UniProtKB - P31939 (PUR9_HUMAN)
Bifunctional purine biosynthesis protein ATIC
ATIC
Functioni
Miscellaneous
Catalytic activityi
- (6S)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide = (6S)-5,6,7,8-tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide3 PublicationsEC:2.1.2.33 PublicationsThis reaction proceeds in the forward3 Publications direction.
- 10-formyldihydrofolate + 5-amino-1-(5-phospho-β-D-ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + 7,8-dihydrofolate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- EC:3.5.4.102 PublicationsThis reaction proceeds in the backward2 Publications direction.
- 10-formyldihydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-thiocarboxamide = 6-thio-IMP + 7,8-dihydrofolate + H2O1 PublicationThis reaction proceeds in the forward1 Publication direction.
Activity regulationi
Kineticsi
- KM=10 µM for 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate)1 Publication
- KM=1.5 µM for 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with 10-formyldihydrofolate as cosubstrate)1 Publication
- KM=1.9 µM for 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide (with (6S)-10-formyltetrahydrofolate as cosubstrate)1 Publication
- KM=110 µM for (6S)-10-formyltetrahydrofolate1 Publication
- KM=100 µM for (6S)-10-formyltetrahydrofolate1 Publication
- KM=39 µM for (6S)-10-formyltetrahydrofolate1 Publication
- KM=11 µM for 10-formyldihydrofolate1 Publication
- KM=1.4 µM for 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide1 Publication
- KM=0.9 µM for 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide1 Publication
: IMP biosynthesis via de novo pathway Pathwayi
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 PublicationProteins known to be involved in this subpathway in this organism are:
- 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, Bifunctional purine biosynthesis protein ATIC (ATIC), 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (HEL-S-70p)
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 PublicationProteins known to be involved in this subpathway in this organism are:
- 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, Bifunctional purine biosynthesis protein ATIC (ATIC), 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase (HEL-S-70p)
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Active sitei | 137 | Proton donor/acceptor; for FAICAR cyclization activity1 Publication | 1 | |
Sitei | 266 | Transition state stabilizer1 Publication | 1 | |
Active sitei | 267 | Proton acceptor; for AICAR formyltransferase activity1 Publication | 1 | |
Binding sitei | 267 | AICARCombined sources2 Publications | 1 | |
Binding sitei | 316 | AICAR; via carbonyl oxygenCombined sources2 Publications | 1 | |
Binding sitei | 339 | AICARCombined sources2 Publications | 1 | |
Binding sitei | 431 | AICAR; shared with dimeric partnerCombined sources2 Publications | 1 | |
Binding sitei | 451 | AICAR; shared with dimeric partnerCombined sources2 Publications | 1 | |
Binding sitei | 452 | 10-formyltetrahydrofolate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 541 | AICAR; via carbonyl oxygen; shared with dimeric partnerCombined sources2 Publications | 1 | |
Binding sitei | 546 | 10-formyltetrahydrofolateBy similarity | 1 | |
Binding sitei | 588 | AICAR; shared with dimeric partnerCombined sources2 Publications | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 12 – 14 | IMPCombined sources2 Publications | 3 | |
Nucleotide bindingi | 34 – 37 | IMPCombined sources2 Publications | 4 | |
Nucleotide bindingi | 64 – 67 | IMPCombined sources2 Publications | 4 | |
Nucleotide bindingi | 101 – 102 | IMPCombined sources2 Publications | 2 | |
Nucleotide bindingi | 125 – 126 | IMPCombined sources2 Publications | 2 |
GO - Molecular functioni
- cadherin binding Source: BHF-UCL
