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O15067

- PUR4_HUMAN

UniProt

O15067 - PUR4_HUMAN

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Protein

Phosphoribosylformylglycinamidine synthase

Gene

PFAS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate By similarity.By similarity

Catalytic activityi

ATP + N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide + L-glutamine + H2O = ADP + phosphate + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei706 – 7061ATP; via carbonyl oxygenBy similarity
Metal bindingi707 – 7071MagnesiumBy similarity
Metal bindingi746 – 7461MagnesiumBy similarity
Metal bindingi750 – 7501MagnesiumBy similarity
Metal bindingi909 – 9091MagnesiumBy similarity
Binding sitei911 – 9111ATPBy similarity
Active sitei1158 – 11581NucleophileBy similarity
Active sitei1297 – 12971By similarity
Active sitei1299 – 12991By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi322 – 33312ATPSequence AnalysisAdd
BLAST
Nucleotide bindingi402 – 4043ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. phosphoribosylformylglycinamidine synthase activity Source: UniProtKB

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB
  2. glutamine metabolic process Source: UniProtKB-KW
  3. nucleobase-containing small molecule metabolic process Source: Reactome
  4. purine nucleobase metabolic process Source: Reactome
  5. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
  6. response to drug Source: Ensembl
  7. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Purine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS11329-MONOMER.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
UniPathwayiUPA00074; UER00128.

Protein family/group databases

MEROPSiC56.972.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoribosylformylglycinamidine synthase (EC:6.3.5.3)
Short name:
FGAM synthase
Short name:
FGAMS
Alternative name(s):
Formylglycinamide ribonucleotide amidotransferase
Short name:
FGAR amidotransferase
Short name:
FGAR-AT
Formylglycinamide ribotide amidotransferase
Gene namesi
Name:PFAS
Synonyms:KIAA0361
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:8863. PFAS.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13381338Phosphoribosylformylglycinamidine synthasePRO_0000100401Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei569 – 5691Phosphoserine3 Publications
Modified residuei619 – 6191Phosphothreonine2 Publications
Modified residuei623 – 6231Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO15067.
PaxDbiO15067.
PRIDEiO15067.

PTM databases

PhosphoSiteiO15067.

Expressioni

Gene expression databases

BgeeiO15067.
CleanExiHS_PFAS.
ExpressionAtlasiO15067. baseline and differential.
GenevestigatoriO15067.

Organism-specific databases

HPAiHPA022140.
HPA022886.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
EPB41P111711EBI-1052653,EBI-1050906
HLA-BP304801EBI-1052653,EBI-1054175
MCCP235081EBI-1052653,EBI-307531
TFE3P195321EBI-1052653,EBI-1048957
TNFRSF10DQ9UBN61EBI-1052653,EBI-1044859
TRAF6Q9Y4K31EBI-1052653,EBI-359276
VHLP403371EBI-1052653,EBI-301246

Protein-protein interaction databases

BioGridi111221. 50 interactions.
IntActiO15067. 5 interactions.
STRINGi9606.ENSP00000313490.

Structurei

3D structure databases

ProteinModelPortaliO15067.
SMRiO15067. Positions 304-572, 1063-1302.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1064 – 1302239Glutamine amidotransferase type-1Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the FGAMS family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiCOG0046.
GeneTreeiENSGT00390000007600.
HOGENOMiHOG000261358.
HOVERGENiHBG108309.
InParanoidiO15067.
KOiK01952.
OMAiPEPLNGP.
OrthoDBiEOG7353X4.
PhylomeDBiO15067.
TreeFamiTF106371.

