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USC-OGP 2-DE database

Two-dimensional polyacrylamide gel electrophoresis database


USC-OGP 2-DE database 
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Searching in 'USC-OGP 2-DE database' for entry matching: P30153




USC-OGP 2-DE database:  P30153


P30153


General information about the entry
View entry in simple text format
Entry name2AAA_HUMAN
Primary accession numberP30153
integrated into USC-OGP 2-DE database on January 17, 2017 (release 1)
2D Annotations were last modified onJanuary 17, 2017 (version 1)
General Annotations were last modified on April 5, 2017 (version 2)
Name and origin of the protein
DescriptionRecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform; AltName: Full=Medium tumor antigen-associated 61 kDa protein; AltName: Full=PP2A subunit A isoform PR65-alpha; AltName: Full=PP2A subunit A isoform R1-alpha;.
Gene nameName=PPP2R1A
Annotated speciesHomo sapiens (Human) [TaxID: 9606]
TaxonomyEukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
References
[1]   2D GEL CHARACTERIZATION
Author 1., Author 2.
Submitted (Mar-2011) to Current
2D PAGE maps for identified proteins
How to interpret a protein

PLATELET_4-5 {PLATELET 4-5}
Homo sapiens (Human)
PLATELET_4-5
  map experimental info
 
PLATELET_4-5

MAP LOCATIONS:
pI=5.00; Mw=61375

Cross-references
UniProtKB/Swiss-ProtP30153; 2AAA_HUMAN.



2D PAGE maps for identified proteins
  • How to interpret a protein map
  • You may obtain an estimated location of the protein on various 2D PAGE maps, provided the whole amino acid sequence is known. The estimation is obtained according to the computed protein's pI and Mw.
  • Warning 1: the displayed region reflects an area around the theoretical pI and molecular weight of the protein and is only provided for the user's information. It should be used with caution, as the experimental and theoretical positions of a protein may differ significantly.
  • Warning 2: the 2D PAGE map is built on demand. This may take some few seconds to be computed.