- IMP cyclohydrolase activity Source: GO_Central
- phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: GO_Central
- protein homodimerization activity Source: UniProtKB
GO - Biological processi
- 'de novo' IMP biosynthetic process Source: GO_Central
- animal organ regeneration Source: Ensembl
- brainstem development Source: Ensembl
- cellular response to interleukin-7 Source: Ensembl
- cerebellum development Source: Ensembl
- cerebral cortex development Source: Ensembl
- dihydrofolate metabolic process Source: Ensembl
- nucleobase-containing compound metabolic process Source: ProtInc
- nucleoside metabolic process Source: Ensembl
- purine ribonucleoside monophosphate biosynthetic process Source: Reactome
- response to inorganic substance Source: Ensembl
- tetrahydrofolate biosynthetic process Source: Ensembl
Keywordsi
Molecular function | Hydrolase, Multifunctional enzyme, Transferase |
Biological process | Purine biosynthesis |
Enzyme and pathway databases
BioCyci | MetaCyc:HS06490-MONOMER |
BRENDAi | 2.1.2.3, 2681 3.5.4.10, 2681 |
PathwayCommonsi | P31939 |
Reactomei | R-HSA-73817, Purine ribonucleoside monophosphate biosynthesis |
SABIO-RKi | P31939 |
SIGNORi | P31939 |
UniPathwayi | UPA00074;UER00133 UPA00074;UER00135 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional purine biosynthesis protein ATICAlternative 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 |
Gene namesi | ORF Names:OK/SW-cl.86 |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:794, ATIC |
MIMi | 601731, gene |
neXtProti | NX_P31939 |
VEuPathDBi | HostDB:ENSG00000138363.14 |
Subcellular locationi
Cytosol
- cytosol Source: HPA
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Plasma Membrane
- plasma membrane Source: HPA
Other locations
- membrane Source: UniProtKB
Pathology & Biotechi
Involvement in diseasei
AICAR transformylase/IMP cyclohydrolase deficiency (AICAR)1 Publication
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_019307 | 426 | K → R in AICAR; loss of transformylase activity. 1 PublicationCorresponds to variant dbSNP:rs121434478EnsemblClinVar. | 1 |
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 66 | K → A: Decreased affinity to FAICAR; no change in FAICAR cyclization activity. 1 Publication | 1 | |
Mutagenesisi | 104 | Y → A or F: Decreased FAICAR cyclization activity; no change in affinity to FAICAR. 1 Publication | 1 | |
Mutagenesisi | 125 | D → A, E or N: Decreased FAICAR cyclization activity; no change in affinity to FAICAR. 1 Publication | 1 | |
Mutagenesisi | 137 | K → A: Decreased affinity to FAICAR; no change in FAICAR cyclization activity. 1 Publication | 1 | |
Mutagenesisi | 137 | K → R: Decreased FAICAR cyclization activity; no change in affinity to FAICAR. 1 Publication | 1 | |
Mutagenesisi | 213 | H → A: Loss of AICAR transformylase activity. 1 Publication | 1 | |
Mutagenesisi | 267 | H → A: Loss of AICAR transformylase activity. 1 Publication | 1 |
Keywords - Diseasei
Disease variant, EpilepsyOrganism-specific databases
DisGeNETi | 471 |
MalaCardsi | ATIC |
MIMi | 608688, phenotype |
OpenTargetsi | ENSG00000138363 |
Orphaneti | 250977, AICA-ribosiduria |
PharmGKBi | PA25094 |
Miscellaneous databases
Pharosi | P31939, Tchem |
Chemistry databases
ChEMBLi | CHEMBL2518 |
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
BioMutai | ATIC |
DMDMi | 23831360 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000192156 | 1 – 592 | Bifunctional purine biosynthesis protein ATICAdd BLAST | 592 | |
Initiator methioninei | Removed; alternateCombined sources | |||
ChainiPRO_0000434376 | 2 – 592 | Bifunctional purine biosynthesis protein ATIC, N-terminally processed1 PublicationAdd BLAST | 591 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineCombined sources | 1 | |
Modified residuei | 199 | N6-acetyllysineCombined sources | 1 |
Keywords - PTMi
AcetylationProteomic databases
