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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: Q15172




USC-OGP 2-DE database:  Q15172


Q15172


General information about the entry
View entry in simple text format
Entry name2A5A_HUMAN
Primary accession numberQ15172
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 56 kDa regulatory subunit alpha isoform; AltName: Full=PP2A B subunit isoform B'-alpha; AltName: Full=PP2A B subunit isoform B56-alpha; AltName: Full=PP2A B subunit isoform PR61-alpha; Short=PR61alpha; AltName: Full=PP2A B subunit isoform R5-alpha;.
Gene nameName=PPP2R5A
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-ProtQ15172; 2A5A_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 name2A5A_HUMAN
Primary accession numberQ15172
Secondary accession number(s) B2R6D2 B7Z7L2 D3DT99 Q2NL72 Q5VVB2 Q8TBI9
Sequence was last modified on November 1, 1996 (version 1)
Annotations were last modified on March 15, 2017 (version 160)
Name and origin of the protein
DescriptionRecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform; AltName: Full=PP2A B subunit isoform B'-alpha; AltName: Full=PP2A B subunit isoform B56-alpha; AltName: Full=PP2A B subunit isoform PR61-alpha; Short=PR61alpha; AltName: Full=PP2A B subunit isoform R5-alpha;
Gene nameName=PPP2R5A
Encoded onName=PPP2R5A
KeywordsAcetylation; Alternative splicing; Centromere; Chromosome; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLL42373; AAC37601.1; -; mRNA
EMBLAK302202; BAH13648.1; -; mRNA
EMBLAK312530; BAG35429.1; -; mRNA
EMBLAL451060; CAH71821.1; -; Genomic_DNA
EMBLAL360091; CAH71821.1; JOINED; Genomic_DNA
EMBLAL360091; CAH73229.1; -; Genomic_DNA
EMBLAL451060; CAH73229.1; JOINED; Genomic_DNA
EMBLCH471100; EAW93392.1; -; Genomic_DNA
EMBLCH471100; EAW93393.1; -; Genomic_DNA
EMBLBC022474; AAH22474.1; -; mRNA
EMBLBC110883; AAI10884.1; -; mRNA
CCDSCCDS1503.1; -. [Q15172-1]; .
CCDSCCDS55686.1; -. [Q15172-2]; .
PIRI55449; I55449; .
RefSeqNP_001186685.1; NM_001199756.1. [Q15172-2]; .
RefSeqNP_006234.1; NM_006243.3. [Q15172-1]; .
UniGeneHs.744012; -; .
ProteinModelPortalQ15172; -; .
SMRQ15172; -; .
BioGrid111517; 32; .
DIPDIP-459N; -; .
IntActQ15172; 27; .
MINTMINT-88251; -; .
STRING9606.ENSP00000261461; -; .
BindingDBQ15172; -; .
ChEMBLCHEMBL4763; -; .
iPTMnetQ15172; -; .
PhosphoSitePlusQ15172; -; .
BioMutaPPP2R5A; -; .
DMDM7387496; -; .
OGPQ15172; -; .
EPDQ15172; -; .
MaxQBQ15172; -; .
PaxDbQ15172; -; .
PeptideAtlasQ15172; -; .
PRIDEQ15172; -; .
DNASU5525; -; .
EnsemblENST00000261461; ENSP00000261461; ENSG00000066027. [Q15172-1]; .
EnsemblENST00000537030; ENSP00000442866; ENSG00000066027. [Q15172-2]; .
GeneID5525; -; .
KEGGhsa:5525; -; .
UCSCuc001hjb.3; human. [Q15172-1]; .
CTD5525; -; .
DisGeNET5525; -; .
GeneCardsPPP2R5A; -; .
HGNCHGNC:9309; PPP2R5A; .
HPAHPA059288; -; .
MIM601643; gene; .
neXtProtNX_Q15172; -; .
OpenTargetsENSG00000066027; -; .
PharmGKBPA33672; -; .
eggNOGKOG2085; Eukaryota; .
eggNOGENOG410XQJW; LUCA; .
GeneTreeENSGT00550000074525; -; .
HOGENOMHOG000067326; -; .
HOVERGENHBG000009; -; .
InParanoidQ15172; -; .
KOK11584; -; .
OMAKLQNCCF; -; .
OrthoDBEOG091G06HU; -; .
PhylomeDBQ15172; -; .
TreeFamTF105556; -; .
ReactomeR-HSA-195253; Degradation of beta-catenin by the destruction complex; .
ReactomeR-HSA-196299; Beta-catenin phosphorylation cascade; .
ReactomeR-HSA-2467813; Separation of Sister Chromatids; .
ReactomeR-HSA-2500257; Resolution of Sister Chromatid Cohesion; .
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-5663220; RHO GTPases Activate Formins; .
ReactomeR-HSA-5673000; RAF activation; .
ReactomeR-HSA-5675221; Negative regulation of MAPK pathway; .
ReactomeR-HSA-6811558; PI5P; PP2A and IER3 Regulate PI3K/AKT Signaling; .
ReactomeR-HSA-68877; Mitotic Prometaphase; .
SignaLinkQ15172; -; .
SIGNORQ15172; -; .
GeneWikiPPP2R5A; -; .
GenomeRNAi5525; -; .
PROPR:Q15172; -; .
ProteomesUP000005640; Chromosome 1; .
BgeeENSG00000066027; -; .
CleanExHS_PPP2R5A; -; .
GenevisibleQ15172; HS; .
GOGO:0000775; C:chromosome; centromeric region; IEA:UniProtKB-SubCell
GOGO:0005737; C:cytoplasm; IDA:BHF-UCL; .
GOGO:0005829; C:cytosol; IDA:HPA; .
GOGO:0031430; C:M band; ISS:BHF-UCL; .
GOGO:0005634; C:nucleus; IEA:UniProtKB-SubCell; .
GOGO:0000159; C:protein phosphatase type 2A complex; IDA:UniProtKB; .
GOGO:0030018; C:Z disc; IDA:BHF-UCL; .
GOGO:0019900; F:kinase binding; IPI:BHF-UCL; .
GOGO:0019888; F:protein phosphatase regulator activity; TAS:ProtInc; .
GOGO:0090005; P:negative regulation of establishment of protein localization to plasma membrane; IMP:BHF-UCL; .
GOGO:0090219; P:negative regulation of lipid kinase activity; IMP:BHF-UCL; .
GOGO:0035307; P:positive regulation of protein dephosphorylation; IMP:BHF-UCL; .
GOGO:0007165; P:signal transduction; IEA:InterPro; .
InterProIPR016024; ARM-type_fold; .
InterProIPR002554; PP2A_B56; .
PANTHERPTHR10257; PTHR10257; 1; .
PfamPF01603; B56; 1; .
PIRSFPIRSF028043; PP2A_B56; 1; .
SUPFAMSSF48371; SSF48371; 1; .



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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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