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UniProtKB/Swiss-Prot entry P31939


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PUR9_HUMAN
Primary accession number P31939
Secondary accession number Q13856
Integrated into Swiss-Prot on July 1, 1993
Sequence was last modified on October 10, 2002 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 91)
Name and origin of the protein
Protein name Bifunctional purine biosynthesis protein PURH
Synonyms None
Includes Phosphoribosylaminoimidazolecarboxamide formyltransferase
     (EC 2.1.2.3)
     (5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase)
     (AICAR transformylase)
IMP cyclohydrolase
     (EC 3.5.4.10)
     (Inosinicase)
     (IMP synthetase)
     (ATIC)
Gene name
Name: ATIC
Synonyms: PURH
ORFNames: OK/SW-cl.86
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hepatoma;
DOI=10.1074/jbc.271.4.2225; PubMed=8567683 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Testis;
DOI=10.1093/dnares/2.6.269; PubMed=8867801 [NCBI, ExPASy, EBI, Israel, Japan]
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].
TISSUE=Placenta;
PubMed=9378707 [NCBI, ExPASy, EBI, Israel, Japan]
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].
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].
TISSUE=Pancreas;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
PROTEIN SEQUENCE OF 178-194, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 178-189 AND 267-281.
TISSUE=Keratinocyte;
DOI=10.1002/elps.11501301199; PubMed=1286667 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[9]
VARIANT AICA-RIBOSURIA ARG-426, AND CHARACTERIZATION OF VARIANT AICA-RIBOSURIA ARG-426.
DOI=10.1086/421475; PubMed=15114530 [NCBI, ExPASy, EBI, Israel, Japan]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U37436; AAA97405.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D82348; BAA11559.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D89976; BAA21762.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB062403; BAB93490.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC008879; AAH08879.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR JC4642; JC4642.
RefSeq NP_004035.2; -.
UniGene Hs.90280
3D structure databases
PDB
1P4R; X-ray; 2.55 A; A/B=1-592.[ExPASy / RCSB / EBI]
1PKX; X-ray; 1.90 A; A/B/C/D=1-592.[ExPASy / RCSB / EBI]
1PL0; X-ray; 2.60 A; A/B/C/D=1-592.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1P4R; -.
1PKX; -.
1PL0; -.
ModBase P31939.
Protein-protein interaction databases
IntAct P31939; -.
PTM databases
PhosphoSite P31939; -.
Enzyme and pathway databases
Reactome REACT_1698; Nucleotide metabolism.
2D gel databases
Aarhus/Ghent-2DPAGE 2403; IEF.
REPRODUCTION-2DPAGE IPI00289499; -.
Organism-specific databases
H-InvDB HIX0002802; -.
HGNC HGNC:794; ATIC.
GenAtlas ATIC.
HPA CAB013462; -.
MIM 601731; gene. [NCBI / EBI]
608688; phenotype. [NCBI / EBI]
PharmGKB PA25094; -.
GeneCards P31939.
Gene expression databases
ArrayExpress P31939; -.
CleanEx HS_ATIC; -.
GermOnline ENSG00000138363; Homo sapiens.
Ontologies
GO
GO:0003937; Molecular function: IMP cyclohydrolase activity (traceable author statement from ProtInc).
GO:0004643; Molecular function: phosphoribosylaminoimidazolecarboxamide formyltransferase activity (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006188; Biological process: IMP biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR002695; AICARFT_IMPCHas.
IPR013982; AICARFT_IMPCHas_formly.
IPR011607; MGS.
Graphical view of domain structure.
PANTHER PTHR11692; AICARFT_IMPCHas; 1.
Pfam PF01808; AICARFT_IMPCHas; 1.
PF02142; MGS; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000414; AICARFT_IMPCHas; 1.
SMART SM00798; AICARFT_IMPCHas; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00355; purH; 1.
BLOCKS P31939.
ProtoNet P31939.
Proteomic databases
PeptideAtlas P31939; -.
Genome annotation databases
Ensembl ENSG00000138363; Homo sapiens. [Contig view]
GeneID 471; -.
KEGG hsa:471; -.
Phylogenomic databases
