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UniProtKB - P31939 (PUR9_HUMAN)

Entry version 211 (29 Sep 2021)
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_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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_section">'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 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 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_section">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_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding 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_section">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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P31939

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_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein ATIC
Alternative name(s):
AICAR transformylase/inosine monophosphate cyclohydrolase
Short name:
ATIC
Cleaved into the following chain:
Bifunctional purine biosynthesis protein ATIC, N-terminally processed
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_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ATICImported
Synonyms:PURH
ORF Names:OK/SW-cl.86
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

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

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000138363

<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 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 variants 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_and_biotech_section">'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 variant, 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
DB01972, Guanosine-5'-Monophosphate
DB00563, Methotrexate
DB04057, N-[4-([(2-Amino-4-oxo-1,4-dihydropyrido[3,2-d]pyrimidin-6-yl)methyl]{(2E)-3-[4-carbamoyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-imidazol-5-yl]-2-propenoyl}amino)benzoyl]-L-glutamic acid
DB00642, Pemetrexed
DB00116, Tetrahydrofolic acid

Genetic variation 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_processing_section">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

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		P31939, 1 site, 1 O-linked glycan (1 site)

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 241 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_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		106961, 103 interactors

Protein interaction database and analysis system

More...IntActi		P31939, 15 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_and_domains_section">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

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

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is 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.<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
AICAR transformylase/inosine monoph...
ATIC
170Annotation score:

Annotation score:2 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
AICAR transformylase/inosine monoph...
ATIC
84Annotation score:

Annotation score:2 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>
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:rs2372536EnsemblClinVar.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

<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_references_section">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, 103 interactors
IntActiP31939, 15 interactors
STRINGi9606.ENSP00000236959

Chemistry databases

BindingDBiP31939
ChEMBLiCHEMBL2518
DrugBankiDB02309, 5-monophosphate-9-beta-D-ribofuranosyl xanthine
DB03442, Acid yellow 54 free acid
DB01700, AICA ribonucleotide
DB01972, Guanosine-5'-Monophosphate
DB00563, Methotrexate
DB04057, N-[4-([(2-Amino-4-oxo-1,4-dihydropyrido[3,2-d]pyrimidin-6-yl)methyl]{(2E)-3-[4-carbamoyl-1-(5-O-phosphono-beta-D-ribofuranosyl)-1H-imidazol-5-yl]-2-propenoyl}amino)benzoyl]-L-glutamic acid
DB00642, Pemetrexed
DB00116, Tetrahydrofolic acid

PTM databases

GlyGeniP31939, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP31939
MetOSiteiP31939
PhosphoSitePlusiP31939
SwissPalmiP31939

Genetic variation 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, 406 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

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
VEuPathDBiHostDB:ENSG00000138363

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2555, Eukaryota
GeneTreeiENSGT00390000004553
HOGENOMiCLU_016316_3_2_1
InParanoidiP31939
OMAiWRVAKFV
PhylomeDBiP31939
TreeFamiTF105642

Enzyme and pathway databases

UniPathwayiUPA00074;UER00133
UPA00074;UER00135
BioCyciMetaCyc:HS06490-MONOMER
BRENDAi2.1.2.3, 2681
3.5.4.10, 2681
PathwayCommonsiP31939
ReactomeiR-HSA-73817, Purine ribonucleoside monophosphate biosynthesis
SABIO-RKiP31939
SIGNORiP31939

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		471, 194 hits in 1024 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 241 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

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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 10, 2002
Last modified: September 29, 2021
This is version 211 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. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families
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