Full text data of PFAS
PFAS
(KIAA0361)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Phosphoribosylformylglycinamidine synthase; FGAM synthase; FGAMS; 6.3.5.3 (Formylglycinamide ribotide amidotransferase; FGARAT; Formylglycinamide ribotide synthetase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphoribosylformylglycinamidine synthase; FGAM synthase; FGAMS; 6.3.5.3 (Formylglycinamide ribotide amidotransferase; FGARAT; Formylglycinamide ribotide synthetase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00004534
IPI00004534 Phosphoribosylformylglycinamidine synthase ATP binding, de novo IMP biosynthesis soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00004534 Phosphoribosylformylglycinamidine synthase ATP binding, de novo IMP biosynthesis soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
O15067
ID PUR4_HUMAN Reviewed; 1338 AA.
AC O15067; A6H8V8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase;
DE Short=FGAM synthase;
DE Short=FGAMS;
DE EC=6.3.5.3;
DE AltName: Full=Formylglycinamide ribotide amidotransferase;
DE Short=FGARAT;
DE AltName: Full=Formylglycinamide ribotide synthetase;
GN Name=PFAS; Synonyms=KIAA0361;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-19; LEU-367 AND PRO-621.
RX PubMed=10548741; DOI=10.1016/S0378-1119(99)00378-9;
RA Patterson D., Bleskan J., Gardiner K., Bowersox J.;
RT "Human phosphoribosylformylglycinamide amidotransferase (FGARAT):
RT regional mapping, complete coding sequence, isolation of a functional
RT genomic clone, and DNA sequence analysis.";
RL Gene 239:381-391(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-19; LEU-367
RP AND PRO-621.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-19; LEU-367
RP AND PRO-621.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-619 AND THR-623, VARIANT
RP [LARGE SCALE ANALYSIS] PRO-621, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND THR-619, VARIANT
RP [LARGE SCALE ANALYSIS] PRO-621, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, VARIANT [LARGE
RP SCALE ANALYSIS] PRO-621, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-621, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D-
CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC -!- INTERACTION:
CC P11171:EPB41; NbExp=1; IntAct=EBI-1052653, EBI-1050906;
CC P30480:HLA-B; NbExp=1; IntAct=EBI-1052653, EBI-1054175;
CC P23508:MCC; NbExp=1; IntAct=EBI-1052653, EBI-307531;
CC P19532:TFE3; NbExp=1; IntAct=EBI-1052653, EBI-1048957;
CC Q9UBN6:TNFRSF10D; NbExp=1; IntAct=EBI-1052653, EBI-1044859;
CC Q9Y4K3:TRAF6; NbExp=1; IntAct=EBI-1052653, EBI-359276;
CC P40337:VHL; NbExp=1; IntAct=EBI-1052653, EBI-301246;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS
CC family.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20816.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB002359; BAA20816.1; ALT_INIT; mRNA.
DR EMBL; AC135178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146768; AAI46769.1; -; mRNA.
DR EMBL; BC167158; AAI67158.1; -; mRNA.
DR RefSeq; NP_036525.1; NM_012393.2.
DR UniGene; Hs.573976; -.
DR ProteinModelPortal; O15067; -.
DR SMR; O15067; 304-572, 1063-1302.
DR IntAct; O15067; 5.
DR STRING; 9606.ENSP00000313490; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB00130; L-Glutamine.
DR MEROPS; C56.972; -.
DR PhosphoSite; O15067; -.
DR PaxDb; O15067; -.
DR PRIDE; O15067; -.
DR Ensembl; ENST00000314666; ENSP00000313490; ENSG00000178921.
DR GeneID; 5198; -.
DR KEGG; hsa:5198; -.
DR UCSC; uc002gkr.3; human.
DR CTD; 5198; -.
DR GeneCards; GC17P008152; -.
DR H-InvDB; HIX0019361; -.
DR HGNC; HGNC:8863; PFAS.
DR HPA; HPA022140; -.
DR HPA; HPA022886; -.
DR MIM; 602133; gene.
DR neXtProt; NX_O15067; -.
DR eggNOG; COG0046; -.
DR HOGENOM; HOG000261358; -.
DR HOVERGEN; HBG108309; -.
DR InParanoid; O15067; -.
DR KO; K01952; -.
DR OMA; VCLLEMA; -.
DR OrthoDB; EOG7353X4; -.
DR PhylomeDB; O15067; -.
DR BioCyc; MetaCyc:HS11329-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00074; UER00128.
DR ChiTaRS; PFAS; human.
DR GenomeRNAi; 5198; -.
DR NextBio; 20106; -.
DR PRO; PR:O15067; -.
DR ArrayExpress; O15067; -.
DR Bgee; O15067; -.
DR CleanEx; HS_PFAS; -.
DR Genevestigator; O15067; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IDA:UniProtKB.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; NAS:UniProtKB.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR InterPro; IPR010918; AIR_synth_C_dom.
DR InterPro; IPR000728; AIR_synth_N_dom.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR010073; PRibForGlyAmidine_synth.
DR InterPro; IPR016188; PurM_N-like.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Glutamine amidotransferase;
KW Ligase; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1 1338 Phosphoribosylformylglycinamidine
FT synthase.
FT /FTId=PRO_0000100401.
FT DOMAIN 1064 1302 Glutamine amidotransferase type-1.
FT NP_BIND 322 333 ATP (Potential).
FT ACT_SITE 1158 1158 For GATase activity (By similarity).
FT MOD_RES 569 569 Phosphoserine.
FT MOD_RES 619 619 Phosphothreonine.
FT MOD_RES 623 623 Phosphothreonine.
FT VARIANT 19 19 P -> S (in dbSNP:rs9891699).
FT /FTId=VAR_055008.
FT VARIANT 367 367 P -> L (in dbSNP:rs4791641).
FT /FTId=VAR_055009.
FT VARIANT 481 481 F -> Y (in dbSNP:rs35217368).
FT /FTId=VAR_055010.
FT VARIANT 621 621 L -> P (in dbSNP:rs11078738).
FT /FTId=VAR_055011.
FT CONFLICT 1326 1326 F -> S (in Ref. 1, 2; BAA20816 and 4;
FT AAI46769/AAI67158).
SQ SEQUENCE 1338 AA; 144734 MW; 273405025B701DAF CRC64;
MSPVLHFYVR PSGHEGAAPG HTRRKLQGKL PELQGVETEL CYNVNWTAEA LPSAEETKKL
MWLFGCPLLL DDVARESWLL PGSNDLLLEV GPRLNFSTPT STNIVSVCRA TGLGPVDRVE
TTRRYRLSFA HPPSAEVEAI ALATLHDRMT EQHFPHPIQS FSPESMPEPL NGPINILGEG
RLALEKANQE LGLALDSWDL DFYTKRFQEL QRNPSTVEAF DLAQSNSEHS RHWFFKGQLH
VDGQKLVHSL FESIMSTQES SNPNNVLKFC DNSSAIQGKE VRFLRPEDPT RPSRFQQQQG
LRHVVFTAET HNFPTGVCPF SGATTGTGGR IRDVQCTGRG AHVVAGTAGY CFGNLHIPGY
NLPWEDPSFQ YPGNFARPLE VAIEASNGAS DYGNKFGEPV LAGFARSLGL QLPDGQRREW
IKPIMFSGGI GSMEADHISK EAPEPGMEVV KVGGPVYRIG VGGGAASSVQ VQGDNTSDLD
FGAVQRGDPE MEQKMNRVIR ACVEAPKGNP ICSLHDQGAG GNGNVLKELS DPAGAIIYTS
RFQLGDPTLN ALEIWGAEYQ ESNALLLRSP NRDFLTHVSA RERCPACFVG TITGDRRIVL
VDDRECPVRR NGQGDAPPTP LPTPVDLELE WVLGKMPRKE FFLQRKPPML QPLALPPGLS
VHQALERVLR LPAVASKRYL TNKVDRSVGG LVAQQQCVGP LQTPLADVAV VALSHEELIG
AATALGEQPV KSLLDPKVAA RLAVAEALTN LVFALVTDLR DVKCSGNWMW AAKLPGEGAA
LADACEAMVA VMAALGVAVD GGKDSLSMAA RVGTETVRAP GSLVISAYAV CPDITATVTP
DLKHPEGRGH LLYVALSPGQ HRLGGTALAQ CFSQLGEHPP DLDLPENLVR AFSITQGLLK
DRLLCSGHDV SDGGLVTCLL EMAFAGNCGL QVDVPVPRVD VLSVLFAEEP GLVLEVQEPD
LAQVLKRYRD AGLHCLELGH TGEAGPHAMV RVSVNGAVVL EEPVGELRAL WEETSFQLDR
LQAEPRCVAE EERGLRERMG PSYCLPPTFP KASVPREPGG PSPRVAILRE EGSNGDREMA
DAFHLAGFEV WDVTMQDLCS GAIGLDTFRG VAFVGGFSYA DVLGSAKGWA AAVTFHPRAG
AELRRFRKRP DTFSLGVCNG CQLLALLGWV GGDPNEDAAE MGPDSQPARP GLLLRHNLSG
RYESRWASVR VGPGPALMLR GMEGAVLPVW SAHGEGYVAF SSPELQAQIE ARGLAPLHWA
DDDGNPTEQY PLNPNGSPGG VAGICSCDGR HLAVMPHPER AVRPWQWAWR PPPFDTLTTS
PWLQLFINAR NWTLEGSC
//
ID PUR4_HUMAN Reviewed; 1338 AA.
AC O15067; A6H8V8;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 4.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Phosphoribosylformylglycinamidine synthase;
DE Short=FGAM synthase;
DE Short=FGAMS;
DE EC=6.3.5.3;
DE AltName: Full=Formylglycinamide ribotide amidotransferase;
DE Short=FGARAT;
DE AltName: Full=Formylglycinamide ribotide synthetase;
GN Name=PFAS; Synonyms=KIAA0361;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS SER-19; LEU-367 AND PRO-621.
RX PubMed=10548741; DOI=10.1016/S0378-1119(99)00378-9;
RA Patterson D., Bleskan J., Gardiner K., Bowersox J.;
RT "Human phosphoribosylformylglycinamide amidotransferase (FGARAT):
RT regional mapping, complete coding sequence, isolation of a functional
RT genomic clone, and DNA sequence analysis.";
RL Gene 239:381-391(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-19; LEU-367
RP AND PRO-621.
RC TISSUE=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII.
RT The complete sequences of 100 new cDNA clones from brain which can
RT code for large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS SER-19; LEU-367
RP AND PRO-621.
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-619 AND THR-623, VARIANT
RP [LARGE SCALE ANALYSIS] PRO-621, AND MASS SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND THR-619, VARIANT
RP [LARGE SCALE ANALYSIS] PRO-621, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, VARIANT [LARGE
RP SCALE ANALYSIS] PRO-621, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] PRO-621, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D-
CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2-
CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway;
CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-
CC phospho-D-ribosyl)glycinamide: step 1/2.
CC -!- INTERACTION:
CC P11171:EPB41; NbExp=1; IntAct=EBI-1052653, EBI-1050906;
CC P30480:HLA-B; NbExp=1; IntAct=EBI-1052653, EBI-1054175;
CC P23508:MCC; NbExp=1; IntAct=EBI-1052653, EBI-307531;
CC P19532:TFE3; NbExp=1; IntAct=EBI-1052653, EBI-1048957;
CC Q9UBN6:TNFRSF10D; NbExp=1; IntAct=EBI-1052653, EBI-1044859;
CC Q9Y4K3:TRAF6; NbExp=1; IntAct=EBI-1052653, EBI-359276;
CC P40337:VHL; NbExp=1; IntAct=EBI-1052653, EBI-301246;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: In the N-terminal section; belongs to the FGAMS
CC family.
CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20816.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB002359; BAA20816.1; ALT_INIT; mRNA.
DR EMBL; AC135178; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC146768; AAI46769.1; -; mRNA.
DR EMBL; BC167158; AAI67158.1; -; mRNA.
DR RefSeq; NP_036525.1; NM_012393.2.
DR UniGene; Hs.573976; -.
DR ProteinModelPortal; O15067; -.
DR SMR; O15067; 304-572, 1063-1302.
