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Entry version 168 (08 May 2019)
Sequence version 1 (01 Apr 1993)
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Protein

Protein farnesyltransferase subunit beta

Gene

Fntb

Organism
Rattus norvegicus (Rat)
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 the farnesyltransferase complex. Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X.4 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 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+12 PublicationsNote: Binds 1 zinc ion per subunit.12 Publications

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>Sitei102Important for selectivity against geranylgeranyl diphosphateBy similarity1
<p>This subsection of the ‘Function’ 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 bindingi297Zinc; catalytic3 Publications1
Metal bindingi299Zinc; catalytic3 Publications1
Metal bindingi362Zinc; via tele nitrogen; catalytic3 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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.5.1.58 5301

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-2514859 Inactivation, recovery and regulation of the phototransduction cascade

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q02293

<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 subunit beta (EC:2.5.1.58)
Short name:
FTase-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_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:Fntb
<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>OrganismiRattus norvegicus (Rat)
<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 identifieri10116 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<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
  • UP000002494 <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 6

Organism-specific databases

Rat genome database

More...
RGDi
620119 Fntb

<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

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL2095197

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001197631 – 437Protein farnesyltransferase subunit betaAdd BLAST437

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 residuei432PhosphoserineBy similarity1
Modified residuei436PhosphothreonineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q02293

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

More...
PaxDbi
Q02293

PRoteomics IDEntifications database

More...
PRIDEi
Q02293

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q02293

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

More...
PhosphoSitePlusi
Q02293

<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

More...
Bgeei
ENSRNOG00000007660 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q02293 RN

<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

Heterodimer of FNTA and FNTB.14 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
FntaQ0463116EBI-602454,EBI-602447

Protein-protein interaction databases

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-2181 Protein farnesyltransferase complex

Database of interacting proteins

More...
DIPi
DIP-6132N

Protein interaction database and analysis system

More...
IntActi
Q02293, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000010588

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q02293

<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

1437
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00B1-437[»]
1D8EX-ray3.00B1-437[»]
1FPPX-ray2.75B1-437[»]
1FT1X-ray2.25B1-437[»]
1FT2X-ray3.40B22-422[»]
1FTImodel-B22-422[»]
1HZ7model-B41-406[»]
1JCRX-ray2.00B1-437[»]
1JCSX-ray2.20B1-437[»]
1KZOX-ray2.20B1-437[»]
1KZPX-ray2.10B1-437[»]
1KZRmodel-B17-423[»]
1N94X-ray3.50B22-418[»]
1N95X-ray2.30B22-423[»]
1N9AX-ray3.20B22-423[»]
1NI1X-ray2.30B22-423[»]
1NL4X-ray2.70B23-423[»]
1O1RX-ray2.30B1-427[»]
1O1SX-ray2.30B1-427[»]
1O1TX-ray2.10B1-427[»]
1O5MX-ray2.30B1-437[»]
1QBQX-ray2.40B1-437[»]
1QE2model-B41-406[»]
1SA5X-ray2.60B1-437[»]
1TN7X-ray2.30B1-437[»]
1TN8X-ray2.25B1-437[»]
1X81X-ray3.50B22-418[»]
2BEDX-ray2.70B23-423[»]
2FTImodel-B22-422[»]
2R2LX-ray2.23B23-423[»]
2ZIRX-ray2.40B1-437[»]
2ZISX-ray2.60B1-437[»]
3DPYX-ray2.70B1-437[»]
3E30X-ray2.45B1-437[»]
3E32X-ray2.45B1-437[»]
3E33X-ray1.90B1-437[»]
3E34X-ray2.05B1-437[»]
3EU5X-ray2.80B1-427[»]
3EUVX-ray2.75B1-427[»]
3FTImodel-B22-422[»]
3KSLX-ray2.05B1-437[»]
3KSQX-ray2.10B1-437[»]
4GTMX-ray2.20B1-427[»]
4GTOX-ray2.15B1-427[»]
4GTPX-ray2.75B1-427[»]
4GTQX-ray2.60B1-427[»]
4GTRX-ray2.20B1-427[»]

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

More...
SMRi
Q02293

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q02293

<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>Repeati123 – 164PFTB 1Add BLAST42
Repeati174 – 215PFTB 2Add BLAST42
Repeati222 – 263PFTB 3Add BLAST42
Repeati270 – 312PFTB 4Add BLAST43
Repeati332 – 374PFTB 5Add BLAST43

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>Regioni248 – 251Farnesyl diphosphate binding4
Regioni291 – 294Farnesyl diphosphate binding4
Regioni300 – 303Farnesyl diphosphate binding4

<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
COG5029 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183128

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000190594

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q02293

KEGG Orthology (KO)

More...
KOi
K05954

Identification of Orthologs from Complete Genome Data

More...
OMAi
LYHTCYT

Database of Orthologous Groups

More...
OrthoDBi
1042804at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q02293

TreeFam database of animal gene trees

More...
TreeFami
TF353162

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_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>Sequencei

<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.

Q02293-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASSSSFTYY CPPSSSPVWS EPLYSLRPEH ARERLQDDSV ETVTSIEQAK
60 70 80 90 100
VEEKIQEVFS SYKFNHLVPR LVLQREKHFH YLKRGLRQLT DAYECLDASR
110 120 130 140 150
PWLCYWILHS LELLDEPIPQ IVATDVCQFL ELCQSPDGGF GGGPGQYPHL
160 170 180 190 200
APTYAAVNAL CIIGTEEAYN VINREKLLQY LYSLKQPDGS FLMHVGGEVD
210 220 230 240 250
VRSAYCAASV ASLTNIITPD LFEGTAEWIA RCQNWEGGIG GVPGMEAHGG
260 270 280 290 300
YTFCGLAALV ILKKERSLNL KSLLQWVTSR QMRFEGGFQG RCNKLVDGCY
310 320 330 340 350
SFWQAGLLPL LHRALHAQGD PALSMSHWMF HQQALQEYIL MCCQCPAGGL
360 370 380 390 400
LDKPGKSRDF YHTCYCLSGL SIAQHFGSGA MLHDVVMGVP ENVLQPTHPV
410 420 430
YNIGPDKVIQ ATTHFLQKPV PGFEECEDAV TSDPATD
Length:437
Mass (Da):48,673
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:i41A9D6D79CD319A8
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
M69056 mRNA Translation: AAA41176.1
BC087675 mRNA Translation: AAH87675.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A40037

NCBI Reference Sequences

More...
RefSeqi
NP_742031.1, NM_172034.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
64511

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:64511

UCSC genome browser

More...
UCSCi
RGD:620119 rat

<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
M69056 mRNA Translation: AAA41176.1
BC087675 mRNA Translation: AAH87675.1
PIRiA40037
RefSeqiNP_742031.1, NM_172034.2

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1D8DX-ray2.00B1-437[»]
1D8EX-ray3.00B1-437[»]
1FPPX-ray2.75B1-437[»]
1FT1X-ray2.25B1-437[»]
1FT2X-ray3.40B22-422[»]
1FTImodel-B22-422[»]
1HZ7model-B41-406[»]
1JCRX-ray2.00B1-437[»]
1JCSX-ray2.20B1-437[»]
1KZOX-ray2.20B1-437[»]
1KZPX-ray2.10B1-437[»]
1KZRmodel-B17-423[»]
1N94X-ray3.50B22-418[»]
1N95X-ray2.30B22-423[»]
1N9AX-ray3.20B22-423[»]
1NI1X-ray2.30B22-423[»]
1NL4X-ray2.70B23-423[»]
1O1RX-ray2.30B1-427[»]
1O1SX-ray2.30B1-427[»]
1O1TX-ray2.10B1-427[»]
1O5MX-ray2.30B1-437[»]
1QBQX-ray2.40B1-437[»]
1QE2model-B41-406[»]
1SA5X-ray2.60B1-437[»]
1TN7X-ray2.30B1-437[»]
1TN8X-ray2.25B1-437[»]
1X81X-ray3.50B22-418[»]
2BEDX-ray2.70B23-423[»]
2FTImodel-B22-422[»]
2R2LX-ray2.23B23-423[»]
2ZIRX-ray2.40B1-437[»]
2ZISX-ray2.60B1-437[»]
3DPYX-ray2.70B1-437[»]
3E30X-ray2.45B1-437[»]
3E32X-ray2.45B1-437[»]
3E33X-ray1.90B1-437[»]
3E34X-ray2.05B1-437[»]
3EU5X-ray2.80B1-427[»]
3EUVX-ray2.75B1-427[»]
3FTImodel-B22-422[»]
3KSLX-ray2.05B1-437[»]
3KSQX-ray2.10B1-437[»]
4GTMX-ray2.20B1-427[»]
4GTOX-ray2.15B1-427[»]
4GTPX-ray2.75B1-427[»]
4GTQX-ray2.60B1-427[»]
4GTRX-ray2.20B1-427[»]
SMRiQ02293
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

ComplexPortaliCPX-2181 Protein farnesyltransferase complex
DIPiDIP-6132N
IntActiQ02293, 1 interactor
STRINGi10116.ENSRNOP00000010588

Chemistry databases

BindingDBiQ02293
ChEMBLiCHEMBL2095197

PTM databases

iPTMnetiQ02293
PhosphoSitePlusiQ02293

Proteomic databases

jPOSTiQ02293
PaxDbiQ02293
PRIDEiQ02293

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000010588; ENSRNOP00000010588; ENSRNOG00000007660
GeneIDi64511
KEGGirno:64511
UCSCiRGD:620119 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2342
RGDi620119 Fntb

Phylogenomic databases

eggNOGiKOG0365 Eukaryota
COG5029 LUCA
GeneTreeiENSGT00950000183128
HOGENOMiHOG000190594
InParanoidiQ02293
KOiK05954
OMAiLYHTCYT
OrthoDBi1042804at2759
PhylomeDBiQ02293
TreeFamiTF353162

Enzyme and pathway databases

BRENDAi2.5.1.58 5301
ReactomeiR-RNO-2514859 Inactivation, recovery and regulation of the phototransduction cascade
SABIO-RKiQ02293

Miscellaneous databases

EvolutionaryTraceiQ02293

Protein Ontology

More...
PROi
PR:Q02293

Gene expression databases

BgeeiENSRNOG00000007660 Expressed in 10 organ(s), highest expression level in skeletal muscle tissue
GenevisibleiQ02293 RN

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

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<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_RAT
<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: Q02293
<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: April 1, 1993
Last sequence update: April 1, 1993
Last modified: May 8, 2019
This is version 168 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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