EPDi | P31939 |
jPOSTi | P31939 |
MassIVEi | P31939 |
PaxDbi | P31939 |
PeptideAtlasi | P31939 |
PRIDEi | P31939 |
ProteomicsDBi | 19298 54805 [P31939-1] |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00289499 |
UCD-2DPAGEi | P31939 |
PTM databases
iPTMneti | P31939 |
MetOSitei | P31939 |
PhosphoSitePlusi | P31939 |
SwissPalmi | P31939 |
Expressioni
Tissue specificityi
Gene expression databases
Bgeei | ENSG00000138363, Expressed in adrenal gland and 241 other tissues |
ExpressionAtlasi | P31939, baseline and differential |
Genevisiblei | P31939, HS |
Organism-specific databases
HPAi | ENSG00000138363, Low tissue specificity |
Interactioni
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 PublicationsGO - Molecular functioni
- cadherin binding Source: BHF-UCL
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 106961, 95 interactors |
IntActi | P31939, 15 interactors |
STRINGi | 9606.ENSP00000236959 |
Chemistry databases
BindingDBi | P31939 |
Miscellaneous databases
RNActi | P31939, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P31939 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P31939 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 2 – 146 | MGS-likePROSITE-ProRule annotationAdd BLAST | 145 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 2 – 198 | IMP cyclohydrolaseBy similarityAdd BLAST | 197 | |
Regioni | 199 – 592 | AICAR formyltransferaseBy similarityAdd BLAST | 394 | |
Regioni | 207 – 208 | AICAR bindingCombined sources1 Publication | 2 | |
Regioni | 565 – 566 | 10-formyltetrahydrofolate bindingBy similarity | 2 |
Domaini
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2555, Eukaryota |
GeneTreei | ENSGT00390000004553 |
HOGENOMi | CLU_016316_3_2_1 |
InParanoidi | P31939 |
OMAi | WRVAKFV |
PhylomeDBi | P31939 |
TreeFami | TF105642 |
Family and domain databases
Gene3Di | 1.10.287.440, 1 hit 3.40.140.20, 2 hits 3.40.50.1380, 1 hit |
HAMAPi | MF_00139, PurH, 1 hit |
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 |
PANTHERi | PTHR11692, PTHR11692, 1 hit |
Pfami | View protein in Pfam PF01808, AICARFT_IMPCHas, 1 hit PF02142, MGS, 1 hit |
PIRSFi | PIRSF000414, AICARFT_IMPCHas, 1 hit |
SMARTi | View protein in SMART SM00798, AICARFT_IMPCHas, 1 hit SM00851, MGS, 1 hit |
SUPFAMi | SSF52335, SSF52335, 1 hit SSF53927, SSF53927, 1 hit |
TIGRFAMsi | TIGR00355, purH, 1 hit |
PROSITEi | View protein in PROSITE PS51855, MGS, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketC9JLK0 | C9JLK0_HUMAN | AICAR transformylase/inosine monoph... | ATIC | 170 | Annotation score: | ||
F8WEF0 | F8WEF0_HUMAN | AICAR transformylase/inosine monoph... | ATIC | 84 | Annotation score: | ||
H7C1S2 | H7C1S2_HUMAN | Bifunctional purine biosynthesis pr... | ATIC | 231 | Annotation score: | ||
F2Z3E8 | F2Z3E8_HUMAN | Bifunctional purine biosynthesis pr... | ATIC | 43 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 165 | D → G in AAA97405 (PubMed:8567683).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_019306 | 116 | T → S2 PublicationsCorresponds to variant dbSNP:rs2372536EnsemblClinVar. | 1 | |
Natural variantiVAR_019307 | 426 | K → R in AICAR; loss of transformylase activity. 1 PublicationCorresponds to variant dbSNP:rs121434478EnsemblClinVar. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_053495 | 1 – 6 | MAPGQL → MSSLS in isoform 2. 2 Publications | 6 |
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 |
CCDSi | CCDS2398.1 [P31939-1] |
PIRi | JC4642 |
RefSeqi | NP_004035.2, NM_004044.6 [P31939-1] |
Genome annotation databases
Ensembli | ENST00000236959; ENSP00000236959; ENSG00000138363 [P31939-1] ENST00000435675; ENSP00000415935; ENSG00000138363 [P31939-2] |
GeneIDi | 471 |
KEGGi | hsa:471 |
UCSCi | uc002vey.5, human [P31939-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
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 |
CCDSi | CCDS2398.1 [P31939-1] |
PIRi | JC4642 |
RefSeqi | NP_004035.2, NM_004044.6 [P31939-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1P4R | X-ray | 2.55 | A/B | 1-592 | [»] | |
1PKX | X-ray | 1.90 | A/B/C/D | 1-592 | [»] | |
1PL0 | X-ray | 2.60 | A/B/C/D | 1-592 | [»] | |
5UY8 | X-ray | 2.39 | A/B/C/D | 2-592 | [»] | |
5UZ0 | X-ray | 1.79 | A/B/C/D | 2-592 | [»] | |
SMRi | P31939 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 106961, 95 interactors |
IntActi | P31939, 15 interactors |
STRINGi | 9606.ENSP00000236959 |
Chemistry databases
BindingDBi | P31939 |
ChEMBLi | CHEMBL2518 |
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 |
PTM databases
iPTMneti | P31939 |
MetOSitei | P31939 |
PhosphoSitePlusi | P31939 |
SwissPalmi | P31939 |
Genetic variation databases
BioMutai | ATIC |
DMDMi | 23831360 |
2D gel databases
REPRODUCTION-2DPAGEi | IPI00289499 |
UCD-2DPAGEi | P31939 |
Proteomic databases
EPDi | P31939 |
jPOSTi | P31939 |
MassIVEi | P31939 |
PaxDbi | P31939 |
PeptideAtlasi | P31939 |
PRIDEi | P31939 |
ProteomicsDBi | 19298 54805 [P31939-1] |
Protocols and materials databases
Antibodypediai | 4601, 391 antibodies |
DNASUi | 471 |
Genome annotation databases
Ensembli | ENST00000236959; ENSP00000236959; ENSG00000138363 [P31939-1] ENST00000435675; ENSP00000415935; ENSG00000138363 [P31939-2] |
GeneIDi | 471 |
KEGGi | hsa:471 |
UCSCi | uc002vey.5, human [P31939-1] |
Organism-specific databases
CTDi | 471 |
DisGeNETi | 471 |
GeneCardsi | ATIC |
HGNCi | HGNC:794, ATIC |
HPAi | ENSG00000138363, Low tissue specificity |
MalaCardsi | ATIC |
MIMi | 601731, gene 608688, phenotype |
neXtProti | NX_P31939 |
OpenTargetsi | ENSG00000138363 |
Orphaneti | 250977, AICA-ribosiduria |
PharmGKBi | PA25094 |
VEuPathDBi | HostDB:ENSG00000138363.14 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG2555, Eukaryota |
GeneTreei | ENSGT00390000004553 |
HOGENOMi | CLU_016316_3_2_1 |
InParanoidi | P31939 |
OMAi | WRVAKFV |
PhylomeDBi | P31939 |
TreeFami | TF105642 |
Enzyme and pathway databases
UniPathwayi | UPA00074;UER00133 UPA00074;UER00135 |
BioCyci | MetaCyc:HS06490-MONOMER |
BRENDAi | 2.1.2.3, 2681 3.5.4.10, 2681 |
PathwayCommonsi | P31939 |
Reactomei | R-HSA-73817, Purine ribonucleoside monophosphate biosynthesis |
SABIO-RKi | P31939 |
SIGNORi | P31939 |
Miscellaneous databases
BioGRID-ORCSi | 471, 178 hits in 881 CRISPR screens |
ChiTaRSi | ATIC, human |
EvolutionaryTracei | P31939 |
GeneWikii | Inosine_monophosphate_synthase |
GenomeRNAii | 471 |
Pharosi | P31939, Tchem |
PROi | PR:P31939 |
RNActi | P31939, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000138363, Expressed in adrenal gland and 241 other tissues |
ExpressionAtlasi | P31939, baseline and differential |
Genevisiblei | P31939, HS |
Family and domain databases
Gene3Di | 1.10.287.440, 1 hit 3.40.140.20, 2 hits 3.40.50.1380, 1 hit |
HAMAPi | MF_00139, PurH, 1 hit |
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 |
PANTHERi | PTHR11692, PTHR11692, 1 hit |
Pfami | View protein in Pfam PF01808, AICARFT_IMPCHas, 1 hit PF02142, MGS, 1 hit |
PIRSFi | PIRSF000414, AICARFT_IMPCHas, 1 hit |
SMARTi | View protein in SMART SM00798, AICARFT_IMPCHas, 1 hit SM00851, MGS, 1 hit |
SUPFAMi | SSF52335, SSF52335, 1 hit SSF53927, SSF53927, 1 hit |
TIGRFAMsi | TIGR00355, purH, 1 hit |
PROSITEi | View protein in PROSITE PS51855, MGS, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PUR9_HUMAN | |
Accessioni | P31939Primary (citable) accession number: P31939 Secondary accession number(s): A8K202 Q53S28 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1993 |
Last sequence update: | October 10, 2002 | |
Last modified: | February 10, 2021 | |
This is version 208 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any 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. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants