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P22234

- PUR6_HUMAN

UniProt

P22234 - PUR6_HUMAN

Protein

Multifunctional protein ADE2

Gene

PAICS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 156 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    ATP + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate.
    5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate = 5-amino-1-(5-phospho-D-ribosyl)imidazole + CO2.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei101 – 1011For SAICAR synthetase activity1 Publication
    Active sitei107 – 1071For SAICAR synthetase activity1 Publication
    Active sitei215 – 2151For SAICAR synthetase activity1 Publication
    Active sitei303 – 3031For AIR carboxylase activity1 Publication
    Active sitei332 – 3321For AIR carboxylase activity1 Publication
    Sitei334 – 3341Essential for AIR carboxylase activity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. phosphoribosylaminoimidazole carboxylase activity Source: Reactome
    4. phosphoribosylaminoimidazolesuccinocarboxamide synthase activity Source: Reactome
    5. protein binding Source: IntAct

    GO - Biological processi

    1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
    2. nucleobase-containing small molecule metabolic process Source: Reactome
    3. purine nucleobase biosynthetic process Source: ProtInc
    4. purine nucleobase metabolic process Source: Reactome
    5. purine ribonucleoside monophosphate biosynthetic process Source: Reactome
    6. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Decarboxylase, Ligase, Lyase

    Keywords - Biological processi

    Purine biosynthesis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05155-MONOMER.
    ReactomeiREACT_1776. Purine ribonucleoside monophosphate biosynthesis.
    UniPathwayiUPA00074; UER00130.
    UPA00074; UER00131.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Multifunctional protein ADE2
    Including the following 2 domains:
    Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC:6.3.2.6)
    Alternative name(s):
    SAICAR synthetase
    Phosphoribosylaminoimidazole carboxylase (EC:4.1.1.21)
    Alternative name(s):
    AIR carboxylase
    Short name:
    AIRC
    Gene namesi
    Name:PAICS
    Synonyms:ADE2, AIRC, PAIS
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:8587. PAICS.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt
    3. membrane Source: UniProtKB

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi303 – 3031H → Y: Loss of AIR carboxylase activity. 1 Publication
    Mutagenesisi332 – 3321S → A: Loss of AIR carboxylase activity. 1 Publication
    Mutagenesisi334 – 3341G → A: Loss of AIR carboxylase activity. 1 Publication
    Mutagenesisi400 – 4001S → A: No change of AIR carboxylase activity.

    Organism-specific databases

    PharmGKBiPA32914.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 425424Multifunctional protein ADE2PRO_0000075030Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei22 – 221PhosphotyrosineBy similarity
    Modified residuei27 – 271Phosphoserine8 Publications
    Modified residuei36 – 361N6-acetyllysineBy similarity
    Modified residuei107 – 1071Phosphoserine1 Publication
    Modified residuei238 – 2381Phosphothreonine1 Publication
    Modified residuei247 – 2471N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP22234.
    PaxDbiP22234.
    PRIDEiP22234.

    PTM databases

    PhosphoSiteiP22234.

    Expressioni

    Gene expression databases

    ArrayExpressiP22234.
    BgeeiP22234.
    CleanExiHS_PAICS.
    GenevestigatoriP22234.

    Organism-specific databases

    HPAiHPA035895.
    HPA041538.

    Interactioni

    Subunit structurei

    Homooctamer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-712261,EBI-712261
    FXR2P511163EBI-712261,EBI-740459
    NUDT18Q6ZVK83EBI-712261,EBI-740486

    Protein-protein interaction databases

    BioGridi115852. 49 interactions.
    IntActiP22234. 16 interactions.
    MINTiMINT-5006326.
    STRINGi9606.ENSP00000382595.

    Structurei

    Secondary structure

    1
    425
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 223
    Beta strandi32 – 354
    Helixi54 – 7118
    Beta strandi82 – 887
    Beta strandi91 – 933
    Beta strandi97 – 1037
    Helixi106 – 1116
    Beta strandi126 – 1305
    Helixi142 – 1465
    Turni147 – 1493
    Helixi159 – 18022
    Helixi181 – 1833
    Beta strandi186 – 1927
    Beta strandi194 – 1974
    Turni198 – 2003
    Beta strandi203 – 2053
    Beta strandi213 – 2175
    Beta strandi241 – 2433
    Helixi249 – 2535
    Helixi256 – 2605
    Beta strandi267 – 2737
    Helixi275 – 2773
    Helixi278 – 29013
    Beta strandi295 – 2995
    Turni302 – 3043
    Helixi306 – 31712
    Beta strandi323 – 3286
    Helixi335 – 3428
    Beta strandi347 – 3493
    Turni355 – 3573
    Helixi358 – 3614
    Helixi362 – 3643
    Helixi380 – 39213
    Helixi396 – 42126

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H31X-ray2.80A1-425[»]
    ProteinModelPortaliP22234.
    SMRiP22234. Positions 7-425.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22234.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 260259SAICAR synthetaseAdd
    BLAST
    Regioni261 – 2666Linker
    Regioni267 – 425159AIR carboxylaseAdd
    BLAST

    Sequence similaritiesi

    In the N-terminal section; belongs to the SAICAR synthetase family.Curated
    In the C-terminal section; belongs to the AIR carboxylase family.Curated

    Phylogenomic databases

    eggNOGiCOG0041.
    HOGENOMiHOG000082628.
    HOVERGENiHBG008335.
    InParanoidiP22234.
    KOiK01587.
    OMAiTAFTRKC.
    PhylomeDBiP22234.
    TreeFamiTF106384.

