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P30153

- 2AAA_HUMAN

UniProt

P30153 - 2AAA_HUMAN

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Protein

Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform

Gene

PPP2R1A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

The PR65 subunit of protein phosphatase 2A serves as a scaffolding molecule to coordinate the assembly of the catalytic subunit and a variable regulatory B subunit. Required for proper chromosome segregation and for centromeric localization of SGOL1 in mitosis.1 Publication

GO - Molecular functioni

  1. antigen binding Source: UniProtKB
  2. protein heterodimerization activity Source: UniProtKB
  3. protein phosphatase type 2A regulator activity Source: UniProtKB
  4. protein serine/threonine phosphatase activity Source: Ensembl

GO - Biological processi

  1. apoptotic process Source: UniProtKB
  2. ceramide metabolic process Source: UniProtKB
  3. chromosome segregation Source: UniProtKB
  4. fibroblast growth factor receptor signaling pathway Source: Reactome
  5. G2/M transition of mitotic cell cycle Source: Reactome
  6. gene expression Source: Reactome
  7. inactivation of MAPK activity Source: UniProtKB
  8. mitotic cell cycle Source: Reactome
  9. mitotic nuclear envelope reassembly Source: Reactome
  10. mRNA metabolic process Source: Reactome
  11. negative regulation of cell growth Source: UniProtKB
  12. negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  13. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: Reactome
  14. peptidyl-serine dephosphorylation Source: Ensembl
  15. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  16. protein complex assembly Source: UniProtKB
  17. protein dephosphorylation Source: UniProtKB
  18. regulation of cell adhesion Source: UniProtKB
  19. regulation of cell differentiation Source: UniProtKB
  20. regulation of DNA replication Source: UniProtKB
  21. regulation of growth Source: UniProtKB
  22. regulation of transcription, DNA-templated Source: UniProtKB
  23. regulation of Wnt signaling pathway Source: UniProtKB
  24. response to organic substance Source: UniProtKB
  25. RNA metabolic process Source: Reactome
  26. RNA splicing Source: UniProtKB
  27. second-messenger-mediated signaling Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Chromosome partition

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000105568-MONOMER.
ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_111080. Spry regulation of FGF signaling.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_1383. Glycolysis.
REACT_150182. MASTL Facilitates Mitotic Progression.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1505. Integration of energy metabolism.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15334. DARPP-32 events.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_23879. Platelet sensitization by LDL.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_682. Mitotic Prometaphase.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_821. Cyclin D associated events in G1.
SignaLinkiP30153.

Names & Taxonomyi

Protein namesi
Recommended name:
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Alternative name(s):
Medium tumor antigen-associated 61 kDa protein
PP2A subunit A isoform PR65-alpha
PP2A subunit A isoform R1-alpha
Gene namesi
Name:PPP2R1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9302. PPP2R1A.

Subcellular locationi

Cytoplasm By similarity. Chromosomecentromere 1 Publication
Note: Centromeric localization requires the presence of BUB1.

GO - Cellular componenti

  1. chromosome, centromeric region Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. membrane Source: UniProtKB
  5. microtubule cytoskeleton Source: UniProtKB
  6. mitochondrion Source: UniProtKB
  7. nucleus Source: UniProtKB
  8. protein phosphatase type 2A complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33666.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 589588Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoformPRO_0000071400Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine3 Publications
Modified residuei280 – 2801N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP30153.
PaxDbiP30153.
PRIDEiP30153.

2D gel databases

OGPiP30153.
REPRODUCTION-2DPAGEIPI00554737.

PTM databases

PhosphoSiteiP30153.

Miscellaneous databases

PMAP-CutDBP30153.

Expressioni

Gene expression databases

BgeeiP30153.
CleanExiHS_PPP2R1A.
ExpressionAtlasiP30153. baseline and differential.
GenevestigatoriP30153.

Organism-specific databases

HPAiCAB018599.

