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Protein

Bifunctional purine biosynthesis protein PURH

Gene

ATIC

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

Functioni

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.1 Publication

Catalytic activityi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei137 – 1371Proton acceptorSequence Analysis
Sitei266 – 2661Transition state stabilizerSequence Analysis
Active sitei267 – 2671Proton acceptorCurated
Binding sitei316 – 3161AICAR; via carbonyl oxygen1 Publication
Binding sitei339 – 3391AICAR1 Publication
Binding sitei431 – 4311AICAR; shared with dimeric partner1 Publication
Binding sitei451 – 4511AICAR; shared with dimeric partner1 Publication
Binding sitei541 – 5411AICAR; via carbonyl oxygen; shared with dimeric partner1 Publication
Binding sitei588 – 5881AICAR; shared with dimeric partner1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 143IMP
Nucleotide bindingi34 – 374IMP
Nucleotide bindingi64 – 674IMP
Nucleotide bindingi101 – 1044IMP
Nucleotide bindingi125 – 1273IMP

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: Reactome
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: Reactome
  3. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
  2. brainstem development Source: Ensembl
  3. cerebellum development Source: Ensembl
  4. cerebral cortex development Source: Ensembl
  5. dihydrofolate metabolic process Source: Ensembl
  6. nucleobase-containing compound metabolic process Source: ProtInc
  7. nucleobase-containing small molecule metabolic process Source: Reactome
  8. nucleoside metabolic process Source: Ensembl
  9. organ regeneration Source: Ensembl
  10. purine nucleobase metabolic process Source: Reactome
  11. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
  12. response to inorganic substance Source: Ensembl
  13. small molecule metabolic process Source: Reactome
  14. tetrahydrofolate biosynthetic process Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciMetaCyc:HS06490-MONOMER.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP31939.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PURH
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC:2.1.2.3)
Alternative name(s):
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
AICAR transformylase
IMP cyclohydrolase (EC:3.5.4.10)
Alternative name(s):
ATIC
IMP synthase
Inosinicase
Gene namesi
Name:ATIC
Synonyms:PURH
ORF Names:OK/SW-cl.86
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:794. ATIC.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProtKB
  3. membrane Source: UniProtKB
  4. mitochondrion Source: Ensembl
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

AICAR transformylase/IMP cyclohydrolase deficiency1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA neurologically devastating inborn error of purine biosynthesis. Patients excrete massive amounts of AICA-riboside in the urine and accumulate AICA-ribotide and its derivatives in erythrocytes and fibroblasts. AICAR causes profound mental retardation, epilepsy, dysmorphic features and congenital blindness.

See also OMIM:608688
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti426 – 4261K → R in AICAR; loss of transformylase activity. 1 Publication
VAR_019307

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MIMi608688. phenotype.
Orphaneti250977. AICA-ribosiduria.
PharmGKBiPA25094.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Bifunctional purine biosynthesis protein PURHPRO_0000192156Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei199 – 1991N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP31939.
PaxDbiP31939.
PeptideAtlasiP31939.
PRIDEiP31939.

2D gel databases

REPRODUCTION-2DPAGEIPI00289499.
UCD-2DPAGEP31939.

PTM databases

PhosphoSiteiP31939.

Expressioni

Gene expression databases

BgeeiP31939.
CleanExiHS_ATIC.
ExpressionAtlasiP31939. baseline and differential.
GenevestigatoriP31939.

Organism-specific databases

HPAiCAB013462.
HPA021012.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

BioGridi106961. 49 interactions.
IntActiP31939. 4 interactions.
MINTiMINT-4999053.
STRINGi9606.ENSP00000236959.

Structurei

Secondary structure

1
592
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 105Combined sources
Helixi17 – 259Combined sources
Turni26 – 283Combined sources
Beta strandi30 – 334Combined sources
Helixi35 – 428Combined sources
Turni43 – 453Combined sources
Helixi51 – 555Combined sources
Turni61 – 644Combined sources
Beta strandi65 – 673Combined sources
Helixi70 – 778Combined sources
Helixi82 – 9110Combined sources
Beta strandi96 – 1016Combined sources
Helixi106 – 1116Combined sources
Helixi117 – 1226Combined sources
Helixi127 – 13711Combined sources
Turni138 – 1414Combined sources
Beta strandi143 – 1453Combined sources
Helixi148 – 1503Combined sources
Helixi151 – 16010Combined sources
Beta strandi161 – 1655Combined sources
Helixi168 – 19730Combined sources
Turni200 – 2023Combined sources
Beta strandi203 – 2075Combined sources
Beta strandi209 – 2113Combined sources
Beta strandi217 – 2204Combined sources
Beta strandi222 – 2254Combined sources
Beta strandi227 – 2337Combined sources
Helixi237 – 25721Combined sources
Beta strandi261 – 2666Combined sources
Beta strandi269 – 2757Combined sources
Helixi281 – 2866Combined sources
Helixi290 – 2956Combined sources
Helixi298 – 30811Combined sources
Turni311 – 3166Combined sources
Beta strandi317 – 3237Combined sources
Helixi327 – 3348Combined sources
Beta strandi338 – 3447Combined sources
Helixi348 – 36013Combined sources
Beta strandi363 – 3675Combined sources
Beta strandi375 – 3817Combined sources
Beta strandi384 – 3896Combined sources
Helixi397 – 4004Combined sources
Helixi412 – 42615Combined sources
Beta strandi433 – 4375Combined sources
Beta strandi440 – 4456Combined sources
Helixi451 – 46717Combined sources
Helixi471 – 4744Combined sources
Helixi486 – 49611Combined sources
Helixi503 – 5097Combined sources
Beta strandi512 – 5143Combined sources
Helixi521 – 5288Combined sources
Beta strandi534 – 5407Combined sources
Beta strandi543 – 5453Combined sources
Helixi546 – 5527Combined sources
Turni553 – 5553Combined sources
Beta strandi556 – 5627Combined sources
Helixi568 – 57811Combined sources
Beta strandi581 – 5866Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P4RX-ray2.55A/B1-592[»]
1PKXX-ray1.90A/B/C/D1-592[»]
1PL0X-ray2.60A/B/C/D1-592[»]
ProteinModelPortaliP31939.
SMRiP31939. Positions 4-592.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31939.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni207 – 2082AICAR binding

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiP31939.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG74N5GD.
PhylomeDBiP31939.
TreeFamiTF105642.

Family and domain databases

Gene3Di1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P31939-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAPGQLALFS VSDKTGLVEF ARNLTALGLN LVASGGTAKA LRDAGLAVRD
60 70 80 90 100
VSELTGFPEM LGGRVKTLHP AVHAGILARN IPEDNADMAR LDFNLIRVVA
110 120 130 140 150
CNLYPFVKTV ASPGVTVEEA VEQIDIGGVT LLRAAAKNHA RVTVVCEPED
160 170 180 190 200
YVVVSTEMQS SESKDTSLET RRQLALKAFT HTAQYDEAIS DYFRKQYSKG
210 220 230 240 250
VSQMPLRYGM NPHQTPAQLY TLQPKLPITV LNGAPGFINL CDALNAWQLV
260 270 280 290 300
KELKEALGIP AAASFKHVSP AGAAVGIPLS EDEAKVCMVY DLYKTLTPIS
310 320 330 340 350
AAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IIAPGYEEEA
360 370 380 390 400
LTILSKKKNG NYCVLQMDQS YKPDENEVRT LFGLHLSQKR NNGVVDKSLF
410 420 430 440 450
SNVVTKNKDL PESALRDLIV ATIAVKYTQS NSVCYAKNGQ VIGIGAGQQS
460 470 480 490 500
RIHCTRLAGD KANYWWLRHH PQVLSMKFKT GVKRAEISNA IDQYVTGTIG
510 520 530 540 550
EDEDLIKWKA LFEEVPELLT EAEKKEWVEK LTEVSISSDA FFPFRDNVDR
560 570 580 590
AKRSGVAYIA APSGSAADKV VIEACDELGI ILAHTNLRLF HH
Length:592
Mass (Da):64,616
Last modified:October 10, 2002 - v3
Checksum:iAD778892021F0888
GO
Isoform 2 (identifier: P31939-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-6: MAPGQL → MSSLS

Show »
Length:591
Mass (Da):64,524
Checksum:i372861CF93D74887
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti165 – 1651D → G in AAA97405 (PubMed:8567683).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti116 – 1161T → S.2 Publications
Corresponds to variant rs2372536 [ dbSNP | Ensembl ].
VAR_019306
Natural varianti426 – 4261K → R in AICAR; loss of transformylase activity. 1 Publication
VAR_019307

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 66MAPGQL → MSSLS in isoform 2. 2 PublicationsVSP_053495

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37436 mRNA. Translation: AAA97405.1.
D82348 mRNA. Translation: BAA11559.1.
D89976 mRNA. Translation: BAA21762.1.
AB062403 mRNA. Translation: BAB93490.1.
AK290067 mRNA. Translation: BAF82756.1.
AC073284 Genomic DNA. Translation: AAY24062.1.
CH471063 Genomic DNA. Translation: EAW70529.1.
BC008879 mRNA. Translation: AAH08879.1.
CCDSiCCDS2398.1. [P31939-1]
PIRiJC4642.
RefSeqiNP_004035.2. NM_004044.6. [P31939-1]
UniGeneiHs.90280.

