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Entry version 178 (07 Apr 2021)
Sequence version 2 (01 Nov 1997)
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Protein

Protein farnesyltransferase subunit beta

Gene

RAM1

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

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 where X is Ser, Ala, Met, Cys, or Gln. Required for the membrane localization of proteins such as a-factor, Ras proteins and other membrane proteins containing the C-terminal CAAX motif (PubMed:3533274, PubMed:2124698, PubMed:1860864, PubMed:1763050, PubMed:8424764, PubMed:8527442, PubMed:17142567). The beta subunit is responsible for isoprenoid and peptide-binding (PubMed:7878044, PubMed:8995312, PubMed:9380709, PubMed:9545274, PubMed:12667062).12 Publications

Miscellaneous

Present with 3910 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

Zn2+2 PublicationsNote: Binds 1 zinc ion per subunit.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 4.5 sec(-1) with dansyl-GCVIA as substrate.1 Publication
  1. KM=8.1 µM for farnesyl diphosphate1 Publication
  2. KM=0.16 µM for farnesyl diphosphate1 Publication
  3. KM=0.9 µM for dansyl-GCVIA1 Publication
  4. KM=3.59 µM for geranylgeranyl diphosphate1 Publication
  5. KM=0.46 µM for Ras-CIIS1 Publication
  6. KM=4.12 µM for Ras-CIIM (for farnesyl transferase reaction)1 Publication
  7. KM=0.28 µM for Ras-CIIM (for geranyl-geranyl transferase reaction)1 Publication
  8. KM=10.2 µM for Ras-CIIL1 Publication
  1. Vmax=3.4 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 7.8.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei108Important for selectivity against geranylgeranyl diphosphateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi307Zinc; catalyticBy similarity2 Publications1
Metal bindingi309Zinc; catalyticBy similarity2 Publications1
Metal bindingi363Zinc; via tele nitrogen; catalyticBy similarity2 Publications1

<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
LigandMetal-binding, Zinc

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 subunit beta (EC:2.5.1.582 Publications)
Short name:
FTase-beta
Short name:
PFTase beta
Alternative name(s):
CAAX farnesyltransferase subunit beta
Ras proteins prenyltransferase subunit beta
<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:RAM11 Publication
Synonyms:DPR1, SCG2, STE16
Ordered Locus Names:YDL090C
ORF Names:D2412
<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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<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 IV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002248, RAM1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YDL090C

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Decreases SKT5 farnesylation.1 Publication

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>Mutagenesisi57 – 64RYKVLQSV → HYKFFQRH: Impairs isoprenyl transferase activity. 1 Publication8
Mutagenesisi74I → D: Farnesylates only Ras-CIIS and not Ras-CII(M,L), and it geranylgeranylates all three substrates as well or better than wild type. 1 Publication1
Mutagenesisi149G → D or E: Alters protein substrate specificity. Able to farnesylate Ras2 variants with positively charged C-terminal amino acids (CIIR and CIIK). 1 Publication1
Mutagenesisi149G → R or K: Alters protein substrate specificity. Able to farnesylate Ras2 variants with a negatively charged C-terminal aspartate (CIID). 1 Publication1
Mutagenesisi159S → D or N: Can substitute for PGGT-I beta subunit (CDC43) in vivo. Has increased activity to farnesylate a substrate for PGGT-I. On the other hand, the ability to farnesylate its own substrate is reduced, due to its increased affinity for PGGT-I protein substrates. Increases the kcat/Km value for PGGTase-I substrates about 20-fold. 2 Publications1
Mutagenesisi206 – 212GEVDTRG → DEDDLRF: Farnesylates Ras-CII(S,M,L) at wild type levels but can no longer geranylgeranylate the RasCII(M,L) substrates. 1 Publication7
Mutagenesisi209D → N in ram1-1; causes a defect in a-factor production. 2 Publications1
Mutagenesisi259G → V in ram1-2; abolishes farnesyltransferase activity. 2 Publications1
Mutagenesisi308G → T: Impairs isoprenyl transferase activity. 1 Publication1
Mutagenesisi310Y → K: Impairs isoprenyl transferase activity. 1 Publication1
Mutagenesisi351 – 354LRDK → FSKN: Farnesylates Ras-CIIS and Ras-CIIM but not Ras-CIIL, and is not capable of geranylgeranylating the Ras-CII(M,L) substrates. 1 Publication4
Mutagenesisi362Y → H: Can substitute for PGGT-I beta subunit, by modulating the substrate specificity for the peptide substrate. 1 Publication1
Mutagenesisi362Y → L, M or I: Can substitute for PGGT-I beta subunit, by modulating the substrate specificity for the peptide substrate. Increases the kcat/Km value for PGGTase-I substrates about 20-fold. 1 Publication1
Mutagenesisi366Y → N: Can substitute for PGGT-I beta subunit, by modulating the substrate specificity for the peptide substrate. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2111393

<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_00001197681 – 431Protein farnesyltransferase subunit betaAdd BLAST431

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P22007

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

More...
PaxDbi
P22007

PRoteomics IDEntifications database

More...
PRIDEi
P22007

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P22007

<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

Heterodimer of an alpha (RAM2) and a beta (RAM1) subunit.

