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UniProtKB - P29703 (FNTA_YEAST)

Entry version 166 (02 Dec 2020)
Sequence version 1 (01 Apr 1993)
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Protein

Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha

Gene

RAM2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. If X is Ser, Ala, Met, Cys, or Gln, then the protein is farnesylated, if X is Leu or Phe, then the protein is geranylgeranylated. The alpha subunit wraps partly around the beta subunit forming part of the active site. The beta subunit is responsible for isoprenoid and peptide-binding.5 Publications

Miscellaneous

Present with 396 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+2 Publications

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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
LigandMagnesium

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-9648002, RAS processing

<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%5Fand%5Ftaxonomy%5Fsection">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:2.5.1.583 Publications, EC:2.5.1.593 Publications)
Short name:
PFTase/PGGTase I alpha
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%5Fand%5Ftaxonomy%5Fsection">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:RAM2
Ordered Locus Names:YKL019W
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 XI

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...EuPathDBi		FungiDB:YKL019W

Saccharomyces Genome Database

More...SGDi		S000001502, RAM2

<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

Keywords - Cellular componenti

Cytoplasm

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi140D → N: Decreases catalytic activity 5-fold, but retains substrate binding properties. 1 Publication1
Mutagenesisi143N → K in ram2-1; completely abolishes farnesyltransferase activity, but still has about 30% geranyl-geranyl transferase activity. 2 Publications1
Mutagenesisi145H → D: Increases KM for peptide substrate 4-fold, but retains catalytic activity. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2406

<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 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001197541 – 316Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alphaAdd BLAST316

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P29703

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

More...PaxDbi		P29703

PRoteomics IDEntifications database

More...PRIDEi		P29703

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Farnesyltransferase and geranyl-geranyltransferase share a common alpha subunit (RAM2) (Probable). Protein farnesyltransferase is a heterodimer of alpha subunit RAM2 and beta subunit RAM1 (PubMed:1763050). Protein geranyl-geranyltransferase type-1 is a heterodimer of alpha subunit RAM2 and beta subunit CDC43 (PubMed:1400380, PubMed:9174352).

1 Publication3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		34112, 136 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-1634, Protein farnesyltransferase complex
CPX-1635, Protein geranylgeranyltransferase type I complex

Database of interacting proteins

More...DIPi		DIP-1233N

Protein interaction database and analysis system

More...IntActi		P29703, 6 interactors

Molecular INTeraction database

More...MINTi		P29703

STRING: functional protein association networks

More...STRINGi		4932.YKL019W

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P29703

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P29703, protein

<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

3D structure databases

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

More...SMRi		P29703

Database of comparative protein structure models

More...ModBasei		Search...

<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>Repeati47 – 81PFTA 1PROSITE-ProRule annotationAdd BLAST35
Repeati89 – 123PFTA 2PROSITE-ProRule annotationAdd BLAST35
Repeati125 – 159PFTA 3PROSITE-ProRule annotationAdd BLAST35
Repeati160 – 193PFTA 4PROSITE-ProRule annotationAdd BLAST34
Repeati199 – 233PFTA 5PROSITE-ProRule annotationAdd BLAST35

<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

Belongs to the protein prenyltransferase subunit alpha family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0530, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00550000074935

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_026582_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P29703

Identification of Orthologs from Complete Genome Data

More...OMAi		KGNESAW

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR002088, Prenyl_trans_a

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01239, PPTA, 4 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P29703-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEEYDYSDVK PLPIETDLQD ELCRIMYTED YKRLMGLARA LISLNELSPR 
        60         70         80         90        100
ALQLTAEIID VAPAFYTIWN YRFNIVRHMM SESEDTVLYL NKELDWLDEV 
       110        120        130        140        150
TLNNPKNYQI WSYRQSLLKL HPSPSFKREL PILKLMIDDD SKNYHVWSYR 
       160        170        180        190        200
KWCCLFFSDF QHELAYASDL IETDIYNNSA WTHRMFYWVN AKDVISKVEL 
       210        220        230        240        250
ADELQFIMDK IQLVPQNISP WTYLRGFQEL FHDRLQWDSK VVDFATTFIG 
       260        270        280        290        300
DVLSLPIGSP EDLPEIESSY ALEFLAYHWG ADPCTRDNAV KAYSLLAIKY 
       310 
DPIRKNLWHH KINNLN
Length:316
Mass (Da):37,508
Last modified:April 1, 1993 - 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:iD828519BB9914608
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M88584 Genomic DNA Translation: AAA34957.1
Z28019 Genomic DNA Translation: CAA81854.1
L24760 Genomic DNA Translation: AAA20574.1
BK006944 Genomic DNA Translation: DAA09136.1

Protein sequence database of the Protein Information Resource

More...PIRi		A41626

NCBI Reference Sequences

More...RefSeqi		NP_012906.3, NM_001179585.3

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YKL019W_mRNA; YKL019W; YKL019W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		853849

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YKL019W

<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
M88584 Genomic DNA Translation: AAA34957.1
Z28019 Genomic DNA Translation: CAA81854.1
L24760 Genomic DNA Translation: AAA20574.1
BK006944 Genomic DNA Translation: DAA09136.1
PIRiA41626
RefSeqiNP_012906.3, NM_001179585.3

3D structure databases

SMRiP29703
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi34112, 136 interactors
ComplexPortaliCPX-1634, Protein farnesyltransferase complex
CPX-1635, Protein geranylgeranyltransferase type I complex
DIPiDIP-1233N
IntActiP29703, 6 interactors
MINTiP29703
STRINGi4932.YKL019W

Chemistry databases

BindingDBiP29703
ChEMBLiCHEMBL2406

Proteomic databases

MaxQBiP29703
PaxDbiP29703
PRIDEiP29703

Genome annotation databases

EnsemblFungiiYKL019W_mRNA; YKL019W; YKL019W
GeneIDi853849
KEGGisce:YKL019W

Organism-specific databases

EuPathDBiFungiDB:YKL019W
SGDiS000001502, RAM2

Phylogenomic databases

eggNOGiKOG0530, Eukaryota
GeneTreeiENSGT00550000074935
HOGENOMiCLU_026582_1_0_1
InParanoidiP29703
OMAiKGNESAW

Enzyme and pathway databases

ReactomeiR-SCE-9648002, RAS processing

Miscellaneous databases

Protein Ontology

More...PROi		PR:P29703
RNActiP29703, protein

Family and domain databases

InterProiView protein in InterPro
IPR002088, Prenyl_trans_a
PfamiView protein in Pfam
PF01239, PPTA, 4 hits
PROSITEiView protein in PROSITE
PS51147, PFTA, 5 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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_YEAST
<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: P29703
Secondary accession number(s): D6VXR6
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: December 2, 2020
This is version 166 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 programFungal Protein Annotation Program

<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

Reference proteome

Documents

  1. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
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