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Entry version 130 (02 Jun 2021)
Sequence version 1 (01 Jul 1993)
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Protein

Bifunctional purine biosynthesis protein ATIC

Gene

ATIC

Organism
Gallus gallus (Chicken)
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:12501179).

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:12501179).

Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction. Also catalyzes the cyclization of FAICAR to IMP. Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (By similarity).

By similarity1 Publication

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.By similarity

<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 (By similarity). AICAR formyltransferase activity is competitively inhibited by 2-[5-hydroxy-3-methyl-1-(2-methyl-4-sulfo-phenyl)-1H-pyrazol-4-ylazo]-4-sulfo-benzoic acid (326203-A) (PubMed:15355974). FAICAR cyclization is competitively inhibited by 1,5-dihydroimidazo[4,5-c][1,2,6]thiadiazin-4(3H)-one-2,2-dioxide and the corresponding nucleoside and nucleoside monophosphate (PubMed:17324932).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 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.By similarity 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 sitei138Proton donor/acceptor; for FAICAR cyclization activityBy similarity1
<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>Sitei267Transition state stabilizerBy similarity1
Active sitei268Proton acceptor; for AICAR formyltransferase activityBy similarity1
<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 sitei268AICARCombined sources1 Publication1
Binding sitei317AICAR; via carbonyl oxygenCombined sources1 Publication1
Binding sitei340AICARCombined sources1 Publication1
Binding sitei432AICAR; shared with dimeric partnerBy similarity1
Binding sitei452AICAR; shared with dimeric partnerBy similarity1
Binding sitei45310-formyltetrahydrofolate; via amide nitrogenCombined sources1 Publication1
Binding sitei542AICAR; via carbonyl oxygen; shared with dimeric partnerCombined sources1 Publication1
Binding sitei54710-formyltetrahydrofolateCombined sources1 Publication1
Binding sitei589AICAR; shared with dimeric partnerCombined sources1 Publication1

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 bindingi13 – 15IMPCombined sources2 Publications3
Nucleotide bindingi35 – 38IMPCombined sources2 Publications4
Nucleotide bindingi65 – 68IMPCombined sources2 Publications4
Nucleotide bindingi102 – 103IMPCombined sources1 Publication2
Nucleotide bindingi126 – 127IMPCombined 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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.1.2.3, 1306
3.5.4.10, 1306

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-GGA-419140, De novo synthesis of IMP

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P31335

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 cyclohydrolase1 Publication
Short name:
ATIC1 Publication
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.31 Publication)
Alternative name(s):
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
Short name:
AICAR formyltransferase
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10By similarity)
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:ATIC
Synonyms:PURH
<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>OrganismiGallus gallus (Chicken)
<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 identifieri9031 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
<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
  • UP000000539 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<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 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_00001921551 – 593Bifunctional purine biosynthesis protein ATICAdd BLAST593

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 residuei200N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

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

More...
PaxDbi
P31335

<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:11323713, PubMed:12501179). Associates with internalized INSR complexes on Golgi/endosomal membranes.

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 (By similarity).

By similarity2 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
9031.ENSGALP00000005643

<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

1593
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

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SMRi
P31335

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P31335

<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>Domaini1 – 147MGS-likePROSITE-ProRule annotationAdd BLAST147

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>Regioni1 – 199IMP cyclohydrolase1 PublicationAdd BLAST199
Regioni200 – 593AICAR formyltransferase1 PublicationAdd BLAST394
Regioni208 – 209AICAR bindingCombined sources1 Publication2
Regioni566 – 56710-formyltetrahydrofolate bindingCombined sources1 Publication2

<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.1 Publication

<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

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P31335

Database of Orthologous Groups

More...
OrthoDBi
324473at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P31335

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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P31335-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAARQQLALL SVSEKAGLVE FARSLNALGL GLIASGGTAT ALRDAGLPVR
60 70 80 90 100
DVSDLTGFPE MLGGRVKTLH PAVHAGILAR NIPEDNADMN KQDFSLVRVV
110 120 130 140 150
VCNLYPFVKT VSSPGVTVPE AVEKIDIGGV ALLRAAAKNH ARVTVVCDPA
160 170 180 190 200
DYSSVAKEMA ASKDKDTSVE TRRHLALKAF THTAQYDAAI SDYFRKEYSK
210 220 230 240 250
GVSQLPLRYG MNPHQSPAQL YTTRPKLPLT VVNGSPGFIN LCDALNAWQL
260 270 280 290 300
VKELKQALGI PAAASFKHVS PAGAAVGIPL SEEEAQVCMV HDLHKTLTPL
310 320 330 340 350
ASAYARSRGA DRMSSFGDFI ALSDICDVPT AKIISREVSD GVVAPGYEEE
360 370 380 390 400
ALKILSKKKN GGYCVLQMDP NYEPDDNEIR TLYGLQLMQK RNNAVIDRSL
410 420 430 440 450
FKNIVTKNKT LPESAVRDLI VASIAVKYTQ SNSVCYAKDG QVIGIGAGQQ
460 470 480 490 500
SRIHCTRLAG DKANSWWLRH HPRVLSMKFK AGVKRAEVSN AIDQYVTGTI
510 520 530 540 550
GEDEDLVKWQ AMFEEVPAQL TEAEKKQWIA KLTAVSLSSD AFFPFRDNVD
560 570 580 590
RAKRIGVQFI VAPSGSAADE VVIEACNELG ITLIHTNLRL FHH
Length:593
Mass (Da):64,415
Last modified:July 1, 1993 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBD1A34F03D96A136
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
S64492 mRNA Translation: AAB20309.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JQ1281, DTCHPH

NCBI Reference Sequences

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RefSeqi
NP_990509.1, NM_205178.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
396091

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
gga:396091

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S64492 mRNA Translation: AAB20309.1
PIRiJQ1281, DTCHPH
RefSeqiNP_990509.1, NM_205178.1

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
1G8MX-ray1.75A/B1-593[»]
1M9NX-ray1.93A/B1-593[»]
1OZ0X-ray2.50A/B1-593[»]
1THZX-ray1.80A/B1-593[»]
2B1GX-ray2.10A/B/C/D1-593[»]
2B1IX-ray2.02A/B1-593[»]
2IU0X-ray2.53A/B1-593[»]
2IU3X-ray2.90A/B1-593[»]
SMRiP31335
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005643

Proteomic databases

PaxDbiP31335

Genome annotation databases

GeneIDi396091
KEGGigga:396091

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
471

Phylogenomic databases

eggNOGiKOG2555, Eukaryota
InParanoidiP31335
OrthoDBi324473at2759
PhylomeDBiP31335

Enzyme and pathway databases

UniPathwayiUPA00074;UER00133
UPA00074;UER00135
BRENDAi2.1.2.3, 1306
3.5.4.10, 1306
ReactomeiR-GGA-419140, De novo synthesis of IMP
SABIO-RKiP31335

Miscellaneous databases

EvolutionaryTraceiP31335

Protein Ontology

More...
PROi
PR:P31335

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_CHICK
<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: P31335
<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: July 1, 1993
Last modified: June 2, 2021
This is version 130 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

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