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UniProtKB/Swiss-Prot entry P22234


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

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Entry information
Entry name PUR6_HUMAN
Primary accession number P22234
Secondary accession numbers None
Integrated into Swiss-Prot on August 1, 1991
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 88)
Name and origin of the protein
Protein name Multifunctional protein ADE2
Synonyms None
Includes Phosphoribosylaminoimidazole-succinocarboxamide synthase
     (EC 6.3.2.6)
     (SAICAR synthetase)
Phosphoribosylaminoimidazole carboxylase
     (EC 4.1.1.21)
     (AIR carboxylase)
     (AIRC)
Gene name
Name: PAICS
Synonyms: ADE2, AIRC, PAIS
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].
DOI=10.1007/BF00318209; PubMed=2253271 [NCBI, ExPASy, EBI, Israel, Japan]
Minet M., Lacroute F.;
"Cloning and sequencing of a human cDNA coding for a multifunctional polypeptide of the purine pathway by complementation of the ade2-101 mutant in Saccharomyces cerevisiae.";
Curr. Genet. 18:287-291(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, and Placenta;
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).
[4]
PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V., Potts A., Brablan J., Quadroni M.;
Submitted (JUL-2004) to UniProtKB.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
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
X53793; CAA37801.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006988; AAP35634.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010273; AAH10273.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC019255; AAH19255.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S14147; S14147.
RefSeq NP_001072992.1; -.
NP_006443.1; -.
UniGene Hs.518774
3D structure databases
PDB
2H31; X-ray; 2.80 A; A=1-425.[ExPASy / RCSB / EBI]
PDBsum 2H31; -.
ModBase P22234.
Protein-protein interaction databases
IntAct P22234; -.
PTM databases
PhosphoSite P22234; -.
Enzyme and pathway databases
Reactome REACT_1698; Nucleotide metabolism.
Organism-specific databases
H-InvDB HIX0004234; -.
HGNC HGNC:8587; PAICS.
GenAtlas PAICS.
MIM 172439; gene. [NCBI / EBI]
PharmGKB PA32914; -.
GeneCards P22234.
Gene expression databases
ArrayExpress P22234; -.
CleanEx HS_PAICS; -.
GermOnline ENSG00000128050; Homo sapiens.
Ontologies
GO
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0004639; Molecular function: phosphoribosylaminoimidazolesuccinocarboxamide synthase activity (traceable author statement from ProtInc).
GO:0009113; Biological process: purine base biosynthetic process (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000031; AIR_COase_core.
IPR013816; ATP_grasp_subdomain_2.
IPR001636; SAICAR_synt.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.7700; AIR_carboxyl; 1.
G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 1.
PANTHER PTHR11609; SAICAR_synt; 1.
Pfam PF00731; AIRC; 1.
PF01259; SAICAR_synt; 1.
Pfam graphical view of domain structure.
ProDom PD002193; AIR_carboxyl; 1.
PD003043; SAICAR_synt; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01162; purE; 1.
PROSITE PS01057; SAICAR_SYNTHETASE_1; 1.
PS01058; SAICAR_SYNTHETASE_2; 1.
BLOCKS P22234.
Genome annotation databases
Ensembl ENSG00000128050; Homo sapiens. [Contig view]
GeneID 10606; -.
KEGG hsa:10606; -.
NMPDR fig|9606.3.peg.24135; -.
Phylogenomic databases
HOVERGEN P22234; -.
Other
DrugBank DB00128; L-Aspartic Acid.
LinkHub P22234; -.
SOURCE PAICS; Homo sapiens.
ProtoNet P22234.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Decarboxylase; Direct protein sequencing; Ligase; Lyase; Multifunctional enzyme; Phosphoprotein; Purine biosynthesis.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   425  424     Multifunctional protein ADE2. PRO_0000075030
REGION   2   260  259     SAICAR synthetase. 
REGION   261   425  165     AIR carboxylase. 
MOD_RES   2     2        N-acetylalanine. 
MOD_RES   27    27        Phosphoserine. 
STRAND   20    22  3      
STRAND   32    35  4      
HELIX   54    71  18      
STRAND   82    88  7      
STRAND   91    93  3      
STRAND   97   103  7      
HELIX   106   111  6      
STRAND   126   130  5      
HELIX   142   146  5      
TURN   147   149  3      
HELIX   159   180  22      
HELIX   181   183  3      
STRAND   186   192  7      
STRAND   194   197  4      
TURN   198   200  3      
STRAND   203   205  3      
STRAND   213   217  5      
STRAND   241   243  3      
HELIX   249   253  5      
HELIX   256   260  5      
STRAND   267   273  7      
HELIX   275   277  3      
HELIX   278   290  13      
STRAND   295   299  5      
TURN   302   304  3      
HELIX   306   317  12      
STRAND   323   328  6      
HELIX   335   342  8      
STRAND   347   349  3      
TURN   355   357  3      
HELIX   358   361  4      
HELIX   362   364  3      
HELIX   380   392  13      
HELIX   396   421  26      
Sequence information
Length: 425 AA [This is the length of the unprocessed precursor] Molecular weight: 47079 Da [This is the MW of the unprocessed precursor] CRC64: E08CF19BC8898F29 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATAEVLNIG KKLYEGKTKE VYELLDSPGK VLLQSKDQIT AGNAARKNHL EGKAAISNKI 

        70         80         90        100        110        120 
TSCIFQLLQE AGIKTAFTRK CGETAFIAPQ CEMIPIEWVC RRIATGSFLK RNPGVKEGYK 

       130        140        150        160        170        180 
FYPPKVELFF KDDANNDPQW SEEQLIAAKF CFAGLLIGQT EVDIMSHATQ AIFEILEKSW 

       190        200        210        220        230        240 
LPQNCTLVDM KIEFGVDVTT KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE 

       250        260        270        280        290        300 
GLQMVKKNFE WVAERVELLL KSESQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT 

       310        320        330        340        350        360 
SAHKGPDETL RIKAEYEGDG IPTVFVAVAG RSNGLGPVMS GNTAYPVISC PPLTPDWGVQ 

       370        380        390        400        410        420 
DVWSSLRLPS GLGCSTVLSP EGSAQFAAQI FGLSNHLVWS KLRASILNTW ISLKQADKKI 


RECNL 

P22234 in FASTA format

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