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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: PP2AB_HUMAN




USC-OGP 2-DE database:  PP2AB_HUMAN


PP2AB_HUMAN


General information about the entry
View entry in simple text format
Entry namePP2AB_HUMAN
Primary accession numberP62714
Secondary accession number(s) P11082
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 catalytic subunit beta isoform; Short=PP2A-beta; EC=3.1.3.16;.
Gene nameName=PPP2CB
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_5-6 {PLATELET 5-6}
Homo sapiens (Human)
PLATELET_5-6
  map experimental info
 
PLATELET_5-6

MAP LOCATIONS:
pI=5.15; Mw=32720

Cross-references
UniProtKB/Swiss-ProtP62714; PP2AB_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 namePP2AB_HUMAN
Primary accession numberP62714
Secondary accession number(s) D3DSV4 P11082 Q6FHK5
Sequence was last modified on July 19, 2004 (version 1)
Annotations were last modified on March 15, 2017 (version 140)
Name and origin of the protein
DescriptionRecName: Full=Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform; Short=PP2A-beta; EC=3.1.3.16;
Gene nameName=PPP2CB
Encoded onName=PPP2CB
KeywordsCentromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Hydrolase; Manganese; Metal-binding; Methylation; Nucleus; Phosphoprotein; Protein phosphatase; Reference proteome; Ubl conjugation.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/help/license. Distributed under the Creative Commons Attribution-NoDerivs License
Cross-references
EMBLX12656; CAA31183.1; -; mRNA
EMBLCR541747; CAG46547.1; -; mRNA
EMBLJ03805; AAB38020.1; -; mRNA
EMBLCH471080; EAW63434.1; -; Genomic_DNA
EMBLCH471080; EAW63435.1; -; Genomic_DNA
EMBLCH471080; EAW63436.1; -; Genomic_DNA
EMBLBC012022; AAH12022.1; -; mRNA
EMBLM60484; AAA36467.1; -; Genomic_DNA
CCDSCCDS6079.1; -; .
PIRB37135; PAHU2B; .
RefSeqNP_001009552.1; NM_001009552.1; .
UniGeneHs.491440; -; .
ProteinModelPortalP62714; -; .
SMRP62714; -; .
BioGrid111508; 141; .
DIPDIP-42325N; -; .
IntActP62714; 130; .
MINTMINT-1348293; -; .
STRING9606.ENSP00000221138; -; .
DrugBankDB00163; Vitamin E; .
DEPODP62714; -; .
iPTMnetP62714; -; .
PhosphoSitePlusP62714; -; .
SwissPalmP62714; -; .
BioMutaPPP2CB; -; .
DMDM50402236; -; .
OGPP62714; -; .
REPRODUCTION-2DPAGEIPI00429689; -; .
EPDP62714; -; .
MaxQBP62714; -; .
PaxDbP62714; -; .
PeptideAtlasP62714; -; .
PRIDEP62714; -; .
DNASU5516; -; .
EnsemblENST00000221138; ENSP00000221138; ENSG00000104695; .
GeneID5516; -; .
KEGGhsa:5516; -; .
UCSCuc003xik.4; human; .
CTD5516; -; .
DisGeNET5516; -; .
GeneCardsPPP2CB; -; .
HGNCHGNC:9300; PPP2CB; .
HPACAB018600; -; .
HPAHPA043236; -; .
MIM176916; gene; .
neXtProtNX_P62714; -; .
OpenTargetsENSG00000104695; -; .
PharmGKBPA33664; -; .
eggNOGKOG0371; Eukaryota; .
eggNOGCOG0639; LUCA; .
GeneTreeENSGT00550000074618; -; .
HOGENOMHOG000172696; -; .
HOVERGENHBG000216; -; .
InParanoidP62714; -; .
KOK04382; -; .
OMAMDDKTFT; -; .
OrthoDBEOG091G0B6S; -; .
PhylomeDBP62714; -; .
TreeFamTF105559; -; .
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-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-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; .
SIGNORP62714; -; .
ChiTaRSPPP2CB; human; .
GeneWikiPPP2CB; -; .
GenomeRNAi5516; -; .
PROPR:P62714; -; .
ProteomesUP000005640; Chromosome 8; .
BgeeENSG00000104695; -; .
CleanExHS_PPP2CB; -; .
ExpressionAtlasP62714; baseline and differential; .
GenevisibleP62714; HS; .
GOGO:0000775; C:chromosome; centromeric region; IEA:UniProtKB-SubCell
GOGO:0005829; C:cytosol; TAS:Reactome; .
GOGO:0070062; C:extracellular exosome; IDA:UniProtKB; .
GOGO:0005634; C:nucleus; IEA:UniProtKB-SubCell; .
GOGO:0000159; C:protein phosphatase type 2A complex; TAS:UniProtKB; .
GOGO:0000922; C:spindle pole; IEA:UniProtKB-SubCell; .
GOGO:0046872; F:metal ion binding; IEA:UniProtKB-KW; .
GOGO:0004722; F:protein serine/threonine phosphatase activity; IEA:Ensembl; .
GOGO:0008637; P:apoptotic mitochondrial changes; IEA:Ensembl; .
GOGO:0046580; P:negative regulation of Ras protein signal transduction; IEA:Ensembl; .
GOGO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl; .
GOGO:0006470; P:protein dephosphorylation; TAS:UniProtKB; .
GOGO:0010468; P:regulation of gene expression; IEA:Ensembl; .
GOGO:0046677; P:response to antibiotic; IEA:Ensembl; .
GOGO:0034976; P:response to endoplasmic reticulum stress; IEA:Ensembl; .
GOGO:0042542; P:response to hydrogen peroxide; IEA:Ensembl; .
Gene3D3.60.21.10; -; 1; .
InterProIPR004843; Calcineurin-like_PHP_ApaH; .
InterProIPR029052; Metallo-depent_PP-like; .
InterProIPR006186; Ser/Thr-sp_prot-phosphatase; .
PfamPF00149; Metallophos; 1; .
PRINTSPR00114; STPHPHTASE; .
SMARTSM00156; PP2Ac; 1; .
SUPFAMSSF56300; SSF56300; 1; .
PROSITEPS00125; SER_THR_PHOSPHATASE; 1; .



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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