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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionPrenyltransferase, Transferase

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.5.1.58 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-111465 Apoptotic cleavage of cellular proteins
R-HSA-2514859 Inactivation, recovery and regulation of the phototransduction cascade

SIGNOR Signaling Network Open Resource

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SIGNORi
P49354

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FNTA
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000168522.12

Human Gene Nomenclature Database

More...
HGNCi
HGNC:3782 FNTA

Online Mendelian Inheritance in Man (OMIM)

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MIMi
134635 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P49354

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi164K → N: Reduced activity. 1 Publication1
Mutagenesisi199N → K: Reduced catalytic efficiency. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
2339

Open Targets

More...
OpenTargetsi
ENSG00000168522

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28199

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL271

Drug and drug target database

More...
DrugBanki
DB08180 2-[METHYL-(5-GERANYL-4-METHYL-PENT-3-ENYL)-AMINO]-ETHYL-DIPHOSPHATE
DB06953 2-CHLORO-5-(3-CHLORO-PHENYL)-6-[(4-CYANO-PHENYL)-(3-METHYL-3H-IMIDAZOL-4-YL)- METHOXYMETHYL]-NICOTINONITRILE
DB07227 4-[(5-{[4-(3-CHLOROPHENYL)-3-OXOPIPERAZIN-1-YL]METHYL}-1H-IMIDAZOL-1-YL)METHYL]BENZONITRILE
DB07895 ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID
DB04893 AZD3409
DB07780 FARNESYL DIPHOSPHATE
DB07841 GERANYLGERANYL DIPHOSPHATE

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
FNTA

Domain mapping of disease mutations (DMDM)

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DMDMi
1346694

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001197462 – 379Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaAdd BLAST378

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1
Modified residuei373PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
P49354

MaxQB - The MaxQuant DataBase

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MaxQBi
P49354

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P49354

PeptideAtlas

More...
PeptideAtlasi
P49354

PRoteomics IDEntifications database

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PRIDEi
P49354

ProteomicsDB human proteome resource

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ProteomicsDBi
55993
55994 [P49354-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P49354

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P49354

SwissPalm database of S-palmitoylation events

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SwissPalmi
P49354

Miscellaneous databases

CutDB - Proteolytic event database

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PMAP-CutDBi
P49354

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000168522 Expressed in 241 organ(s), highest expression level in C1 segment of cervical spinal cord

CleanEx database of gene expression profiles

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CleanExi
HS_FNTA

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P49354 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P49354 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB010149
HPA018830

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108625, 47 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-2157 Protein geranylgeranyl transferase type I complex
CPX-2165 Protein farnesyltransferase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P49354

Protein interaction database and analysis system

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IntActi
P49354, 14 interactors

Molecular INTeraction database

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MINTi
P49354

STRING: functional protein association networks

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STRINGi
9606.ENSP00000303423

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P49354

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1379
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

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DisProti
DP00558

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P49354

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P49354

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P49354

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi22 – 31Pro-rich10

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0530 Eukaryota
COG5536 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00550000074935

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000188957

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG004498

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P49354

KEGG Orthology (KO)

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KOi
K05955

Identification of Orthologs from Complete Genome Data

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OMAi
GDAKNYH

Database of Orthologous Groups

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OrthoDBi
EOG091G0CNT

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P49354

TreeFam database of animal gene trees

More...
TreeFami
TF313038

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR002088 Prenyl_trans_a

Pfam protein domain database

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Pfami
View protein in Pfam
PF01239 PPTA, 5 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51147 PFTA, 5 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 6 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 6 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B3KVN2B3KVN2_HUMAN
Farnesyltransferase, CAAX box, alph...
FNTA hCG_1993221
228Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PQP6E9PQP6_HUMAN
Protein farnesyltransferase/geranyl...
FNTA
249Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YCW1H0YCW1_HUMAN
Protein farnesyltransferase/geranyl...
FNTA
196Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PPM9E9PPM9_HUMAN
Protein farnesyltransferase/geranyl...
FNTA
60Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PN85E9PN85_HUMAN
Protein farnesyltransferase/geranyl...
FNTA
117Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
E9PK84E9PK84_HUMAN
Protein farnesyltransferase/geranyl...
FNTA
67Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti241Y → H (PubMed:8419339).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_03646868 – 134Missing in isoform 2. 1 PublicationAdd BLAST67

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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.

The Consensus CDS (CCDS) project

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CCDSi
CCDS6140.1 [P49354-1]

Protein sequence database of the Protein Information Resource

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PIRi
A47659

NCBI Reference Sequences

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RefSeqi
NP_002018.1, NM_002027.2 [P49354-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.370312

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000302279; ENSP00000303423; ENSG00000168522 [P49354-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
2339

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2339

UCSC genome browser

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UCSCi
uc003xps.5 human [P49354-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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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, 47 interactors
ComplexPortaliCPX-2157 Protein geranylgeranyl transferase type I complex
CPX-2165 Protein farnesyltransferase complex
CORUMiP49354
IntActiP49354, 14 interactors
MINTiP49354
STRINGi9606.ENSP00000303423

Chemistry databases

BindingDBiP49354
ChEMBLiCHEMBL271
DrugBankiDB08180 2-[METHYL-(5-GERANYL-4-METHYL-PENT-3-ENYL)-AMINO]-ETHYL-DIPHOSPHATE
DB06953 2-CHLORO-5-(3-CHLORO-PHENYL)-6-[(4-CYANO-PHENYL)-(3-METHYL-3H-IMIDAZOL-4-YL)- METHOXYMETHYL]-NICOTINONITRILE
DB07227 4-[(5-{[4-(3-CHLOROPHENYL)-3-OXOPIPERAZIN-1-YL]METHYL}-1H-IMIDAZOL-1-YL)METHYL]BENZONITRILE
DB07895 ALPHA-HYDROXYFARNESYLPHOSPHONIC ACID
DB04893 AZD3409
DB07780 FARNESYL DIPHOSPHATE
DB07841 GERANYLGERANYL DIPHOSPHATE

PTM databases

iPTMnetiP49354
PhosphoSitePlusiP49354
SwissPalmiP49354

Polymorphism and mutation databases

BioMutaiFNTA
DMDMi1346694

Proteomic databases

EPDiP49354
MaxQBiP49354
PaxDbiP49354
PeptideAtlasiP49354
PRIDEiP49354
ProteomicsDBi55993
55994 [P49354-2]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
2339
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2339
DisGeNETi2339
EuPathDBiHostDB:ENSG00000168522.12

GeneCards: human genes, protein and diseases

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GeneCardsi
FNTA
HGNCiHGNC:3782 FNTA
HPAiCAB010149
HPA018830
MIMi134635 gene
neXtProtiNX_P49354
OpenTargetsiENSG00000168522
PharmGKBiPA28199

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

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

Enzyme and pathway databases

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

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
FNTA human
EvolutionaryTraceiP49354

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
FNTA

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
2339
PMAP-CutDBiP49354

Protein Ontology

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PROi
PR:P49354

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000168522 Expressed in 241 organ(s), highest expression level in C1 segment of cervical spinal cord
CleanExiHS_FNTA
ExpressionAtlasiP49354 baseline and differential
GenevisibleiP49354 HS

Family and domain databases

InterProiView protein in InterPro
IPR002088 Prenyl_trans_a
PfamiView protein in Pfam
PF01239 PPTA, 5 hits
PROSITEiView protein in PROSITE
PS51147 PFTA, 5 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFNTA_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P49354
Secondary accession number(s): A6NJW0, Q53XJ9, Q9UDC1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: December 5, 2018
This is version 189 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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