Interactioni

Subunit structurei

Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD. Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphoylation sites (By similarity). PP2A consists of a common heterodimeric core enzyme, composed of PPP2CA a 36 kDa catalytic subunit (subunit C) and PPP2R1A a 65 kDa constant regulatory subunit (PR65 or subunit A), that associates with a variety of regulatory subunits. Proteins that associate with the core dimer include three families of regulatory subunits B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56 families), the 48 kDa variable regulatory subunit, viral proteins, and cell signaling molecules. Interacts with IPO9. Interacts with TP53 and SGOL1. Interacts with PLA2G16; this interaction might decrease PP2A activity. Interacts with CTTNBP2NL.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P030813EBI-302388,EBI-1266256From a different organism.
AKT1P317492EBI-302388,EBI-296087
E7P031293EBI-302388,EBI-866453From a different organism.
E7P040202EBI-302388,EBI-7005254From a different organism.
KIAA1524Q8TCG14EBI-302388,EBI-1379376
NxnP973462EBI-302388,EBI-309684From a different organism.
PLA2G16P538167EBI-302388,EBI-746318
PPP2CAP6777514EBI-302388,EBI-712311
PPP2R2AP631518EBI-302388,EBI-1048931
PPP2R2BQ000055EBI-302388,EBI-1052159
PPP2R5AQ151723EBI-302388,EBI-641666
PPP2R5CQ133626EBI-302388,EBI-1266156
PPP2R5CQ13362-15EBI-302388,EBI-1266170
PPP2R5CQ13362-22EBI-302388,EBI-1266173
Ppp2r5cQ60996-32EBI-302388,EBI-1369292From a different organism.
PPP2R5DQ147384EBI-302388,EBI-396563
PPP2R5EQ165373EBI-302388,EBI-968374
PPP4CP605103EBI-302388,EBI-1046072
PPP5CP530413EBI-302388,EBI-716663
RELAQ042062EBI-302388,EBI-73886
STRNO438154EBI-302388,EBI-1046642
TP53P046373EBI-302388,EBI-366083

Protein-protein interaction databases

BioGridi111510. 169 interactions.
DIPiDIP-29394N.
IntActiP30153. 116 interactions.
MINTiMINT-1141071.
STRINGi9606.ENSP00000324804.

Structurei

Secondary structure

1
589
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni6 – 83
Helixi11 – 199
Helixi25 – 339
Helixi35 – 417
Helixi44 – 496
Helixi51 – 577
Helixi63 – 7311
Helixi78 – 803
Helixi83 – 897
Helixi90 – 967
Beta strandi99 – 1013
Helixi102 – 11615
Helixi121 – 1266
Helixi128 – 1369
Beta strandi138 – 1403
Helixi141 – 1477
Helixi148 – 1503
Helixi151 – 1544
Turni155 – 1573
Helixi160 – 17415
Helixi179 – 19416
Helixi198 – 2036
Helixi205 – 2139
Helixi218 – 2214
Helixi224 – 23411
Helixi237 – 2393
Helixi240 – 2434
Helixi245 – 2528
Helixi257 – 2659
Helixi267 – 2748
Helixi276 – 2816
Helixi283 – 2919
Helixi296 – 31116
Turni315 – 3173
Helixi318 – 3247
Helixi326 – 3349
Helixi339 – 3468
Helixi349 – 3524
Helixi353 – 3564
Helixi358 – 3647
Helixi366 – 3738
Helixi378 – 3858
Helixi389 – 3946
Helixi397 – 41216
Helixi417 – 43418
Helixi436 – 4383
Helixi441 – 4499
Helixi450 – 4523
Helixi456 – 47318
Helixi475 – 4817
Helixi483 – 4886
Turni489 – 4913
Helixi495 – 52026
Helixi522 – 5276
Helixi528 – 5303
Helixi534 – 54714
Helixi548 – 5503
Helixi553 – 56715
Helixi573 – 58513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B3UX-ray2.30A/B2-589[»]
2IE3X-ray2.80A1-589[»]
2IE4X-ray2.60A1-589[»]
2NPPX-ray3.30A/D1-589[»]
2NYLX-ray3.80A/D8-589[»]
2NYMX-ray3.60A/D8-589[»]
2PKGX-ray3.30A/B10-589[»]
3C5WX-ray2.80A9-589[»]
3DW8X-ray2.85A/D9-589[»]
3K7VX-ray2.85A1-589[»]
3K7WX-ray2.96A1-589[»]
4I5LX-ray2.43A/D6-589[»]
4I5NX-ray2.80A/D6-589[»]
4LACX-ray2.82A404-589[»]
ProteinModelPortaliP30153.
SMRiP30153. Positions 2-589.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30153.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati8 – 4639HEAT 1Add
BLAST
Repeati47 – 8438HEAT 2Add
BLAST
Repeati85 – 12339HEAT 3Add
BLAST
Repeati124 – 16138HEAT 4Add
BLAST
Repeati162 – 20039HEAT 5Add
BLAST
Repeati201 – 23939HEAT 6Add
BLAST
Repeati240 – 27839HEAT 7Add
BLAST
Repeati279 – 32143HEAT 8Add
BLAST
Repeati322 – 36039HEAT 9Add
BLAST
Repeati361 – 39939HEAT 10Add
BLAST
Repeati400 – 43839HEAT 11Add
BLAST
Repeati439 – 47739HEAT 12Add
BLAST
Repeati478 – 51639HEAT 13Add
BLAST
Repeati517 – 55539HEAT 14Add
BLAST
Repeati556 – 58934HEAT 15Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni8 – 399392PP2A subunit B bindingAdd
BLAST
Regioni47 – 321275Polyoma small and medium T antigens BindingAdd
BLAST
Regioni85 – 239155SV40 small T antigen bindingAdd
BLAST
Regioni400 – 589190PP2A subunit C bindingAdd
BLAST

Domaini

Each HEAT repeat appears to consist of two alpha helices joined by a hydrophilic region, the intrarepeat loop. The repeat units may be arranged laterally to form a rod-like structure.