DR IntAct; O15067; 5.
DR STRING; 9606.ENSP00000313490; -.
DR DrugBank; DB00142; L-Glutamic Acid.
DR DrugBank; DB00130; L-Glutamine.
DR MEROPS; C56.972; -.
DR PhosphoSite; O15067; -.
DR PaxDb; O15067; -.
DR PRIDE; O15067; -.
DR Ensembl; ENST00000314666; ENSP00000313490; ENSG00000178921.
DR GeneID; 5198; -.
DR KEGG; hsa:5198; -.
DR UCSC; uc002gkr.3; human.
DR CTD; 5198; -.
DR GeneCards; GC17P008152; -.
DR H-InvDB; HIX0019361; -.
DR HGNC; HGNC:8863; PFAS.
DR HPA; HPA022140; -.
DR HPA; HPA022886; -.
DR MIM; 602133; gene.
DR neXtProt; NX_O15067; -.
DR eggNOG; COG0046; -.
DR HOGENOM; HOG000261358; -.
DR HOVERGEN; HBG108309; -.
DR InParanoid; O15067; -.
DR KO; K01952; -.
DR OMA; VCLLEMA; -.
DR OrthoDB; EOG7353X4; -.
DR PhylomeDB; O15067; -.
DR BioCyc; MetaCyc:HS11329-MONOMER; -.
DR Reactome; REACT_111217; Metabolism.
DR UniPathway; UPA00074; UER00128.
DR ChiTaRS; PFAS; human.
DR GenomeRNAi; 5198; -.
DR NextBio; 20106; -.
DR PRO; PR:O15067; -.
DR ArrayExpress; O15067; -.
DR Bgee; O15067; -.
DR CleanEx; HS_PFAS; -.
DR Genevestigator; O15067; -.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IDA:UniProtKB.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; NAS:UniProtKB.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006144; P:purine nucleobase metabolic process; TAS:Reactome.
DR GO; GO:0042493; P:response to drug; IEA:Ensembl.
DR InterPro; IPR010918; AIR_synth_C_dom.
DR InterPro; IPR000728; AIR_synth_N_dom.
DR InterPro; IPR017926; GATASE.
DR InterPro; IPR010073; PRibForGlyAmidine_synth.
DR InterPro; IPR016188; PurM_N-like.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 2.
DR SUPFAM; SSF55326; SSF55326; 2.
DR SUPFAM; SSF56042; SSF56042; 2.
DR TIGRFAMs; TIGR01735; FGAM_synt; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Complete proteome; Cytoplasm; Glutamine amidotransferase;
KW Ligase; Nucleotide-binding; Phosphoprotein; Polymorphism;
KW Purine biosynthesis; Reference proteome.
FT CHAIN 1 1338 Phosphoribosylformylglycinamidine
FT synthase.
FT /FTId=PRO_0000100401.
FT DOMAIN 1064 1302 Glutamine amidotransferase type-1.
FT NP_BIND 322 333 ATP (Potential).
FT ACT_SITE 1158 1158 For GATase activity (By similarity).
FT MOD_RES 569 569 Phosphoserine.
FT MOD_RES 619 619 Phosphothreonine.
FT MOD_RES 623 623 Phosphothreonine.
FT VARIANT 19 19 P -> S (in dbSNP:rs9891699).
FT /FTId=VAR_055008.
FT VARIANT 367 367 P -> L (in dbSNP:rs4791641).
FT /FTId=VAR_055009.
FT VARIANT 481 481 F -> Y (in dbSNP:rs35217368).
FT /FTId=VAR_055010.
FT VARIANT 621 621 L -> P (in dbSNP:rs11078738).
FT /FTId=VAR_055011.
FT CONFLICT 1326 1326 F -> S (in Ref. 1, 2; BAA20816 and 4;
FT AAI46769/AAI67158).
SQ SEQUENCE 1338 AA; 144734 MW; 273405025B701DAF CRC64;
MSPVLHFYVR PSGHEGAAPG HTRRKLQGKL PELQGVETEL CYNVNWTAEA LPSAEETKKL
MWLFGCPLLL DDVARESWLL PGSNDLLLEV GPRLNFSTPT STNIVSVCRA TGLGPVDRVE
TTRRYRLSFA HPPSAEVEAI ALATLHDRMT EQHFPHPIQS FSPESMPEPL NGPINILGEG
RLALEKANQE LGLALDSWDL DFYTKRFQEL QRNPSTVEAF DLAQSNSEHS RHWFFKGQLH
VDGQKLVHSL FESIMSTQES SNPNNVLKFC DNSSAIQGKE VRFLRPEDPT RPSRFQQQQG
LRHVVFTAET HNFPTGVCPF SGATTGTGGR IRDVQCTGRG AHVVAGTAGY CFGNLHIPGY
NLPWEDPSFQ YPGNFARPLE VAIEASNGAS DYGNKFGEPV LAGFARSLGL QLPDGQRREW
IKPIMFSGGI GSMEADHISK EAPEPGMEVV KVGGPVYRIG VGGGAASSVQ VQGDNTSDLD
FGAVQRGDPE MEQKMNRVIR ACVEAPKGNP ICSLHDQGAG GNGNVLKELS DPAGAIIYTS
RFQLGDPTLN ALEIWGAEYQ ESNALLLRSP NRDFLTHVSA RERCPACFVG TITGDRRIVL
VDDRECPVRR NGQGDAPPTP LPTPVDLELE WVLGKMPRKE FFLQRKPPML QPLALPPGLS
VHQALERVLR LPAVASKRYL TNKVDRSVGG LVAQQQCVGP LQTPLADVAV VALSHEELIG
AATALGEQPV KSLLDPKVAA RLAVAEALTN LVFALVTDLR DVKCSGNWMW AAKLPGEGAA
LADACEAMVA VMAALGVAVD GGKDSLSMAA RVGTETVRAP GSLVISAYAV CPDITATVTP
DLKHPEGRGH LLYVALSPGQ HRLGGTALAQ CFSQLGEHPP DLDLPENLVR AFSITQGLLK
DRLLCSGHDV SDGGLVTCLL EMAFAGNCGL QVDVPVPRVD VLSVLFAEEP GLVLEVQEPD
LAQVLKRYRD AGLHCLELGH TGEAGPHAMV RVSVNGAVVL EEPVGELRAL WEETSFQLDR
LQAEPRCVAE EERGLRERMG PSYCLPPTFP KASVPREPGG PSPRVAILRE EGSNGDREMA
DAFHLAGFEV WDVTMQDLCS GAIGLDTFRG VAFVGGFSYA DVLGSAKGWA AAVTFHPRAG
AELRRFRKRP DTFSLGVCNG CQLLALLGWV GGDPNEDAAE MGPDSQPARP GLLLRHNLSG
RYESRWASVR VGPGPALMLR GMEGAVLPVW SAHGEGYVAF SSPELQAQIE ARGLAPLHWA
DDDGNPTEQY PLNPNGSPGG VAGICSCDGR HLAVMPHPER AVRPWQWAWR PPPFDTLTTS
PWLQLFINAR NWTLEGSC
//
MIM
602133
*RECORD*
*FIELD* NO
602133
*FIELD* TI
*602133 PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; PFAS
;;PHOSPHORIBOSYLFORMYLGLYCINAMIDE AMIDOTRANSFERASE; FGARAT
read more*FIELD* TX
DESCRIPTION
Five-prime-phosphoribosyl N-formylglycinamide (FGAR) amidotransferase
(EC 6.3.5.3) catalyzes the fourth reaction in the de novo synthesis of
purines, that is, the conversion of FGAR to 5-prime-phosphoribosyl
N-formylglycinamidine (FGAM) (summary by Barnes et al., 1994).
CLONING
Barnes et al. (1994) purified and characterized
phosphoribosylformylglycinamide amidotransferase (FGARAT) the fourth
enzyme in the de novo purine pathway.
GENE FUNCTION
The human GARS-AIRS-GART locus (138440), located on chromosome 21,
encodes 3 of the 10 enzymatic steps necessary for the conversion of
phosphoribosyl pyrophosphate to inosine monophosphate by the de novo
purine pathway. The 3 enzyme activities are encoded in a linear,
nonoverlapping fashion on the GARS-AIRS-GART mRNA, starting at the
5-prime end of the cDNA. These enzymatic activities catalyze the second,
fifth, and third step of the de novo purine pathway, respectively.
FGARAT catalyzes the fourth step in the pathway (summary by Brodsky et
al., 1997).
Brodsky et al. (1997) reported that, unlike the developmentally
regulated expression of the GARS-AIRS-GART locus, expression of the
FGARAT gene appears to be constitutive.
MAPPING
By analysis of somatic cell hybrids, Barnes et al. (1994) mapped the
PFAS gene to chromosome 17p.
*FIELD* RF
1. Barnes, T. S.; Bleskan, J. H.; Hart, I. M.; Walton, K. A.; Barton,
J. W.; Patterson, D.: Purification of, generation of monoclonal antibodies
to, and mapping of phosphoribosyl N-formylglycinamide amidotransferase. Biochemistry 33:
1850-1860, 1994.
2. Brodsky, G.; Barnes, T.; Bleskan, J.; Becker, L.; Cox, M.; Patterson,
D.: The human GARS-AIRS-GART gene encodes two proteins which are
differentially expressed during human brain development and temporally
overexpressed in cerebellum of individuals with Down syndrome. Hum.
Molec. Genet. 6: 2043-2050, 1997.
*FIELD* CD
Victor A. McKusick: 11/26/1997
*FIELD* ED
alopez: 03/02/2012
alopez: 3/16/2010
mark: 12/20/1997
jenny: 12/2/1997
jenny: 11/26/1997
*RECORD*
*FIELD* NO
602133
*FIELD* TI
*602133 PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE; PFAS
;;PHOSPHORIBOSYLFORMYLGLYCINAMIDE AMIDOTRANSFERASE; FGARAT
read more*FIELD* TX
DESCRIPTION
Five-prime-phosphoribosyl N-formylglycinamide (FGAR) amidotransferase
(EC 6.3.5.3) catalyzes the fourth reaction in the de novo synthesis of
purines, that is, the conversion of FGAR to 5-prime-phosphoribosyl
N-formylglycinamidine (FGAM) (summary by Barnes et al., 1994).
CLONING
Barnes et al. (1994) purified and characterized
phosphoribosylformylglycinamide amidotransferase (FGARAT) the fourth
enzyme in the de novo purine pathway.
GENE FUNCTION
The human GARS-AIRS-GART locus (138440), located on chromosome 21,
encodes 3 of the 10 enzymatic steps necessary for the conversion of
phosphoribosyl pyrophosphate to inosine monophosphate by the de novo
purine pathway. The 3 enzyme activities are encoded in a linear,
nonoverlapping fashion on the GARS-AIRS-GART mRNA, starting at the
5-prime end of the cDNA. These enzymatic activities catalyze the second,
fifth, and third step of the de novo purine pathway, respectively.
FGARAT catalyzes the fourth step in the pathway (summary by Brodsky et
al., 1997).
Brodsky et al. (1997) reported that, unlike the developmentally
regulated expression of the GARS-AIRS-GART locus, expression of the
FGARAT gene appears to be constitutive.
MAPPING
By analysis of somatic cell hybrids, Barnes et al. (1994) mapped the
PFAS gene to chromosome 17p.
*FIELD* RF
1. Barnes, T. S.; Bleskan, J. H.; Hart, I. M.; Walton, K. A.; Barton,
J. W.; Patterson, D.: Purification of, generation of monoclonal antibodies
to, and mapping of phosphoribosyl N-formylglycinamide amidotransferase. Biochemistry 33:
1850-1860, 1994.
2. Brodsky, G.; Barnes, T.; Bleskan, J.; Becker, L.; Cox, M.; Patterson,
D.: The human GARS-AIRS-GART gene encodes two proteins which are
differentially expressed during human brain development and temporally
overexpressed in cerebellum of individuals with Down syndrome. Hum.
Molec. Genet. 6: 2043-2050, 1997.
*FIELD* CD
Victor A. McKusick: 11/26/1997
*FIELD* ED
alopez: 03/02/2012
alopez: 3/16/2010
mark: 12/20/1997
jenny: 12/2/1997
jenny: 11/26/1997