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Entry version 204 (17 Jun 2020)
Sequence version 3 (10 Oct 2002)
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Protein

Bifunctional purine biosynthesis protein ATIC

Gene

ATIC

Organism
Homo sapiens (Human)
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

Bifunctional enzyme that catalyzes the last two steps of purine biosynthesis (PubMed:11948179, PubMed:14756554). Acts as a transformylase that incorporates a formyl group to the AMP analog AICAR (5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) to produce the intermediate formyl-AICAR (FAICAR) (PubMed:9378707, PubMed:11948179, PubMed:10985775). Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction (PubMed:10985775). Also catalyzes the cyclization of FAICAR to IMP (PubMed:11948179, PubMed:14756554). Is able to convert thio-AICAR to 6-mercaptopurine ribonucleotide, an inhibitor of purine biosynthesis used in the treatment of human leukemias (PubMed:10985775). Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (PubMed:25687571).5 Publications

Miscellaneous

The de novo purine synthesis pathway includes 10 sequential steps, beginning with phosphoribosyl pyrophosphate and ending with inositol monophosphate (IMP), the first purin compound of the pathway.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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

AMP and XMP inhibit AICAR formyltransferase activity (PubMed:10985775). AICAR formyltransferase activity is inhibited by N-(6-fluoro-1-oxo-1,2-dihydroisoquinolin-7-yl)-5- [(3R)-3-hydroxypyrrolidin-1-yl]thiophene-2-sulfonamide (LSN 3213128), which acts as a tumor suppression in cancer cell lines (PubMed:29072452).2 Publications

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

kcat is 3.7 sec(-1) for AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:10985775). kcat is 4.1 sec(-1) for AICAR formyltransferase activity with 10-formyldihydrofolate as substrate (PubMed:10985775). kcat is 2.9 sec(-1) for AICAR formyltransferase activity with (6S)-10-formyltetrahydrofolate as substrate (PubMed:11948179). kcat is 6.0 sec(-1) for FAICAR cyclization activity (PubMed:11948179). kcat is 8.6 sec(-1) for FAICAR cyclization activity (PubMed:14756554).3 Publications
  1. KM=10 µM for 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate)1 Publication
  2. KM=1.5 µM for 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with 10-formyldihydrofolate as cosubstrate)1 Publication
  3. KM=1.9 µM for 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate)1 Publication
  4. KM=110 µM for (6S)-10-formyltetrahydrofolate1 Publication
  5. KM=100 µM for (6S)-10-formyltetrahydrofolate1 Publication
  6. KM=39 µM for (6S)-10-formyltetrahydrofolate1 Publication
  7. KM=11 µM for 10-formyldihydrofolate1 Publication
  8. KM=1.4 µM for 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide1 Publication
  9. KM=0.9 µM for 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide1 Publication

    <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: IMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route).1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional purine biosynthesis protein ATIC (ATIC)
    This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    Pathwayi: IMP biosynthesis via de novo pathway

    This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.1 Publication
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional purine biosynthesis protein ATIC (ATIC)
    This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei137Proton donor/acceptor; for FAICAR cyclization activity1 Publication1
    <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>Sitei266Transition state stabilizer1 Publication1
    Active sitei267Proton acceptor; for AICAR formyltransferase activity1 Publication1
    <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 sitei267AICARCombined sources2 Publications1
    Binding sitei316AICAR; via carbonyl oxygenCombined sources2 Publications1
    Binding sitei339AICARCombined sources2 Publications1
    Binding sitei431AICAR; shared with dimeric partnerCombined sources2 Publications1
    Binding sitei451AICAR; shared with dimeric partnerCombined sources2 Publications1
    Binding sitei45210-formyltetrahydrofolate; via amide nitrogenBy similarity1
    Binding sitei541AICAR; via carbonyl oxygen; shared with dimeric partnerCombined sources2 Publications1
    Binding sitei54610-formyltetrahydrofolateBy similarity1
    Binding sitei588AICAR; shared with dimeric partnerCombined sources2 Publications1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi12 – 14IMPCombined sources2 Publications3
    Nucleotide bindingi34 – 37IMPCombined sources2 Publications4
    Nucleotide bindingi64 – 67IMPCombined sources2 Publications4
    Nucleotide bindingi101 – 102IMPCombined sources2 Publications2
    Nucleotide bindingi125 – 126IMPCombined sources2 Publications2