Genome annotation databases

EnsembliENST00000236959; ENSP00000236959; ENSG00000138363. [P31939-1]
ENST00000435675; ENSP00000415935; ENSG00000138363. [P31939-2]
GeneIDi471.
KEGGihsa:471.
UCSCiuc002vex.4. human. [P31939-1]

Polymorphism databases

DMDMi23831360.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U37436 mRNA. Translation: AAA97405.1.
D82348 mRNA. Translation: BAA11559.1.
D89976 mRNA. Translation: BAA21762.1.
AB062403 mRNA. Translation: BAB93490.1.
AK290067 mRNA. Translation: BAF82756.1.
AC073284 Genomic DNA. Translation: AAY24062.1.
CH471063 Genomic DNA. Translation: EAW70529.1.
BC008879 mRNA. Translation: AAH08879.1.
CCDSiCCDS2398.1. [P31939-1]
PIRiJC4642.
RefSeqiNP_004035.2. NM_004044.6. [P31939-1]
UniGeneiHs.90280.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1P4RX-ray2.55A/B1-592[»]
1PKXX-ray1.90A/B/C/D1-592[»]
1PL0X-ray2.60A/B/C/D1-592[»]
ProteinModelPortaliP31939.
SMRiP31939. Positions 4-592.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106961. 49 interactions.
IntActiP31939. 4 interactions.
MINTiMINT-4999053.
STRINGi9606.ENSP00000236959.

Chemistry

BindingDBiP31939.
ChEMBLiCHEMBL2518.
DrugBankiDB00563. Methotrexate.
DB00642. Pemetrexed.
DB00116. Tetrahydrofolic acid.

PTM databases

PhosphoSiteiP31939.

Polymorphism databases

DMDMi23831360.

2D gel databases

REPRODUCTION-2DPAGEIPI00289499.
UCD-2DPAGEP31939.

Proteomic databases

MaxQBiP31939.
PaxDbiP31939.
PeptideAtlasiP31939.
PRIDEiP31939.

Protocols and materials databases

DNASUi471.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000236959; ENSP00000236959; ENSG00000138363. [P31939-1]
ENST00000435675; ENSP00000415935; ENSG00000138363. [P31939-2]
GeneIDi471.
KEGGihsa:471.
UCSCiuc002vex.4. human. [P31939-1]

Organism-specific databases

CTDi471.
GeneCardsiGC02P216176.
HGNCiHGNC:794. ATIC.
HPAiCAB013462.
HPA021012.
MIMi601731. gene.
608688. phenotype.
neXtProtiNX_P31939.
Orphaneti250977. AICA-ribosiduria.
PharmGKBiPA25094.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0138.
GeneTreeiENSGT00390000004553.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiP31939.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG74N5GD.
PhylomeDBiP31939.
TreeFamiTF105642.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciMetaCyc:HS06490-MONOMER.
ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RKP31939.

Miscellaneous databases

ChiTaRSiATIC. human.
EvolutionaryTraceiP31939.
GeneWikiiInosine_monophosphate_synthase.
GenomeRNAii471.
NextBioi1945.
PROiP31939.
SOURCEiSearch...

Gene expression databases

BgeeiP31939.
CleanExiHS_ATIC.
ExpressionAtlasiP31939. baseline and differential.
GenevestigatoriP31939.

Family and domain databases

Gene3Di1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    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] (ISOFORM 1).
    Tissue: Colon adenocarcinoma.
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANT SER-116.
    Tissue: Substantia nigra.
  6. "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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-116.
  8. "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] (ISOFORM 1).
    Tissue: Pancreas.
  9. 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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "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] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 178-189 AND 267-281.
    Tissue: Keratinocyte.
  11. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "Structural insights into the human and avian IMP cyclohydrolase mechanism via crystal structures with the bound XMP inhibitor."
    Wolan D.W., Cheong C.-G., Greasley S.E., Wilson I.A.
    Biochemistry 43:1171-1183(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH XMP, SUBUNIT.
  17. "Crystal structures of human bifunctional enzyme aminoimidazole-4-carboxamide ribonucleotide transformylase/IMP cyclohydrolase in complex with potent sulfonyl-containing antifolates."
    Cheong C.-G., Wolan D.W., Greasley S.E., Horton P.A., Beardsley G.P., Wilson I.A.
    J. Biol. Chem. 279:18034-18045(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) IN COMPLEX WITH AICAR; XMP AND THE INHIBITORS BW1540 AND BW2315, FUNCTION, SUBUNIT.
  18. "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] [Europe PMC] [Abstract]
    Cited for: VARIANT AICAR ARG-426, CHARACTERIZATION OF VARIANT AICAR ARG-426.

Entry informationi

Entry nameiPUR9_HUMAN
AccessioniPrimary (citable) accession number: P31939
Secondary accession number(s): A8K202
, E9PBU3, Q13856, Q53S28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: October 10, 2002
Last modified: March 4, 2015
This is version 156 of the entry and version 3 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

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.