External data extracted from UniProtKB/Swiss-Prot
Extracted from UniProtKB/Swiss-Prot, release: 0.0
Entry name2AAA_HUMAN
Primary accession numberP30153
Secondary accession number(s) Q13773 Q6ICQ3 Q96DH3
Sequence was last modified on April 3, 2007 (version 4)
Annotations were last modified on March 15, 2017 (version 180)
Name and origin of the protein
DescriptionRecName: Full=Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform; AltName: Full=Medium tumor antigen-associated 61 kDa protein; AltName: Full=PP2A subunit A isoform PR65-alpha; AltName: Full=PP2A subunit A isoform R1-alpha;
Gene nameName=PPP2R1A
Encoded onName=PPP2R1A
Keywords3D-structure; Acetylation; Centromere; Chromosome; Chromosome partition; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Mental retardation; Reference proteome; Repeat.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLM31786; AAA35531.1; -; mRNA
EMBLJ02902; AAA36399.1; -; mRNA
EMBLCR450340; CAG29336.1; -; mRNA
EMBLBC001537; AAH01537.1; -; mRNA
CCDSCCDS12849.1; -; .
PIRA34541; A34541; .
RefSeqNP_055040.2; NM_014225.5; .
UniGeneHs.467192; -; .
PDB1B3U; X-ray; 2.30 A; A/B=2-589
PDB2IE3; X-ray; 2.80 A; A=1-589
PDB2IE4; X-ray; 2.60 A; A=1-589
PDB2NPP; X-ray; 3.30 A; A/D=1-589
PDB2NYL; X-ray; 3.80 A; A/D=8-589
PDB2NYM; X-ray; 3.60 A; A/D=8-589
PDB2PKG; X-ray; 3.30 A; A/B=10-589
PDB3C5W; X-ray; 2.80 A; A=9-589
PDB3DW8; X-ray; 2.85 A; A/D=9-589
PDB3K7V; X-ray; 2.85 A; A=1-589
PDB3K7W; X-ray; 2.96 A; A=1-589
PDB4I5L; X-ray; 2.43 A; A/D=6-589
PDB4I5N; X-ray; 2.80 A; A/D=6-589
PDB4LAC; X-ray; 2.82 A; A=404-589
PDBsum1B3U; -; .
PDBsum2IE3; -; .
PDBsum2IE4; -; .
PDBsum2NPP; -; .
PDBsum2NYL; -; .
PDBsum2NYM; -; .
PDBsum2PKG; -; .
PDBsum3C5W; -; .
PDBsum3DW8; -; .
PDBsum3K7V; -; .
PDBsum3K7W; -; .
PDBsum4I5L; -; .
PDBsum4I5N; -; .
PDBsum4LAC; -; .
ProteinModelPortalP30153; -; .
SMRP30153; -; .
BioGrid111510; 272; .
DIPDIP-29394N; -; .
IntActP30153; 187; .
MINTMINT-1141071; -; .
STRING9606.ENSP00000324804; -; .
iPTMnetP30153; -; .
PhosphoSitePlusP30153; -; .
SwissPalmP30153; -; .
BioMutaPPP2R1A; -; .
DMDM143811355; -; .
OGPP30153; -; .
REPRODUCTION-2DPAGEIPI00554737; -; .
EPDP30153; -; .
MaxQBP30153; -; .
PaxDbP30153; -; .
PeptideAtlasP30153; -; .
PRIDEP30153; -; .
DNASU5518; -; .
EnsemblENST00000322088; ENSP00000324804; ENSG00000105568; .
GeneID5518; -; .
KEGGhsa:5518; -; .
UCSCuc002pyp.4; human; .
CTD5518; -; .
DisGeNET5518; -; .
GeneCardsPPP2R1A; -; .
HGNCHGNC:9302; PPP2R1A; .
HPACAB018599; -; .
MalaCardsPPP2R1A; -; .
MIM605983; gene; .
MIM616362; phenotype; .
neXtProtNX_P30153; -; .
OpenTargetsENSG00000105568; -; .
PharmGKBPA33666; -; .
eggNOGKOG0211; Eukaryota; .
eggNOGENOG410XQVI; LUCA; .
GeneTreeENSGT00730000110944; -; .
HOGENOMHOG000078539; -; .
HOVERGENHBG000011; -; .
InParanoidP30153; -; .
KOK03456; -; .
OMAMSNILPC; -; .
OrthoDBEOG091G045V; -; .
PhylomeDBP30153; -; .
TreeFamTF105552; -; .
BioCycMetaCyc:ENSG00000105568-MONOMER; -; .
ReactomeR-HSA-113501; Inhibition of replication initiation of damaged DNA by RB1/E2F1; .
ReactomeR-HSA-1295596; Spry regulation of FGF signaling; .
ReactomeR-HSA-163685; Integration of energy metabolism; .
ReactomeR-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors; .
ReactomeR-HSA-180024; DARPP-32 events; .
ReactomeR-HSA-195253; Degradation of beta-catenin by the destruction complex; .
ReactomeR-HSA-196299; Beta-catenin phosphorylation cascade; .
ReactomeR-HSA-198753; ERK/MAPK targets; .
ReactomeR-HSA-202670; ERKs are inactivated; .
ReactomeR-HSA-2465910; MASTL Facilitates Mitotic Progression; .
ReactomeR-HSA-2467813; Separation of Sister Chromatids; .
ReactomeR-HSA-2500257; Resolution of Sister Chromatid Cohesion; .
ReactomeR-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition; .
ReactomeR-HSA-2995383; Initiation of Nuclear Envelope Reformation; .
ReactomeR-HSA-380259; Loss of Nlp from mitotic centrosomes; .
ReactomeR-HSA-380270; Recruitment of mitotic centrosome proteins and complexes; .
ReactomeR-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome; .
ReactomeR-HSA-389513; CTLA4 inhibitory signaling; .
ReactomeR-HSA-432142; Platelet sensitization by LDL; .
ReactomeR-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane; .
ReactomeR-HSA-5339716; Misspliced GSK3beta mutants stabilize beta-catenin; .
ReactomeR-HSA-5358747; S33 mutants of beta-catenin aren't phosphorylated; .
ReactomeR-HSA-5358749; S37 mutants of beta-catenin aren't phosphorylated; .
ReactomeR-HSA-5358751; S45 mutants of beta-catenin aren't phosphorylated; .
