Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Bifunctional purine biosynthesis protein PURH  

UniProtKB / Swiss-Prot ID :  PUR9_HUMAN

Gene Name (Synonyms) : 
ATIC, PURH OK/SW-cl.86  

Species :  Homo sapiens (Human). 

Subcellular Localization :   

Protein Function :  Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. 

Protein Sequence MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHP...
Predicted Secondary Structure CCCCEEEEEEEECCCCHHHHHHHHHHCCCEEEECHHHHHHHHHCCCCEEEECCCCCCCCEECCCEEEECH...
Protein Variant
LocationDescription
116T -> S (in dbSNP:rs2372536). VAR_019306
426K -> R (in AICAR; loss of transformylaseactivity).
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
1N-acetylmethionine.----MAPGQ
----CCCCE
10.29UniProtKB
Link-
14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SVSDKTGLV
EEECCCCHH
36.67Phosphositeplus
Link
25PhosphothreonineARNLTALGL
HHHHHHCCC
24.32HPRD
Link
25PhosphothreonineARNLTALGL
HHHHHHCCC
24.32Phosphositeplus
Link
34PhosphoserineNLVASGGTA
EEEECHHHH
30.21HPRD
Link
34PhosphoserineNLVASGGTA
EEEECHHHH
30.21Phosphositeplus
Link
37PhosphothreonineASGGTAKAL
ECHHHHHHH
28.63HPRD
Link
37PhosphothreonineASGGTAKAL
ECHHHHHHH
28.63Phosphositeplus
Link
39Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GGTAKALRD
HHHHHHHHH
48.03Phosphositeplus
Link
66Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GGRVKTLHP
CCCEEEECH
43.97Phosphositeplus
Link
104PhosphotyrosineACNLYPFVK
EECCCCHHH
4.80HPRD
Link
104PhosphotyrosineACNLYPFVK
EECCCCHHH
4.80PhosphoELM
Link
104PhosphotyrosineACNLYPFVK
EECCCCHHH
4.80Phosphositeplus
Link
104Phosphotyrosine.ACNLYPFVK
EECCCCHHH
4.80UniProtKB
Link
177Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)QLALKAFTH
HHHHHHHHH
35.53Phosphositeplus
Link
197PhosphotyrosineFRKQYSKGV
HHHHHCCCC
18.51Phosphositeplus
Link
199Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)KQYSKGVSQ
HHHCCCCCC
59.40Phosphositeplus
Link
199N6-acetyllysineKQYSKGVSQ
HHHCCCCCC
59.40HPRD
Link
199N6-acetyllysineKQYSKGVSQ
HHHCCCCCC
59.40Phosphositeplus
Link
199N6-acetyllysine.KQYSKGVSQ
HHHCCCCCC
59.40UniProtKB
Link
290PhosphotyrosineVCMVYDLYK
HHHHCCCCC
3.55Phosphositeplus
Link
293PhosphotyrosineVYDLYKTLT
HCCCCCCCC
10.07Phosphositeplus
Link
295PhosphothreonineDLYKTLTPI
CCCCCCCCH
23.47Phosphositeplus
Link
300PhosphoserineLTPISAAYA
CCCHHHHHH
14.19Phosphositeplus
Link
303PhosphotyrosineISAAYARAR
HHHHHHHHH
9.06Phosphositeplus
Link
356Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TILSKKKNG
HHHHHCCCC
65.41Phosphositeplus
Link
356N6-acetyllysineTILSKKKNG
HHHHHCCCC
65.41HPRD
Link
389Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HLSQKRNNG
EEEEECCCC
54.43Phosphositeplus
Link
397Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GVVDKSLFS
CCCCHHHHH
37.13Phosphositeplus
Link
405PhosphothreonineSNVVTKNKD
HHHHCCCCC
25.31HPRD
Link
406Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NVVTKNKDL
HHHCCCCCC
50.84Phosphositeplus
Link
434S-nitrosocysteineSNSVCYAKN
CCEEEEEEC
2.47dbSNO
Link
507Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)EDLIKWKAL
CCCCCCHHH
50.36Phosphositeplus
Link
509Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LIKWKALFE
CCCCHHHHH
30.15Phosphositeplus
Link
524Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TEAEKKEWV
HHHHHHHCC
64.14Phosphositeplus
Link
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
Q9H376_HUMANphysical interactionEBI-1067839
intact17353931
HNRDL_HUMANphysical interactionEBI-1068047
intact17353931
CIA30_HUMANphysical interactionEBI-1062884
intact17353931
SNRPA_HUMANphysical interactionEBI-1064848
intact17353931
CMBL_HUMANphysical interactionEBI-1074019
intact17353931
PUR9_HUMANin vitroHPRD:03434HPRD9598063
11096114
PUR8_HUMANENSP00000236959STRING
C1TC_HUMANENSP00000236959STRING
5NT1A_HUMANENSP00000236959STRING
5NT3_HUMANENSP00000236959STRING
NT5C_HUMANENSP00000236959STRING
AMPD3_HUMANENSP00000236959STRING
AMPD2_HUMANENSP00000236959STRING
5NTD_HUMANENSP00000236959STRING
GMPR1_HUMANENSP00000236959STRING
PUR1_HUMANENSP00000236959STRING
PUR6_HUMANENSP00000236959STRING
GCST_HUMANENSP00000236959STRING
ENTP3_HUMANENSP00000236959STRING
CANT1_HUMANENSP00000236959STRING
GLYC_HUMANENSP00000236959STRING
IMDH2_HUMANENSP00000236959STRING
GLYM_HUMANENSP00000236959STRING
ENTP5_HUMANENSP00000236959STRING
5NTC_HUMANENSP00000236959STRING
ENTP8_HUMANENSP00000236959STRING
ENTP8_HUMANENSP00000236959STRING
IMDH1_HUMANENSP00000236959STRING
GMPR2_HUMANENSP00000236959STRING
ENTP4_HUMANENSP00000236959STRING
5NT1B_HUMANENSP00000236959STRING
- top -

Disease Reference
Kegg disease
OMIM disease
608688AICAR transformylase/IMP cyclohydrolase deficiency (AICAR)
Drug Reference
DrugBank
DB00563Methotrexate
DB00642Pemetrexed
DB00116Tetrahydrofolic acid
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104, AND MASSSPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures