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Entry version 147 (07 Apr 2021)
Sequence version 1 (01 Aug 1990)
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Protein

Aconitate hydratase, mitochondrial

Gene

ACO2

Organism
Sus scrofa (Pig)
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 isomerization of citrate to isocitrate via cis-aconitate.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

[4Fe-4S] cluster3 PublicationsNote: Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.2 Publications

<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.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase (CS), Citrate synthase (CS), Citrate synthase, mitochondrial (CS)
  2. Aconitate hydratase, mitochondrial (ACO2), Aconitate hydratase, mitochondrial (ACO2), Aconitate hydratase, mitochondrial (ACO2), Aconitate hydratase, mitochondrial, Aconitate hydratase, mitochondrial, Aconitate hydratase, mitochondrial (ACO2)
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.

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 sitei99Substrate1 Publication1
<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 bindingi385Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi448Iron-sulfur (4Fe-4S)2 Publications1
Metal bindingi451Iron-sulfur (4Fe-4S)2 Publications1
Binding sitei474Substrate1 Publication1
Binding sitei479Substrate1 Publication1
Binding sitei607Substrate1 Publication1

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

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.3, 6170

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

More...
UniPathwayi
UPA00223;UER00718

<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, mitochondrial (EC:4.2.1.31 Publication)
Short name:
Aconitase
Alternative name(s):
Citrate hydro-lyase
<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:ACO2
<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>OrganismiSus scrofa (Pig)
<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 identifieri9823 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaArtiodactylaSuinaSuidaeSus
<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
  • UP000314985 <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: Unplaced
  • UP000008227 Componenti: Unplaced

<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

Mitochondrion

<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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 27MitochondrionAdd BLAST27
<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_000000054328 – 781Aconitate hydratase, mitochondrialAdd BLAST754

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 residuei28Pyrrolidone carboxylic acid1 Publication1
Modified residuei31N6-succinyllysineBy similarity1
Modified residuei50N6-acetyllysine; alternateBy similarity1
Modified residuei50N6-succinyllysine; alternateBy similarity1
Modified residuei138N6-acetyllysine; alternateBy similarity1
Modified residuei138N6-succinyllysine; alternateBy similarity1
Modified residuei144N6-acetyllysine; alternateBy similarity1
Modified residuei144N6-succinyllysine; alternateBy similarity1
Modified residuei233N6-acetyllysine; alternateBy similarity1
Modified residuei233N6-succinyllysine; alternateBy similarity1
Modified residuei411N6-succinyllysineBy similarity1
Modified residuei517N6-acetyllysine; alternateBy similarity1
Modified residuei517N6-succinyllysine; alternateBy similarity1
Modified residuei523N6-acetyllysine; alternateBy similarity1
Modified residuei523N6-succinyllysine; alternateBy similarity1
Modified residuei549N6-succinyllysineBy similarity1
Modified residuei559PhosphoserineBy similarity1
Modified residuei573N6-acetyllysine; alternateBy similarity1
Modified residuei573N6-succinyllysine; alternateBy similarity1
Modified residuei577N6-succinyllysineBy similarity1
Modified residuei591N6-succinyllysineBy similarity1
Modified residuei605N6-acetyllysine; alternateBy similarity1
Modified residuei605N6-succinyllysine; alternateBy similarity1
Modified residuei628N6-succinyllysineBy similarity1
Modified residuei670PhosphoserineBy similarity1
Modified residuei689N6-succinyllysineBy similarity1
Modified residuei723N6-acetyllysine; alternateBy similarity1
Modified residuei723N6-succinyllysine; alternateBy similarity1
Modified residuei730N6-acetyllysine; alternateBy similarity1
Modified residuei730N6-succinyllysine; alternateBy similarity1
Modified residuei736N6-acetyllysineBy similarity1
Modified residuei739N6-acetyllysineBy similarity1
Modified residuei743N6-acetyllysineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Pyrrolidone carboxylic acid

Proteomic databases

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

More...
PaxDbi
P16276

PeptideAtlas

More...
PeptideAtlasi
P16276

PRoteomics IDEntifications database

More...
PRIDEi
P16276

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P16276

<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.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9823.ENSSSCP00000000070

<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

1781
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P16276

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P16276

<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>Regioni192 – 194Substrate binding1 Publication3
Regioni670 – 671Substrate binding1 Publication2

<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

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0453, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P16276

Database of Orthologous Groups

More...
OrthoDBi
190960at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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
IPR015932, Aconitase_dom2
IPR006248, Aconitase_mito-like
IPR000573, AconitaseA/IPMdHydase_ssu_swvl