    Family and domain databases

    Gene3Di3.30.470.20. 1 hit.
    3.40.50.7700. 1 hit.
    HAMAPiMF_00137. SAICAR_synth.
    InterProiIPR013816. ATP_grasp_subdomain_2.
    IPR000031. PurE_dom.
    IPR028923. SAICAR_synt/ADE2_N.
    IPR018236. SAICAR_synthetase_CS.
    [Graphical view]
    PfamiPF00731. AIRC. 1 hit.
    PF01259. SAICAR_synt. 1 hit.
    [Graphical view]
    SMARTiSM01001. AIRC. 1 hit.
    [Graphical view]
    SUPFAMiSSF52255. SSF52255. 1 hit.
    TIGRFAMsiTIGR01162. purE. 1 hit.
    PROSITEiPS01057. SAICAR_SYNTHETASE_1. 1 hit.
    PS01058. SAICAR_SYNTHETASE_2. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P22234-1) [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

    MATAEVLNIG KKLYEGKTKE VYELLDSPGK VLLQSKDQIT AGNAARKNHL    50
    EGKAAISNKI TSCIFQLLQE AGIKTAFTRK CGETAFIAPQ CEMIPIEWVC 100
    RRIATGSFLK RNPGVKEGYK FYPPKVELFF KDDANNDPQW SEEQLIAAKF 150
    CFAGLLIGQT EVDIMSHATQ AIFEILEKSW LPQNCTLVDM KIEFGVDVTT 200
    KEIVLADVID NDSWRLWPSG DRSQQKDKQS YRDLKEVTPE GLQMVKKNFE 250
    WVAERVELLL KSESQCRVVV LMGSTSDLGH CEKIKKACGN FGIPCELRVT 300
    SAHKGPDETL RIKAEYEGDG IPTVFVAVAG RSNGLGPVMS GNTAYPVISC 350
    PPLTPDWGVQ DVWSSLRLPS GLGCSTVLSP EGSAQFAAQI FGLSNHLVWS 400
    KLRASILNTW ISLKQADKKI RECNL 425
    Length:425
    Mass (Da):47,079
    Last modified:January 23, 2007 - v3
    Checksum:iE08CF19BC8898F29
    GO
    Isoform 2 (identifier: P22234-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         72-72: G → VTSYKSNR

    Show »
    Length:432
    Mass (Da):47,958
    Checksum:i1F8F3B240AD1C137
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti217 – 2171W → R in CAH18683. (PubMed:17974005)Curated
    Sequence conflicti340 – 3401S → T in CAH18683. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti201 – 2011K → N.
    Corresponds to variant rs11549976 [ dbSNP | Ensembl ].
    VAR_051884

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei72 – 721G → VTSYKSNR in isoform 2. 1 PublicationVSP_041265

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53793 mRNA. Translation: CAA37801.1.
    BT006988 mRNA. Translation: AAP35634.1.
    CR749824 mRNA. Translation: CAH18683.1.
    AC068620 Genomic DNA. No translation available.
    AC114766 Genomic DNA. No translation available.
    BC010273 mRNA. Translation: AAH10273.1.
    BC019255 mRNA. Translation: AAH19255.1.
    CCDSiCCDS47060.1. [P22234-2]
    CCDS47061.1. [P22234-1]
    PIRiS14147.
    RefSeqiNP_001072992.1. NM_001079524.1. [P22234-1]
    NP_001072993.1. NM_001079525.1. [P22234-2]
    NP_006443.1. NM_006452.3. [P22234-1]
    UniGeneiHs.518774.
    Hs.709570.

    Genome annotation databases

    EnsembliENST00000264221; ENSP00000264221; ENSG00000128050. [P22234-1]
    ENST00000399688; ENSP00000382595; ENSG00000128050. [P22234-2]
    ENST00000512576; ENSP00000421096; ENSG00000128050. [P22234-1]
    GeneIDi10606.
    KEGGihsa:10606.
    UCSCiuc003hbs.1. human. [P22234-1]
    uc003hbt.1. human. [P22234-2]

    Polymorphism databases

    DMDMi131628.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X53793 mRNA. Translation: CAA37801.1 .
    BT006988 mRNA. Translation: AAP35634.1 .
    CR749824 mRNA. Translation: CAH18683.1 .
    AC068620 Genomic DNA. No translation available.
    AC114766 Genomic DNA. No translation available.
    BC010273 mRNA. Translation: AAH10273.1 .
    BC019255 mRNA. Translation: AAH19255.1 .
    CCDSi CCDS47060.1. [P22234-2 ]
    CCDS47061.1. [P22234-1 ]
    PIRi S14147.
    RefSeqi NP_001072992.1. NM_001079524.1. [P22234-1 ]
    NP_001072993.1. NM_001079525.1. [P22234-2 ]
    NP_006443.1. NM_006452.3. [P22234-1 ]
    UniGenei Hs.518774.
    Hs.709570.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2H31 X-ray 2.80 A 1-425 [» ]
    ProteinModelPortali P22234.
    SMRi P22234. Positions 7-425.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115852. 49 interactions.
    IntActi P22234. 16 interactions.
    MINTi MINT-5006326.
    STRINGi 9606.ENSP00000382595.

    Chemistry

    ChEMBLi CHEMBL5922.
    DrugBanki DB00128. L-Aspartic Acid.

    PTM databases

    PhosphoSitei P22234.

    Polymorphism databases

    DMDMi 131628.

    Proteomic databases

    MaxQBi P22234.
    PaxDbi P22234.
    PRIDEi P22234.

    Protocols and materials databases

    DNASUi 10606.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264221 ; ENSP00000264221 ; ENSG00000128050 . [P22234-1 ]
    ENST00000399688 ; ENSP00000382595 ; ENSG00000128050 . [P22234-2 ]
    ENST00000512576 ; ENSP00000421096 ; ENSG00000128050 . [P22234-1 ]
    GeneIDi 10606.
    KEGGi hsa:10606.
    UCSCi uc003hbs.1. human. [P22234-1 ]
    uc003hbt.1. human. [P22234-2 ]

    Organism-specific databases

    CTDi 10606.
    GeneCardsi GC04P057301.
    HGNCi HGNC:8587. PAICS.
    HPAi HPA035895.
    HPA041538.
    MIMi 172439. gene.
    neXtProti NX_P22234.
    PharmGKBi PA32914.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0041.
    HOGENOMi HOG000082628.
    HOVERGENi HBG008335.
    InParanoidi P22234.
    KOi K01587.
    OMAi TAFTRKC.
    PhylomeDBi P22234.
    TreeFami TF106384.

    Enzyme and pathway databases

    UniPathwayi UPA00074 ; UER00130 .
    UPA00074 ; UER00131 .
    BioCyci MetaCyc:HS05155-MONOMER.
    Reactomei REACT_1776. Purine ribonucleoside monophosphate biosynthesis.

    Miscellaneous databases

    ChiTaRSi PAICS. human.
    EvolutionaryTracei P22234.
    GenomeRNAii 10606.
    NextBioi 40280.
    PROi P22234.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22234.
    Bgeei P22234.
    CleanExi HS_PAICS.
    Genevestigatori P22234.

    Family and domain databases

    Gene3Di 3.30.470.20. 1 hit.
    3.40.50.7700. 1 hit.
    HAMAPi MF_00137. SAICAR_synth.
    InterProi IPR013816. ATP_grasp_subdomain_2.
    IPR000031. PurE_dom.
    IPR028923. SAICAR_synt/ADE2_N.
    IPR018236. SAICAR_synthetase_CS.
    [Graphical view ]
    Pfami PF00731. AIRC. 1 hit.
    PF01259. SAICAR_synt. 1 hit.
    [Graphical view ]
    SMARTi SM01001. AIRC. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52255. SSF52255. 1 hit.
    TIGRFAMsi TIGR01162. purE. 1 hit.
    PROSITEi PS01057. SAICAR_SYNTHETASE_1. 1 hit.
    PS01058. SAICAR_SYNTHETASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Minet M., Lacroute F.
      Curr. Genet. 18:287-291(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      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.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Retina.
    4. "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].
    5. "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: Lung and Placenta.
    6. Bienvenut W.V., Potts A., Brablan J., Quadroni M.
      Submitted (JUL-2004) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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."
      Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
      J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND THR-238, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "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-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis."
      Li S.-X., Tong Y.-P., Xie X.-C., Wang Q.-H., Zhou H.-N., Han Y., Zhang Z.-Y., Gao W., Li S.-G., Zhang X.C., Bi R.-C.
      J. Mol. Biol. 366:1603-1614(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS), SUBUNIT, ACTIVE SITE, MUTAGENESIS OF HIS-303; SER-332 AND GLY-334.

    Entry informationi

    Entry nameiPUR6_HUMAN
    AccessioniPrimary (citable) accession number: P22234
    Secondary accession number(s): E9PDH9, Q68CQ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    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 4
      Human chromosome 4: 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