2 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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
31970, 244 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1634, Protein farnesyltransferase complex

Database of interacting proteins

More...
DIPi
DIP-1556N

Protein interaction database and analysis system

More...
IntActi
P22007, 10 interactors

Molecular INTeraction database

More...
MINTi
P22007

STRING: functional protein association networks

More...
STRINGi
4932.YDL090C

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P22007

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P22007, 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
P22007

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>Repeati130 – 171PFTB 1Sequence analysisAdd BLAST42
Repeati182 – 224PFTB 2Sequence analysisAdd BLAST43
Repeati231 – 273PFTB 3Sequence analysisAdd BLAST43
Repeati280 – 322PFTB 4Sequence analysisAdd BLAST43
Repeati332 – 375PFTB 5Sequence analysisAdd BLAST44

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni258 – 261Farnesyl diphosphate bindingBy similarity4
Regioni301 – 304Farnesyl diphosphate bindingBy similarity4
Regioni310 – 313Farnesyl diphosphate bindingBy similarity4

<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

More...
eggNOGi
KOG0365, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183128

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_028946_0_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P22007

Identification of Orthologs from Complete Genome Data

More...
OMAi
ENCIDFI

Family and domain databases

Conserved Domains Database

More...
CDDi
cd02893, FTase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR026872, FTB
IPR001330, PFTB_repeat
IPR008930, Terpenoid_cyclase/PrenylTrfase

The PANTHER Classification System

More...
PANTHERi
PTHR11774:SF6, PTHR11774:SF6, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00432, Prenyltrans, 5 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48239, SSF48239, 1 hit

<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.

P22007-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRQRVGRSIA RAKFINTALL GRKRPVMERV VDIAHVDSSK AIQPLMKELE
60 70 80 90 100
TDTTEARYKV LQSVLEIYDD EKNIEPALTK EFHKMYLDVA FEISLPPQMT
110 120 130 140 150
ALDASQPWML YWIANSLKVM DRDWLSDDTK RKIVDKLFTI SPSGGPFGGG
160 170 180 190 200
PGQLSHLAST YAAINALSLC DNIDGCWDRI DRKGIYQWLI SLKEPNGGFK
210 220 230 240 250
TCLEVGEVDT RGIYCALSIA TLLNILTEEL TEGVLNYLKN CQNYEGGFGS
260 270 280 290 300
CPHVDEAHGG YTFCATASLA ILRSMDQINV EKLLEWSSAR QLQEERGFCG
310 320 330 340 350
RSNKLVDGCY SFWVGGSAAI LEAFGYGQCF NKHALRDYIL YCCQEKEQPG
360 370 380 390 400
LRDKPGAHSD FYHTNYCLLG LAVAESSYSC TPNDSPHNIK CTPDRLIGSS
410 420 430
KLTDVNPVYG LPIENVRKII HYFKSNLSSP S
Length:431
Mass (Da):48,190
Last modified:November 1, 1997 - v2
<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:i2E3B64F30D2FF13A
GO

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 conflicti47K → R in AAT92990 (PubMed:17322287).Curated1

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
M22753 Genomic DNA Translation: AAA34579.1
X95644 Genomic DNA Translation: CAA64921.1
Z74138 Genomic DNA Translation: CAA98656.1
AY692971 Genomic DNA Translation: AAT92990.1
BK006938 Genomic DNA Translation: DAA11768.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S67626, BVBYDP

NCBI Reference Sequences

More...
RefSeqi
NP_010193.1, NM_001180149.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDL090C_mRNA; YDL090C; YDL090C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851468

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDL090C

<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
M22753 Genomic DNA Translation: AAA34579.1
X95644 Genomic DNA Translation: CAA64921.1
Z74138 Genomic DNA Translation: CAA98656.1
AY692971 Genomic DNA Translation: AAT92990.1
BK006938 Genomic DNA Translation: DAA11768.1
PIRiS67626, BVBYDP
RefSeqiNP_010193.1, NM_001180149.1

3D structure databases

SMRiP22007
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi31970, 244 interactors
ComplexPortaliCPX-1634, Protein farnesyltransferase complex
DIPiDIP-1556N
IntActiP22007, 10 interactors
MINTiP22007
STRINGi4932.YDL090C

Chemistry databases

BindingDBiP22007
ChEMBLiCHEMBL2111393

PTM databases

iPTMnetiP22007

Proteomic databases

MaxQBiP22007
PaxDbiP22007
PRIDEiP22007

Genome annotation databases

EnsemblFungiiYDL090C_mRNA; YDL090C; YDL090C
GeneIDi851468
KEGGisce:YDL090C

Organism-specific databases

SGDiS000002248, RAM1
VEuPathDBiFungiDB:YDL090C

Phylogenomic databases

eggNOGiKOG0365, Eukaryota
GeneTreeiENSGT00950000183128
HOGENOMiCLU_028946_0_2_1
InParanoidiP22007
OMAiENCIDFI

Enzyme and pathway databases

ReactomeiR-SCE-9648002, RAS processing

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P22007
RNActiP22007, protein

Family and domain databases

CDDicd02893, FTase, 1 hit
InterProiView protein in InterPro
IPR026872, FTB
IPR001330, PFTB_repeat
IPR008930, Terpenoid_cyclase/PrenylTrfase
PANTHERiPTHR11774:SF6, PTHR11774:SF6, 1 hit
PfamiView protein in Pfam
PF00432, Prenyltrans, 5 hits
SUPFAMiSSF48239, SSF48239, 1 hit

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 nameiFNTB_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: P22007
Secondary accession number(s): D6VRQ8, E9P902, Q12422
<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: August 1, 1991
Last sequence update: November 1, 1997
Last modified: April 7, 2021
This is version 178 of the entry and version 2 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
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
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