NKTR

Protein-coding gene in the species Homo sapiens
NKTR
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2HE9

Identifiers
AliasesNKTR, p104, natural killer cell triggering receptor
External IDsOMIM: 161565; MGI: 97346; HomoloGene: 122148; GeneCards: NKTR; OMA:NKTR - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for NKTR
Genomic location for NKTR
Band3p22.1Start42,600,655 bp[1]
End42,648,735 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for NKTR
Genomic location for NKTR
Band9 F4|9 72.57 cMStart121,719,169 bp[2]
End121,756,843 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pylorus

  • cardia

  • caput epididymis

  • tail of epididymis

  • optic nerve

  • Achilles tendon

  • corpus epididymis

  • superior surface of tongue

  • visceral pleura

  • corpus callosum
Top expressed in
  • ascending aorta

  • neural layer of retina

  • aortic valve

  • tail of embryo

  • genital tubercle

  • cerebellar cortex

  • dorsomedial hypothalamic nucleus

  • Rostral migratory stream

  • habenula

  • superior frontal gyrus
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • isomerase activity
  • peptidyl-prolyl cis-trans isomerase activity
  • cyclosporin A binding
  • unfolded protein binding
Cellular component
  • membrane
  • nucleoplasm
  • mitochondrion
  • cytosol
  • plasma membrane
  • nucleus
Biological process
  • protein folding
  • protein peptidyl-prolyl isomerization
  • protein refolding
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4820

18087

Ensembl

ENSG00000114857

ENSMUSG00000032525

UniProt

P30414

P30415

RefSeq (mRNA)

NM_001012651
NM_005385
NM_001349124
NM_001349125
NM_001349126

NM_010918

RefSeq (protein)

NP_005376
NP_001336053
NP_001336054
NP_001336055

NP_035048

Location (UCSC)Chr 3: 42.6 – 42.65 MbChr 9: 121.72 – 121.76 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

NK-tumor recognition protein is a protein that in humans is encoded by the NKTR gene.[5][6][7]

This gene encodes a membrane-anchored protein with a hydrophobic amino terminal domain and a cyclophilin-like PPIase domain. It is present on the surface of natural killer cells and facilitates their binding to targets. Its expression is regulated by IL2 activation of the cells.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000114857 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000032525 – Ensembl, 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. ^ Young HA, Jenkins NA, Copeland NG, Simek S, Lerman MI, Zbar B, Glenn G, Ortaldo JR, Anderson SK (Jul 1993). "Localization of a novel natural killer triggering receptor locus to human chromosome 3p23-p21 and mouse chromosome 9". Genomics. 16 (2): 548–549. doi:10.1006/geno.1993.1229. PMID 8314596.
  6. ^ Chambers CA, Gallinger S, Anderson SK, Giardina S, Ortaldo JR, Hozumi N, Roder J (May 1994). "Expression of the NK-TR gene is required for NK-like activity in human T cells". J Immunol. 152 (6): 2669–74. doi:10.4049/jimmunol.152.6.2669. PMID 8144875. S2CID 20265645.
  7. ^ a b "Entrez Gene: NKTR natural killer-tumor recognition sequence".

Further reading

  • Frey JL, Bino T, Kantor RR, et al. (1992). "Mechanism of target cell recognition by natural killer cells: characterization of a novel triggering molecule restricted to CD3- large granular lymphocytes". J. Exp. Med. 174 (6): 1527–1536. doi:10.1084/jem.174.6.1527. PMC 2119033. PMID 1720812.
  • Rinfret A, Anderson SK (1993). "IL-2 regulates the expression of the NK-TR gene via an alternate RNA splicing mechanism". Mol. Immunol. 30 (14): 1307–1313. doi:10.1016/0161-5890(93)90047-F. PMID 8413330.
  • Anderson SK, Gallinger S, Roder J, et al. (1993). "A cyclophilin-related protein involved in the function of natural killer cells". Proc. Natl. Acad. Sci. U.S.A. 90 (2): 542–546. Bibcode:1993PNAS...90..542A. doi:10.1073/pnas.90.2.542. PMC 45699. PMID 8421688.
  • 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): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.
  • Sakashita E, Tatsumi S, Werner D, et al. (2004). "Human RNPS1 and its associated factors: a versatile alternative pre-mRNA splicing regulator in vivo". Mol. Cell. Biol. 24 (3): 1174–1187. doi:10.1128/MCB.24.3.1174-1187.2004. PMC 321435. PMID 14729963.
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.
  • Davis TL, Walker JR, Campagna-Slater V, et al. (2010). "Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases". PLOS Biol. 8 (7): e1000439. doi:10.1371/journal.pbio.1000439. PMC 2911226. PMID 20676357.
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  • 2he9: Structure of the peptidylprolyl isomerase domain of the human NK-tumour recognition protein
    2he9: Structure of the peptidylprolyl isomerase domain of the human NK-tumour recognition protein


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