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TIMP4

From Wikipedia, the free encyclopedia
Protein-coding gene in the species Homo sapiens

TIMP4
Identifiers
AliasesTIMP4, TIMP metallopeptidase inhibitor 4, TIMP-4
External IDsOMIM:601915;MGI:109125;HomoloGene:37748;GeneCards:TIMP4;OMA:TIMP4 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for TIMP4
Genomic location for TIMP4
Band3p25.2Start12,153,068bp[1]
End12,158,912bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for TIMP4
Genomic location for TIMP4
Band6 E3|6 53.29 cMStart115,218,853bp[2]
End115,229,166bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • abdominal fat

  • subcutaneous adipose tissue

  • thoracic aorta

  • left coronary artery

  • ascending aorta

  • apex of heart

  • synovial joint

  • right hemisphere of cerebellum

  • Descending thoracic aorta

  • popliteal artery
Top expressed in
  • interventricular septum

  • white adipose tissue

  • lobe of cerebellum

  • cerebellar vermis

  • lumbar subsegment of spinal cord

  • motor neuron

  • deep cerebellar nuclei

  • tunica media of zone of aorta

  • substantia nigra

  • brown adipose tissue
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

7079

110595

Ensembl

ENSG00000157150

ENSMUSG00000030317

UniProt

Q99727

Q9JHB3

RefSeq (mRNA)

NM_003256

NM_080639
NM_001356406

RefSeq (protein)

NP_003247

NP_542370
NP_001343335

Location (UCSC)Chr 3: 12.15 – 12.16 MbChr 6: 115.22 – 115.23 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Metalloproteinase inhibitor 4 is anenzyme that in humans is encoded by theTIMP4gene.[5][6][7]

This gene belongs to thetissue inhibitor of metalloproteinases gene family. The proteins encoded by this gene family are inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. The secreted, netrin domain-containing protein encoded by this gene is involved in regulation of platelet aggregation and recruitment and may play role in hormonal regulation and endometrial tissue remodeling.[7]

Interactions

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TIMP4 has been shown tointeract withMMP2.[8][9]

See also

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References

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  1. ^abcGRCh38: Ensembl release 89: ENSG00000157150Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000030317Ensembl, May 2017
  3. ^"Human PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^"Mouse PubMed Reference:".National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^Greene J, Wang M, Liu YE, Raymond LA, Rosen C, Shi YE (Jan 1997)."Molecular cloning and characterization of human tissue inhibitor of metalloproteinase 4".J Biol Chem.271 (48):30375–30380.doi:10.1074/jbc.271.48.30375.PMID 8939999.
  6. ^Olson TM, Hirohata S, Ye J, Leco K, Seldin MF, Apte SS (Sep 1998). "Cloning of the human tissue inhibitor of metalloproteinase-4 gene (TIMP4) and localization of the TIMP4 and Timp4 genes to human chromosome 3p25 and mouse chromosome 6, respectively".Genomics.51 (1):148–151.doi:10.1006/geno.1998.5362.PMID 9693046.
  7. ^ab"Entrez Gene: TIMP4 TIMP metallopeptidase inhibitor 4".
  8. ^Bigg HF, Shi Y E, Liu Y E, Steffensen B, Overall C M (Jun 1997)."Specific, high affinity binding of tissue inhibitor of metalloproteinases-4 (TIMP-4) to the COOH-terminal hemopexin-like domain of human gelatinase A. TIMP-4 binds progelatinase A and the COOH-terminal domain in a similar manner to TIMP-2".J. Biol. Chem.272 (24):15496–15500.doi:10.1074/jbc.272.24.15496.ISSN 0021-9258.PMID 9182583.
  9. ^Kai HS, Butler Georgina S, Morrison Charlotte J, King Angela E, Pelman Gayle R, Overall Christopher M (Dec 2002)."Utilization of a novel recombinant myoglobin fusion protein expression system to characterize the tissue inhibitor of metalloproteinase (TIMP)-4 and TIMP-2 C-terminal domain and tails by mutagenesis. The importance of acidic residues in binding the MMP-2 hemopexin C-domain".J. Biol. Chem.277 (50):48696–48707.doi:10.1074/jbc.M209177200.ISSN 0021-9258.PMID 12374789.

Further reading

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External links

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  • TheMEROPS online database for peptidases and their inhibitors:I35.004
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