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Reviewed, UniProtKB/Swiss-Prot P31939 (PUR9_HUMAN)

Last modified June 16, 2009. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional purine biosynthesis protein PURH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC
Gene names
Name: ATIC
Synonyms: PURH
ORF Names: OK/SW-cl.86
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1.

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region.

Involvement in disease

Defects in ATIC are the cause of AICA-ribosuria [MIM:608688]; also known as AICA-ribosiduria. AICA-ribosuria is a neurologically devastating inborn error of purine biosynthesis. AICA-ribosuria patients excrete massive amounts of AICA-riboside in the urine and accumulate AICA-ribotide and its derivatives in erythrocytes and fibroblasts. AICA-ribosuria causes profound mental retardation, epilepsy, dysmorphic features and congenital blindness. Ref.11

Sequence similarities

Belongs to the purH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Bifunctional purine biosynthesis protein PURH
PRO_0000192156

Amino acid modifications

Modified residue1041Phosphotyrosine Ref.9

Natural variations

Natural variant1161T → S: dbSNP rs2372536.
VAR_019306
Natural variant4261K → R in AICA-ribosuria; loss of AICAR transformylase activity.
VAR_019307

Experimental info

Sequence conflict1 – 66MAPGQL → MSSLS Ref.1
Sequence conflict1651D → G in AAA97405. Ref.1

Secondary structure

........................................................................................................ 592
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31939-1 [UniParc].

Last modified October 10, 2002. Version 3.
Checksum: AD778892021F0888

FASTA59264,616
        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 

« Hide

References

« Hide 'large scale' references
[1]"The human purH gene product, 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase. Cloning, sequencing, expression, purification, kinetic analysis, and domain mapping."
Rayl E.A., Moroson B.A., Beardsley G.P.
J. Biol. Chem. 271:2225-2233(1996) [PubMed: 8567683] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Hepatoma.
[2]"Isolation of human purH gene expressed in the rodent transformant cells by subtractive enrichment of 3'-untranslated region of human transcript."
Yamauchi M., Seki N., Mita K., Saito T., Tsuji S., Hongo E., Morimyo M., Shiomi T., Koyama H.
DNA Res. 2:269-275(1995) [PubMed: 8867801] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[3]"Characterization of molecularly cloned human 5-aminoimidazole-4-carboxamide ribonucleotide transformylase."
Sugita T., Aya H., Ueno M., Ishizuka T., Kawashima K.
J. Biochem. 122:309-313(1997) [PubMed: 9378707] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Placenta.
[4]"Identification of immuno-peptidmics that are recognized by tumor-reactive CTL generated from TIL of colon cancer patients."
Shichijo S., Itoh K.
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon adenocarcinoma.
[5]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed: 15815621] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[7]Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 15-39; 91-97; 178-194; 208-225; 267-285 AND 417-426, MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[8]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed: 1286667] [Abstract]
Cited for: PROTEIN SEQUENCE OF 178-189 AND 267-281.
Tissue: Keratinocyte.
[9]"Global survey of phosphotyrosine signaling identifies oncogenic kinases 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. expand/collapse author list , 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) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-104, MASS SPECTROMETRY.
[10]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[11]"AICA-ribosiduria: a novel, neurologically devastating inborn error of purine biosynthesis caused by mutation of ATIC."
Marie S., Heron B., Bitoun P., Timmerman T., Van Den Berghe G., Vincent M.-F.
Am. J. Hum. Genet. 74:1276-1281(2004) [PubMed: 15114530] [Abstract]
Cited for: VARIANT AICA-RIBOSURIA ARG-426, CHARACTERIZATION OF VARIANT AICA-RIBOSURIA ARG-426.
+Additional computationally mapped references.

Cross-references

Sequence databases

U37436 mRNA. Translation: AAA97405.1.
D82348 mRNA. Translation: BAA11559.1.
D89976 mRNA. Translation: BAA21762.1.
AB062403 mRNA. Translation: BAB93490.1.
AC073284 Genomic DNA. Translation: AAY24062.1.
BC008879 mRNA. Translation: AAH08879.1.
IPIIPI00289499.
PIRJC4642.
RefSeqNP_004035.2.
UniGeneHs.90280

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1P4RX-ray2.55A/B1-592[»]
1PKXX-ray1.90A/B/C/D1-592[»]
1PL0X-ray2.60A/B/C/D1-592[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP31939. 15 interactions.

PTM databases

PhosphoSiteP31939.

2-D gel databases

Aarhus/Ghent-2DPAGE2403. IEF.
REPRODUCTION-2DPAGEIPI00289499.

Proteomic databases

PeptideAtlasP31939.
PRIDEP31939.

Genome annotation databases

EnsemblENSG00000138363. Homo sapiens. [Contig view]
GeneID471.
KEGGhsa:471.

Organism-specific databases

GeneCardsGC02P215885.
H-InvDBHIX0002802.
HGNCHGNC:794. ATIC.
HPACAB013462.
MIM601731. gene.
608688. phenotype.
PharmGKBPA25094.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP31939.
HOVERGENP31939.
OMAP31939. VVKHVKS.

Enzyme and pathway databases

BRENDA2.1.2.3. 247.
3.5.4.10. 247.
ReactomeREACT_1698. Nucleotide metabolism.

Gene expression databases

ArrayExpressP31939.
BgeeP31939.
CleanExHS_ATIC.
GermOnlineENSG00000138363. Homo sapiens.

Family and domain databases

InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHas_formly.
IPR011607. MGS.
[Graphical view]
PANTHERPTHR11692. AICARFT_IMPCHas. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
[Graphical view]
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Other Resources

BindingDBP31939.
DrugBankDB00116. Tetrahydrofolic acid.
NextBio1945.
SOURCESearch...

Entry information

Entry namePUR9_HUMAN
AccessionPrimary (citable) accession number: P31939
Secondary accession number(s): Q13856, Q53S28
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 10, 2002
Last modified: June 16, 2009
This is version 97 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents