Q02293 · FNTB_RAT
- ProteinProtein farnesyltransferase subunit beta
- GeneFntb
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids437 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential subunit of the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.
Catalytic activity
- (2E,6E)-farnesyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-(2E,6E)-farnesyl-L-cysteinyl-[protein]
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 102 | Important for selectivity against geranylgeranyl diphosphate | ||||
Sequence: W | ||||||
Binding site | 248-251 | (2E,6E)-farnesyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: HGGY | ||||||
Binding site | 291-294 | (2E,6E)-farnesyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: RCNK | ||||||
Binding site | 297 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 299 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: C | ||||||
Binding site | 300-303 | (2E,6E)-farnesyl diphosphate (UniProtKB | ChEBI) | ||||
Sequence: YSFW | ||||||
Binding site | 362 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | microtubule associated complex | |
Cellular Component | protein farnesyltransferase complex | |
Molecular Function | farnesyltranstransferase activity | |
Molecular Function | protein farnesyltransferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | cell population proliferation | |
Biological Process | fibroblast proliferation | |
Biological Process | lipid metabolic process | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | positive regulation of cell cycle | |
Biological Process | positive regulation of cell population proliferation | |
Biological Process | positive regulation of fibroblast proliferation | |
Biological Process | positive regulation of nitric-oxide synthase biosynthetic process | |
Biological Process | protein farnesylation | |
Biological Process | regulation of fibroblast proliferation | |
Biological Process | response to cytokine | |
Biological Process | response to organic cyclic compound | |
Biological Process | wound healing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProtein farnesyltransferase subunit beta
- EC number
- Short namesFTase-beta
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ02293
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000119763 | 1-437 | Protein farnesyltransferase subunit beta | |||
Sequence: MASSSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYNVINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKKERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVMGVPENVLQPTHPVYNIGPDKVIQATTHFLQKPVPGFEECEDAVTSDPATD | ||||||
Modified residue | 432 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 436 | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Heterodimer of FNTA and FNTB.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q02293 | Fnta Q04631 | 16 | EBI-602454, EBI-602447 |
Protein-protein interaction databases
Chemistry
Structure
Family & Domains
Features
Showing features for repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 123-164 | PFTB 1 | ||||
Sequence: ATDVCQFLELCQSPDGGFGGGPGQYPHLAPTYAAVNALCIIG | ||||||
Repeat | 174-215 | PFTB 2 | ||||
Sequence: REKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTN | ||||||
Repeat | 222-263 | PFTB 3 | ||||
Sequence: FEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILK | ||||||
Repeat | 270-312 | PFTB 4 | ||||
Sequence: LKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLH | ||||||
Repeat | 332-374 | PFTB 5 | ||||
Sequence: QQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQ |
Sequence similarities
Belongs to the protein prenyltransferase subunit beta family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length437
- Mass (Da)48,673
- Last updated1993-04-01 v1
- Checksum41A9D6D79CD319A8
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6GKJ2 | A0A8I6GKJ2_RAT | Churc1 | 78 | ||
A0A8I6GKV7 | A0A8I6GKV7_RAT | Churc1 | 35 | ||
B5DER2 | B5DER2_RAT | Churc1 | 112 | ||
A0A8I5ZMQ9 | A0A8I5ZMQ9_RAT | Fntb | 408 | ||
A0A8I5ZP53 | A0A8I5ZP53_RAT | Churc1 | 104 | ||
A0A8I5ZQQ4 | A0A8I5ZQQ4_RAT | Churc1 | 471 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M69056 EMBL· GenBank· DDBJ | AAA41176.1 EMBL· GenBank· DDBJ | mRNA | ||
BC087675 EMBL· GenBank· DDBJ | AAH87675.1 EMBL· GenBank· DDBJ | mRNA |