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Bifunctional purine biosynthesis protein PURH [Cleaved into: Bifunctional purine biosynthesis protein PURH, N-terminally processed] [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase) (AICAR transformylase); IMP cyclohydrolase (EC 3.5.4.10) (ATIC) (IMP synthase) (Inosinicase)]

 PUR9_HUMAN              Reviewed;         592 AA.
P31939; A8K202; E9PBU3; Q13856; Q53S28;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
10-OCT-2002, sequence version 3.
12-SEP-2018, entry version 191.
RecName: Full=Bifunctional purine biosynthesis protein PURH;
Includes:
RecName: Full=Phosphoribosylaminoimidazolecarboxamide formyltransferase;
EC=2.1.2.3;
AltName: Full=5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase;
AltName: Full=AICAR transformylase;
Includes:
RecName: Full=IMP cyclohydrolase;
EC=3.5.4.10;
AltName: Full=ATIC;
AltName: Full=IMP synthase;
AltName: Full=Inosinicase;
Contains:
RecName: Full=Bifunctional purine biosynthesis protein PURH, N-terminally processed;
Name=ATIC; Synonyms=PURH; ORFNames=OK/SW-cl.86;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Hepatoma;
PubMed=8567683; DOI=10.1074/jbc.271.4.2225;
Rayl E.A., Moroson B.A., Beardsley G.P.;
"The human purH gene product, 5-aminoimidazole-4-carboxamide
ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning,
sequencing, expression, purification, kinetic analysis, and domain
mapping.";
J. Biol. Chem. 271:2225-2233(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=8867801; DOI=10.1093/dnares/2.6.269;
Yamauchi M., Seki N., Mita K., Saito T., Tsuji S., Hongo E.,
Morimyo M., Shiomi T., Koyama H.;
"Isolation of human purH gene expressed in the rodent transformant
cells by subtractive enrichment of 3'-untranslated region of human
transcript.";
DNA Res. 2:269-275(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=9378707; DOI=10.1093/oxfordjournals.jbchem.a021754;
Sugita T., Aya H., Ueno M., Ishizuka T., Kawashima K.;
"Characterization of molecularly cloned human 5-aminoimidazole-4-
carboxamide ribonucleotide transformylase.";
J. Biochem. 122:309-313(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
Shichijo S., Itoh K.;
"Identification of immuno-peptidmics that are recognized by tumor-
reactive CTL generated from TIL of colon cancer patients.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
SER-116.
TISSUE=Substantia nigra;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-116.
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 15-39; 91-97; 178-194; 208-225; 267-285 AND
417-426, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 178-189 AND 267-281.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
FUNCTION, AND SUBUNIT.
PubMed=25687571; DOI=10.1074/mcp.M114.047159;
Boutchueng-Djidjou M., Collard-Simard G., Fortier S., Hebert S.S.,
Kelly I., Landry C.R., Faure R.L.;
"The last enzyme of the de novo purine synthesis pathway 5-
aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP
cyclohydrolase (ATIC) plays a central role in insulin signaling and
the Golgi/endosomes protein network.";
Mol. Cell. Proteomics 14:1079-1092(2015).
[18]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH XMP, AND
SUBUNIT.
PubMed=14756553; DOI=10.1021/bi030162i;
Wolan D.W., Cheong C.-G., Greasley S.E., Wilson I.A.;
"Structural insights into the human and avian IMP cyclohydrolase
mechanism via crystal structures with the bound XMP inhibitor.";
Biochemistry 43:1171-1183(2004).
[19]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH AICAR; XMP AND
THE INHIBITORS BW1540 AND BW2315, FUNCTION, AND SUBUNIT.
PubMed=14966129; DOI=10.1074/jbc.M313691200;
Cheong C.-G., Wolan D.W., Greasley S.E., Horton P.A., Beardsley G.P.,
Wilson I.A.;
"Crystal structures of human bifunctional enzyme aminoimidazole-4-
carboxamide ribonucleotide transformylase/IMP cyclohydrolase in
complex with potent sulfonyl-containing antifolates.";
J. Biol. Chem. 279:18034-18045(2004).
[20]
VARIANT AICAR ARG-426, AND CHARACTERIZATION OF VARIANT AICAR ARG-426.
