Human Gene FNTB (ENST00000246166.3_4) from GENCODE V47lift37
  Description: farnesyltransferase, CAAX box, beta (from RefSeq NM_002028.4)
Gencode Transcript: ENST00000246166.3_4
Gencode Gene: ENSG00000257365.8_8
Transcript (Including UTRs)
   Position: hg19 chr14:65,453,613-65,529,368 Size: 75,756 Total Exon Count: 12 Strand: +
Coding Region
   Position: hg19 chr14:65,453,672-65,528,030 Size: 74,359 Coding Exon Count: 12 

Page IndexSequence and LinksUniProtKB CommentsPrimersCTDGene Alleles
RNA-Seq ExpressionMicroarray ExpressionRNA StructureProtein StructureOther SpeciesGO Annotations
mRNA DescriptionsPathwaysOther NamesModel InformationMethods
Data last updated at UCSC: 2024-08-22 23:36:26

-  Sequence and Links to Tools and Databases
 
Genomic Sequence (chr14:65,453,613-65,529,368)mRNA (may differ from genome)Protein (437 aa)
Gene SorterGenome BrowserOther Species FASTAVisiGeneGene interactionsTable Schema
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HGNCMGIOMIMPubMedReactomeUniProtKB
WikipediaBioGrid CRISPR DB

-  Comments and Description Text from UniProtKB
  ID: FNTB_HUMAN
DESCRIPTION: RecName: Full=Protein farnesyltransferase subunit beta; Short=FTase-beta; EC=2.5.1.58; AltName: Full=CAAX farnesyltransferase subunit beta; AltName: Full=Ras proteins prenyltransferase subunit beta;
FUNCTION: Catalyzes the transfer of a farnesyl moiety from farnesyl pyrophosphate to a cysteine at the fourth position from the C-terminus of several proteins. The beta subunit is responsible for peptide-binding.
CATALYTIC ACTIVITY: Farnesyl diphosphate + protein-cysteine = S- farnesyl protein + diphosphate.
COFACTOR: Binds 1 zinc ion per subunit.
SUBUNIT: Heterodimer of an alpha and a beta subunit.
INTERACTION: P49354:FNTA; NbExp=7; IntAct=EBI-602349, EBI-602336;
SIMILARITY: Belongs to the protein prenyltransferase subunit beta family.
SIMILARITY: Contains 5 PFTB repeats.

-  Primer design for this transcript
 

Primer3Plus can design qPCR Primers that straddle exon-exon-junctions, which amplify only cDNA, not genomic DNA.
Click here to load the transcript sequence and exon structure into Primer3Plus

Exonprimer can design one pair of Sanger sequencing primers around every exon, located in non-genic sequence.
Click here to open Exonprimer with this transcript

To design primers for a non-coding sequence, zoom to a region of interest and select from the drop-down menu: View > In External Tools > Primer3


-  Comparative Toxicogenomics Database (CTD)
  The following chemicals interact with this gene           more ... click here to view the complete list

+  Common Gene Haplotype Alleles
  Press "+" in the title bar above to open this section.

-  RNA-Seq Expression Data from GTEx (53 Tissues, 570 Donors)
  Highest median expression: 3.99 RPKM in Brain - Spinal cord (cervical c-1)
Total median expression: 43.98 RPKM



View in GTEx track of Genome Browser    View at GTEx portal     View GTEx Body Map

+  Microarray Expression Data
  Press "+" in the title bar above to open this section.

-  mRNA Secondary Structure of 3' and 5' UTRs
 
RegionFold EnergyBasesEnergy/Base
Display As
5' UTR -10.1059-0.171 Picture PostScript Text
3' UTR -469.301338-0.351 Picture PostScript Text

The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR001330 - Prenyltrans
IPR008930 - Terpenoid_cyclase/PrenylTrfase

Pfam Domains:
PF00432 - Prenyltransferase and squalene oxidase repeat

SCOP Domains:
48239 - Terpenoid cyclases/Protein prenyltransferases
81853 - Family 10 polysaccharide lyase

Protein Data Bank (PDB) 3-D Structure
MuPIT help
1JCQ - X-ray MuPIT 1LD7 - X-ray MuPIT 1LD8 - X-ray MuPIT 1MZC - X-ray MuPIT 1S63 - X-ray MuPIT 1SA4 - X-ray MuPIT 1TN6 - X-ray MuPIT 2F0Y - X-ray MuPIT 2H6F - X-ray MuPIT 2H6G - X-ray MuPIT 2H6H - X-ray MuPIT 2H6I - X-ray MuPIT 2IEJ - X-ray MuPIT 3E37 - X-ray


ModBase Predicted Comparative 3D Structure on P49356
FrontTopSide
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
MouseRatZebrafishD. melanogasterC. elegansS. cerevisiae
No orthologNo orthologNo orthologNo orthologNo orthologGenome Browser
Gene DetailsGene Details Gene Details Gene Details
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 RGDEnsembl  SGD
     Protein Sequence
     Alignment

-  Gene Ontology (GO) Annotations with Structured Vocabulary
  Molecular Function:
GO:0003824 catalytic activity
GO:0004311 farnesyltranstransferase activity
GO:0004659 prenyltransferase activity
GO:0004660 protein farnesyltransferase activity
GO:0005515 protein binding
GO:0008144 drug binding
GO:0008270 zinc ion binding
GO:0016740 transferase activity
GO:0019840 isoprenoid binding
GO:0042277 peptide binding
GO:0046872 metal ion binding

