ATIC

Functionⁱ

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.1 Publication

Promotes insulin receptor/INSR autophosphorylation and is involved in INSR internalization (PubMed:25687571).1 Publication

Catalytic activityⁱ

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

IMP + H₂O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

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).
Proteins known to be involved in this subpathway in this organism are:

Bifunctional purine biosynthesis protein PURH (ATIC)

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

Pathwayⁱ: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Proteins known to be involved in this subpathway in this organism are:

Bifunctional purine biosynthesis protein PURH (ATIC)

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

Sites

Feature key	Position(s)	DescriptionActions	Length
Active siteⁱ	137	Proton acceptorSequence analysis	1
Siteⁱ	266	Transition state stabilizerSequence analysis	1
Active siteⁱ	267	Proton acceptorCurated	1
Binding siteⁱ	316	AICAR; via carbonyl oxygen1 Publication	1
Binding siteⁱ	339	AICAR1 Publication	1
Binding siteⁱ	431	AICAR; shared with dimeric partner1 Publication	1
Binding siteⁱ	451	AICAR; shared with dimeric partner1 Publication	1
Binding siteⁱ	541	AICAR; via carbonyl oxygen; shared with dimeric partner1 Publication	1
Binding siteⁱ	588	AICAR; shared with dimeric partner1 Publication	1

Regions

Feature key	Position(s)	DescriptionActions	Length
Nucleotide bindingⁱ	12 – 14	IMP	3
Nucleotide bindingⁱ	34 – 37	IMP	4
Nucleotide bindingⁱ	64 – 67	IMP	4
Nucleotide bindingⁱ	101 – 104	IMP	4
Nucleotide bindingⁱ	125 – 127	IMP	3

GO - Molecular functionⁱ

cadherin binding
Source: BHF-UCL
Inferred from high throughput direct assayⁱ
- 25468996
IMP cyclohydrolase activity Source: Reactome
phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: Reactome
protein homodimerization activity
Source: UniProtKB
Inferred from physical interactionⁱ
- 14756553
- 14966129

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
animal organ regeneration Source: Ensembl
brainstem development Source: Ensembl
cerebellum development Source: Ensembl
cerebral cortex development Source: Ensembl
dihydrofolate metabolic process Source: Ensembl
nucleobase-containing compound metabolic process
Source: ProtInc
Traceable author statementⁱ
- 8567683
nucleoside metabolic process Source: Ensembl
purine ribonucleoside monophosphate biosynthetic process Source: Reactome
response to inorganic substance Source: Ensembl
tetrahydrofolate biosynthetic process Source: Ensembl

View the complete GO annotation on QuickGO ...

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
Reactomeⁱ	R-HSA-73817 Purine ribonucleoside monophosphate biosynthesis
SABIO-RKⁱ	P31939
UniPathwayⁱ	UPA00074;UER00133 UPA00074;UER00135

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Bifunctional purine biosynthesis protein PURH Cleaved into the following chain: Bifunctional purine biosynthesis protein PURH, N-terminally processed Including the following 2 domains: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3) Alternative name(s): 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase AICAR transformylase IMP cyclohydrolase (EC:3.5.4.10) Alternative name(s): ATIC IMP synthase Inosinicase
Gene namesⁱ	Name:ATIC Synonyms:PURH ORF Names:OK/SW-cl.86
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 2

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000138363.14
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:794 ATIC
MIMⁱ	601731 gene
neXtProtⁱ	NX_P31939

Subcellular locationⁱ

GO - Cellular component

Pathology & Biotechⁱ

Involvement in diseaseⁱ

AICAR transformylase/IMP cyclohydrolase deficiency (AICAR)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA neurologically devastating inborn error of purine biosynthesis. Patients excrete massive amounts of AICA-riboside in the urine and accumulate AICA-ribotide and its derivatives in erythrocytes and fibroblasts. AICAR causes profound mental retardation, epilepsy, dysmorphic features and congenital blindness.