PubMed=15114530; DOI=10.1086/421475;
Marie S., Heron B., Bitoun P., Timmerman T., Van Den Berghe G.,
Vincent M.-F.;
"AICA-ribosiduria: a novel, neurologically devastating inborn error of
purine biosynthesis caused by mutation of ATIC.";
Am. J. Hum. Genet. 74:1276-1281(2004).
-!- FUNCTION: Bifunctional enzyme that catalyzes 2 steps in purine
biosynthesis. {ECO:0000269|PubMed:14966129}.
-!- FUNCTION: Promotes insulin receptor/INSR autophosphorylation and
is involved in INSR internalization (PubMed:25687571).
{ECO:0000269|PubMed:25687571}.
-!- CATALYTIC ACTIVITY: 10-formyltetrahydrofolate + 5-amino-1-(5-
phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-
formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
-!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D-
ribosyl)imidazole-4-carboxamide.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
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): step 1/1.
-!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-
carboxamide: step 1/1.
-!- SUBUNIT: 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). {ECO:0000269|PubMed:14756553,
ECO:0000269|PubMed:14966129, ECO:0000269|PubMed:25687571}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P31939-1; Sequence=Displayed;
Name=2;
IsoId=P31939-2; Sequence=VSP_053495;
-!- DOMAIN: The IMP cyclohydrolase activity resides in the N-terminal
region.
-!- DISEASE: AICAR transformylase/IMP cyclohydrolase deficiency
(AICAR) [MIM:608688]: A 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. {ECO:0000269|PubMed:15114530}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the PurH family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ATICID227.html";
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EMBL; U37436; AAA97405.1; -; mRNA.
EMBL; D82348; BAA11559.1; -; mRNA.
EMBL; D89976; BAA21762.1; -; mRNA.
EMBL; AB062403; BAB93490.1; -; mRNA.
EMBL; AK290067; BAF82756.1; -; mRNA.
EMBL; AC073284; AAY24062.1; -; Genomic_DNA.
EMBL; CH471063; EAW70529.1; -; Genomic_DNA.
EMBL; BC008879; AAH08879.1; -; mRNA.
CCDS; CCDS2398.1; -. [P31939-1]
PIR; JC4642; JC4642.
RefSeq; NP_004035.2; NM_004044.6. [P31939-1]
UniGene; Hs.90280; -.
PDB; 1P4R; X-ray; 2.55 A; A/B=1-592.
PDB; 1PKX; X-ray; 1.90 A; A/B/C/D=1-592.
PDB; 1PL0; X-ray; 2.60 A; A/B/C/D=1-592.
PDB; 5UY8; X-ray; 2.39 A; A/B/C/D=2-592.
PDB; 5UZ0; X-ray; 1.79 A; A/B/C/D=2-592.
PDBsum; 1P4R; -.
PDBsum; 1PKX; -.
PDBsum; 1PL0; -.
PDBsum; 5UY8; -.
PDBsum; 5UZ0; -.
ProteinModelPortal; P31939; -.
SMR; P31939; -.
BioGrid; 106961; 73.
IntAct; P31939; 9.
STRING; 9606.ENSP00000236959; -.
BindingDB; P31939; -.
ChEMBL; CHEMBL2518; -.
DrugBank; DB03442; 2-[5-Hydroxy-3-Methyl-1-(2-Methyl-4-Sulfo-Phenyl)-1h-Pyrazol-4-Ylazo]-4-Sulfo-Benzoic Acid.
DrugBank; DB02309; 5--Monophosphate-9-Beta-D-Ribofuranosyl Xanthine.
DrugBank; DB01700; Aicar.
DrugBank; DB01972; Guanosine-5'-Monophosphate.
DrugBank; DB00563; Methotrexate.
DrugBank; DB00642; Pemetrexed.
DrugBank; DB00116; Tetrahydrofolic acid.
iPTMnet; P31939; -.
PhosphoSitePlus; P31939; -.
SwissPalm; P31939; -.
BioMuta; ATIC; -.
DMDM; 23831360; -.
REPRODUCTION-2DPAGE; IPI00289499; -.
UCD-2DPAGE; P31939; -.
EPD; P31939; -.
PaxDb; P31939; -.
PeptideAtlas; P31939; -.
PRIDE; P31939; -.
ProteomicsDB; 54805; -.
DNASU; 471; -.
Ensembl; ENST00000236959; ENSP00000236959; ENSG00000138363. [P31939-1]
Ensembl; ENST00000435675; ENSP00000415935; ENSG00000138363. [P31939-2]
GeneID; 471; -.
KEGG; hsa:471; -.
UCSC; uc002vey.5; human. [P31939-1]
CTD; 471; -.
DisGeNET; 471; -.
EuPathDB; HostDB:ENSG00000138363.14; -.
GeneCards; ATIC; -.
HGNC; HGNC:794; ATIC.
HPA; CAB013462; -.
HPA; HPA021012; -.
MalaCards; ATIC; -.
MIM; 601731; gene.
MIM; 608688; phenotype.
neXtProt; NX_P31939; -.
OpenTargets; ENSG00000138363; -.
Orphanet; 250977; AICA-ribosiduria.
PharmGKB; PA25094; -.
eggNOG; KOG2555; Eukaryota.
eggNOG; COG0138; LUCA.
GeneTree; ENSGT00390000004553; -.
HOGENOM; HOG000230372; -.
HOVERGEN; HBG006912; -.
InParanoid; P31939; -.
KO; K00602; -.
OMA; DLLFAWK; -.
OrthoDB; EOG091G03H4; -.
PhylomeDB; P31939; -.
TreeFam; TF105642; -.
BioCyc; MetaCyc:HS06490-MONOMER; -.
BRENDA; 2.1.2.3; 2681.
BRENDA; 3.5.4.10; 2681.
Reactome; R-HSA-73817; Purine ribonucleoside monophosphate biosynthesis.
SABIO-RK; P31939; -.
UniPathway; UPA00074; UER00133.
UniPathway; UPA00074; UER00135.
ChiTaRS; ATIC; human.
EvolutionaryTrace; P31939; -.
GeneWiki; Inosine_monophosphate_synthase; -.
GenomeRNAi; 471; -.
PRO; PR:P31939; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000138363; Expressed in 229 organ(s), highest expression level in adrenal gland.
CleanEx; HS_ATIC; -.
ExpressionAtlas; P31939; baseline and differential.
Genevisible; P31939; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0003937; F:IMP cyclohydrolase activity; TAS:Reactome.
GO; GO:0004643; F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl.
GO; GO:0003360; P:brainstem development; IEA:Ensembl.
GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
GO; GO:0046452; P:dihydrofolate metabolic process; IEA:Ensembl.
GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
GO; GO:0009116; P:nucleoside metabolic process; IEA:Ensembl.
GO; GO:0009168; P:purine ribonucleoside monophosphate biosynthetic process; TAS:Reactome.
GO; GO:0010035; P:response to inorganic substance; IEA:Ensembl.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:Ensembl.
Gene3D; 1.10.287.440; -; 1.
Gene3D; 3.40.140.20; -; 3.
Gene3D; 3.40.50.1380; -; 1.
HAMAP; MF_00139; PurH; 1.
InterPro; IPR024051; AICAR_Tfase_dup_dom_sf.
InterPro; IPR024050; AICAR_Tfase_insert_dom_sf.
InterPro; IPR016193; Cytidine_deaminase-like.
InterPro; IPR011607; MGS-like_dom.
InterPro; IPR036914; MGS-like_dom_sf.
InterPro; IPR002695; PurH-like.
PANTHER; PTHR11692; PTHR11692; 1.