Family and domain databases

Gene3Di3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPiMF_00419. PurL_1.
InterProiIPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM_N-like.
[Graphical view]
PfamiPF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 2 hits.
TIGRFAMsiTIGR01735. FGAM_synt. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15067-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSPVLHFYVR PSGHEGAAPG HTRRKLQGKL PELQGVETEL CYNVNWTAEA
60 70 80 90 100
LPSAEETKKL MWLFGCPLLL DDVARESWLL PGSNDLLLEV GPRLNFSTPT
110 120 130 140 150
STNIVSVCRA TGLGPVDRVE TTRRYRLSFA HPPSAEVEAI ALATLHDRMT
160 170 180 190 200
EQHFPHPIQS FSPESMPEPL NGPINILGEG RLALEKANQE LGLALDSWDL
210 220 230 240 250
DFYTKRFQEL QRNPSTVEAF DLAQSNSEHS RHWFFKGQLH VDGQKLVHSL
260 270 280 290 300
FESIMSTQES SNPNNVLKFC DNSSAIQGKE VRFLRPEDPT RPSRFQQQQG
310 320 330 340 350
LRHVVFTAET HNFPTGVCPF SGATTGTGGR IRDVQCTGRG AHVVAGTAGY
360 370 380 390 400
CFGNLHIPGY NLPWEDPSFQ YPGNFARPLE VAIEASNGAS DYGNKFGEPV
410 420 430 440 450
LAGFARSLGL QLPDGQRREW IKPIMFSGGI GSMEADHISK EAPEPGMEVV
460 470 480 490 500
KVGGPVYRIG VGGGAASSVQ VQGDNTSDLD FGAVQRGDPE MEQKMNRVIR
510 520 530 540 550
ACVEAPKGNP ICSLHDQGAG GNGNVLKELS DPAGAIIYTS RFQLGDPTLN
560 570 580 590 600
ALEIWGAEYQ ESNALLLRSP NRDFLTHVSA RERCPACFVG TITGDRRIVL
610 620 630 640 650
VDDRECPVRR NGQGDAPPTP LPTPVDLELE WVLGKMPRKE FFLQRKPPML
660 670 680 690 700
QPLALPPGLS VHQALERVLR LPAVASKRYL TNKVDRSVGG LVAQQQCVGP
710 720 730 740 750
LQTPLADVAV VALSHEELIG AATALGEQPV KSLLDPKVAA RLAVAEALTN
760 770 780 790 800
LVFALVTDLR DVKCSGNWMW AAKLPGEGAA LADACEAMVA VMAALGVAVD
810 820 830 840 850
GGKDSLSMAA RVGTETVRAP GSLVISAYAV CPDITATVTP DLKHPEGRGH
860 870 880 890 900
LLYVALSPGQ HRLGGTALAQ CFSQLGEHPP DLDLPENLVR AFSITQGLLK
910 920 930 940 950
DRLLCSGHDV SDGGLVTCLL EMAFAGNCGL QVDVPVPRVD VLSVLFAEEP
960 970 980 990 1000
GLVLEVQEPD LAQVLKRYRD AGLHCLELGH TGEAGPHAMV RVSVNGAVVL
1010 1020 1030 1040 1050
EEPVGELRAL WEETSFQLDR LQAEPRCVAE EERGLRERMG PSYCLPPTFP
1060 1070 1080 1090 1100
KASVPREPGG PSPRVAILRE EGSNGDREMA DAFHLAGFEV WDVTMQDLCS
1110 1120 1130 1140 1150
GAIGLDTFRG VAFVGGFSYA DVLGSAKGWA AAVTFHPRAG AELRRFRKRP
1160 1170 1180 1190 1200
DTFSLGVCNG CQLLALLGWV GGDPNEDAAE MGPDSQPARP GLLLRHNLSG
1210 1220 1230 1240 1250
RYESRWASVR VGPGPALMLR GMEGAVLPVW SAHGEGYVAF SSPELQAQIE
1260 1270 1280 1290 1300
ARGLAPLHWA DDDGNPTEQY PLNPNGSPGG VAGICSCDGR HLAVMPHPER
1310 1320 1330
AVRPWQWAWR PPPFDTLTTS PWLQLFINAR NWTLEGSC
Length:1,338
Mass (Da):144,734
Last modified:January 11, 2011 - v4
Checksum:i273405025B701DAF
GO

Sequence cautioni

The sequence BAA20816.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1326 – 13261F → S(PubMed:10548741)Curated
Sequence conflicti1326 – 13261F → S in BAA20816. (PubMed:9205841)Curated
Sequence conflicti1326 – 13261F → S in AAI46769. (PubMed:15489334)Curated
Sequence conflicti1326 – 13261F → S in AAI67158. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti19 – 191P → S.3 Publications
Corresponds to variant rs9891699 [ dbSNP | Ensembl ].
VAR_055008
Natural varianti367 – 3671P → L.3 Publications
Corresponds to variant rs4791641 [ dbSNP | Ensembl ].
VAR_055009
Natural varianti481 – 4811F → Y.
Corresponds to variant rs35217368 [ dbSNP | Ensembl ].
VAR_055010
Natural varianti621 – 6211L → P.7 Publications
Corresponds to variant rs11078738 [ dbSNP | Ensembl ].
VAR_055011

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002359 mRNA. Translation: BAA20816.1. Different initiation.
AC135178 Genomic DNA. No translation available.
BC146768 mRNA. Translation: AAI46769.1.
BC167158 mRNA. Translation: AAI67158.1.
CCDSiCCDS11136.1.
RefSeqiNP_036525.1. NM_012393.2.
UniGeneiHs.573976.