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

Keywords - Diseaseⁱ

Disease mutation, Epilepsy

Organism-specific databases

DisGeNET More...DisGeNETⁱ	471
MalaCards human disease database More...MalaCardsⁱ	ATIC
MIMⁱ	608688 phenotype
Open Targets More...OpenTargetsⁱ	ENSG00000138363
Orphanetⁱ	250977 AICA-ribosiduria
PharmGKBⁱ	PA25094

Chemistry databases

ChEMBLⁱ	CHEMBL2518
Drug and drug target database More...DrugBankⁱ	DB03442 2-[5-Hydroxy-3-Methyl-1-(2-Methyl-4-Sulfo-Phenyl)-1h-Pyrazol-4-Ylazo]-4-Sulfo-Benzoic Acid DB02309 5--Monophosphate-9-Beta-D-Ribofuranosyl Xanthine DB01700 Aicar DB01972 Guanosine-5'-Monophosphate DB00563 Methotrexate DB00642 Pemetrexed DB00116 Tetrahydrofolic acid

Polymorphism and mutation databases

BioMutaⁱ	ATIC
DMDMⁱ	23831360

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
ChainⁱPRO_0000192156	1 – 592	Bifunctional purine biosynthesis protein PURHAdd BLAST	592
Initiator methionineⁱ		Removed; alternateCombined sources
ChainⁱPRO_0000434376	2 – 592	Bifunctional purine biosynthesis protein PURH, N-terminally processedAdd 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

Acetylation

Proteomic databases

EPDⁱ	P31939
PaxDbⁱ	P31939
PeptideAtlas More...PeptideAtlasⁱ	P31939
PRIDEⁱ	P31939
ProteomicsDBⁱ	54805

2D gel databases

REPRODUCTION-2DPAGE More...REPRODUCTION-2DPAGEⁱ	IPI00289499
UCD-2DPAGEⁱ	P31939

PTM databases

iPTMnetⁱ	P31939
PhosphoSitePlusⁱ	P31939
SwissPalmⁱ	P31939

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000138363 Expressed in 229 organ(s), highest expression level in adrenal gland
CleanExⁱ	HS_ATIC
ExpressionAtlasⁱ	P31939 baseline and differential
Genevisibleⁱ	P31939 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	CAB013462 HPA021012

HPAⁱ

CAB013462
HPA021012

Interactionⁱ

Subunit structureⁱ

Homodimer (PubMed:14756553, PubMed:14966129). 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 (PubMed:25687571).3 Publications

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	106961, 73 interactors
IntActⁱ	P31939, 9 interactors
STRINGⁱ	9606.ENSP00000236959

