Fntb | ENSRNOG00000007660 | NCBI 64511

Details for: Fntb

Gene ID: 64511

Symbol: Fntb

Ensembl ID: ENSRNOG00000007660

Description: farnesyltransferase, CAAX box, beta

Associated with

Inactivation, recovery and regulation of the phototransduction cascade
(R-RNO-2514859)
Mapk1/mapk3 signaling
(R-RNO-5684996)
Mapk family signaling cascades
(R-RNO-5683057)
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)
Cell population proliferation
(GO:0008283)
Farnesyltranstransferase activity
(GO:0004311)
Fibroblast proliferation
(GO:0048144)
Lipid metabolic process
(GO:0006629)
Microtubule associated complex
(GO:0005875)
Negative regulation of cell population proliferation
(GO:0008285)
Peptide binding
(GO:0042277)
Positive regulation of cell cycle
(GO:0045787)
Positive regulation of cell population proliferation
(GO:0008284)
Positive regulation of dna-templated transcription
(GO:0045893)
Positive regulation of fibroblast proliferation
(GO:0048146)
Positive regulation of nitric-oxide synthase biosynthetic process
(GO:0051770)
Prenylation
(GO:0097354)
Protein binding
(GO:0005515)
Protein farnesylation
(GO:0018343)
Protein farnesyltransferase activity
(GO:0004660)
Protein farnesyltransferase complex
(GO:0005965)
Regulation of fibroblast proliferation
(GO:0048145)
Response to cytokine
(GO:0034097)
Response to inorganic substance
(GO:0010035)
Response to organic cyclic compound
(GO:0014070)
Wound healing
(GO:0042060)
Zinc ion binding
(GO:0008270)

Other Information

Proteins

Protein farnesyltransferase subunit beta

Genular Protein ID: 699852996

Symbol: FNTB_RAT

Name: Protein farnesyltransferase subunit beta

UniProtKB Accession Codes:

Q02293

Database IDs:

Citations:

PubMed ID: 1855253

Title: cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1.

PubMed ID: 1855253

DOI: 10.1016/0092-8674(91)90622-6

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: 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: 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: 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: 19246009

Title: Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase.

PubMed ID: 19246009

DOI: 10.1016/j.chembiol.2009.01.014

PubMed ID: 19219049

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

PubMed ID: 19219049

DOI: 10.1038/nchembio.149

PubMed ID: 20056542

Title: Discovery of C-imidazole azaheptapyridine FPT inhibitors.

PubMed ID: 20056542

DOI: 10.1016/j.bmcl.2009.12.013

PubMed ID: 22963166

Title: Development of selective, potent RabGGTase inhibitors.

PubMed ID: 22963166

DOI: 10.1021/jm300624s

Sequence Information:

Length: 437
Mass: 48673
Checksum: 41A9D6D79CD319A8
Sequence:

MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK VEEKIQEVFS 
SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR PWLCYWILHS LELLDEPIPQ 
IVATDVCQFL ELCQSPDGGF GGGPGQYPHL APTYAAVNAL CIIGTEEAYN VINREKLLQY 
LYSLKQPDGS FLMHVGGEVD VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG 
GVPGMEAHGG YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY 
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL LDKPGKSRDF 
YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV YNIGPDKVIQ ATTHFLQKPV 
PGFEECEDAV TSDPATD

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: Fntb

Associated with

Other Information

cDNA cloning and expression of the peptide-binding beta subunit of rat p21ras farnesyltransferase, the counterpart of yeast DPR1/RAM1. PubMed ID: 1855253

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

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

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

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

Structural basis for binding and selectivity of antimalarial and anticancer ethylenediamine inhibitors to protein farnesyltransferase. PubMed ID: 19246009

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

Discovery of C-imidazole azaheptapyridine FPT inhibitors. PubMed ID: 20056542

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