    <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 functionHydrolase, Multifunctional enzyme, Transferase
    Biological processPurine biosynthesis

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:HS06490-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.1.2.3 2681
    3.5.4.10 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-73817 Purine ribonucleoside monophosphate biosynthesis

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P31939

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    P31939

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

    More...
    UniPathwayi
    UPA00074;UER00133
    UPA00074;UER00135

    <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:
    Bifunctional purine biosynthesis protein ATIC
    Alternative name(s):
    AICAR transformylase/inosine monophosphate cyclohydrolase
    Short name:
    ATIC
    Cleaved into the following chain:
    Including the following 2 domains:
    Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.33 Publications)
    Alternative name(s):
    5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase1 Publication
    Short name:
    AICAR formyltransferase1 Publication
    AICAR transformylase
    Inosine 5'-monophosphate cyclohydrolase1 Publication (EC:3.5.4.102 Publications)
    Short name:
    IMP cyclohydrolase1 Publication
    Alternative name(s):
    IMP synthase
    Inosinicase
    <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:ATICImported
    Synonyms:PURH
    ORF Names:OK/SW-cl.86
    <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>OrganismiHomo sapiens (Human)
    <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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <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
    • UP000005640 <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 2

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000138363.14

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:794 ATIC

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    601731 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P31939

    <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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

    <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 provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

    AICAR transformylase/IMP cyclohydrolase deficiency (AICAR)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA neurologically devastating inborn error of purine biosynthesis. Patients excrete massive amounts of AICA-riboside in the urine and accumulate AICA-ribotide and its derivatives in erythrocytes and fibroblasts. AICAR causes profound mental retardation, epilepsy, dysmorphic features and congenital blindness.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_019307426K → R in AICAR; loss of transformylase activity. 1 PublicationCorresponds to variant dbSNP:rs121434478EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi66K → A: Decreased affinity to FAICAR; no change in FAICAR cyclization activity. 1 Publication1
    Mutagenesisi104Y → A or F: Decreased FAICAR cyclization activity; no change in affinity to FAICAR. 1 Publication1
    Mutagenesisi125D → A, E or N: Decreased FAICAR cyclization activity; no change in affinity to FAICAR. 1 Publication1
    Mutagenesisi137K → A: Decreased affinity to FAICAR; no change in FAICAR cyclization activity. 1 Publication1
    Mutagenesisi137K → R: Decreased FAICAR cyclization activity; no change in affinity to FAICAR. 1 Publication1
    Mutagenesisi213H → A: Loss of AICAR transformylase activity. 1 Publication1
    Mutagenesisi267H → A: Loss of AICAR transformylase activity. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    471

    MalaCards human disease database

    More...
    MalaCardsi
    ATIC
    MIMi608688 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000138363

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    250977 AICA-ribosiduria

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA25094

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P31939 Tchem

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2518

    Drug and drug target database

    More...
    DrugBanki
    DB02309 5-monophosphate-9-beta-D-ribofuranosyl xanthine
    DB03442 Acid yellow 54 free acid
    DB01700 AICA ribonucleotide
    DB04057 Beta-Dadf, Msa, Multisubstrate Adduct Inhibitor
    DB01972 Guanosine-5'-Monophosphate
    DB00563 Methotrexate
    DB00642 Pemetrexed
    DB00116 Tetrahydrofolic acid

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    ATIC

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    23831360

    <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_00001921561 – 592Bifunctional purine biosynthesis protein ATICAdd BLAST592
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; alternateCombined sources
    ChainiPRO_00004343762 – 592Bifunctional purine biosynthesis protein ATIC, N-terminally processed1 PublicationAdd BLAST591

    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 residuei1N-acetylmethionineCombined sources1
    Modified residuei199N6-acetyllysineCombined sources1

    Keywords - PTMi

    Acetylation

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P31939

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P31939

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P31939

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

    More...
    PaxDbi
    P31939

    PeptideAtlas

    More...
    PeptideAtlasi
    P31939

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P31939

    ProteomicsDB: a multi-organism proteome resource

    More...
    ProteomicsDBi
    19298
    54805 [P31939-1]