Chemistry databases

BindingDBⁱ

P31939

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	6 – 13	Combined sources	8
Helixⁱ	17 – 26	Combined sources	10
Beta strandⁱ	30 – 33	Combined sources	4
Helixⁱ	35 – 42	Combined sources	8
Turnⁱ	43 – 45	Combined sources	3
Helixⁱ	51 – 55	Combined sources	5
Helixⁱ	61 – 63	Combined sources	3
Beta strandⁱ	65 – 67	Combined sources	3
Helixⁱ	70 – 77	Combined sources	8
Helixⁱ	82 – 91	Combined sources	10
Beta strandⁱ	96 – 102	Combined sources	7
Helixⁱ	106 – 110	Combined sources	5
Helixⁱ	117 – 122	Combined sources	6
Helixⁱ	127 – 137	Combined sources	11
Turnⁱ	138 – 141	Combined sources	4
Beta strandⁱ	143 – 145	Combined sources	3
Helixⁱ	148 – 150	Combined sources	3
Helixⁱ	151 – 160	Combined sources	10
Beta strandⁱ	161 – 165	Combined sources	5
Helixⁱ	168 – 197	Combined sources	30
Turnⁱ	200 – 202	Combined sources	3
Beta strandⁱ	203 – 205	Combined sources	3
Beta strandⁱ	209 – 211	Combined sources	3
Beta strandⁱ	217 – 220	Combined sources	4
Beta strandⁱ	222 – 225	Combined sources	4
Beta strandⁱ	227 – 233	Combined sources	7
Helixⁱ	237 – 257	Combined sources	21
Beta strandⁱ	261 – 266	Combined sources	6
Beta strandⁱ	269 – 275	Combined sources	7
Helixⁱ	281 – 286	Combined sources	6
Helixⁱ	290 – 295	Combined sources	6
Helixⁱ	298 – 308	Combined sources	11
Turnⁱ	309 – 316	Combined sources	8
Beta strandⁱ	317 – 323	Combined sources	7
Helixⁱ	327 – 334	Combined sources	8
Beta strandⁱ	338 – 344	Combined sources	7
Helixⁱ	348 – 355	Combined sources	8
Helixⁱ	358 – 360	Combined sources	3
Beta strandⁱ	363 – 367	Combined sources	5
Beta strandⁱ	375 – 381	Combined sources	7
Beta strandⁱ	384 – 389	Combined sources	6
Helixⁱ	397 – 400	Combined sources	4
Helixⁱ	412 – 426	Combined sources	15
Beta strandⁱ	433 – 437	Combined sources	5
Beta strandⁱ	440 – 445	Combined sources	6
Helixⁱ	451 – 467	Combined sources	17
Helixⁱ	471 – 474	Combined sources	4
Helixⁱ	484 – 496	Combined sources	13
Helixⁱ	502 – 509	Combined sources	8
Beta strandⁱ	512 – 514	Combined sources	3
Helixⁱ	521 – 528	Combined sources	8
Beta strandⁱ	534 – 540	Combined sources	7
Beta strandⁱ	543 – 545	Combined sources	3
Helixⁱ	546 – 552	Combined sources	7
Turnⁱ	553 – 555	Combined sources	3
Beta strandⁱ	556 – 562	Combined sources	7
Helixⁱ	568 – 577	Combined sources	10
Beta strandⁱ	581 – 586	Combined sources	6

Show more details

3D structure databases

ProteinModelPortalⁱ	P31939
SMRⁱ	P31939
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P31939

EvolutionaryTraceⁱ

P31939

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	1 – 146	MGS-likePROSITE-ProRule annotationAdd BLAST		146

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	207 – 208	AICAR binding		2

Domainⁱ

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

Sequence similaritiesⁱ

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGⁱ	KOG2555 Eukaryota COG0138 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000004553
HOGENOMⁱ	HOG000230372
HOVERGENⁱ	HBG006912
InParanoidⁱ	P31939
KEGG Orthology (KO) More...KOⁱ	K00602
OMAⁱ	DLLFAWK
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G03H4
PhylomeDBⁱ	P31939
TreeFamⁱ	TF105642

Family and domain databases

Gene3Dⁱ	1.10.287.440, 1 hit 3.40.140.20, 3 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
Pfam protein domain database More...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

Sequences (2+)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.ⁱShow all

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

This isoform has been chosen as the 'canonical' 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

Checksum:ⁱAD778892021F0888

GO

Isoform 2 (identifier: P31939-2) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MSSLSALFSV SDKTGLVEFA RNLTALGLNL VASGGTAKAL RDAGLAVRDV 
        60         70         80         90        100
SELTGFPEML GGRVKTLHPA VHAGILARNI PEDNADMARL DFNLIRVVAC 
       110        120        130        140        150
NLYPFVKTVA SPGVTVEEAV EQIDIGGVTL LRAAAKNHAR VTVVCEPEDY 
       160        170        180        190        200
VVVSTEMQSS ESKDTSLETR RQLALKAFTH TAQYDEAISD YFRKQYSKGV 
       210        220        230        240        250
SQMPLRYGMN PHQTPAQLYT LQPKLPITVL NGAPGFINLC DALNAWQLVK 
       260        270        280        290        300
ELKEALGIPA AASFKHVSPA GAAVGIPLSE DEAKVCMVYD LYKTLTPISA 
       310        320        330        340        350
AYARARGADR MSSFGDFVAL SDVCDVPTAK IISREVSDGI IAPGYEEEAL 
       360        370        380        390        400
TILSKKKNGN YCVLQMDQSY KPDENEVRTL FGLHLSQKRN NGVVDKSLFS 
       410        420        430        440        450
NVVTKNKDLP ESALRDLIVA TIAVKYTQSN SVCYAKNGQV IGIGAGQQSR 
       460        470        480        490        500
IHCTRLAGDK ANYWWLRHHP QVLSMKFKTG VKRAEISNAI DQYVTGTIGE 
       510        520        530        540        550
DEDLIKWKAL FEEVPELLTE AEKKEWVEKL TEVSISSDAF FPFRDNVDRA 
       560        570        580        590 
KRSGVAYIAA PSGSAADKVV IEACDELGII LAHTNLRLFH H

