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P22234

- PUR6_HUMAN

UniProt

P22234 - PUR6_HUMAN

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Protein
Multifunctional protein ADE2
Gene
PAICS, ADE2, AIRC, PAIS
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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
Complete GO annotation...

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 – 11Removed1 Publication
Chaini2 – 425424Multifunctional protein ADE2
PRO_0000075030Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei22 – 221Phosphotyrosine By similarity
Modified residuei27 – 271Phosphoserine8 Publications
Modified residuei36 – 361N6-acetyllysine By 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

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.

Miscellaneous databases

EvolutionaryTraceiP22234.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 260259SAICAR synthetase
Add
BLAST
Regioni261 – 2666Linker
Regioni267 – 425159AIR carboxylase
Add
BLAST

Sequence similaritiesi

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

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.
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

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.
VSP_041265

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti217 – 2171W → R in CAH18683. 1 Publication
Sequence conflicti340 – 3401S → T in CAH18683. 1 Publication

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...

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.
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 155 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

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