SLC28A2

From Wikipedia, the free encyclopedia

Solute carrier family 28 (sodium-coupled nucleoside transporter), member 2

Identifiers

SLC28A2; CNT2; HCNT2; HsT17153; MGC138252; SPNT1

External IDs

OMIM: 606208 MGI: 1913105 HomoloGene: 20891

Gene ontology
Molecular Function:	• nucleoside binding • nucleoside:sodium symporter activity • purine nucleoside transmembrane transporter activity
Cellular Component:	• membrane fraction • integral to plasma membrane • membrane
Biological Process:	• nucleobase, nucleoside, nucleotide and nucleic acid metabolic process • transport • purine nucleoside transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_004212 (mRNA)
NP_004203 (protein)

XM_988760 (mRNA)
XP_993854 (protein)

Location

Chr 15: 43.33 - 43.36 Mb

n/a

Pubmed search

[1]

[2]

Solute carrier family 28 (sodium-coupled nucleoside transporter), member 2, also known as SLC28A2, is a human gene.^[1]

[edit] See also

Solute carrier family

[edit] References

^ Entrez Gene: SLC28A2 solute carrier family 28 (sodium-coupled nucleoside transporter), member 2.

[edit] Further reading

Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides.". Gene 138 (1-2): 171–4. PMID 8125298.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library.". Gene 200 (1-2): 149–56. PMID 9373149.
Wang J, Su SF, Dresser MJ, et al. (1998). "Na(+)-dependent purine nucleoside transporter from human kidney: cloning and functional characterization.". Am. J. Physiol. 273 (6 Pt 2): F1058–65. PMID 9435697.
Ritzel MW, Yao SY, Ng AM, et al. (1999). "Molecular cloning, functional expression and chromosomal localization of a cDNA encoding a human Na+/nucleoside cotransporter (hCNT2) selective for purine nucleosides and uridine.". Mol. Membr. Biol. 15 (4): 203–11. PMID 10087507.
Loewen SK, Ng AM, Yao SY, et al. (1999). "Identification of amino acid residues responsible for the pyrimidine and purine nucleoside specificities of human concentrative Na(+) nucleoside cotransporters hCNT1 and hCNT2.". J. Biol. Chem. 274 (35): 24475–84. PMID 10455109.
Pennycooke M, Chaudary N, Shuralyova I, et al. (2001). "Differential expression of human nucleoside transporters in normal and tumor tissue.". Biochem. Biophys. Res. Commun. 280 (3): 951–9. doi:10.1006/bbrc.2000.4205. PMID 11162617.
Li JY, Boado RJ, Pardridge WM (2001). "Differential kinetics of transport of 2',3'-dideoxyinosine and adenosine via concentrative Na+ nucleoside transporter CNT2 cloned from rat blood-brain barrier.". J. Pharmacol. Exp. Ther. 299 (2): 735–40. PMID 11602688.
Gerstin KM, Dresser MJ, Giacomini KM (2002). "Specificity of human and rat orthologs of the concentrative nucleoside transporter, SPNT.". Am. J. Physiol. Renal Physiol. 283 (2): F344–9. doi:10.1152/ajprenal.00274.2001. PMID 12110519.
Molina-Arcas M, Bellosillo B, Casado FJ, et al. (2003). "Fludarabine uptake mechanisms in B-cell chronic lymphocytic leukemia.". Blood 101 (6): 2328–34. doi:10.1182/blood-2002-07-2236. PMID 12411296.
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.
Shin HC, Landowski CP, Sun D, et al. (2003). "Functional expression and characterization of a sodium-dependent nucleoside transporter hCNT2 cloned from human duodenum.". Biochem. Biophys. Res. Commun. 307 (3): 696–703. PMID 12893280.
Lang TT, Young JD, Cass CE (2004). "Interactions of nucleoside analogs, caffeine, and nicotine with human concentrative nucleoside transporters 1 and 2 stably produced in a transport-defective human cell line.". Mol. Pharmacol. 65 (4): 925–33. doi:10.1124/mol.65.4.925. PMID 15044622.
Damaraju VL, Visser F, Zhang J, et al. (2005). "Role of human nucleoside transporters in the cellular uptake of two inhibitors of IMP dehydrogenase, tiazofurin and benzamide riboside.". Mol. Pharmacol. 67 (1): 273–9. doi:10.1124/mol.104.004408. PMID 15486050.
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.
Owen RP, Gray JH, Taylor TR, et al. (2005). "Genetic analysis and functional characterization of polymorphisms in the human concentrative nucleoside transporter, CNT2.". Pharmacogenet. Genomics 15 (2): 83–90. PMID 15861032.
Owen RP, Badagnani I, Giacomini KM (2006). "Molecular determinants of specificity for synthetic nucleoside analogs in the concentrative nucleoside transporter, CNT2.". J. Biol. Chem. 281 (36): 26675–82. doi:10.1074/jbc.M513421200. PMID 16840788.
Fernández-Veledo S, Jover R, Casado FJ, et al. (2007). "Transcription factors involved in the expression of SLC28 genes in human liver parenchymal cells.". Biochem. Biophys. Res. Commun. 353 (2): 381–8. doi:10.1016/j.bbrc.2006.12.021. PMID 17187757.
Smith KM, Slugoski MD, Cass CE, et al. (2007). "Cation coupling properties of human concentrative nucleoside transporters hCNT1, hCNT2 and hCNT3.". Mol. Membr. Biol. 24 (1): 53–64. doi:10.1080/09687860600942534. PMID 17453413.
Hirsh AJ, Stonebraker JR, van Heusden CA, et al. (2007). "Adenosine deaminase 1 and concentrative nucleoside transporters 2 and 3 regulate adenosine on the apical surface of human airway epithelia: implications for inflammatory lung diseases.". Biochemistry 46 (36): 10373–83. doi:10.1021/bi7009647. PMID 17696452.
Li L, Tan CM, Koo SH, et al. (2007). "Identification and functional analysis of variants in the human concentrative nucleoside transporter 2, hCNT2 (SLC28A2) in Chinese, Malays and Indians.". Pharmacogenet. Genomics 17 (9): 783–6. doi:10.1097/FPC.0b013e3281c10e41. PMID 17700367.

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v • d • e Membrane proteins, carrier proteins: membrane transport proteins

ABC-transporter	A1, A2, A3, A4, A7, A8, A12, B1 B2-3, B2, B3, B4, B5, B6, B7, B9, B11 C1, C2, C3, C4, C5, C6, C8, C8-9, C10, C13, C11 D1, D2, D3, D4, E1, F1, F2 G1, G2, G4, Sterolin (G5, G8)

Solute carrier	1A1-7, 1A1, 1A2, 1A3, 1A4, 1A5, 2A1, 2A2, 2A3, 2A4, 2A5, 2A6, 2A8, 2A9, 2A10, 2A12, 3A1, 3A2, 4A1, 4A2, 4A3, 4A4, 4A5, 4A7, 4A8, 4A11, 5A1-2, 5A1, 5A3, 5A5, 5A8, 6A1, 6A2, 6A3, 6A4, 6A5, 6A8, 6A9, 6A19, 7A1, 7A2, 7A3, 7A4, 7A5, 7A7, 7A8, 7A9, 7A11, 8A1-3, 9A1, 9A2, 9A3, 9A3R1, 9A3R2, 9A5, 9A6, 9A8, 10A1, 10A2, 10A3, 10A7, 11A1, 11A2, 11A3, 12A1-2, 12A3, 12A4, 12A5, 12A6, 12A7, 14A1, 13A3, 14A2, 15A1, 15A2, 16A1, 16A2, 16A3, 16A4, 17A1, 17A5, 17A6-8, 17A7, 18A1, 18A2, 18A3, 19A1, 19A2, 19A3, 20A1, 20A2, 22A1, 22A2, 22A3, 22A4, 22A5, 22A6, 22A7, 22A9, 22A11, 22A12, 22A18, 23A1, 23A2, 24A1-2, 24A5, 25A1, 25A3, 25A4, 25A4-6, 25A8, 25A10, 25A11, 25A12, 25A13, 25A14, 25A15, 25A17, 25A19, 25A20, 25A27, 25A31, 25A37, 25A39, 26A2, 26A3, 26A4, 26A5, 26A6, 26A7, 26A8, 27A1, 27A2, 27A3, 27A4, 28A1, 28A2, 29A1, 29A2, 29A4, 30A4, 30A7, 30A8, 31A1, 31A2, 32A1, 34A1, 34A2, 34A3, 35A1, 35A2, 35B2, 35B4, 35C1, 36A1, 37A4, 38A2, 38A3, 39A1, 39A2, 39A3, 39A4, 39A6, 39A7, 40A1, 43A1 44A1, 44A2, 44A4, 45A2, O1A2, O1B1, O1B3, O2B1, O431, O4A1

Monosaccharide	GLUT1, GLUT2, GLUT3, GLUT4, GLUT5, GLUT6, GLUT8, GLUT9

Other	Amino acid (CD98) - Fatty acid (CD36) - Ion channels - Ion pumps - Mitochondrial membrane transport protein - Neurotransmitter transport proteins - Nuclear (Importin, Karyopherin)