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Entry version 112 (10 Feb 2021)
Sequence version 1 (01 Mar 2002)
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Protein

Aconitate hydratase B

Gene

acnB

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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 catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein which regulates FliC synthesis via interaction with the ftsH transcript to decrease the intracellular levels of FtsH. The lower levels of FtsH protease activity then influence sigma-32, DnaK and ultimately FliC production.

2 Publications

<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

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tricarboxylic acid cycle

This protein is involved in step 2 of the subpathway that synthesizes isocitrate from oxaloacetate.1 Publication This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

Pathwayi: propanoate degradation

This protein is involved in the pathway propanoate degradation, which is part of Organic acid metabolism.1 Publication
View all proteins of this organism that are known to be involved in the pathway propanoate degradation and in Organic acid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei191SubstrateBy similarity1
Binding sitei498SubstrateBy 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 bindingi710Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi769Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi772Iron-sulfur (4Fe-4S)By similarity1
Binding sitei791SubstrateBy similarity1
Binding sitei796SubstrateBy 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

  • propionate catabolic process, 2-methylcitrate cycle Source: UniProtKB
  • tricarboxylic acid cycle Source: UniProtKB

<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 functionLyase, RNA-binding
Biological processTricarboxylic acid cycle
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:MONOMER-13618

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

More...
UniPathwayi
UPA00223;UER00718
UPA00946

<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:
Aconitate hydratase B1 Publication (EC:4.2.1.31 Publication)
Short name:
ACN1 Publication
Short name:
Aconitase1 Publication
Alternative name(s):
(2R,3S)-2-methylisocitrate dehydratase1 Publication
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase1 Publication
2-methyl-cis-aconitate hydratase1 Publication (EC:4.2.1.991 Publication)
Iron-responsive protein-like1 Publication
Short name:
IRP-like1 Publication
RNA-binding protein1 Publication
<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:acnB
Ordered Locus Names:STM0158
<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>OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
<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 identifieri99287 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
<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
  • UP000001014 <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

<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

<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

Cells lacking this gene do not grow on propionate unless glutamate is added, and the addition of glutamate does not restore growth to the level of wild-type. Also unable to grow on acetate and citrate and only slight improvements are observed when glutamate is added. AcnB mutant also shows an impaired binding to the surface of macrophage-like cells, is less motile and possesses fewer flagella due to a level of the flagellum protein FliC lower. The acnAB double mutant does not grow on propionate even when supplemented with glutamate and is unable to respire propionate under anaerobic growth conditions.2 Publications

<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_00004329811 – 865Aconitate hydratase BAdd BLAST865

Proteomic databases

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

More...
PaxDbi
Q8ZRS8

PRoteomics IDEntifications database

More...
PRIDEi
Q8ZRS8

<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

Monomer.

By similarity

<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
Q8ZRS8

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

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>Regioni244 – 246Substrate bindingBy similarity3
Regioni414 – 416Substrate bindingBy similarity3

<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 aconitase/IPM isomerase family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_016536_0_0_6

Identification of Orthologs from Complete Genome Data

More...
OMAi
QDTTGAM

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q8ZRS8

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01576, AcnB_Swivel, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.25.40.310, 1 hit
3.20.19.10, 1 hit
3.30.499.10, 2 hits
3.40.1060.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR015931, Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030, Acoase/IPM_deHydtase_lsu_aba
IPR015928, Aconitase/3IPM_dehydase_swvl
IPR018136, Aconitase_4Fe-4S_BS
IPR036008, Aconitase_4Fe-4S_dom
IPR004406, Aconitase_B
IPR015933, Aconitase_B_HEAT-like_dom
IPR036288, Aconitase_B_HEAT-like_dom_sf
IPR015929, Aconitase_B_swivel
IPR015932, Aconitase_dom2

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00330, Aconitase, 1 hit
PF06434, Aconitase_2_N, 1 hit
PF11791, Aconitase_B_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036687, AcnB, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53732, SSF53732, 1 hit
SSF74778, SSF74778, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00117, acnB, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00450, ACONITASE_1, 1 hit
PS01244, ACONITASE_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%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.

Q8ZRS8-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLEEYRKHVA ERAAQGIVPK PLDATQMAAL VELLKTPPVG EEEFLLDLLI
60 70 80 90 100
NRVPPGVDEA AYVKAGFLAA VAKGDTTSPL VSPEKAIELL GTMQGGYNIH
110 120 130 140 150
PLIDALDDAK LAPIAAKALS HTLLMFDNFY DVEEKAKAGN EYAKQVMQSW
160 170 180 190 200
ADAEWFLSRP PLAEKITVTV FKVTGETNTD DLSPAPDAWS RPDIPLHAQA
210 220 230 240 250
MLKNAREGIE PDQPGVVGPI KQIEALQKKG YPLAYVGDVV GTGSSRKSAT
260 270 280 290 300
NSVLWFMGDD IPNVPNKRGG GLCLGGKIAP IFFNTMEDAG ALPIEVDVSN
310 320 330 340 350
LNMGDVIDVY PYKGEVRNHE TGELLATFEL KTDVLIDEVR AGGRIPLIIG
360 370 380 390 400
RGLTTKAREA LGLPHSDVFR QAKDVAESSR GFSLAQKMVG RACGVKGIRP
410 420 430 440 450
GAYCEPKMTS VGSQDTTGPM TRDELKDLAC LGFSADLVMQ SFCHTAAYPK
460 470 480 490 500
PVDVTTHHTL PDFIMNRGGV SLRPGDGVIH SWLNRMLLPD TVGTGGDSHT
510 520 530 540 550
RFPIGISFPA GSGLVAFAAA TGVMPLDMPE SVLVRFKGKM QPGITLRDLV
560 570 580 590 600
HAIPLYAIKQ GLLTVEKKGK KNIFSGRILE IEGLPDLKVE QAFELTDASA
610 620 630 640 650
ERSAAGCTIK LNKEPIVEYL TSNIVLLKWM IAEGYGDRRT LERRIQGMEK
660 670 680 690 700
WLADPQLLEA DADAEYAAVI DIDLADIKEP ILCAPNDPDD ARLLSDVQGE
710 720 730 740 750
KIDEVFIGSC MTNIGHFRAA GKLLDNHKGQ LPTRLWVAPP TRMDAAQLTE
760 770 780 790 800
EGYYSVFGKS GARIEIPGCS LCMGNQARVA DGATVVSTST RNFPNRLGTG
810 820 830 840 850
ANVFLASAEL AAVAALIGKL PTPEEYQTYV AQVDKTAVDT YRYLNFDQLS
860
QYTEKADGVI FQTAV
Length:865
Mass (Da):93,529
Last modified:March 1, 2002 - 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:iD287309CB026151D
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
AE006468 Genomic DNA Translation: AAL19122.1

NCBI Reference Sequences

More...
RefSeqi
NP_459163.1, NC_003197.2
WP_000888962.1, NC_003197.2

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAL19122; AAL19122; STM0158

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1251676

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
stm:STM0158

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|99287.12.peg.168

<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
AE006468 Genomic DNA Translation: AAL19122.1
RefSeqiNP_459163.1, NC_003197.2
WP_000888962.1, NC_003197.2

3D structure databases

SMRiQ8ZRS8
ModBaseiSearch...

Proteomic databases

PaxDbiQ8ZRS8
PRIDEiQ8ZRS8

Genome annotation databases

EnsemblBacteriaiAAL19122; AAL19122; STM0158
GeneIDi1251676
KEGGistm:STM0158
PATRICifig|99287.12.peg.168

Phylogenomic databases

HOGENOMiCLU_016536_0_0_6
OMAiQDTTGAM
PhylomeDBiQ8ZRS8

Enzyme and pathway databases

UniPathwayiUPA00223;UER00718
UPA00946
BioCyciMetaCyc:MONOMER-13618

Family and domain databases

CDDicd01576, AcnB_Swivel, 1 hit
Gene3Di1.25.40.310, 1 hit
3.20.19.10, 1 hit
3.30.499.10, 2 hits
3.40.1060.10, 1 hit
InterProiView protein in InterPro
IPR015931, Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030, Acoase/IPM_deHydtase_lsu_aba
IPR015928, Aconitase/3IPM_dehydase_swvl
IPR018136, Aconitase_4Fe-4S_BS
IPR036008, Aconitase_4Fe-4S_dom
IPR004406, Aconitase_B
IPR015933, Aconitase_B_HEAT-like_dom
IPR036288, Aconitase_B_HEAT-like_dom_sf
IPR015929, Aconitase_B_swivel
IPR015932, Aconitase_dom2
PfamiView protein in Pfam
PF00330, Aconitase, 1 hit
PF06434, Aconitase_2_N, 1 hit
PF11791, Aconitase_B_N, 1 hit
PIRSFiPIRSF036687, AcnB, 1 hit
SUPFAMiSSF53732, SSF53732, 1 hit
SSF74778, SSF74778, 1 hit
TIGRFAMsiTIGR00117, acnB, 1 hit
PROSITEiView protein in PROSITE
PS00450, ACONITASE_1, 1 hit
PS01244, ACONITASE_2, 1 hit

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 nameiACNB_SALTY
<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: Q8ZRS8
<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 29, 2015
Last sequence update: March 1, 2002
Last modified: February 10, 2021
This is version 112 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 programProkaryotic 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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