Show »

Length:591

Mass (Da):64,524

Checksum:ⁱ372861CF93D74887

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation
C9JLK0	C9JLK0_HUMAN	Bifunctional purine biosynthesis pr... Bifunctional purine biosynthesis protein PURH	ATIC	170	Annotation score:
H7C1S2	H7C1S2_HUMAN	Bifunctional purine biosynthesis pr... Bifunctional purine biosynthesis protein PURH	ATIC	231	Annotation score:
F8WEF0	F8WEF0_HUMAN	Bifunctional purine biosynthesis pr... Bifunctional purine biosynthesis protein PURH	ATIC	84	Annotation score:
F2Z3E8	F2Z3E8_HUMAN	Bifunctional purine biosynthesis pr... Bifunctional purine biosynthesis protein PURH	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:rs2372536Ensembl.		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
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS2398.1 [P31939-1]
PIRⁱ	JC4642
NCBI Reference Sequences More...RefSeqⁱ	NP_004035.2, NM_004044.6 [P31939-1]
UniGeneⁱ	Hs.90280

Genome annotation databases

Ensemblⁱ	ENST00000236959; ENSP00000236959; ENSG00000138363 [P31939-1] ENST00000435675; ENSP00000415935; ENSG00000138363 [P31939-2]
GeneIDⁱ	471
KEGGⁱ	hsa:471
UCSC genome browser More...UCSCⁱ	uc002vey.5 human [P31939-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
P31939	Epididymis secretory sperm binding protein Li 70p		HUMAN		592	UniRef100_P31939
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase		PANTR		592
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase		PANPA		592
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase		GORGO		592

Protein	Similar proteins		Species	Score	Length	Source
P31939	Bifunctional purine biosynthesis protein PURH		RAT		592	UniRef90_P31939
Bifunctional purine biosynthesis protein PURH		PONAB		592
Bifunctional purine biosynthesis protein PURH		MOUSE		592
Bifunctional purine biosynthesis protein PURH		BOVIN		592
Epididymis secretory sperm binding protein Li 70p		HUMAN		592
+128

Protein	Similar proteins		Species	Score	Length	Source
P31939	Bifunctional purine biosynthesis protein PURH		BOVIN		592	UniRef50_P31939
Bifunctional purine biosynthesis protein PURH		PONAB		592
Bifunctional purine biosynthesis protein PURH		RAT		592
Bifunctional purine biosynthesis protein PURH		MOUSE		592
Epididymis secretory sperm binding protein Li 70p		HUMAN		592
+170

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]
UniGeneⁱ	Hs.90280

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 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	[»]
ProteinModelPortalⁱ	P31939
SMRⁱ	P31939
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	106961, 73 interactors
IntActⁱ	P31939, 9 interactors
STRINGⁱ	9606.ENSP00000236959

Chemistry databases

BindingDBⁱ	P31939
ChEMBLⁱ	CHEMBL2518
DrugBankⁱ	DB03442 2-[5-Hydroxy-3-Methyl-1-(2-Methyl-4-Sulfo-Phenyl)-1h-Pyrazol-4-Ylazo]-4-Sulfo-Benzoic Acid DB02309 5--Monophosphate-9-Beta-D-Ribofuranosyl Xanthine DB01700 Aicar DB01972 Guanosine-5'-Monophosphate DB00563 Methotrexate DB00642 Pemetrexed DB00116 Tetrahydrofolic acid

