GLTP

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Glycolipid transfer protein
PDB rendering based on 1swx.
Available structures: 1swx, 1sx6, 1tfj, 1wbe, 2bv7, 2euk, 2eum, 2evd, 2evl, 2evs, 2evt
Identifiers
Symbol(s) GLTP;
External IDs OMIM: 608949 MGI: 1929253 HomoloGene: 41133
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 51228 56356
Ensembl ENSG00000139433 ENSMUSG00000011884
Uniprot Q9NZD2 Q3U011
Refseq NM_016433 (mRNA)
NP_057517 (protein)		 NM_019821 (mRNA)
NP_062795 (protein)
Location Chr 12: 108.77 - 108.8 Mb Chr 5: 114.93 - 114.95 Mb
Pubmed search [1] [2]

Glycolipid transfer protein, also known as GLTP, is a human gene.[1]

The protein encoded by this gene is similar to bovine and porcine proteins which accelerate transfer of certain glycosphingolipids and glyceroglycolipids between membranes. It is thought to be a cytoplasmic protein.[1]

[edit] References

  1. ^ a b Entrez Gene: GLTP glycolipid transfer protein.

[edit] Further reading

  • Brown RE, Mattjus P (2007). "Glycolipid transfer proteins.". Biochim. Biophys. Acta 1771 (6): 746-60. doi:10.1016/j.bbalip.2007.01.011. PMID 17320476. 
  • Abe A (1990). "Primary structure of glycolipid transfer protein from pig brain.". J. Biol. Chem. 265 (17): 9634-7. PMID 2190982. 
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791-806. PMID 8889548. 
  • Mattjus P, Pike HM, Molotkovsky JG, Brown RE (2000). "Charged membrane surfaces impede the protein-mediated transfer of glycosphingolipids between phospholipid bilayers.". Biochemistry 39 (5): 1067-75. PMID 10653652. 
  • Lin X, Mattjus P, Pike HM, et al. (2000). "Cloning and expression of glycolipid transfer protein from bovine and porcine brain.". J. Biol. Chem. 275 (7): 5104-10. PMID 10671554. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899-903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Li XM, Malakhova ML, Lin X, et al. (2004). "Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy.". Biochemistry 43 (31): 10285-94. doi:10.1021/bi0495432. PMID 15287756. 
  • Malinina L, Malakhova ML, Teplov A, et al. (2004). "Structural basis for glycosphingolipid transfer specificity.". Nature 430 (7003): 1048-53. doi:10.1038/nature02856. PMID 15329726. 
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121-7. doi:10.1101/gr.2596504. PMID 15489334. 
  • Rao CS, Lin X, Pike HM, et al. (2004). "Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses.". Biochemistry 43 (43): 13805-15. doi:10.1021/bi0492197. PMID 15504043. 
  • Malakhova ML, Malinina L, Pike HM, et al. (2005). "Point mutational analysis of the liganding site in human glycolipid transfer protein. Functionality of the complex.". J. Biol. Chem. 280 (28): 26312-20. doi:10.1074/jbc.M500481200. PMID 15901739. 
  • Rao CS, Chung T, Pike HM, Brown RE (2006). "Glycolipid transfer protein interaction with bilayer vesicles: modulation by changing lipid composition.". Biophys. J. 89 (6): 4017-28. doi:10.1529/biophysj.105.070631. PMID 16169991. 
  • Malinina L, Malakhova ML, Kanack AT, et al. (2006). "The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.". PLoS Biol. 4 (11): e362. doi:10.1371/journal.pbio.0040362. PMID 17105344. 
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