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Entry version 82 (11 Dec 2019)
Sequence version 2 (18 Sep 2019)
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Protein

Farnesyl pyrophosphate synthase

Gene

FPS1

Organism
Artemisia annua (Sweet wormwood)
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

Involved in the biosynthesis of the antimalarial endoperoxide artemisinin (Ref. 7, Ref. 9, PubMed:24689216, PubMed:10814821). Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (PubMed:8682304). Promotes anti-malarial and antimicrobial (toward Gram-positive bacteria B.subtilis and S.aureus) activities of plant crude extract probably by triggering artemisinin levels (PubMed:24689216).5 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

Mg2+By similarityNote: Binds 2 Mg2+ ions per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: farnesyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate.2 Publications
Proteins known to be involved in this subpathway in this organism are:
  1. Farnesyl pyrophosphate synthase (FPS1)
This subpathway is part of the pathway farnesyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate, the pathway farnesyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Pathwayi: Sesquiterpene biosynthesis

This protein is involved in Sesquiterpene biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in Sesquiterpene biosynthesis.

Pathwayi: geranyl diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate.1 Publication
Proteins known to be involved in this subpathway in this organism are:
  1. Farnesyl pyrophosphate synthase (FPS1)
This subpathway is part of the pathway geranyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate, the pathway geranyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei49Isopentenyl diphosphateBy similarity1
Binding sitei52Isopentenyl diphosphateBy similarity1
Binding sitei87Isopentenyl diphosphateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi94Magnesium 1By similarity1
Metal bindingi94Magnesium 2By similarity1
Metal bindingi98Magnesium 1By similarity1
Metal bindingi98Magnesium 2By similarity1
Binding sitei103Dimethylallyl diphosphateBy similarity1
Binding sitei104Isopentenyl diphosphateBy similarity1
Binding sitei191Dimethylallyl diphosphateBy similarity1
Binding sitei192Dimethylallyl diphosphateBy similarity1
Binding sitei230Dimethylallyl diphosphateBy similarity1
Binding sitei247Dimethylallyl diphosphateBy similarity1
Binding sitei256Dimethylallyl diphosphateBy similarity1

<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 functionTransferase
Biological processCholesterol biosynthesis, Cholesterol metabolism, Isoprene biosynthesis, Lipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-17882

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00259;UER00368
UPA00260;UER00369

<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:
Farnesyl pyrophosphate synthase (EC:2.5.1.102 Publications)
Short name:
FPP synthase1 Publication
Short name:
FPS1 Publication
Alternative name(s):
(2E,6E)-farnesyl diphosphate synthase1 Publication
Dimethylallyltranstransferase (EC:2.5.1.11 Publication)
Farnesyl diphosphate synthase1 Publication
Geranyltranstransferase
<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:FPS11 Publication
Synonyms:FDS1 Publication, FPPS1 Publication
ORF Names:CTI12_AA043570Imported
<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>OrganismiArtemisia annua (Sweet wormwood)
<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 identifieri35608 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeAnthemideaeArtemisiinaeArtemisia
<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
  • UP000245207 <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: Unassembled WGS sequence

<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 Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<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 use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Plants overexpressing FPS1 accumulate higher levels of artemisinin.3 Publications

<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

Reduced growth and lower artemisinin levels.1 Publication

<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_00001239541 – 343Farnesyl pyrophosphate synthaseAdd BLAST343

<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

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed both in apical and sub-apical cells of glandular secretory trichomes.2 Publications

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Strongly induced by gibberellic acid (GA3) leading to an increased artemisinin yield.1 Publication

<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

<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 FPP/GGPP synthase family.Curated

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.600.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR039702 FPS1-like
IPR008949 Isoprenoid_synthase_dom_sf
IPR000092 Polyprenyl_synt
IPR033749 Polyprenyl_synt_CS

The PANTHER Classification System

More...
PANTHERi
PTHR11525 PTHR11525, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00348 polyprenyl_synt, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48576 SSF48576, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00723 POLYPRENYL_SYNTHASE_1, 1 hit
PS00444 POLYPRENYL_SYNTHASE_2, 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>. 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_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.

P49350-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSIDLKSKF LKVYDTLKSE LINDPAFEFD DDSRQWIEKM LDYNVPGGKL
60 70 80 90 100
NRGLSVVDSY QLLKGGELSD DEIFLSSALG WCIEWLQAYF LVLDDIMDES
110 120 130 140 150
HTRRGQPCWF RLPKVGMIAA NDGILLRNHV PRILKKHFRG KPYYVDLVDL
160 170 180 190 200
FNEVEFQTAS GQMIDLITTL VGEKDLSKYS LSIHRRIVQY KTAYYSFYLP
210 220 230 240 250
VACALLMFGE DLDKHVEVKN VLVEMGTYFQ VQDDYLDCFG APEVIGKIGT
260 270 280 290 300
DIEDFKCSWL VVKALELANE EQKKVLHENY GKKDPASVAK VKEVYHTLNL
310 320 330 340
QAVFEDYEAT SYKKLITSIE NHPSKAVQAV LKSFLGKIYK RQK
Length:343
Mass (Da):39,404
Last modified:September 18, 2019 - 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:i0A49F4F28B4FE1A3
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 conflicti4I → T in AAC49452 (PubMed:8682304).Curated1
Sequence conflicti45V → I in ADJ67472 (Ref. 4) Curated1
Sequence conflicti45V → I in AIC83778 (Ref. 5) Curated1
Sequence conflicti113P → L in AAD17204 (PubMed:10814821).Curated1
Sequence conflicti113P → L in ADJ67472 (Ref. 4) Curated1
Sequence conflicti113P → L in AIC83778 (Ref. 5) Curated1
Sequence conflicti113P → L in AAD32648 (Ref. 2) Curated1
Sequence conflicti145V → E in ADJ67472 (Ref. 4) Curated1
Sequence conflicti145V → E in AIC83778 (Ref. 5) Curated1
Sequence conflicti154 – 156VEF → GVI in AAD32648 (Ref. 2) Curated3
Sequence conflicti168T → P in AAD32648 (Ref. 2) Curated1
Sequence conflicti221V → M in AAD17204 (PubMed:10814821).Curated1
Sequence conflicti221V → M in ADJ67472 (Ref. 4) Curated1
Sequence conflicti221V → M in AIC83778 (Ref. 5) Curated1
Sequence conflicti221V → M in AAD32648 (Ref. 2) Curated1
Sequence conflicti268A → P in AAC49452 (PubMed:8682304).Curated1
Sequence conflicti275V → T in AAC49452 (PubMed:8682304).Curated1
Sequence conflicti322H → R in AAD17204 (PubMed:10814821).Curated1
Sequence conflicti322H → R in ADJ67472 (Ref. 4) Curated1
Sequence conflicti322H → R in AIC83778 (Ref. 5) Curated1
Sequence conflicti322H → R in AAD32648 (Ref. 2) 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
U36376 mRNA Translation: AAC49452.1
AF136602 mRNA Translation: AAD32648.1
AF112881 mRNA Translation: AAD17204.1
GQ420346 mRNA Translation: ADJ67472.1
KJ609177 mRNA Translation: AIC83778.1
PKPP01000340 Genomic DNA Translation: PWA94011.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JC4846

<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
U36376 mRNA Translation: AAC49452.1
AF136602 mRNA Translation: AAD32648.1
AF112881 mRNA Translation: AAD17204.1
GQ420346 mRNA Translation: ADJ67472.1
KJ609177 mRNA Translation: AIC83778.1
PKPP01000340 Genomic DNA Translation: PWA94011.1
PIRiJC4846

3D structure databases

Database of comparative protein structure models

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ModBasei
Search...

SWISS-MODEL Interactive Workspace

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SWISS-MODEL-Workspacei
Submit a new modelling project...

Enzyme and pathway databases

UniPathwayiUPA00259;UER00368
UPA00260;UER00369
BioCyciMetaCyc:MONOMER-17882

Family and domain databases

Gene3Di1.10.600.10, 1 hit
InterProiView protein in InterPro
IPR039702 FPS1-like
IPR008949 Isoprenoid_synthase_dom_sf
IPR000092 Polyprenyl_synt
IPR033749 Polyprenyl_synt_CS
PANTHERiPTHR11525 PTHR11525, 1 hit
PfamiView protein in Pfam
PF00348 polyprenyl_synt, 1 hit
SUPFAMiSSF48576 SSF48576, 1 hit
PROSITEiView protein in PROSITE
PS00723 POLYPRENYL_SYNTHASE_1, 1 hit
PS00444 POLYPRENYL_SYNTHASE_2, 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 nameiFPPS_ARTAN
<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: P49350
Secondary accession number(s): A0A2U1Q7M0
, E2D028, Q9SYX3, Q9ZPJ3
<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: September 18, 2019
Last modified: December 11, 2019
This is version 82 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 programPlant 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
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