PTM databases

iPTMnetⁱ	P31939
PhosphoSitePlusⁱ	P31939
SwissPalmⁱ	P31939

Polymorphism and mutation databases

BioMutaⁱ	ATIC
DMDMⁱ	23831360

2D gel databases

REPRODUCTION-2DPAGEⁱ	IPI00289499
UCD-2DPAGEⁱ	P31939

Proteomic databases

EPDⁱ	P31939
PaxDbⁱ	P31939
PeptideAtlasⁱ	P31939
PRIDEⁱ	P31939
ProteomicsDBⁱ	54805

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	471
Structural Biology Knowledgebase	Search...

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
EuPathDBⁱ	HostDB:ENSG00000138363.14
GeneCardsⁱ	ATIC
HGNCⁱ	HGNC:794 ATIC
HPAⁱ	CAB013462 HPA021012
MalaCardsⁱ	ATIC
MIMⁱ	601731 gene 608688 phenotype
neXtProtⁱ	NX_P31939
OpenTargetsⁱ	ENSG00000138363
Orphanetⁱ	250977 AICA-ribosiduria
PharmGKBⁱ	PA25094
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG2555 Eukaryota COG0138 LUCA
GeneTreeⁱ	ENSGT00390000004553
HOGENOMⁱ	HOG000230372
HOVERGENⁱ	HBG006912
InParanoidⁱ	P31939
KOⁱ	K00602
OMAⁱ	DLLFAWK
OrthoDBⁱ	EOG091G03H4
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
Reactomeⁱ	R-HSA-73817 Purine ribonucleoside monophosphate biosynthesis
SABIO-RKⁱ	P31939

Miscellaneous databases

ChiTaRSⁱ	ATIC human
EvolutionaryTraceⁱ	P31939
GeneWikiⁱ	Inosine_monophosphate_synthase
GenomeRNAiⁱ	471
Protein Ontology More...PROⁱ	PR:P31939
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000138363 Expressed in 229 organ(s), highest expression level in adrenal gland
CleanExⁱ	HS_ATIC
ExpressionAtlasⁱ	P31939 baseline and differential
Genevisibleⁱ	P31939 HS

Family and domain databases

Gene3Dⁱ	1.10.287.440, 1 hit 3.40.140.20, 3 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...

Entry informationⁱ

Entry nameⁱ	PUR9_HUMAN
Accessionⁱ	P31939Primary (citable) accession number: P31939 Secondary accession number(s): A8K202 , E9PBU3, Q13856, Q53S28
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
	Last sequence update:	October 10, 2002
	Last modified:	September 12, 2018
	This is version 191 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, Complete proteome, Direct protein sequencing, Reference proteome

UniProtKB

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Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P31939 (PUR9_HUMAN)

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Bifunctional purine biosynthesis protein PURH

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<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

<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

Pathwayi: IMP biosynthesis via de novo pathway

Sites

Regions

<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

Enzyme and pathway databases

<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

Organism-specific databases

<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

Cytosol

Extracellular region or secreted

Plasma Membrane

Other locations

<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

Keywords - Diseasei

Organism-specific databases

Chemistry databases

Polymorphism and mutation databases

<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

Amino acid modifications

Keywords - PTMi

Proteomic databases

2D gel databases

PTM databases

<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

Gene expression databases

Organism-specific databases

<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

GO - Molecular functioni

Protein-protein interaction databases

Chemistry databases

<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

3D structure databases

Miscellaneous databases

<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

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

Phylogenomic databases

Family and domain databases

Computationally mapped potential isoform sequencesi

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityi

<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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

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Functionⁱ

Pathwayⁱ: IMP biosynthesis via de novo pathway

Pathwayⁱ: IMP biosynthesis via de novo pathway

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Pathology & Biotechⁱ

Keywords - Diseaseⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Computationally mapped potential isoform sequencesⁱ

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Web resourcesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