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00330, Aconitase, 1 hit
PF00694, Aconitase_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00415, ACONITASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53732, SSF53732, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01340, aconitase_mito, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P16276-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPYSLLVTR LQKALGVRQY HVASVLCQRA KVAMSHFEPH EYIRYDLLEK
60 70 80 90 100
NIDIVRKRLN RPLTLSEKIV YGHLDDPANQ EIERGKTYLR LRPDRVAMQD
110 120 130 140 150
ATAQMAMLQF ISSGLPKVAV PSTIHCDHLI EAQLGGEKDL RRAKDINQEV
160 170 180 190 200
YNFLATAGAK YGVGFWRPGS GIIHQIILEN YAYPGVLLIG TDSHTPNGGG
210 220 230 240 250
LGGICIGVGG ADAVDVMAGI PWELKCPKVI GVKLTGSLSG WTSPKDVILK
260 270 280 290 300
VAGILTVKGG TGAIVEYHGP GVDSISCTGM ATICNMGAEI GATTSVFPYN
310 320 330 340 350
HRMKKYLSKT GRADIANLAD EFKDHLVPDP GCHYDQVIEI NLSELKPHIN
360 370 380 390 400
GPFTPDLAHP VAEVGSVAEK EGWPLDIRVG LIGSCTNSSY EDMGRSAAVA
410 420 430 440 450
KQALAHGLKC KSQFTITPGS EQIRATIERD GYAQVLRDVG GIVLANACGP
460 470 480 490 500
CIGQWDRKDI KKGEKNTIVT SYNRNFTGRN DANPETHAFV TSPEIVTALA
510 520 530 540 550
IAGTLKFNPE TDFLTGKDGK KFKLEAPDAD ELPRAEFDPG QDTYQHPPKD
560 570 580 590 600
SSGQRVDVSP TSQRLQLLEP FDKWDGKDLE DLQILIKVKG KCTTDHISAA
610 620 630 640 650
GPWLKFRGHL DNISNNLLIG AINIENRKAN SVRNAVTQEF GPVPDTARYY
660 670 680 690 700
KQHGIRWVVI GDENYGEGSS REHRALEPRH LGGRAIITKS FARIHETNLK
710 720 730 740 750
KQGLLPLTFA DPADYNKIHP VDKLTIQGLK DFAPGKPLKC IIKHPNGTQE
760 770 780
TILLNHTFNE TQIEWFRAGS ALNRMKELQQ K
Length:781
Mass (Da):85,761
Last modified:August 1, 1990 - 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:i5737FD9BCFCEF184
GO

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
J05224 mRNA Translation: AAA30987.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A35544

NCBI Reference Sequences

More...
RefSeqi
NP_999119.1, NM_213954.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
396999

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ssc:396999

<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
J05224 mRNA Translation: AAA30987.1
PIRiA35544
RefSeqiNP_999119.1, NM_213954.1

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
1B0JX-ray2.50A28-781[»]
1B0KX-ray2.50A29-781[»]
1B0MX-ray2.50A29-781[»]
5ACNX-ray2.10A29-781[»]
6ACNX-ray2.50A29-781[»]
7ACNX-ray2.00A29-781[»]
SMRiP16276
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000000070

PTM databases

CarbonylDBiP16276

Proteomic databases

PaxDbiP16276
PeptideAtlasiP16276
PRIDEiP16276

Genome annotation databases

GeneIDi396999
KEGGissc:396999

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
50

Phylogenomic databases

eggNOGiKOG0453, Eukaryota
InParanoidiP16276
OrthoDBi190960at2759

Enzyme and pathway databases

UniPathwayiUPA00223;UER00718
BRENDAi4.2.1.3, 6170

Miscellaneous databases

EvolutionaryTraceiP16276

Family and domain databases

Gene3Di3.20.19.10, 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
IPR015932, Aconitase_dom2
IPR006248, Aconitase_mito-like
IPR000573, AconitaseA/IPMdHydase_ssu_swvl
PfamiView protein in Pfam
PF00330, Aconitase, 1 hit
PF00694, Aconitase_C, 1 hit
PRINTSiPR00415, ACONITASE
SUPFAMiSSF53732, SSF53732, 1 hit
TIGRFAMsiTIGR01340, aconitase_mito, 1 hit
PROSITEiView protein in PROSITE
PS00450, ACONITASE_1, 1 hit
PS01244, ACONITASE_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 nameiACON_PIG
<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: P16276
<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, 1990
Last sequence update: August 1, 1990
Last modified: April 7, 2021
This is version 147 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, Direct protein sequencing, Reference proteome

Documents

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