Pfam; PF01808; AICARFT_IMPCHas; 1.
Pfam; PF02142; MGS; 1.
PIRSF; PIRSF000414; AICARFT_IMPCHas; 1.
SMART; SM00798; AICARFT_IMPCHas; 1.
SMART; SM00851; MGS; 1.
SUPFAM; SSF52335; SSF52335; 1.
SUPFAM; SSF53927; SSF53927; 1.
TIGRFAMs; TIGR00355; purH; 1.
PROSITE; PS51855; MGS; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Disease mutation; Epilepsy; Hydrolase;
Multifunctional enzyme; Polymorphism; Purine biosynthesis;
Reference proteome; Transferase.
CHAIN 1 592 Bifunctional purine biosynthesis protein
PURH.
/FTId=PRO_0000192156.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:22223895}.
CHAIN 2 592 Bifunctional purine biosynthesis protein
PURH, N-terminally processed.
/FTId=PRO_0000434376.
DOMAIN 1 146 MGS-like. {ECO:0000255|PROSITE-
ProRule:PRU01202}.
NP_BIND 12 14 IMP.
NP_BIND 34 37 IMP.
NP_BIND 64 67 IMP.
NP_BIND 101 104 IMP.
NP_BIND 125 127 IMP.
REGION 207 208 AICAR binding.
ACT_SITE 137 137 Proton acceptor. {ECO:0000255}.
ACT_SITE 267 267 Proton acceptor. {ECO:0000305}.
BINDING 316 316 AICAR; via carbonyl oxygen.
{ECO:0000269|PubMed:14966129}.
BINDING 339 339 AICAR. {ECO:0000269|PubMed:14966129}.
BINDING 431 431 AICAR; shared with dimeric partner.
{ECO:0000269|PubMed:14966129}.
BINDING 451 451 AICAR; shared with dimeric partner.
{ECO:0000269|PubMed:14966129}.
BINDING 541 541 AICAR; via carbonyl oxygen; shared with
dimeric partner.
{ECO:0000269|PubMed:14966129}.
BINDING 588 588 AICAR; shared with dimeric partner.
{ECO:0000269|PubMed:14966129}.
SITE 266 266 Transition state stabilizer.
{ECO:0000255}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 199 199 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 6 MAPGQL -> MSSLS (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:8567683}.
/FTId=VSP_053495.
VARIANT 116 116 T -> S (in dbSNP:rs2372536).
{ECO:0000269|PubMed:14702039,
ECO:0000269|Ref.7}.
/FTId=VAR_019306.
VARIANT 426 426 K -> R (in AICAR; loss of transformylase
activity; dbSNP:rs121434478).
{ECO:0000269|PubMed:15114530}.
/FTId=VAR_019307.
CONFLICT 165 165 D -> G (in Ref. 1; AAA97405).
{ECO:0000305}.
STRAND 6 13 {ECO:0000244|PDB:5UZ0}.
HELIX 17 26 {ECO:0000244|PDB:5UZ0}.
STRAND 30 33 {ECO:0000244|PDB:5UZ0}.
HELIX 35 42 {ECO:0000244|PDB:5UZ0}.
TURN 43 45 {ECO:0000244|PDB:5UZ0}.
HELIX 51 55 {ECO:0000244|PDB:5UZ0}.
HELIX 61 63 {ECO:0000244|PDB:5UZ0}.
STRAND 65 67 {ECO:0000244|PDB:5UZ0}.
HELIX 70 77 {ECO:0000244|PDB:5UZ0}.
HELIX 82 91 {ECO:0000244|PDB:5UZ0}.
STRAND 96 102 {ECO:0000244|PDB:5UZ0}.
HELIX 106 110 {ECO:0000244|PDB:5UZ0}.
HELIX 117 122 {ECO:0000244|PDB:5UZ0}.
HELIX 127 137 {ECO:0000244|PDB:5UZ0}.
TURN 138 141 {ECO:0000244|PDB:5UZ0}.
STRAND 143 145 {ECO:0000244|PDB:5UZ0}.
HELIX 148 150 {ECO:0000244|PDB:5UZ0}.
HELIX 151 160 {ECO:0000244|PDB:5UZ0}.
STRAND 161 165 {ECO:0000244|PDB:1P4R}.
HELIX 168 197 {ECO:0000244|PDB:5UZ0}.
TURN 200 202 {ECO:0000244|PDB:5UZ0}.
STRAND 203 205 {ECO:0000244|PDB:5UZ0}.
STRAND 209 211 {ECO:0000244|PDB:5UZ0}.
STRAND 217 220 {ECO:0000244|PDB:5UZ0}.
STRAND 222 225 {ECO:0000244|PDB:5UZ0}.
STRAND 227 233 {ECO:0000244|PDB:5UZ0}.
HELIX 237 257 {ECO:0000244|PDB:5UZ0}.
STRAND 261 266 {ECO:0000244|PDB:5UZ0}.
STRAND 269 275 {ECO:0000244|PDB:5UZ0}.
HELIX 281 286 {ECO:0000244|PDB:5UZ0}.
HELIX 290 295 {ECO:0000244|PDB:5UZ0}.
HELIX 298 308 {ECO:0000244|PDB:5UZ0}.
TURN 309 316 {ECO:0000244|PDB:5UZ0}.
STRAND 317 323 {ECO:0000244|PDB:5UZ0}.
HELIX 327 334 {ECO:0000244|PDB:5UZ0}.
STRAND 338 344 {ECO:0000244|PDB:5UZ0}.
HELIX 348 355 {ECO:0000244|PDB:5UZ0}.
HELIX 358 360 {ECO:0000244|PDB:5UZ0}.
STRAND 363 367 {ECO:0000244|PDB:5UZ0}.
STRAND 375 381 {ECO:0000244|PDB:5UZ0}.
STRAND 384 389 {ECO:0000244|PDB:5UZ0}.
HELIX 397 400 {ECO:0000244|PDB:5UZ0}.
HELIX 412 426 {ECO:0000244|PDB:5UZ0}.
STRAND 433 437 {ECO:0000244|PDB:5UZ0}.
STRAND 440 445 {ECO:0000244|PDB:5UZ0}.
HELIX 451 467 {ECO:0000244|PDB:5UZ0}.
HELIX 471 474 {ECO:0000244|PDB:5UZ0}.
HELIX 484 496 {ECO:0000244|PDB:5UZ0}.
HELIX 502 509 {ECO:0000244|PDB:5UZ0}.
STRAND 512 514 {ECO:0000244|PDB:5UZ0}.
HELIX 521 528 {ECO:0000244|PDB:5UZ0}.
STRAND 534 540 {ECO:0000244|PDB:5UZ0}.
STRAND 543 545 {ECO:0000244|PDB:1PL0}.
HELIX 546 552 {ECO:0000244|PDB:5UZ0}.
TURN 553 555 {ECO:0000244|PDB:5UZ0}.
STRAND 556 562 {ECO:0000244|PDB:5UZ0}.
HELIX 568 577 {ECO:0000244|PDB:5UZ0}.
STRAND 581 586 {ECO:0000244|PDB:5UZ0}.
SEQUENCE 592 AA; 64616 MW; AD778892021F0888 CRC64;
MAPGQLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD VSELTGFPEM
LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA CNLYPFVKTV ASPGVTVEEA
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YVVVSTEMQS SESKDTSLET RRQLALKAFT
HTAQYDEAIS DYFRKQYSKG VSQMPLRYGM NPHQTPAQLY TLQPKLPITV LNGAPGFINL
CDALNAWQLV KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS
AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA LTILSKKKNG
NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF SNVVTKNKDL PESALRDLIV
ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS RIHCTRLAGD KANYWWLRHH PQVLSMKFKT
GVKRAEISNA IDQYVTGTIG EDEDLIKWKA LFEEVPELLT EAEKKEWVEK LTEVSISSDA
FFPFRDNVDR AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH


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