Genome annotation databases

EnsembliENST00000314666; ENSP00000313490; ENSG00000178921.
GeneIDi5198.
KEGGihsa:5198.
UCSCiuc002gkr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB002359 mRNA. Translation: BAA20816.1 . Different initiation.
AC135178 Genomic DNA. No translation available.
BC146768 mRNA. Translation: AAI46769.1 .
BC167158 mRNA. Translation: AAI67158.1 .
CCDSi CCDS11136.1.
RefSeqi NP_036525.1. NM_012393.2.
UniGenei Hs.573976.

3D structure databases

ProteinModelPortali O15067.
SMRi O15067. Positions 304-572, 1063-1302.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111221. 50 interactions.
IntActi O15067. 5 interactions.
STRINGi 9606.ENSP00000313490.

Chemistry

DrugBanki DB00130. L-Glutamine.

Protein family/group databases

MEROPSi C56.972.

PTM databases

PhosphoSitei O15067.

Proteomic databases

MaxQBi O15067.
PaxDbi O15067.
PRIDEi O15067.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000314666 ; ENSP00000313490 ; ENSG00000178921 .
GeneIDi 5198.
KEGGi hsa:5198.
UCSCi uc002gkr.3. human.

Organism-specific databases

CTDi 5198.
GeneCardsi GC17P008152.
H-InvDB HIX0019361.
HGNCi HGNC:8863. PFAS.
HPAi HPA022140.
HPA022886.
MIMi 602133. gene.
neXtProti NX_O15067.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0046.
GeneTreei ENSGT00390000007600.
HOGENOMi HOG000261358.
HOVERGENi HBG108309.
InParanoidi O15067.
KOi K01952.
OMAi PEPLNGP.
OrthoDBi EOG7353X4.
PhylomeDBi O15067.
TreeFami TF106371.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00128 .
BioCyci MetaCyc:HS11329-MONOMER.
Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

Miscellaneous databases

ChiTaRSi PFAS. human.
GenomeRNAii 5198.
NextBioi 20106.
PROi O15067.
SOURCEi Search...

Gene expression databases

Bgeei O15067.
CleanExi HS_PFAS.
ExpressionAtlasi O15067. baseline and differential.
Genevestigatori O15067.

Family and domain databases

Gene3Di 3.30.1330.10. 2 hits.
3.40.50.880. 1 hit.
HAMAPi MF_00419. PurL_1.
InterProi IPR010918. AIR_synth_C_dom.
IPR000728. AIR_synth_N_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR010073. PRibForGlyAmidine_synth.
IPR016188. PurM_N-like.
[Graphical view ]
Pfami PF00586. AIRS. 1 hit.
PF02769. AIRS_C. 2 hits.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
SSF55326. SSF55326. 2 hits.
SSF56042. SSF56042. 2 hits.
TIGRFAMsi TIGR01735. FGAM_synt. 1 hit.
PROSITEi PS51273. GATASE_TYPE_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human phosphoribosylformylglycinamide amidotransferase (FGARAT): regional mapping, complete coding sequence, isolation of a functional genomic clone, and DNA sequence analysis."
    Patterson D., Bleskan J., Gardiner K., Bowersox J.
    Gene 239:381-391(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-19; LEU-367 AND PRO-621.
  2. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
    Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-19; LEU-367 AND PRO-621.
    Tissue: Brain.
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS SER-19; LEU-367 AND PRO-621.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-619 AND THR-623, VARIANT [LARGE SCALE ANALYSIS] PRO-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  7. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569 AND THR-619, VARIANT [LARGE SCALE ANALYSIS] PRO-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-569, VARIANT [LARGE SCALE ANALYSIS] PRO-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] PRO-621, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPUR4_HUMAN
AccessioniPrimary (citable) accession number: O15067
Secondary accession number(s): A6H8V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 141 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3