Biological Process:
GO:0008284 positive regulation of cell proliferation
GO:0008285 negative regulation of cell proliferation
GO:0010035 response to inorganic substance
GO:0014070 response to organic cyclic compound
GO:0018343 protein farnesylation
GO:0034097 response to cytokine
GO:0042060 wound healing
GO:0045787 positive regulation of cell cycle
GO:0048146 positive regulation of fibroblast proliferation
GO:0051770 positive regulation of nitric-oxide synthase biosynthetic process

Cellular Component:
GO:0005829 cytosol
GO:0005875 microtubule associated complex
GO:0005965 protein farnesyltransferase complex
GO:0032991 macromolecular complex


-  Descriptions from all associated GenBank mRNAs
  AK303739 - Homo sapiens cDNA FLJ58825 complete cds, highly similar to Protein farnesyltransferase subunit beta (EC 2.5.1.58).
AK296850 - Homo sapiens cDNA FLJ59570 complete cds, highly similar to Protein farnesyltransferase subunit beta (EC 2.5.1.58).
AK315714 - Homo sapiens cDNA, FLJ96813, Homo sapiens farnesyltransferase, CAAX box, beta (FNTB), mRNA.
BC013574 - Homo sapiens cDNA clone IMAGE:3898137, containing frame-shift errors.
AK225917 - Homo sapiens mRNA for farnesyltransferase, CAAX box, beta variant, clone: FCC118D10.
L00635 - Human farnesyl-protein transferase beta-subunit mRNA, complete cds.
BC020232 - Homo sapiens farnesyltransferase, CAAX box, beta, mRNA (cDNA clone MGC:31935 IMAGE:4652202), complete cds.
GQ901022 - Homo sapiens clone HEL-T-134 epididymis secretory sperm binding protein mRNA, complete cds.
BX248269 - human full-length cDNA clone CS0DC015YK16 of Neuroblastoma of Homo sapiens (human).
DQ895321 - Synthetic construct Homo sapiens clone IMAGE:100009781; FLH183268.01L; RZPDo839A05141D farnesyltransferase, CAAX box, beta (FNTB) gene, encodes complete protein.
KJ891192 - Synthetic construct Homo sapiens clone ccsbBroadEn_00586 FNTB gene, encodes complete protein.
DQ892128 - Synthetic construct clone IMAGE:100004758; FLH183272.01X; RZPDo839A05142D farnesyltransferase, CAAX box, beta (FNTB) gene, encodes complete protein.
L10414 - Human farnesyltransferase beta-subunit mRNA, complete cds.
AK093298 - Homo sapiens cDNA FLJ35979 fis, clone TESTI2013545, highly similar to Protein farnesyltransferase subunit beta (EC 2.5.1.58).
AK295972 - Homo sapiens cDNA FLJ55216 complete cds, highly similar to Protein farnesyltransferase subunit beta (EC 2.5.1.58).
AK024087 - Homo sapiens cDNA FLJ14025 fis, clone HEMBA1003667.
DQ582926 - Homo sapiens piRNA piR-50038, complete sequence.
JD411128 - Sequence 392152 from Patent EP1572962.
JD543619 - Sequence 524643 from Patent EP1572962.
JD545344 - Sequence 526368 from Patent EP1572962.
JD051236 - Sequence 32260 from Patent EP1572962.
JD226673 - Sequence 207697 from Patent EP1572962.
JD519421 - Sequence 500445 from Patent EP1572962.
JD150242 - Sequence 131266 from Patent EP1572962.
JD521238 - Sequence 502262 from Patent EP1572962.
JD513320 - Sequence 494344 from Patent EP1572962.
JD118149 - Sequence 99173 from Patent EP1572962.
JD415471 - Sequence 396495 from Patent EP1572962.
JD057101 - Sequence 38125 from Patent EP1572962.
JD089152 - Sequence 70176 from Patent EP1572962.
JD424414 - Sequence 405438 from Patent EP1572962.
JD309044 - Sequence 290068 from Patent EP1572962.
JD206443 - Sequence 187467 from Patent EP1572962.
JD079050 - Sequence 60074 from Patent EP1572962.
JD342702 - Sequence 323726 from Patent EP1572962.
JD540117 - Sequence 521141 from Patent EP1572962.
JD454778 - Sequence 435802 from Patent EP1572962.
JD189617 - Sequence 170641 from Patent EP1572962.
JD373621 - Sequence 354645 from Patent EP1572962.
JD286535 - Sequence 267559 from Patent EP1572962.
JD230316 - Sequence 211340 from Patent EP1572962.
JD490246 - Sequence 471270 from Patent EP1572962.
JD237566 - Sequence 218590 from Patent EP1572962.
JD074586 - Sequence 55610 from Patent EP1572962.
JD433637 - Sequence 414661 from Patent EP1572962.

-  Biochemical and Signaling Pathways
  Reactome (by CSHL, EBI, and GO)

Protein P49356 (Reactome details) participates in the following event(s):

R-HSA-2530501 FNTA:FNTB transfers FARN to GNGT1
R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade
R-HSA-2514856 The phototransduction cascade
R-HSA-2187338 Visual phototransduction
R-HSA-418594 G alpha (i) signalling events
R-HSA-388396 GPCR downstream signalling
R-HSA-372790 Signaling by GPCR
R-HSA-162582 Signal Transduction

-  Other Names for This Gene
  Alternate Gene Symbols: B2RDX6, B4E1A0, ENST00000246166.1, ENST00000246166.2, FNTB_HUMAN, NM_002028, P49356, uc317eta.1, uc317eta.2
UCSC ID: ENST00000246166.3_4
RefSeq Accession: NM_002028.4
Protein: P49356 (aka FNTB_HUMAN)

-  Gene Model Information
  Click here for a detailed description of the fields of the table above.

-  Methods, Credits, and Use Restrictions
  Click here for details on how this gene model was made and data restrictions if any.