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Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

FNTA

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.6 Publications

Catalytic activityi

Farnesyl diphosphate + protein-cysteine = S-farnesyl protein + diphosphate.6 Publications
Geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate.1 Publication

Enzyme regulationi

Activated by the AGRIN-induced phosphorylation which is mediated by MUSK.By similarity

GO - Molecular functioni

  • acetylcholine receptor regulator activity Source: Ensembl
  • alpha-tubulin binding Source: BHF-UCL
  • CAAX-protein geranylgeranyltransferase activity Source: UniProtKB-EC
  • microtubule binding Source: BHF-UCL
  • protein farnesyltransferase activity Source: UniProtKB
  • protein geranylgeranyltransferase activity Source: UniProtKB
  • Rab geranylgeranyltransferase activity Source: Ensembl

GO - Biological processi

  • cellular component disassembly involved in execution phase of apoptosis Source: Reactome
  • neurotransmitter receptor metabolic process Source: Ensembl
  • positive regulation of deacetylase activity Source: BHF-UCL
  • positive regulation of tubulin deacetylation Source: BHF-UCL
  • protein farnesylation Source: UniProtKB
  • protein geranylgeranylation Source: UniProtKB
  • regulation of rhodopsin mediated signaling pathway Source: Reactome
  • transforming growth factor beta receptor signaling pathway Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Prenyltransferase, Transferase

Enzyme and pathway databases

BioCyciZFISH:HS09779-MONOMER.
BRENDAi2.5.1.58. 2681.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SIGNORiP49354.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha (EC:2.5.1.586 Publications, EC:2.5.1.591 Publication)
Alternative name(s):
CAAX farnesyltransferase subunit alpha
FTase-alpha
Ras proteins prenyltransferase subunit alpha
Type I protein geranyl-geranyltransferase subunit alpha
Short name:
GGTase-I-alpha
Gene namesi
Name:FNTA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3782. FNTA.

Subcellular locationi

GO - Cellular componenti

  • CAAX-protein geranylgeranyltransferase complex Source: UniProtKB
  • cytoplasm Source: ProtInc
  • cytosol Source: Reactome
  • microtubule associated complex Source: BHF-UCL
  • plasma membrane Source: GOC
  • protein farnesyltransferase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi164K → N: Reduced activity. 1 Publication1
Mutagenesisi199N → K: Reduced catalytic efficiency. 1 Publication1

Organism-specific databases

DisGeNETi2339.
OpenTargetsiENSG00000168522.
PharmGKBiPA28199.

Chemistry databases

ChEMBLiCHEMBL271.

Polymorphism and mutation databases

BioMutaiFNTA.
DMDMi1346694.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001197462 – 379Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaAdd BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Modified residuei373PhosphoserineCombined sources1

Post-translational modificationi

Phosphorylated. Phosphorylation is mediated by MUSK upon AGRIN stimulation and results in the activation of FNTA (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP49354.
MaxQBiP49354.
PaxDbiP49354.
PeptideAtlasiP49354.
PRIDEiP49354.

PTM databases

iPTMnetiP49354.
PhosphoSitePlusiP49354.
SwissPalmiP49354.

Miscellaneous databases

PMAP-CutDBP49354.

Expressioni

Gene expression databases

BgeeiENSG00000168522.
CleanExiHS_FNTA.
ExpressionAtlasiP49354. baseline and differential.
GenevisibleiP49354. HS.

Organism-specific databases

HPAiCAB010149.
HPA018830.

Interactioni

Subunit structurei

Interacts with MUSK; the interaction is direct and mediates AGRIN-induced phosphorylation of FNTA (By similarity). Heterodimer of FNTA and FNTB (farnesyltransferase). Heterodimer of FNTA and PGGT1B (geranylgeranyltransferase).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FNTBP4935611EBI-602336,EBI-602349

GO - Molecular functioni

  • alpha-tubulin binding Source: BHF-UCL
  • microtubule binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi108625. 26 interactors.
IntActiP49354. 14 interactors.
MINTiMINT-238861.
STRINGi9606.ENSP00000303423.

Chemistry databases

BindingDBiP49354.

Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi66 – 68Combined sources3
Helixi70 – 72Combined sources3
Beta strandi87 – 90Combined sources4
Helixi94 – 109Combined sources16
Helixi114 – 126Combined sources13
Helixi131 – 143Combined sources13
Helixi148 – 161Combined sources14
Helixi166 – 179Combined sources14
Helixi185 – 195Combined sources11
Helixi200 – 213Combined sources14
Helixi216 – 218Combined sources3
Helixi219 – 229Combined sources11
Helixi234 – 246Combined sources13
Helixi253 – 269Combined sources17
Helixi274 – 284Combined sources11
Turni285 – 287Combined sources3
Helixi289 – 291Combined sources3
Helixi293 – 302Combined sources10
Turni303 – 305Combined sources3
Helixi309 – 324Combined sources16
Helixi330 – 346Combined sources17
Helixi350 – 352Combined sources3
Helixi353 – 367Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JCQX-ray2.30A1-379[»]
1LD7X-ray2.00A1-379[»]
1LD8X-ray1.80A1-379[»]
1MZCX-ray2.00A1-379[»]
1S63X-ray1.90A1-379[»]
1SA4X-ray2.10A1-379[»]
1TN6X-ray1.80A1-379[»]
2F0YX-ray2.70A1-379[»]
2H6FX-ray1.50A1-379[»]
2H6GX-ray1.85A1-379[»]
2H6HX-ray1.80A1-379[»]
2H6IX-ray3.00A1-379[»]
2IEJX-ray1.80A1-379[»]
3E37X-ray1.80A1-379[»]
DisProtiDP00558.
ProteinModelPortaliP49354.
SMRiP49354.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49354.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati112 – 146PFTA 1Add BLAST35
Repeati147 – 180PFTA 2Add BLAST34
Repeati181 – 215PFTA 3Add BLAST35
Repeati216 – 249PFTA 4Add BLAST34
Repeati255 – 289PFTA 5Add BLAST35

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi22 – 31Pro-rich10

Sequence similaritiesi

Contains 5 PFTA repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0530. Eukaryota.
COG5536. LUCA.
GeneTreeiENSGT00550000074935.
HOGENOMiHOG000188957.
HOVERGENiHBG004498.
InParanoidiP49354.
KOiK05955.
OMAiRQWAIRS.
OrthoDBiEOG091G0CNT.
PhylomeDBiP49354.
TreeFamiTF313038.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P49354-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAATEGVGEA AQGGEPGQPA QPPPQPHPPP PQQQHKEEMA AEAGEAVASP
60 70 80 90 100
MDDGFVSLDS PSYVLYRDRA EWADIDPVPQ NDGPNPVVQI IYSDKFRDVY
110 120 130 140 150
DYFRAVLQRD ERSERAFKLT RDAIELNAAN YTVWHFRRVL LKSLQKDLHE
160 170 180 190 200
EMNYITAIIE EQPKNYQVWH HRRVLVEWLR DPSQELEFIA DILNQDAKNY
210 220 230 240 250
HAWQHRQWVI QEFKLWDNEL QYVDQLLKED VRNNSVWNQR YFVISNTTGY
260 270 280 290 300
NDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS KYPNLLNQLL
310 320 330 340 350
DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT
360 370
IRKEYWRYIG RSLQSKHSTE NDSPTNVQQ
Length:379
Mass (Da):44,409
Last modified:February 1, 1996 - v1
Checksum:iE933CBA874AB92B9
GO
Isoform 2 (identifier: P49354-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-134: Missing.

Show »
Length:312
Mass (Da):36,493
Checksum:i789D43774B90D5DA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti241Y → H (PubMed:8419339).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_03646868 – 134Missing in isoform 2. 1 PublicationAdd BLAST67

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10413 mRNA. Translation: AAA86285.1.
L00634 mRNA. Translation: AAA35853.1.
AC110275 Genomic DNA. No translation available.
BT009854 mRNA. Translation: AAP88856.1.
AK292121 mRNA. Translation: BAF84810.1.
AC113191 Genomic DNA. No translation available.
BC017029 mRNA. Translation: AAH17029.2.
BC084566 mRNA. Translation: AAH84566.1.
AL698961 mRNA. No translation available.
CCDSiCCDS6140.1. [P49354-1]
PIRiA47659.
RefSeqiNP_002018.1. NM_002027.2. [P49354-1]
UniGeneiHs.370312.

Genome annotation databases

EnsembliENST00000302279; ENSP00000303423; ENSG00000168522. [P49354-1]
GeneIDi2339.
KEGGihsa:2339.
UCSCiuc003xps.5. human. [P49354-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10413 mRNA. Translation: AAA86285.1.
L00634 mRNA. Translation: AAA35853.1.
AC110275 Genomic DNA. No translation available.
BT009854 mRNA. Translation: AAP88856.1.
AK292121 mRNA. Translation: BAF84810.1.
AC113191 Genomic DNA. No translation available.
BC017029 mRNA. Translation: AAH17029.2.
BC084566 mRNA. Translation: AAH84566.1.
AL698961 mRNA. No translation available.
CCDSiCCDS6140.1. [P49354-1]
PIRiA47659.
RefSeqiNP_002018.1. NM_002027.2. [P49354-1]
UniGeneiHs.370312.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JCQX-ray2.30A1-379[»]
1LD7X-ray2.00A1-379[»]
1LD8X-ray1.80A1-379[»]
1MZCX-ray2.00A1-379[»]
1S63X-ray1.90A1-379[»]
1SA4X-ray2.10A1-379[»]
1TN6X-ray1.80A1-379[»]
2F0YX-ray2.70A1-379[»]
2H6FX-ray1.50A1-379[»]
2H6GX-ray1.85A1-379[»]
2H6HX-ray1.80A1-379[»]
2H6IX-ray3.00A1-379[»]
2IEJX-ray1.80A1-379[»]
3E37X-ray1.80A1-379[»]
DisProtiDP00558.
ProteinModelPortaliP49354.
SMRiP49354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108625. 26 interactors.
IntActiP49354. 14 interactors.
MINTiMINT-238861.
STRINGi9606.ENSP00000303423.

Chemistry databases

BindingDBiP49354.
ChEMBLiCHEMBL271.

PTM databases

iPTMnetiP49354.
PhosphoSitePlusiP49354.
SwissPalmiP49354.

Polymorphism and mutation databases

BioMutaiFNTA.
DMDMi1346694.

Proteomic databases

EPDiP49354.
MaxQBiP49354.
PaxDbiP49354.
PeptideAtlasiP49354.
PRIDEiP49354.

Protocols and materials databases

DNASUi2339.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302279; ENSP00000303423; ENSG00000168522. [P49354-1]
GeneIDi2339.
KEGGihsa:2339.
UCSCiuc003xps.5. human. [P49354-1]

Organism-specific databases

CTDi2339.
DisGeNETi2339.
GeneCardsiFNTA.
HGNCiHGNC:3782. FNTA.
HPAiCAB010149.
HPA018830.
MIMi134635. gene.
neXtProtiNX_P49354.
OpenTargetsiENSG00000168522.
PharmGKBiPA28199.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0530. Eukaryota.
COG5536. LUCA.
GeneTreeiENSGT00550000074935.
HOGENOMiHOG000188957.
HOVERGENiHBG004498.
InParanoidiP49354.
KOiK05955.
OMAiRQWAIRS.
OrthoDBiEOG091G0CNT.
PhylomeDBiP49354.
TreeFamiTF313038.

Enzyme and pathway databases

BioCyciZFISH:HS09779-MONOMER.
BRENDAi2.5.1.58. 2681.
ReactomeiR-HSA-111465. Apoptotic cleavage of cellular proteins.
R-HSA-2514859. Inactivation, recovery and regulation of the phototransduction cascade.
SIGNORiP49354.

Miscellaneous databases

ChiTaRSiFNTA. human.
EvolutionaryTraceiP49354.
GeneWikiiFNTA.
GenomeRNAii2339.
PMAP-CutDBP49354.
PROiP49354.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000168522.
CleanExiHS_FNTA.
ExpressionAtlasiP49354. baseline and differential.
GenevisibleiP49354. HS.

Family and domain databases

InterProiIPR002088. Prenyl_trans_a.
[Graphical view]
PfamiPF01239. PPTA. 5 hits.
[Graphical view]
PROSITEiPS51147. PFTA. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFNTA_HUMAN
AccessioniPrimary (citable) accession number: P49354
Secondary accession number(s): A6NJW0, Q53XJ9, Q9UDC1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 30, 2016
This is version 173 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.