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Protein Page:
ATASE (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
ATASE Homotetramer. Note: This description may include information from UniProtKB.
Protein type: Nucleotide Metabolism - purine; EC 2.4.2.14; Amino Acid Metabolism - alanine, aspartate and glutamate; Transferase
Cellular Component: cytosol
Molecular Function: 4 iron, 4 sulfur cluster binding; metal ion binding; amidophosphoribosyltransferase activity
Biological Process: lactation; organ regeneration; maternal process involved in pregnancy; nucleobase, nucleoside and nucleotide metabolic process; nucleoside metabolic process; purine nucleotide biosynthetic process; purine base metabolic process; protein homotetramerization; 'de novo' IMP biosynthetic process; purine ribonucleoside monophosphate biosynthetic process; purine base biosynthetic process; cellular response to insulin stimulus; glutamine catabolic process; kidney development; G1/S transition of mitotic cell cycle
Reference #:  Q06203 (UniProtKB)
Alt. Names/Synonyms: Amidophosphoribosyltransferase; ATase; glutamine phosphoribosylpyrophosphatate amidotransferase; Glutamine phosphoribosylpyrophosphate amidotransferase; glutamine PRPP amidotransferase; GPAT; phosphoribosyl pyrophosphate amidotransferase; PPAT; PRAT; PUR1
Gene Symbols: PPAT
Molecular weight: 57,399 Da
Basal Isoelectric point: 6.3  Predict pI for various phosphorylation states
Select Structure to View Below

ATASE

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T52-p QESAGIVtSDGSSVP
0 1 T60 SDGSSVPTFkSHKGM
0 1 T60 SDGSSVPTFkSHKGM
0 3 K62-ac GSSVPTFkSHKGMGL
0 1 K62-ub GSSVPTFkSHKGMGL
0 1 K80-ub VFTEDNLkkLYVSNL
0 4 K81-ac FTEDNLkkLYVSNLG
0 8 Y83 EDNLkkLYVSNLGIG
0 8 K99-ac TRYATTGkCELENCQ
0 1 T166-p PPQEQDDtPDWVARI
0 1 K220 PVSDINDKEKKTSET
0 1 T356-p KNRYVGRtFIQPNMR
0 1 K371-ac LRQLGVAkkFGVLSD
0 2 K372-ub RQLGVAkkFGVLSDN
0 1 K381-ub GVLSDNFkGKRIVLV
0 2 K403-ub NTISPIIkLLKEsGA
0 1 S408-p IIkLLKEsGAkEVHI
0 1 K411-ub LLKEsGAkEVHIRVA
0 1 K482-ac FKKQKEKkHDIMIQE
0 1 K499-ac NGLECFEkSGHCTAC
  mouse

 
T52 QESAGIVTSDGSAVP
K60-ac SDGSAVPkFRVHKGM
K60-ub SDGSAVPkFRVHKGM
R62 GSAVPkFRVHKGMGL
R62 GSAVPkFRVHKGMGL
K80 VFTEDNLKKLyDSNL
K81 FTEDNLKKLyDSNLG
Y83-p EDNLKKLyDSNLGIG
K99 TRYATTGKCELENCQ
A166 PPQEKDDAPDWVARI
K220-ub PVSDVNDkEKKSSET
T356 KNRYVGRTFIQPNMR
K371 LRQLGVAKkFGVLSD
K372-ub RQLGVAKkFGVLSDN
K381 GVLSDNFKGKRIVLI
K403-ub NTISPIIkLLKESGA
S408 IIkLLKESGAKEVHI
K411 LLKESGAKEVHIRVA
- gap
- gap
  rat

 
T52 QESAGIVTSDGSSVP
K60 SDGSSVPKFRVHKGM
K60 SDGSSVPKFRVHKGM
R62 GSSVPKFRVHKGMGL
R62 GSSVPKFRVHKGMGL
K80 VFTEDNLKKLYVSNL
K81 FTEDNLKKLYVSNLG
Y83 EDNLKKLYVSNLGIG
K99 TRYATTGKCELENCQ
T166 PPQEQDDTPDWVARI
K220 PVSDINDKEKKSSET
T356 KNRYVGRTFIQPNMR
K371 LRQLGVAKKFGVLSD
K372 RQLGVAKKFGVLSDN
K381 GVLSDNFKGKRIVLI
K403 NTISPIIKLLKESGA
S408 IIKLLKESGAKEVHI
K411 LLKESGAKEVHIRVA
K482 FKKQKVKKRDITIQE
K499 NGLEYFEKTGHCTAC
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