Sequence similaritiesi

Contains 15 HEAT repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG247268.
GeneTreeiENSGT00730000110944.
HOGENOMiHOG000078539.
HOVERGENiHBG000011.
InParanoidiP30153.
KOiK03456.
OMAiRNLCQDD.
OrthoDBiEOG764722.
PhylomeDBiP30153.
TreeFamiTF105552.

Family and domain databases

Gene3Di1.25.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
PfamiPF02985. HEAT. 2 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
PROSITEiPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P30153-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE
60 70 80 90 100
LLPFLTDTIY DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE
110 120 130 140 150
ETVVRDKAVE SLRAISHEHS PSDLEAHFVP LVKRLAGGDW FTSRTSACGL
160 170 180 190 200
FSVCYPRVSS AVKAELRQYF RNLCSDDTPM VRRAAASKLG EFAKVLELDN
210 220 230 240 250
VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL EALVMPTLRQ
260 270 280 290 300
AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA
310 320 330 340 350
AASHKVKEFC ENLSADCREN VIMSQILPCI KELVSDANQH VKSALASVIM
360 370 380 390 400
GLSPILGKDN TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL
410 420 430 440 450
SQSLLPAIVE LAEDAKWRVR LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW
460 470 480 490 500
LVDHVYAIRE AATSNLKKLV EKFGKEWAHA TIIPKVLAMS GDPNYLHRMT
510 520 530 540 550
TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV AKSLQKIGPI
560 570 580
LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA
Length:589
Mass (Da):65,309
Last modified:April 3, 2007 - v4
Checksum:i5174EBE94D537836
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti130 – 1301P → A in AAA35531. (PubMed:2554323)Curated
Sequence conflicti258 – 2581R → A in AAA36399. (PubMed:2159327)Curated
Sequence conflicti272 – 2721K → R AA sequence (PubMed:8694763)Curated
Sequence conflicti551 – 5511L → P in CAG29336. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31786 mRNA. Translation: AAA35531.1.
J02902 mRNA. Translation: AAA36399.1.
CR450340 mRNA. Translation: CAG29336.1.
BC001537 mRNA. Translation: AAH01537.1.
CCDSiCCDS12849.1.
PIRiA34541.
RefSeqiNP_055040.2. NM_014225.5.
UniGeneiHs.467192.

Genome annotation databases

EnsembliENST00000322088; ENSP00000324804; ENSG00000105568.
GeneIDi5518.
KEGGihsa:5518.
UCSCiuc002pyp.3. human.

Polymorphism databases

DMDMi143811355.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31786 mRNA. Translation: AAA35531.1 .
J02902 mRNA. Translation: AAA36399.1 .
CR450340 mRNA. Translation: CAG29336.1 .
BC001537 mRNA. Translation: AAH01537.1 .
CCDSi CCDS12849.1.
PIRi A34541.
RefSeqi NP_055040.2. NM_014225.5.
UniGenei Hs.467192.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1B3U X-ray 2.30 A/B 2-589 [» ]
2IE3 X-ray 2.80 A 1-589 [» ]
2IE4 X-ray 2.60 A 1-589 [» ]
2NPP X-ray 3.30 A/D 1-589 [» ]
2NYL X-ray 3.80 A/D 8-589 [» ]
2NYM X-ray 3.60 A/D 8-589 [» ]
2PKG X-ray 3.30 A/B 10-589 [» ]
3C5W X-ray 2.80 A 9-589 [» ]
3DW8 X-ray 2.85 A/D 9-589 [» ]
3K7V X-ray 2.85 A 1-589 [» ]
3K7W X-ray 2.96 A 1-589 [» ]
4I5L X-ray 2.43 A/D 6-589 [» ]
4I5N X-ray 2.80 A/D 6-589 [» ]
4LAC X-ray 2.82 A 404-589 [» ]
ProteinModelPortali P30153.
SMRi P30153. Positions 2-589.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111510. 169 interactions.
DIPi DIP-29394N.
IntActi P30153. 116 interactions.
MINTi MINT-1141071.
STRINGi 9606.ENSP00000324804.

PTM databases

PhosphoSitei P30153.

Polymorphism databases

DMDMi 143811355.

2D gel databases

OGPi P30153.
REPRODUCTION-2DPAGE IPI00554737.

Proteomic databases

MaxQBi P30153.
PaxDbi P30153.
PRIDEi P30153.

Protocols and materials databases

DNASUi 5518.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322088 ; ENSP00000324804 ; ENSG00000105568 .
GeneIDi 5518.
KEGGi hsa:5518.
UCSCi uc002pyp.3. human.

