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P31939

- PUR9_HUMAN

UniProt

P31939 - PUR9_HUMAN

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Protein

Bifunctional purine biosynthesis protein PURH

Gene

ATIC

Organism
Homo sapiens (Human)
Status
Reviewed - 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 deficiency (AICAR) [MIM:608688]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
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. 48 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 – 105
Helixi17 – 259
Turni26 – 283
Beta strandi30 – 334
Helixi35 – 428
Turni43 – 453
Helixi51 – 555
Turni61 – 644
Beta strandi65 – 673
Helixi70 – 778
Helixi82 – 9110
Beta strandi96 – 1016
Helixi106 – 1116
Helixi117 – 1226
Helixi127 – 13711
Turni138 – 1414
Beta strandi143 – 1453
Helixi148 – 1503
Helixi151 – 16010
Beta strandi161 – 1655
Helixi168 – 19730
Turni200 – 2023
Beta strandi203 – 2075
Beta strandi209 – 2113
Beta strandi217 – 2204
Beta strandi222 – 2254
Beta strandi227 – 2337
Helixi237 – 25721
Beta strandi261 – 2666
Beta strandi269 – 2757
Helixi281 – 2866
Helixi290 – 2956
Helixi298 – 30811
Turni311 – 3166
Beta strandi317 – 3237
Helixi327 – 3348
Beta strandi338 – 3447
Helixi348 – 36013
Beta strandi363 – 3675
Beta strandi375 – 3817
Beta strandi384 – 3896
Helixi397 – 4004
Helixi412 – 42615
Beta strandi433 – 4375
Beta strandi440 – 4456
Helixi451 – 46717
Helixi471 – 4744
Helixi486 – 49611
Helixi503 – 5097
Beta strandi512 – 5143
Helixi521 – 5288
Beta strandi534 – 5407
Beta strandi543 – 5453
Helixi546 – 5527
Turni553 – 5553
Beta strandi556 – 5627
Helixi568 – 57811
Beta strandi581 – 5866

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiAGDKANC.
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. Align

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS2398.1. [P31939-1 ]
PIRi JC4642.
RefSeqi NP_004035.2. NM_004044.6. [P31939-1 ]
UniGenei Hs.90280.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1P4R X-ray 2.55 A/B 1-592 [» ]
1PKX X-ray 1.90 A/B/C/D 1-592 [» ]
1PL0 X-ray 2.60 A/B/C/D 1-592 [» ]
ProteinModelPortali P31939.
SMRi P31939. Positions 4-592.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106961. 48 interactions.
IntActi P31939. 4 interactions.
MINTi MINT-4999053.
STRINGi 9606.ENSP00000236959.

Chemistry

BindingDBi P31939.
ChEMBLi CHEMBL2518.
DrugBanki DB00563. Methotrexate.
DB00642. Pemetrexed.
DB00116. Tetrahydrofolic acid.

PTM databases

PhosphoSitei P31939.

Polymorphism databases

DMDMi 23831360.

2D gel databases

REPRODUCTION-2DPAGE IPI00289499.
UCD-2DPAGE P31939.

Proteomic databases

MaxQBi P31939.
PaxDbi P31939.
PeptideAtlasi P31939.
PRIDEi P31939.

Protocols and materials databases

DNASUi 471.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000236959 ; ENSP00000236959 ; ENSG00000138363 . [P31939-1 ]
ENST00000435675 ; ENSP00000415935 ; ENSG00000138363 . [P31939-2 ]
GeneIDi 471.
KEGGi hsa:471.
UCSCi uc002vex.4. human. [P31939-1 ]

Organism-specific databases

CTDi 471.
GeneCardsi GC02P216176.
HGNCi HGNC:794. ATIC.
HPAi CAB013462.
HPA021012.
MIMi 601731. gene.
608688. phenotype.
neXtProti NX_P31939.
Orphaneti 250977. AICA-ribosiduria.
PharmGKBi PA25094.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0138.
GeneTreei ENSGT00390000004553.
HOGENOMi HOG000230372.
HOVERGENi HBG006912.
InParanoidi P31939.
KOi K00602.
OMAi AGDKANC.
OrthoDBi EOG74N5GD.
PhylomeDBi P31939.
TreeFami TF105642.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci MetaCyc:HS06490-MONOMER.
Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.
SABIO-RK P31939.

Miscellaneous databases

ChiTaRSi ATIC. human.
EvolutionaryTracei P31939.
GeneWikii Inosine_monophosphate_synthase.
GenomeRNAii 471.
NextBioi 1945.
PROi P31939.
SOURCEi Search...

Gene expression databases

Bgeei P31939.
CleanExi HS_ATIC.
ExpressionAtlasi P31939. baseline and differential.
Genevestigatori P31939.

Family and domain databases

Gene3Di 1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

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. "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.
  16. "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.
  17. "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: October 29, 2014
This is version 153 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