Fnta | ENSRNOG00000014462 | NCBI 25318

Details for: Fnta

Gene ID: 25318

Symbol: Fnta

Ensembl ID: ENSRNOG00000014462

Description: farnesyltransferase, CAAX box, alpha

Associated with

Apoptosis
(R-RNO-109581)
Apoptotic cleavage of cellular proteins
(R-RNO-111465)
Apoptotic execution phase
(R-RNO-75153)
Inactivation, recovery and regulation of the phototransduction cascade
(R-RNO-2514859)
Mapk1/mapk3 signaling
(R-RNO-5684996)
Mapk family signaling cascades
(R-RNO-5683057)
Programmed cell death
(R-RNO-5357801)
Raf/map kinase cascade
(R-RNO-5673001)
Ras processing
(R-RNO-9648002)
Sensory perception
(R-RNO-9709957)
Signal transduction
(R-RNO-162582)
The phototransduction cascade
(R-RNO-2514856)
Visual phototransduction
(R-RNO-2187338)
Alpha-tubulin binding
(GO:0043014)
Caax-protein geranylgeranyltransferase activity
(GO:0004662)
Caax-protein geranylgeranyltransferase complex
(GO:0005953)
Cytoplasm
(GO:0005737)
Enzyme-linked receptor protein signaling pathway
(GO:0007167)
Heterocyclic compound binding
(GO:1901363)
Microtubule associated complex
(GO:0005875)
Microtubule binding
(GO:0008017)
Molecular adaptor activity
(GO:0060090)
Negative regulation of apoptotic process
(GO:0043066)
Negative regulation of nitric-oxide synthase biosynthetic process
(GO:0051771)
Peptide binding
(GO:0042277)
Plasma membrane
(GO:0005886)
Positive regulation of cell cycle
(GO:0045787)
Positive regulation of cell population proliferation
(GO:0008284)
Positive regulation of nitric-oxide synthase biosynthetic process
(GO:0051770)
Positive regulation of rac protein signal transduction
(GO:0035022)
Positive regulation of skeletal muscle acetylcholine-gated channel clustering
(GO:1904395)
Positive regulation of tubulin deacetylation
(GO:0090044)
Protein binding
(GO:0005515)
Protein farnesylation
(GO:0018343)
Protein farnesyltransferase activity
(GO:0004660)
Protein farnesyltransferase complex
(GO:0005965)
Protein geranylgeranylation
(GO:0018344)
Protein geranylgeranyltransferase activity
(GO:0004661)
Rab geranylgeranyltransferase activity
(GO:0004663)
Receptor tyrosine kinase binding
(GO:0030971)
Response to cytokine
(GO:0034097)
Response to inorganic substance
(GO:0010035)
Response to organic cyclic compound
(GO:0014070)
Skeletal muscle acetylcholine-gated channel clustering
(GO:0071340)
Small molecule binding
(GO:0036094)
Zinc ion binding
(GO:0008270)

Other Information

Proteins

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
F7FMZ5_RAT

Genular Protein ID: 4093042105

Symbol: FNTA_RAT

Name: Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

UniProtKB Accession Codes:

Q04631

Database IDs:

Citations:

PubMed ID: 1763049

Title: Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase.

PubMed ID: 1763049

DOI: 10.1073/pnas.88.24.11368

PubMed ID: 9065406

Title: Crystal structure of protein farnesyltransferase at 2.25-A resolution.

PubMed ID: 9065406

DOI: 10.1126/science.275.5307.1800

PubMed ID: 9609683

Title: Protein farnesyltransferase: structure and implications for substrate binding.

PubMed ID: 9609683

DOI: 10.1021/bi980531o

PubMed ID: 9657673

Title: Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate.

PubMed ID: 9657673

DOI: 10.1021/bi980708e

PubMed ID: 9843427

Title: Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue.

PubMed ID: 9843427

DOI: 10.1021/bi981197z

PubMed ID: 10377218

Title: Tricyclic farnesyl protein transferase inhibitors: crystallographic and calorimetric studies of structure-activity relationships.

PubMed ID: 10377218

DOI: 10.1021/jm990030g

PubMed ID: 10673434

Title: The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures.

PubMed ID: 10673434

DOI: 10.1016/s0969-2126(00)00096-4

PubMed ID: 11687658

Title: The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.

PubMed ID: 11687658

DOI: 10.1073/pnas.241407898

PubMed ID: 12374986

Title: Reaction path of protein farnesyltransferase at atomic resolution.

PubMed ID: 12374986

DOI: 10.1038/nature00986

PubMed ID: 12667062

Title: Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase.

PubMed ID: 12667062

DOI: 10.1021/bi0266838

PubMed ID: 12657282

Title: Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine, phenylalanine and histidine derivatives.

PubMed ID: 12657282

DOI: 10.1016/s0960-894x(03)00095-7

PubMed ID: 14609943

Title: Structure of mammalian protein geranylgeranyltransferase type-I.

PubMed ID: 14609943

DOI: 10.1093/emboj/cdg571

PubMed ID: 15170324

Title: Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity.

PubMed ID: 15170324

DOI: 10.1021/bi049723b

PubMed ID: 15451670

Title: Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.

PubMed ID: 15451670

DOI: 10.1016/j.jmb.2004.08.056

PubMed ID: 18844669

Title: Caged protein prenyltransferase substrates: tools for understanding protein prenylation.

PubMed ID: 18844669

DOI: 10.1111/j.1747-0285.2008.00698.x

PubMed ID: 19219049

Title: Analysis of the eukaryotic prenylome by isoprenoid affinity tagging.

PubMed ID: 19219049

DOI: 10.1038/nchembio.149

PubMed ID: 22963166

Title: Development of selective, potent RabGGTase inhibitors.

PubMed ID: 22963166

DOI: 10.1021/jm300624s

Sequence Information:

Length: 377
Mass: 44049
Checksum: DFFFECC1B88BC080
Sequence:

MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP MDDGFLSLDS 
PTYVLYRDRA EWADIDPVPQ NDGPSPVVQI IYSEKFRDVY DYFRAVLQRD ERSERAFKLT 
RDAIELNAAN YTVWHFRRVL LRSLQKDLQE EMNYIIAIIE EQPKNYQVWH HRRVLVEWLK 
DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR 
HFVISNTTGY SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL 
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG 
RSLQSKHSRE SDIPASV

Genular Protein ID: 391800078

Symbol: F7FMZ5_RAT

Name: N/A

UniProtKB Accession Codes:

F7FMZ5

Database IDs:

Citations:

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 15632090

Title: Gene and alternative splicing annotation with AIR.

PubMed ID: 15632090

DOI: 10.1101/gr.2889405

Sequence Information:

Length: 377
Mass: 44037
Checksum: C7A8F9B0EF99ED6E
Sequence:

MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP MDDGFLSLDS 
PTYVLYRDRA EWADIDPVPQ NDGPSPVVQI IYSEKFRDVY DYFRAVLQRD ERSERAFKLT 
RDAIELNAAN YTVWHFRRVL LRSLQKDLQE EMNYITAIIE EQPKNYQVWH HRRVLVEWLK 
DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR 
HFVISNTTGY SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL 
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG 
RSLQSKHSRE SDIPASV

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Fnta

Associated with

Other Information

Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase. PubMed ID: 1763049

Crystal structure of protein farnesyltransferase at 2.25-A resolution. PubMed ID: 9065406

Protein farnesyltransferase: structure and implications for substrate binding. PubMed ID: 9609683

Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate. PubMed ID: 9657673

Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue. PubMed ID: 9843427

Tricyclic farnesyl protein transferase inhibitors: crystallographic and calorimetric studies of structure-activity relationships. PubMed ID: 10377218

The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures. PubMed ID: 10673434

The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics. PubMed ID: 11687658

Reaction path of protein farnesyltransferase at atomic resolution. PubMed ID: 12374986

Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase. PubMed ID: 12667062

Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine, phenylalanine and histidine derivatives. PubMed ID: 12657282

Structure of mammalian protein geranylgeranyltransferase type-I. PubMed ID: 14609943

Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity. PubMed ID: 15170324

Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. PubMed ID: 15451670

Caged protein prenyltransferase substrates: tools for understanding protein prenylation. PubMed ID: 18844669

Analysis of the eukaryotic prenylome by isoprenoid affinity tagging. PubMed ID: 19219049

Development of selective, potent RabGGTase inhibitors. PubMed ID: 22963166

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Gene and alternative splicing annotation with AIR. PubMed ID: 15632090