Organism-specific databases

CTDi 5518.
GeneCardsi GC19P052693.
HGNCi HGNC:9302. PPP2R1A.
HPAi CAB018599.
MIMi 605983. gene.
neXtProti NX_P30153.
PharmGKBi PA33666.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG247268.
GeneTreei ENSGT00730000110944.
HOGENOMi HOG000078539.
HOVERGENi HBG000011.
InParanoidi P30153.
KOi K03456.
OMAi RNLCQDD.
OrthoDBi EOG764722.
PhylomeDBi P30153.
TreeFami TF105552.

Enzyme and pathway databases

BioCyci MetaCyc:ENSG00000105568-MONOMER.
Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_111080. Spry regulation of FGF signaling.
REACT_12436. ERKs are inactivated.
REACT_12599. ERK/MAPK targets.
REACT_1383. Glycolysis.
REACT_150182. MASTL Facilitates Mitotic Progression.
REACT_150425. Resolution of Sister Chromatid Cohesion.
REACT_150471. Separation of Sister Chromatids.
REACT_1505. Integration of energy metabolism.
REACT_15296. Recruitment of mitotic centrosome proteins and complexes.
REACT_15334. DARPP-32 events.
REACT_15364. Loss of Nlp from mitotic centrosomes.
REACT_15451. Loss of proteins required for interphase microtubule organization from the centrosome.
REACT_160242. Initiation of Nuclear Envelope Reformation.
REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
REACT_1857. Cyclin A/B1 associated events during G2/M transition.
REACT_19405. CTLA4 inhibitory signaling.
REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_23879. Platelet sensitization by LDL.
REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
REACT_682. Mitotic Prometaphase.
REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_821. Cyclin D associated events in G1.
SignaLinki P30153.

Miscellaneous databases

EvolutionaryTracei P30153.
GeneWikii PPP2R1A.
GenomeRNAii 5518.
NextBioi 21342.
PMAP-CutDB P30153.
PROi P30153.
SOURCEi Search...

Gene expression databases

Bgeei P30153.
CleanExi HS_PPP2R1A.
ExpressionAtlasi P30153. baseline and differential.
Genevestigatori P30153.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
InterProi IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view ]
Pfami PF02985. HEAT. 2 hits.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
PROSITEi PS50077. HEAT_REPEAT. 11 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa protein."
    Walter G., Ferre F., Espiritu O., Carbone-Wiley A.
    Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 242-255.
    Tissue: Placenta.
  2. "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure."
    Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., Merlevede W., Hofsteenge J., Stone S.R.
    Biochemistry 29:3166-3173(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "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].
    Tissue: Colon.
  5. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 34-46, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  6. "The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
    Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
    Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 204-214; 261-272 AND 521-527.
  7. "Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens."
    Ruediger R., Hentz M., Fait J., Mumby M., Walter G.
    J. Virol. 68:123-129(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: BINDING DOMAINS.
  8. "Interaction between protein phosphatase 2A and members of the importin beta superfamily."
    Lubert E.J., Sarge K.D.
    Biochem. Biophys. Res. Commun. 303:908-913(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IPO9.
  9. "PP2A is required for centromeric localization of Sgo1 and proper chromosome segregation."
    Tang Z., Shu H., Qi W., Mahmood N.A., Mumby M.C., Yu H.
    Dev. Cell 10:575-585(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
  10. "A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55."
    Li H.H., Cai X., Shouse G.P., Piluso L.G., Liu X.
    EMBO J. 26:402-411(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TP53.
  11. "Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma cells."
    Nazarenko I., Schafer R., Sers C.
    J. Cell Sci. 120:1393-1404(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PLA2G16.
  12. "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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex linked to the cerebral cavernous malformation 3 (CCM3) protein."
    Goudreault M., D'Ambrosio L.M., Kean M.J., Mullin M.J., Larsen B.G., Sanchez A., Chaudhry S., Chen G.I., Sicheri F., Nesvizhskii A.I., Aebersold R., Raught B., Gingras A.C.
    Mol. Cell. Proteomics 8:157-171(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CTTNBP2NL.
  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-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "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].
  17. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs."
    Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D.
    Cell 96:99-110(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  19. "Structural mechanism of demethylation and inactivation of protein phosphatase 2A."
    Xing Y., Li Z., Chen Y., Stock J.B., Jeffrey P.D., Shi Y.
    Cell 133:154-163(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 9-589 IN COMPLEX WITH WITH PPP2CA AND PPME1.

Entry informationi

Entry namei2AAA_HUMAN
AccessioniPrimary (citable) accession number: P30153
Secondary accession number(s): Q13773, Q6ICQ3, Q96DH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 3, 2007
Last modified: October 29, 2014
This is version 153 of the entry and version 4 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, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3