Fnta (farnesyltransferase, CAAX box, subunit alpha) - Rat Genome Database

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Gene: Fnta (farnesyltransferase, CAAX box, subunit alpha) Rattus norvegicus
Analyze
Symbol: Fnta
Name: farnesyltransferase, CAAX box, subunit alpha (Ensembl:farnesyltransferase, CAAX box, alpha)
RGD ID: 2625
Description: Contributes to several functions, including peptide binding activity; protein prenyltransferase activity; and zinc ion binding activity. Involved in several processes, including negative regulation of apoptotic process; positive regulation of cell population proliferation; and regulation of nitric-oxide synthase biosynthetic process. Part of CAAX-protein geranylgeranyltransferase complex. Orthologous to human FNTA (farnesyltransferase, CAAX box, subunit alpha); INTERACTS WITH (+)-schisandrin B; (S)-(-)-perillyl alcohol; 2,4-dinitrotoluene.
Type: protein-coding
RefSeq Status: PROVISIONAL
Previously known as: CAAX farnesyltransferase subunit alpha; Farnesyltransferase subunit alpha; farnesyltransferase, CAAX box, alpha; Farnesyltransferase, subunit alpha; FTase-alpha; GGTase-I-alpha; PFAS; protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha; ras proteins prenyltransferase subunit alpha; type I protein geranyl-geranyltransferase subunit alpha
RGD Orthologs
Human
Mouse
Chinchilla
Bonobo
Dog
Squirrel
Pig
Green Monkey
Alliance Orthologs
More Info more info ...
Latest Assembly: mRatBN7.2 - mRatBN7.2 Assembly
Position:
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr81672,767,864 - 72,786,193 (+)NCBIGRCr8
mRatBN7.21666,065,131 - 66,083,460 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl1666,065,132 - 66,083,460 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx1671,343,827 - 71,362,199 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.01674,750,156 - 74,768,528 (+)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.01669,990,195 - 70,008,625 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.01670,834,957 - 70,854,724 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl1670,834,957 - 70,854,724 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.01670,499,605 - 70,519,062 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.41670,440,340 - 70,458,433 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.11670,440,604 - 70,458,698 (+)NCBI
Celera1663,976,260 - 63,994,463 (+)NCBICelera
RH 3.4 Map16622.7RGD
Cytogenetic Map16q12.4NCBI
JBrowse: View Region in Genome Browser (JBrowse)
Model


Gene-Chemical Interaction Annotations     Click to see Annotation Detail View
Gene Ontology Annotations     Click to see Annotation Detail View

Cellular Component

References

References - curated
# Reference Title Reference Citation
1. Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase. Chen WJ, etal., Proc Natl Acad Sci U S A 1991 Dec 15;88(24):11368-72.
2. Novel and selective imidazole-containing biphenyl inhibitors of protein farnesyltransferase. Curtin ML, etal., Bioorg Med Chem Lett. 2003 Apr 7;13(7):1367-71.
3. Isothiazole dioxide derivative 6n inhibits vascular smooth muscle cell proliferation and protein farnesylation. Ferri N, etal., Biochem Pharmacol. 2005 Dec 5;70(12):1735-43. Epub 2005 Oct 28.
4. Inhibition of protein geranylgeranylation causes a superinduction of nitric-oxide synthase-2 by interleukin-1beta in vascular smooth muscle cells. Finder JD, etal., J Biol Chem. 1997 May 23;272(21):13484-8.
5. Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Gaudet P, etal., Brief Bioinform. 2011 Sep;12(5):449-62. doi: 10.1093/bib/bbr042. Epub 2011 Aug 27.
6. Rat ISS GO annotations from GOA human gene data--August 2006 GOA data from the GO Consortium
7. Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine, phenylalanine and histidine derivatives. Gwaltney SL 2nd, etal., Bioorg Med Chem Lett. 2003 Apr 7;13(7):1359-62.
8. Aryl tetrahydropyridine inhibitors of farnesyltransferase: bioavailable analogues with improved cellular potency. Gwaltney SL 2nd, etal., Bioorg Med Chem Lett. 2003 Apr 7;13(7):1363-6.
9. Inactivation of farnesyltransferase and geranylgeranyltransferase I by caspase-3: cleavage of the common alpha subunit during apoptosis. Kim KW, etal., Oncogene. 2001 Jan 18;20(3):358-66.
10. High-density rat radiation hybrid maps containing over 24,000 SSLPs, genes, and ESTs provide a direct link to the rat genome sequence. Kwitek AE, etal., Genome Res. 2004 Apr;14(4):750-7
11. Reaction path of protein farnesyltransferase at atomic resolution. Long SB, etal., Nature 2002 Oct 10;419(6907):645-50.
12. The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures. Long SB, etal., Structure. 2000 Feb 15;8(2):209-22.
13. Combination of the novel farnesyltransferase inhibitor RPR130401 and the geranylgeranyltransferase-1 inhibitor GGTI-298 disrupts MAP kinase activation and G(1)-S transition in Ki-Ras-overexpressing transformed adrenocortical cells. Mazet JL, etal., FEBS Lett. 1999 Oct 29;460(2):235-40.
14. Rat ISS GO annotations from MGI mouse gene data--August 2006 MGD data from the GO Consortium
15. Electronic Transfer of LocusLink and RefSeq Data NCBI rat LocusLink and RefSeq merged data July 26, 2002
16. Crystal structure of protein farnesyltransferase at 2.25 angstrom resolution. Park HW, etal., Science. 1997 Mar 21;275(5307):1800-4.
17. Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity. Reid TS and Beese LS, Biochemistry. 2004 Jun 8;43(22):6877-84.
18. Crystallographic analysis reveals that anticancer clinical candidate L-778,123 inhibits protein farnesyltransferase and geranylgeranyltransferase-I by different binding modes. Reid TS, etal., Biochemistry. 2004 Jul 20;43(28):9000-8.
19. Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. Reid TS, etal., J Mol Biol. 2004 Oct 15;343(2):417-33.
20. GOA pipeline RGD automated data pipeline
21. Data Import for Chemical-Gene Interactions RGD automated import pipeline for gene-chemical interactions
22. Role of the carboxyterminal residue in peptide binding to protein farnesyltransferase and protein geranylgeranyltransferase. Roskoski R Jr and Ritchie P, Arch Biochem Biophys. 1998 Aug 15;356(2):167-76.
23. Tricyclic farnesyl protein transferase inhibitors: crystallographic and calorimetric studies of structure-activity relationships. Strickland CL, etal., J Med Chem. 1999 Jun 17;42(12):2125-35.
24. Structure of mammalian protein geranylgeranyltransferase type-I. Taylor JS, etal., EMBO J. 2003 Nov 17;22(22):5963-74.
25. Tentative Sequence Identification Numbers Tentative Sequence Data IDs. TIGR Gene Index, Rat Data
26. Discovery of potent imidazole and cyanophenyl containing farnesyltransferase inhibitors with improved oral bioavailability. Tong Y, etal., Bioorg Med Chem Lett. 2003 May 5;13(9):1571-4.
27. Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase. Turek-Etienne TC, etal., Biochemistry. 2003 Apr 8;42(13):3716-24.
28. Dominant-negative alpha-subunit of farnesyl- and geranyltransferase inhibits glucose-stimulated, but not KCl-stimulated, insulin secretion in INS 832/13 cells. Veluthakal R, etal., Diabetes. 2007 Jan;56(1):204-10.
29. Properties and kinetic mechanism of recombinant mammalian protein geranylgeranyltransferase type I. Zhang FL, etal., J Biol Chem. 1994 Sep 23;269(38):23465-70.
30. TrkB-mediated activation of geranylgeranyltransferase I promotes dendritic morphogenesis. Zhou XP, etal., Proc Natl Acad Sci U S A. 2008 Nov 4;105(44):17181-6. Epub 2008 Oct 28.
Additional References at PubMed
PMID:7673206   PMID:9657673   PMID:9843427   PMID:11687658   PMID:12477932   PMID:14622576   PMID:16893176   PMID:19228685   PMID:23534605   PMID:29282289  


Genomics

Comparative Map Data
Fnta
(Rattus norvegicus - Norway rat)
Rat AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCr81672,767,864 - 72,786,193 (+)NCBIGRCr8
mRatBN7.21666,065,131 - 66,083,460 (+)NCBImRatBN7.2mRatBN7.2
mRatBN7.2 Ensembl1666,065,132 - 66,083,460 (+)EnsemblmRatBN7.2 Ensembl
UTH_Rnor_SHR_Utx1671,343,827 - 71,362,199 (+)NCBIRnor_SHRUTH_Rnor_SHR_Utx
UTH_Rnor_SHRSP_BbbUtx_1.01674,750,156 - 74,768,528 (+)NCBIRnor_SHRSPUTH_Rnor_SHRSP_BbbUtx_1.0
UTH_Rnor_WKY_Bbb_1.01669,990,195 - 70,008,625 (+)NCBIRnor_WKYUTH_Rnor_WKY_Bbb_1.0
Rnor_6.01670,834,957 - 70,854,724 (+)NCBIRnor6.0Rnor_6.0rn6Rnor6.0
Rnor_6.0 Ensembl1670,834,957 - 70,854,724 (+)EnsemblRnor6.0rn6Rnor6.0
Rnor_5.01670,499,605 - 70,519,062 (+)NCBIRnor5.0Rnor_5.0rn5Rnor5.0
RGSC_v3.41670,440,340 - 70,458,433 (+)NCBIRGSC3.4RGSC_v3.4rn4RGSC3.4
RGSC_v3.11670,440,604 - 70,458,698 (+)NCBI
Celera1663,976,260 - 63,994,463 (+)NCBICelera
RH 3.4 Map16622.7RGD
Cytogenetic Map16q12.4NCBI
FNTA
(Homo sapiens - human)
Human AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCh38843,056,323 - 43,085,785 (+)NCBIGRCh38GRCh38hg38GRCh38
GRCh38.p14 Ensembl843,034,194 - 43,085,788 (+)EnsemblGRCh38hg38GRCh38
GRCh37842,911,466 - 42,940,928 (+)NCBIGRCh37GRCh37hg19GRCh37
Build 36843,030,599 - 43,060,088 (+)NCBINCBI36Build 36hg18NCBI36
Build 34843,030,640 - 43,060,080NCBI
Celera841,859,884 - 41,889,630 (+)NCBICelera
Cytogenetic Map8p11.21NCBI
HuRef841,434,064 - 41,463,781 (+)NCBIHuRef
CHM1_1842,958,364 - 42,987,853 (+)NCBICHM1_1
T2T-CHM13v2.0843,325,268 - 43,354,718 (+)NCBIT2T-CHM13v2.0
Fnta
(Mus musculus - house mouse)
Mouse AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
GRCm39826,488,716 - 26,505,638 (-)NCBIGRCm39GRCm39mm39
GRCm39 Ensembl826,488,750 - 26,505,678 (-)EnsemblGRCm39 Ensembl
GRCm38825,998,688 - 26,015,610 (-)NCBIGRCm38GRCm38mm10GRCm38
GRCm38.p6 Ensembl825,998,722 - 26,015,650 (-)EnsemblGRCm38mm10GRCm38
MGSCv37827,109,194 - 27,126,073 (-)NCBIGRCm37MGSCv37mm9NCBIm37
MGSCv36827,464,267 - 27,481,146 (-)NCBIMGSCv36mm8
Celera827,468,460 - 27,485,887 (-)NCBICelera
Cytogenetic Map8A2NCBI
cM Map814.27NCBI
Fnta
(Chinchilla lanigera - long-tailed chinchilla)
Chinchilla AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChiLan1.0 EnsemblNW_00495545713,260,545 - 13,294,025 (+)EnsemblChiLan1.0
ChiLan1.0NW_00495545713,260,825 - 13,294,025 (+)NCBIChiLan1.0ChiLan1.0
FNTA
(Pan paniscus - bonobo/pygmy chimpanzee)
Bonobo AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
NHGRI_mPanPan1-v2761,512,173 - 61,542,875 (+)NCBINHGRI_mPanPan1-v2
NHGRI_mPanPan1837,229,091 - 37,258,862 (+)NCBINHGRI_mPanPan1
Mhudiblu_PPA_v0842,303,987 - 42,333,743 (+)NCBIMhudiblu_PPA_v0Mhudiblu_PPA_v0panPan3
PanPan1.1839,744,142 - 39,774,039 (+)NCBIpanpan1.1PanPan1.1panPan2
PanPan1.1 Ensembl839,743,768 - 39,774,031 (+)Ensemblpanpan1.1panPan2
FNTA
(Canis lupus familiaris - dog)
Dog AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
CanFam3.11622,739,070 - 22,767,942 (-)NCBICanFam3.1CanFam3.1canFam3CanFam3.1
CanFam3.1 Ensembl1622,739,079 - 22,767,914 (-)EnsemblCanFam3.1canFam3CanFam3.1
Dog10K_Boxer_Tasha1623,244,269 - 23,273,147 (-)NCBIDog10K_Boxer_Tasha
ROS_Cfam_1.01624,491,021 - 24,519,909 (-)NCBIROS_Cfam_1.0
ROS_Cfam_1.0 Ensembl1624,491,022 - 24,652,650 (-)EnsemblROS_Cfam_1.0 Ensembl
UMICH_Zoey_3.11622,859,185 - 22,888,061 (-)NCBIUMICH_Zoey_3.1
UNSW_CanFamBas_1.01623,424,042 - 23,452,916 (-)NCBIUNSW_CanFamBas_1.0
UU_Cfam_GSD_1.01623,475,354 - 23,504,242 (-)NCBIUU_Cfam_GSD_1.0
Fnta
(Ictidomys tridecemlineatus - thirteen-lined ground squirrel)
Squirrel AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
HiC_Itri_2NW_02440494345,764,313 - 45,791,302 (-)NCBIHiC_Itri_2
SpeTri2.0NW_004936570362,655 - 389,649 (-)NCBISpeTri2.0SpeTri2.0SpeTri2.0
FNTA
(Sus scrofa - pig)
Pig AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
Sscrofa11.1 Ensembl1711,928,358 - 11,951,684 (+)EnsemblSscrofa11.1susScr11Sscrofa11.1
Sscrofa11.11711,928,327 - 11,953,139 (+)NCBISscrofa11.1Sscrofa11.1susScr11Sscrofa11.1
FNTA
(Chlorocebus sabaeus - green monkey)
Green Monkey AssemblyChrPosition (strand)SourceGenome Browsers
JBrowseNCBIUCSCEnsembl
ChlSab1.1841,057,798 - 41,088,210 (+)NCBIChlSab1.1ChlSab1.1chlSab2
ChlSab1.1 Ensembl841,057,603 - 41,087,705 (+)EnsemblChlSab1.1ChlSab1.1 EnsemblchlSab2
Vero_WHO_p1.0NW_023666052681,570 - 712,699 (-)NCBIVero_WHO_p1.0Vero_WHO_p1.0

Variants

.
Variants in Fnta
75 total Variants
miRNA Target Status

Predicted Target Of
Summary Value
Count of predictions:52
Count of miRNA genes:43
Interacting mature miRNAs:47
Transcripts:ENSRNOT00000019594
Prediction methods:Miranda, Rnahybrid, Targetscan
Result types:miRGate_prediction

The detailed report is available here: Full Report CSV TAB Printer

miRNA Target Status data imported from miRGate (http://mirgate.bioinfo.cnio.es/).
For more information about miRGate, see PMID:25858286 or access the full paper here.


QTLs in Region (mRatBN7.2)
The following QTLs overlap with this region.    Full Report CSV TAB Printer Gviewer
RGD IDSymbolNameLODP ValueTraitSub TraitChrStartStopSpecies
2300163Bmd64Bone mineral density QTL 645.30.0001lumbar vertebra mineral mass (VT:0010511)volumetric bone mineral density (CMO:0001553)163775215682752156Rat
1600378Arunc4Aerobic running capacity QTL 40.03exercise endurance trait (VT:0002332)maximum distance run on treadmill (CMO:0001406)1638024580345693Rat
70215Niddm29Non-insulin dependent diabetes mellitus QTL 293.54blood glucose amount (VT:0000188)blood glucose level area under curve (AUC) (CMO:0000350)161900443575226532Rat
1578768Stresp22Stress response QTL 222.8thymus mass (VT:0004954)thymus wet weight (CMO:0000855)163528887080288870Rat
2302057Pia29Pristane induced arthritis QTL 293.60.001blood autoantibody amount (VT:0003725)serum immunoglobulin M-type rheumatoid factor level relative to an arbitrary reference serum (CMO:0002111)162173597566735975Rat
7205510Activ5Activity QTL 53.780.00028locomotor behavior trait (VT:0001392)number of entries into a discrete space in an experimental apparatus (CMO:0000960)164239634584729064Rat
631525Pia14Pristane induced arthritis QTL 144.4joint integrity trait (VT:0010548)joint inflammation composite score (CMO:0000919)165571108783402471Rat
8694453Bw172Body weight QTL 1728.330.001retroperitoneal fat pad mass (VT:0010430)retroperitoneal fat pad weight to body weight ratio (CMO:0000635)162432551369325513Rat
7411648Foco22Food consumption QTL 22150.001eating behavior trait (VT:0001431)feed conversion ratio (CMO:0001312)165272646484729064Rat
6903294Stl30Serum triglyceride level QTL 302.60.0013blood triglyceride amount (VT:0002644)plasma triglyceride level (CMO:0000548)162515279370152793Rat
2293690Bss45Bone structure and strength QTL 455.130.0001lumbar vertebra morphology trait (VT:0010494)lumbar vertebra cortical cross-sectional area (CMO:0001690)163775215682752156Rat
8694364Abfw7Abdominal fat weight QTL 712.220.001visceral adipose mass (VT:0010063)abdominal fat pad weight to body weight ratio (CMO:0000095)165272646484729064Rat
8694429Bw164Body weight QTL 16450.001body lean mass (VT:0010483)lean tissue morphological measurement (CMO:0002184)165272646484729064Rat
70205Gcr3Gastric cancer resistance QTL 32.3stomach morphology trait (VT:0000470)stomach tumor diameter (CMO:0001889)161769679182635055Rat

Markers in Region
D8Rck2  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.21666,083,188 - 66,083,420 (+)MAPPERmRatBN7.2
Rnor_6.01670,854,453 - 70,854,684NCBIRnor6.0
Rnor_5.01670,518,791 - 70,519,022UniSTSRnor5.0
RGSC_v3.41670,458,162 - 70,458,393UniSTSRGSC3.4
Celera1663,994,192 - 63,994,423UniSTS
Cytogenetic Map16q12.4UniSTS
RH94481  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.21666,083,261 - 66,083,431 (+)MAPPERmRatBN7.2
Rnor_6.01670,854,526 - 70,854,695NCBIRnor6.0
Rnor_5.01670,518,864 - 70,519,033UniSTSRnor5.0
RGSC_v3.41670,458,235 - 70,458,404UniSTSRGSC3.4
Celera1663,994,265 - 63,994,434UniSTS
RH 3.4 Map16622.7UniSTS
Cytogenetic Map16q12.4UniSTS
BI274352  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.21666,083,057 - 66,083,262 (+)MAPPERmRatBN7.2
Rnor_6.01670,854,322 - 70,854,526NCBIRnor6.0
Rnor_5.01670,518,660 - 70,518,864UniSTSRnor5.0
RGSC_v3.41670,458,031 - 70,458,235UniSTSRGSC3.4
Celera1663,994,061 - 63,994,265UniSTS
RH 3.4 Map16620.8UniSTS
Cytogenetic Map16q12.4UniSTS
BI282482  
Rat AssemblyChrPosition (strand)SourceJBrowse
mRatBN7.21666,083,250 - 66,083,402 (+)MAPPERmRatBN7.2
Rnor_6.01670,854,515 - 70,854,666NCBIRnor6.0
Rnor_5.01670,518,853 - 70,519,004UniSTSRnor5.0
RGSC_v3.41670,458,224 - 70,458,375UniSTSRGSC3.4
Celera1663,994,254 - 63,994,405UniSTS
RH 3.4 Map16620.3UniSTS
Cytogenetic Map16q12.4UniSTS


Expression

RNA-SEQ Expression

alimentary part of gastrointestinal system
appendage
circulatory system
ectoderm
endocrine system
endoderm
exocrine system
hemolymphoid system
hepatobiliary system
integumental system
mesenchyme
mesoderm
nervous system
renal system
reproductive system
respiratory system
9 11 49 113 91 90 59 25 59 6 218 97 93 45 60 31

Sequence


Ensembl Acc Id: ENSRNOT00000019594   ⟹   ENSRNOP00000019594
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
mRatBN7.2 Ensembl1666,065,132 - 66,083,460 (+)Ensembl
Rnor_6.0 Ensembl1670,834,957 - 70,854,724 (+)Ensembl
RefSeq Acc Id: NM_012847   ⟹   NP_036979
RefSeq Status: PROVISIONAL
Type: CODING
Position:
Rat AssemblyChrPosition (strand)Source
GRCr81672,767,864 - 72,786,193 (+)NCBI
mRatBN7.21666,065,131 - 66,083,460 (+)NCBI
Rnor_6.01670,834,957 - 70,854,724 (+)NCBI
Rnor_5.01670,499,605 - 70,519,062 (+)NCBI
RGSC_v3.41670,440,340 - 70,458,433 (+)RGD
Celera1663,976,260 - 63,994,463 (+)RGD
Sequence:
Protein Sequences
Protein RefSeqs NP_036979 (Get FASTA)   NCBI Sequence Viewer  
GenBank Protein AAA41833 (Get FASTA)   NCBI Sequence Viewer  
  AAH85758 (Get FASTA)   NCBI Sequence Viewer  
  EDM09075 (Get FASTA)   NCBI Sequence Viewer  
  EDM09076 (Get FASTA)   NCBI Sequence Viewer  
Ensembl Protein ENSRNOP00000019594.2
GenBank Protein Q04631 (Get FASTA)   NCBI Sequence Viewer  
RefSeq Acc Id: NP_036979   ⟸   NM_012847
- UniProtKB: Q04631 (UniProtKB/Swiss-Prot),   Q5RKJ4 (UniProtKB/TrEMBL),   F7FMZ5 (UniProtKB/TrEMBL)
- Sequence:
Ensembl Acc Id: ENSRNOP00000019594   ⟸   ENSRNOT00000019594

Protein Structures
Name Modeler Protein Id AA Range Protein Structure
AF-Q04631-F1-model_v2 AlphaFold Q04631 1-377 view protein structure

Transcriptome

eQTL   View at Phenogen
WGCNA   View at Phenogen
Tissue/Strain Expression   View at Phenogen

Promoters
RGD ID:13700161
Promoter ID:EPDNEW_R10685
Type:multiple initiation site
Name:Fnta_1
Description:farnesyltransferase, CAAX box, alpha
SO ACC ID:SO:0000170
Source:EPDNEW (Eukaryotic Promoter Database, http://epd.vital-it.ch/)
Experiment Methods:Single-end sequencing.
Position:
Rat AssemblyChrPosition (strand)Source
Rnor_6.01670,834,990 - 70,835,050EPDNEW

Additional Information

Database Acc Id Source(s)
AGR Gene RGD:2625 AgrOrtholog
BioCyc Gene G2FUF-10987 BioCyc
Ensembl Genes ENSRNOG00000014462 Ensembl, UniProtKB/TrEMBL
Ensembl Transcript ENSRNOT00000019594.5 UniProtKB/TrEMBL
Gene3D-CATH Protein prenylyltransferase UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
IMAGE_CLONE IMAGE:7189836 IMAGE-MGC_LOAD
InterPro Prenyl_trans_a UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
KEGG Report rno:25318 UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
MGC_CLONE MGC:93617 IMAGE-MGC_LOAD
NCBI Gene 25318 ENTREZGENE
PANTHER PROTEIN FARNESYLTRANSFERASE ALPHA SUBUNIT/RAB GERANYLGERANYL TRANSFERASE ALPHA SUBUNIT UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
  PROTEIN FARNESYLTRANSFERASE/GERANYLGERANYLTRANSFERASE TYPE-1 SUBUNIT ALPHA UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
Pfam PPTA UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
PhenoGen Fnta PhenoGen
PROSITE PFTA UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
RatGTEx ENSRNOG00000014462 RatGTEx
Superfamily-SCOP Protein prenylyltransferase UniProtKB/Swiss-Prot, UniProtKB/TrEMBL
TIGR TC204731
UniProt A6IVZ7_RAT UniProtKB/TrEMBL
  F7FMZ5 ENTREZGENE, UniProtKB/TrEMBL
  FNTA_RAT UniProtKB/Swiss-Prot, ENTREZGENE
  Q5RKJ4 ENTREZGENE, UniProtKB/TrEMBL


Nomenclature History
Date Current Symbol Current Name Previous Symbol Previous Name Description Reference Status
2024-03-29 Fnta  farnesyltransferase, CAAX box, subunit alpha  Fnta  farnesyltransferase, CAAX box, alpha  Nomenclature updated to reflect human and mouse nomenclature 1299863 APPROVED
2002-11-06 Fnta  farnesyltransferase, CAAX box, alpha    Farnesyltransferase, subunit alpha  Name updated 625702 APPROVED
2002-06-10 Fnta  Farnesyltransferase, subunit alpha      Symbol and Name status set to approved 70586 APPROVED

RGD Curation Notes
Note Type Note Reference
gene_drugs inhibitors of farnesyltransferase cause tumour regression in animals and are currently being evaluated in clinical trails for the treatment of human cancer 625725
gene_function catalyzes the formation of thioether linkages between the C1 atom of farnesyl (15-carbon ) isoprenoid lipids and cysteine residues at or near the carboxy-terminus of protein acceptors 625725
gene_protein 377 amino acids 728420