ReactomeR-HSA-5358752; T41 mutants of beta-catenin aren't phosphorylated; .
ReactomeR-HSA-5467337; APC truncation mutants have impaired AXIN binding; .
ReactomeR-HSA-5467340; AXIN missense mutants destabilize the destruction complex; .
ReactomeR-HSA-5467348; Truncations of AMER1 destabilize the destruction complex; .
ReactomeR-HSA-5620912; Anchoring of the basal body to the plasma membrane; .
ReactomeR-HSA-5663220; RHO GTPases Activate Formins; .
ReactomeR-HSA-5673000; RAF activation; .
ReactomeR-HSA-5675221; Negative regulation of MAPK pathway; .
ReactomeR-HSA-6804757; Regulation of TP53 Degradation; .
ReactomeR-HSA-6811558; PI5P; PP2A and IER3 Regulate PI3K/AKT Signaling; .
ReactomeR-HSA-68877; Mitotic Prometaphase; .
ReactomeR-HSA-69231; Cyclin D associated events in G1; .
ReactomeR-HSA-69273; Cyclin A/B1 associated events during G2/M transition; .
ReactomeR-HSA-70171; Glycolysis; .
ReactomeR-HSA-8854518; AURKA Activation by TPX2; .
ReactomeR-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC); .
SignaLinkP30153; -; .
SIGNORP30153; -; .
ChiTaRSPPP2R1A; human; .
EvolutionaryTraceP30153; -; .
GeneWikiPPP2R1A; -; .
GenomeRNAi5518; -; .
PMAP-CutDBP30153; -; .
PROPR:P30153; -; .
ProteomesUP000005640; Chromosome 19; .
BgeeENSG00000105568; -; .
CleanExHS_PPP2R1A; -; .
ExpressionAtlasP30153; baseline and differential; .
GenevisibleP30153; HS; .
GOGO:0000775; C:chromosome; centromeric region; IDA:UniProtKB
GOGO:0005829; C:cytosol; TAS:UniProtKB; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0016020; C:membrane; NAS:UniProtKB; .
GOGO:0015630; C:microtubule cytoskeleton; NAS:UniProtKB; .
GOGO:0005739; C:mitochondrion; NAS:UniProtKB; .
GOGO:0005634; C:nucleus; NAS:UniProtKB; .
GOGO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB; .
GOGO:0003823; F:antigen binding; IPI:UniProtKB; .
GOGO:0046982; F:protein heterodimerization activity; IPI:UniProtKB; .
GOGO:0019888; F:protein phosphatase regulator activity; TAS:UniProtKB; .
GOGO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl; .
GOGO:0006915; P:apoptotic process; TAS:UniProtKB; .
GOGO:0006672; P:ceramide metabolic process; NAS:UniProtKB; .
GOGO:0007059; P:chromosome segregation; IDA:UniProtKB; .
GOGO:0097711; P:ciliary basal body docking; TAS:Reactome; .
GOGO:0007143; P:female meiotic division; IEA:Ensembl; .
GOGO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome; .
GOGO:0000188; P:inactivation of MAPK activity; NAS:UniProtKB; .
GOGO:0051754; P:meiotic sister chromatid cohesion; centromeric; IEA:Ensembl
GOGO:0051232; P:meiotic spindle elongation; IEA:Ensembl; .
GOGO:0007084; P:mitotic nuclear envelope reassembly; TAS:Reactome; .
GOGO:0051306; P:mitotic sister chromatid separation; IEA:Ensembl; .
GOGO:0030308; P:negative regulation of cell growth; NAS:UniProtKB; .
GOGO:0042518; P:negative regulation of tyrosine phosphorylation of Stat3 protein; NAS:UniProtKB; .
GOGO:0000184; P:nuclear-transcribed mRNA catabolic process; nonsense-mediated decay; TAS:Reactome
GOGO:0070262; P:peptidyl-serine dephosphorylation; IEA:Ensembl; .
GOGO:2001241; P:positive regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl; .
GOGO:0006461; P:protein complex assembly; TAS:UniProtKB; .
GOGO:0006470; P:protein dephosphorylation; TAS:UniProtKB; .
GOGO:0030155; P:regulation of cell adhesion; NAS:UniProtKB; .
GOGO:0045595; P:regulation of cell differentiation; NAS:UniProtKB; .
GOGO:0006275; P:regulation of DNA replication; NAS:UniProtKB; .
GOGO:0040008; P:regulation of growth; NAS:UniProtKB; .
GOGO:1903538; P:regulation of meiotic cell cycle process involved in oocyte maturation; IEA:Ensembl; .
GOGO:0006355; P:regulation of transcription; DNA-templated; NAS:UniProtKB
GOGO:0030111; P:regulation of Wnt signaling pathway; NAS:UniProtKB; .
GOGO:0010033; P:response to organic substance; NAS:UniProtKB; .
GOGO:0008380; P:RNA splicing; NAS:UniProtKB; .
GOGO:0019932; P:second-messenger-mediated signaling; NAS:UniProtKB; .
Gene3D1.25.10.10; -; 1; .
InterProIPR011989; ARM-like; .
InterProIPR016024; ARM-type_fold; .
InterProIPR000357; HEAT; .
InterProIPR021133; HEAT_type_2; .
InterProIPR031090; PP2A_A_meta; .
PANTHERPTHR10648:SF16; PTHR10648:SF16; 1; .
PfamPF02985; HEAT; 1; .
SUPFAMSSF48371; SSF48371; 1; .
PROSITEPS50077; HEAT_REPEAT; 11; .



USC-OGP 2-DE database image


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Database constructed and maintained by Angel Garcia, using the Make2D-DB II package (ver. 3.10.2) from the World-2DPAGE Constellation of the ExPASy web server

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