule annotation
Disulfide bondi44 ↔ 56PROSITE-ProRule annotation
Disulfide bondi67 ↔ 80PROSITE-ProRule annotation
Disulfide bondi74 ↔ 100PROSITE-ProRule annotation
Glycosylationi125 – 1251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi131 ↔ 138PROSITE-ProRule annotation
Disulfide bondi170 ↔ 200PROSITE-ProRule annotation
Disulfide bondi211 ↔ 222PROSITE-ProRule annotation
Disulfide bondi224 ↔ 245PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP47879.
PaxDbiP47879.
PRIDEiP47879.

PTM databases

PhosphoSiteiP47879.

Miscellaneous databases

PMAP-CutDBP47879.

Expressioni

Gene expression databases

BgeeiP47879.
CleanExiMM_IGFBP4.
ExpressionAtlasiP47879. baseline and differential.
GenevestigatoriP47879.

Interactioni

Subunit structurei

Binds IGF2 more than IGF1.

Protein-protein interaction databases

DIPiDIP-60633N.
STRINGi10090.ENSMUSP00000017637.

Structurei

3D structure databases

ProteinModelPortaliP47879.
SMRiP47879. Positions 24-103, 168-246.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini23 – 10381IGFBP N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini167 – 24579Thyroglobulin 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.
InParanoidiP47879.
OMAiAIQCPPC.
OrthoDBiEOG74N5HG.
PhylomeDBiP47879.
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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P47879-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLPFGLVAAL LLAAGPRPSL GDEAIHCPPC SEEKLARCRP PVGCEELVRE
60 70 80 90 100
PGCGCCATCA LGLGMPCGVY TPRCGSGMRC YPPRGVEKPL RTLMHGQGVC
110 120 130 140 150
TELSEIEAIQ ESLQTSDKDE SEHPNNSFNP CSAHDHRCLQ KHMAKIRDRS
160 170 180 190 200
KMKIVGTPRE EPRPVPQGSC QSELHRALER LAASQSRTHE DLFIIPIPNC
210 220 230 240 250
DRNGNFHPKQ CHPALDGQRG KCWCVDRKTG VKLPGGLEPK GELDCHQLAD

SFQE
Length:254
Mass (Da):27,807
Last modified:July 15, 1998 - v2
Checksum:i58EF89CB514AEE17
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti4 – 52FG → CS in CAA57272. (PubMed:7529732)Curated
Sequence conflicti13 – 131A → T in CAA57272. (PubMed:7529732)Curated
Sequence conflicti56 – 561C → S in CAA57272. (PubMed:7529732)Curated
Sequence conflicti67 – 671C → G in CAA57272. (PubMed:7529732)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81582 mRNA. Translation: CAA57272.1.
X76066 Genomic DNA. Translation: CAA53667.1.
AK150229 mRNA. Translation: BAE29395.1.
AK165688 mRNA. Translation: BAE38340.1.
BC019836 mRNA. Translation: AAH19836.1.
Z95492 Genomic DNA. Translation: CAB08859.1.
CCDSiCCDS25371.1.
PIRiI48599.
I48603.
RefSeqiNP_034647.1. NM_010517.3.
UniGeneiMm.233799.

Genome annotation databases

EnsembliENSMUST00000017637; ENSMUSP00000017637; ENSMUSG00000017493.
GeneIDi16010.
KEGGimmu:16010.
UCSCiuc007lie.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81582 mRNA. Translation: CAA57272.1.
X76066 Genomic DNA. Translation: CAA53667.1.
AK150229 mRNA. Translation: BAE29395.1.
AK165688 mRNA. Translation: BAE38340.1.
BC019836 mRNA. Translation: AAH19836.1.
Z95492 Genomic DNA. Translation: CAB08859.1.
CCDSiCCDS25371.1.
PIRiI48599.
I48603.
RefSeqiNP_034647.1. NM_010517.3.
UniGeneiMm.233799.

3D structure databases

ProteinModelPortaliP47879.
SMRiP47879. Positions 24-103, 168-246.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60633N.
STRINGi10090.ENSMUSP00000017637.

Protein family/group databases

MEROPSiI31.952.

PTM databases

PhosphoSiteiP47879.

Proteomic databases

MaxQBiP47879.
PaxDbiP47879.
PRIDEiP47879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017637; ENSMUSP00000017637; ENSMUSG00000017493.
GeneIDi16010.
KEGGimmu:16010.
UCSCiuc007lie.1. mouse.

Organism-specific databases

CTDi3487.
MGIiMGI:96439. Igfbp4.

Phylogenomic databases

eggNOGiNOG46496.
GeneTreeiENSGT00550000074457.
HOGENOMiHOG000253012.
HOVERGENiHBG002631.
InParanoidiP47879.
OMAiAIQCPPC.
OrthoDBiEOG74N5HG.
PhylomeDBiP47879.
TreeFamiTF331211.

Enzyme and pathway databases

ReactomeiREACT_235886. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).

Miscellaneous databases

NextBioi288822.
PMAP-CutDBP47879.
PROiP47879.
SOURCEiSearch...

Gene expression databases

BgeeiP47879.
CleanExiMM_IGFBP4.
ExpressionAtlasiP47879. baseline and differential.
GenevestigatoriP47879.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and mRNA expression of the six mouse insulin-like growth factor binding proteins."
    Schuller A.G.P., Groffen C., van Neck J.W., Zwarthoff E.C., Drop S.L.S.
    Mol. Cell. Endocrinol. 104:57-66(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  2. "Molecular cloning of mouse insulin-like growth factor binding protein 4 (IGFBP4) cDNA and expression of a fusion protein with IGF-binding activity."
    Bethel C.R., Vitullo J.C., Miller R.E., Aron D.C.
    Biochem. Mol. Biol. Int. 34:385-392(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Bone marrow.
  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].
    Strain: FVB/N.
    Tissue: Liver.
  5. "Characterization of the mouse insulin-like growth factor binding protein 4 gene regulatory region and expression studies."
    Glantschnig H., Varga F., Luegmayr E., Klaushofer K.
    DNA Cell Biol. 17:51-60(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-114.
    Strain: BALB/c.
    Tissue: Brain.

Entry informationi

Entry nameiIBP4_MOUSE
AccessioniPrimary (citable) accession number: P47879
Secondary accession number(s): O35666, Q3TMV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 15, 1998
Last modified: February 4, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.