    2D gel databases

    REPRODUCTION-2DPAGE

    More...
    REPRODUCTION-2DPAGEi
    IPI00289499

    University College Dublin 2-DE Proteome Database

    More...
    UCD-2DPAGEi
    P31939

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P31939

    MetOSite database of methionine sulfoxide sites

    More...
    MetOSitei
    P31939

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

    More...
    PhosphoSitePlusi
    P31939

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    P31939

    <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

    Present in the heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas.1 Publication

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000138363 Expressed in adrenal gland and 228 other tissues

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P31939 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P31939 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    ENSG00000138363 Low tissue specificity

    <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

    Homodimer (PubMed:14756553, PubMed:14966129). Associates with internalized INSR complexes on Golgi/endosomal membranes (PubMed:25687571).

    Interacts with INSR; ATIC together with PRKAA2/AMPK2 and HACD3/PTPLAD1 is proposed to be part of a signaling network regulating INSR autophosphorylation and endocytosis (PubMed:25687571).

    3 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    106961, 86 interactors

    Protein interaction database and analysis system

    More...
    IntActi
    P31939, 13 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000236959

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    P31939

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P31939 protein

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1592
    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
    P31939

    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
    P31939

    <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 <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini2 – 146MGS-likePROSITE-ProRule annotationAdd BLAST145

    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>Regioni2 – 198IMP cyclohydrolaseBy similarityAdd BLAST197
    Regioni199 – 592AICAR formyltransferaseBy similarityAdd BLAST394
    Regioni207 – 208AICAR bindingCombined sources1 Publication2
    Regioni565 – 56610-formyltetrahydrofolate bindingBy similarity2

    <p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The IMP cyclohydrolase activity resides in the N-terminal region.

    <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 PurH family.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG2555 Eukaryota
    COG0138 LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00390000004553

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_016316_3_2_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P31939

    KEGG Orthology (KO)

    More...
    KOi
    K00602

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    WRVAKFV

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P31939

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF105642

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    1.10.287.440, 1 hit
    3.40.140.20, 2 hits
    3.40.50.1380, 1 hit

    HAMAP database of protein families

    More...
    HAMAPi
    MF_00139 PurH, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR024051 AICAR_Tfase_dup_dom_sf
    IPR024050 AICAR_Tfase_insert_dom_sf
    IPR016193 Cytidine_deaminase-like
    IPR011607 MGS-like_dom
    IPR036914 MGS-like_dom_sf
    IPR002695 PurH-like

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR11692 PTHR11692, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF01808 AICARFT_IMPCHas, 1 hit
    PF02142 MGS, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000414 AICARFT_IMPCHas, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00798 AICARFT_IMPCHas, 1 hit
    SM00851 MGS, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF52335 SSF52335, 1 hit
    SSF53927 SSF53927, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00355 purH, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS51855 MGS, 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>Sequences (2+)i

    <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.

    This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P31939-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MAPGQLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD
    60 70 80 90 100
    VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA
    110 120 130 140 150
    CNLYPFVKTV ASPGVTVEEA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED
    160 170 180 190 200
    YVVVSTEMQS SESKDTSLET RRQLALKAFT HTAQYDEAIS DYFRKQYSKG
    210 220 230 240 250
    VSQMPLRYGM NPHQTPAQLY TLQPKLPITV LNGAPGFINL CDALNAWQLV
    260 270 280 290 300
    KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS
    310 320 330 340 350
    AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA
    360 370 380 390 400
    LTILSKKKNG NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF
    410 420 430 440 450
    SNVVTKNKDL PESALRDLIV ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS
    460 470 480 490 500
    RIHCTRLAGD KANYWWLRHH PQVLSMKFKT GVKRAEISNA IDQYVTGTIG
    510 520 530 540 550
    EDEDLIKWKA LFEEVPELLT EAEKKEWVEK LTEVSISSDA FFPFRDNVDR
    560 570 580 590
    AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH
    Length:592
    Mass (Da):64,616
    Last modified:October 10, 2002 - v3
    <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:iAD778892021F0888
    GO
    Isoform 2 (identifier: P31939-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MAPGQL → MSSLS

    Show »
    Length:591
    Mass (Da):64,524
    Checksum:i372861CF93D74887
    GO

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    C9JLK0C9JLK0_HUMAN
    Bifunctional purine biosynthesis pr...
    ATIC
    170Annotation score:

    Annotation score:1 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>
    H7C1S2H7C1S2_HUMAN
    Bifunctional purine biosynthesis pr...
    ATIC
    231Annotation score:

    Annotation score:1 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>
    F8WEF0F8WEF0_HUMAN
    Bifunctional purine biosynthesis pr...
    ATIC
    84Annotation score:

    Annotation score:1 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>
    F2Z3E8F2Z3E8_HUMAN
    Bifunctional purine biosynthesis pr...
    ATIC
    43Annotation score:

    Annotation score:1 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 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 conflicti165D → G in AAA97405 (PubMed:8567683).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_019306116T → S2 PublicationsCorresponds to variant dbSNP:rs2372536Ensembl.1
    Natural variantiVAR_019307426K → R in AICAR; loss of transformylase activity. 1 PublicationCorresponds to variant dbSNP:rs121434478EnsemblClinVar.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0534951 – 6MAPGQL → MSSLS in isoform 2. 2 Publications6

    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
    U37436 mRNA Translation: AAA97405.1
    D82348 mRNA Translation: BAA11559.1
    D89976 mRNA Translation: BAA21762.1
    AB062403 mRNA Translation: BAB93490.1
    AK290067 mRNA Translation: BAF82756.1
    AC073284 Genomic DNA Translation: AAY24062.1
    CH471063 Genomic DNA Translation: EAW70529.1
    BC008879 mRNA Translation: AAH08879.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS2398.1 [P31939-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    JC4642

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_004035.2, NM_004044.6 [P31939-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000236959; ENSP00000236959; ENSG00000138363 [P31939-1]
    ENST00000435675; ENSP00000415935; ENSG00000138363 [P31939-2]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    471

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:471

    UCSC genome browser

    More...
    UCSCi
    uc002vey.5 human [P31939-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <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

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U37436 mRNA Translation: AAA97405.1
    D82348 mRNA Translation: BAA11559.1
    D89976 mRNA Translation: BAA21762.1
    AB062403 mRNA Translation: BAB93490.1
    AK290067 mRNA Translation: BAF82756.1
    AC073284 Genomic DNA Translation: AAY24062.1
    CH471063 Genomic DNA Translation: EAW70529.1
    BC008879 mRNA Translation: AAH08879.1
    CCDSiCCDS2398.1 [P31939-1]
    PIRiJC4642
    RefSeqiNP_004035.2, NM_004044.6 [P31939-1]

    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
    1P4RX-ray2.55A/B1-592[»]
    1PKXX-ray1.90A/B/C/D1-592[»]
    1PL0X-ray2.60A/B/C/D1-592[»]
    5UY8X-ray2.39A/B/C/D2-592[»]
    5UZ0X-ray1.79A/B/C/D2-592[»]
    SMRiP31939
    ModBaseiSearch...
    PDBe-KBiSearch...

    Protein-protein interaction databases

    BioGRIDi106961, 86 interactors
    IntActiP31939, 13 interactors
    STRINGi9606.ENSP00000236959

    Chemistry databases

    BindingDBiP31939
    ChEMBLiCHEMBL2518
    DrugBankiDB02309 5-monophosphate-9-beta-D-ribofuranosyl xanthine
    DB03442 Acid yellow 54 free acid
    DB01700 AICA ribonucleotide
    DB04057 Beta-Dadf, Msa, Multisubstrate Adduct Inhibitor
    DB01972 Guanosine-5'-Monophosphate
    DB00563 Methotrexate
    DB00642 Pemetrexed
    DB00116 Tetrahydrofolic acid

    PTM databases

    iPTMnetiP31939
    MetOSiteiP31939
    PhosphoSitePlusiP31939
    SwissPalmiP31939

    Polymorphism and mutation databases

    BioMutaiATIC
    DMDMi23831360

    2D gel databases

    REPRODUCTION-2DPAGEiIPI00289499
    UCD-2DPAGEiP31939

    Proteomic databases

    EPDiP31939
    jPOSTiP31939
    MassIVEiP31939
    PaxDbiP31939
    PeptideAtlasiP31939
    PRIDEiP31939
    ProteomicsDBi19298
    54805 [P31939-1]

    Protocols and materials databases

    Antibodypedia a portal for validated antibodies

    More...
    Antibodypediai
    4601 388 antibodies

    The DNASU plasmid repository

    More...
    DNASUi
    471

    Genome annotation databases

    EnsembliENST00000236959; ENSP00000236959; ENSG00000138363 [P31939-1]
    ENST00000435675; ENSP00000415935; ENSG00000138363 [P31939-2]
    GeneIDi471
    KEGGihsa:471
    UCSCiuc002vey.5 human [P31939-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...
    CTDi
    471
    DisGeNETi471
    EuPathDBiHostDB:ENSG00000138363.14

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    ATIC
    HGNCiHGNC:794 ATIC
    HPAiENSG00000138363 Low tissue specificity
    MalaCardsiATIC
    MIMi601731 gene
    608688 phenotype
    neXtProtiNX_P31939
    OpenTargetsiENSG00000138363
    Orphaneti250977 AICA-ribosiduria
    PharmGKBiPA25094

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG2555 Eukaryota
    COG0138 LUCA
    GeneTreeiENSGT00390000004553
    HOGENOMiCLU_016316_3_2_1
    InParanoidiP31939
    KOiK00602
    OMAiWRVAKFV
    PhylomeDBiP31939
    TreeFamiTF105642

    Enzyme and pathway databases

    UniPathwayiUPA00074;UER00133
    UPA00074;UER00135
    BioCyciMetaCyc:HS06490-MONOMER
    BRENDAi2.1.2.3 2681
    3.5.4.10 2681
    ReactomeiR-HSA-73817 Purine ribonucleoside monophosphate biosynthesis
    SABIO-RKiP31939
    SIGNORiP31939

    Miscellaneous databases

    BioGRID ORCS database of CRISPR phenotype screens

    More...
    BioGRID-ORCSi
    471 165 hits in 788 CRISPR screens

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    ATIC human
    EvolutionaryTraceiP31939

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    Inosine_monophosphate_synthase

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    471
    PharosiP31939 Tchem

    Protein Ontology

    More...
    PROi
    PR:P31939
    RNActiP31939 protein

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000138363 Expressed in adrenal gland and 228 other tissues
    ExpressionAtlasiP31939 baseline and differential
    GenevisibleiP31939 HS

    Family and domain databases

    Gene3Di1.10.287.440, 1 hit
    3.40.140.20, 2 hits
    3.40.50.1380, 1 hit
    HAMAPiMF_00139 PurH, 1 hit
    InterProiView protein in InterPro
    IPR024051 AICAR_Tfase_dup_dom_sf
    IPR024050 AICAR_Tfase_insert_dom_sf
    IPR016193 Cytidine_deaminase-like
    IPR011607 MGS-like_dom
    IPR036914 MGS-like_dom_sf
    IPR002695 PurH-like
    PANTHERiPTHR11692 PTHR11692, 1 hit
    PfamiView protein in Pfam
    PF01808 AICARFT_IMPCHas, 1 hit
    PF02142 MGS, 1 hit
    PIRSFiPIRSF000414 AICARFT_IMPCHas, 1 hit
    SMARTiView protein in SMART
    SM00798 AICARFT_IMPCHas, 1 hit
    SM00851 MGS, 1 hit
    SUPFAMiSSF52335 SSF52335, 1 hit
    SSF53927 SSF53927, 1 hit
    TIGRFAMsiTIGR00355 purH, 1 hit
    PROSITEiView protein in PROSITE
    PS51855 MGS, 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 nameiPUR9_HUMAN
    <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: P31939
    Secondary accession number(s): A8K202
    , E9PBU3, Q13856, Q53S28
    <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: July 1, 1993
    Last sequence update: October 10, 2002
    Last modified: June 17, 2020
    This is version 204 of the entry and version 3 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
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    <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
    4. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    5. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    6. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    7. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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