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Overview

Uniprot ID	P31939
Protein Name	Bifunctional purine biosynthesis protein ATIC
Gene Name	ATIC
Organism	Homo sapiens

Kla Sites from experimental identification

Position	Flanking peptide
408	SNVVTKNKDLPESAL
66	EMLGGRVKTLHPAVH

Function

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:10985775, PubMed:11948179, PubMed:9378707). Can use both 10-formyldihydrofolate and 10-formyltetrahydrofolate as the formyl donor in this reaction (PubMed:10985775). Also catalyzes the cyclization of FAICAR to inosine monophosphate (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)

Protein Sequence

10 MAPGQLALFS 20 VSDKTGLVEF 30 ARNLTALGLN 40 LVASGGTAKA 50 LRDAGLAVRD 60 VSELTGFPEM 70 LGGRVKTLHP 80 AVHAGILARN 90 IPEDNADMAR 100 LDFNLIRVVA 110 CNLYPFVKTV 120 ASPGVTVEEA 130 VEQIDIGGVT 140 LLRAAAKNHA 150 RVTVVCEPED 160 YVVVSTEMQS 170 SESKDTSLET 180 RRQLALKAFT 190 HTAQYDEAIS 200 DYFRKQYSKG 210 VSQMPLRYGM 220 NPHQTPAQLY 230 TLQPKLPITV 240 LNGAPGFINL 250 CDALNAWQLV 260 KELKEALGIP 270 AAASFKHVSP 280 AGAAVGIPLS 290 EDEAKVCMVY 300 DLYKTLTPIS 310 AAYARARGAD 320 RMSSFGDFVA 330 LSDVCDVPTA 340 KIISREVSDG 350 IIAPGYEEEA 360 LTILSKKKNG 370 NYCVLQMDQS 380 YKPDENEVRT 390 LFGLHLSQKR 400 NNGVVDKSLF 410 SNVVTKNKDL 420 PESALRDLIV 430 ATIAVKYTQS 440 NSVCYAKNGQ 450 VIGIGAGQQS 460 RIHCTRLAGD 470 KANYWWLRHH 480 PQVLSMKFKT 490 GVKRAEISNA 500 IDQYVTGTIG 510 EDEDLIKWKA 520 LFEEVPELLT 530 EAEKKEWVEK 540 LTEVSISSDA 550 FFPFRDNVDR 560 AKRSGVAYIA 570 APSGSAADKV 580 VIEACDELGI 590 ILAHTNLRLF HH

Gene Ontology

Classification	GO ID	Description
Biological Process	GO:0044208	'de novo' AMP biosynthetic process
Cellular Component	GO:0005829	cytosol
Cellular Component	GO:0070062	extracellular exosome
Cellular Component	GO:0016020	membrane
Molecular Function	GO:0045296	cadherin binding
Molecular Function	GO:0003937	IMP cyclohydrolase activity
Molecular Function	GO:0004643	phosphoribosylaminoimidazolecarboxamide formyltransferase activity
Molecular Function	GO:0042803	protein homodimerization activity
Biological Process	GO:0006189	'de novo' IMP biosynthetic process
Biological Process	GO:0097294	'de novo' XMP biosynthetic process
Biological Process	GO:0031100	animal organ regeneration
Biological Process	GO:0003360	brainstem development
Biological Process	GO:0021549	cerebellum development
Biological Process	GO:0021987	cerebral cortex development
Biological Process	GO:0046452	dihydrofolate metabolic process
Biological Process	GO:0006177	GMP biosynthetic process
Biological Process	GO:0006139	nucleobase-containing compound metabolic process
Biological Process	GO:0046654	tetrahydrofolate biosynthetic process

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.