HOGENOM P31939; -.
HOVERGEN P31939; -.
Other
DrugBank DB00116; Tetrahydrofolic acid.
LinkHub P31939; -.
NextBio 1945; -.
SOURCE ATIC; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; Disease mutation; Epilepsy; Hydrolase; Multifunctional enzyme; Phosphoprotein; Polymorphism; Purine biosynthesis; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   592  592     Bifunctional purine biosynthesis protein PURH. PRO_0000192156
MOD_RES   104   104        Phosphotyrosine. 
VARIANT   116   116  1     T -> S (in dbSNP:rs2372536 [NCBI]). VAR_019306 [3D]
VARIANT   426   426  1     K -> R (in AICA-ribosuria; loss of AICAR transformylase activity). VAR_019307 [3D]
CONFLICT   1     6        MAPGQL -> MSSLS (in Ref. 1). 
CONFLICT   165   165        D -> G (in Ref. 1; AAA97405). 
STRAND   6    10  5      
HELIX   17    25  9      
TURN   26    28  3      
STRAND   30    33  4      
HELIX   35    42  8      
TURN   43    45  3      
HELIX   51    55  5      
TURN   61    64  4      
STRAND   65    67  3      
HELIX   70    77  8      
HELIX   82    91  10      
STRAND   96   101  6      
HELIX   106   111  6      
HELIX   117   122  6      
HELIX   127   137  11      
TURN   138   141  4      
STRAND   143   145  3      
HELIX   148   150  3      
HELIX   151   160  10      
HELIX   168   197  30      
TURN   200   202  3      
STRAND   203   207  5      
STRAND   209   211  3      
STRAND   217   220  4      
STRAND   222   225  4      
STRAND   227   233  7      
HELIX   237   257  21      
STRAND   261   266  6      
STRAND   269   275  7      
HELIX   281   286  6      
HELIX   290   295  6      
HELIX   298   308  11      
TURN   311   316  6      
STRAND   317   323  7      
HELIX   327   334  8      
STRAND   338   344  7      
HELIX   348   360  13      
STRAND   363   367  5      
STRAND   375   381  7      
STRAND   384   389  6      
HELIX   397   400  4      
HELIX   412   426  15      
STRAND   433   437  5      
STRAND   440   445  6      
HELIX   451   467  17      
HELIX   471   474  4      
HELIX   486   496  11      
HELIX   503   509  7      
STRAND   512   514  3      
HELIX   521   528  8      
STRAND   534   540  7      
HELIX   546   552  7      
TURN   553   555  3      
STRAND   556   562  7      
HELIX   568   578  11      
STRAND   581   586  6      
Sequence information
Length: 592 AA [This is the length of the unprocessed precursor] Molecular weight: 64616 Da [This is the MW of the unprocessed precursor] CRC64: AD778892021F0888 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAPGQLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD VSELTGFPEM 

        70         80         90        100        110        120 
LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA CNLYPFVKTV ASPGVTVEEA 

       130        140        150        160        170        180 
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YVVVSTEMQS SESKDTSLET RRQLALKAFT 

       190        200        210        220        230        240 
HTAQYDEAIS DYFRKQYSKG VSQMPLRYGM NPHQTPAQLY TLQPKLPITV LNGAPGFINL 

       250        260        270        280        290        300 
CDALNAWQLV KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS 

       310        320        330        340        350        360 
AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA LTILSKKKNG 

       370        380        390        400        410        420 
NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF SNVVTKNKDL PESALRDLIV 

       430        440        450        460        470        480 
ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS RIHCTRLAGD KANYWWLRHH PQVLSMKFKT 

       490        500        510        520        530        540 
GVKRAEISNA IDQYVTGTIG EDEDLIKWKA LFEEVPELLT EAEKKEWVEK LTEVSISSDA 

       550        560        570        580        590 
FFPFRDNVDR AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH 

P31939 in FASTA format

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