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Q76MZ3 (2AAA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Alternative name(s):
PP2A subunit A isoform PR65-alpha
PP2A subunit A isoform R1-alpha
Gene names
Name:Ppp2r1a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length589 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

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. Found in a complex with at least ARL2, PPP2CB, PPP2R1A, PPP2R2A, PPP2R5E and TBCD By similarity. Interacts with PLA2G16; this interaction might decrease PP2A activity By similarity. Interacts with FOXO1; the interaction dephosphorylates FOXO1 on AKT-mediated phosphoylation sites. Interacts with CTTNBP2NL By similarity. Ref.4

Subcellular location

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

Domain

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 similarities

Belongs to the phosphatase 2A regulatory subunit A family.

Contains 15 HEAT repeats.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P030812EBI-400413,EBI-1266256From a different organism.
Ppp2caP633303EBI-400413,EBI-397144

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 589588Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
PRO_0000071401

Regions

Repeat8 – 4639HEAT 1
Repeat47 – 8438HEAT 2
Repeat85 – 12339HEAT 3
Repeat124 – 16138HEAT 4
Repeat162 – 20039HEAT 5
Repeat201 – 23939HEAT 6
Repeat240 – 27839HEAT 7
Repeat279 – 32143HEAT 8
Repeat322 – 36039HEAT 9
Repeat361 – 39939HEAT 10
Repeat400 – 43839HEAT 11
Repeat439 – 47739HEAT 12
Repeat478 – 51639HEAT 13
Repeat517 – 55539HEAT 14
Repeat556 – 58934HEAT 15

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2801N6-acetyllysine Ref.5

Secondary structure

..................................................................................................... 589
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q76MZ3 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 5175409E4D50A366

FASTA58965,323
        10         20         30         40         50         60 
MAAADGDDSL YPIAVLIDEL RNEDVQLRLN SIKKLSTIAL ALGVERTRSE LLPFLTDTIY 

        70         80         90        100        110        120 
DEDEVLLALA EQLGTFTTLV GGPEYVHCLL PPLESLATVE ETVVRDKAVE SLRAISHEHS 

       130        140        150        160        170        180 
PSDLEAHFVP LVKRLAGGDW FTSRTSACGL FSVCYPRVSS AVKAELRQYF RNLCSDDTPM 

       190        200        210        220        230        240 
VRRAAASKLG EFAKVLELDN VKSEIIPMFS NLASDEQDSV RLLAVEACVN IAQLLPQEDL 

       250        260        270        280        290        300 
EALVMPTLRQ AAEDKSWRVR YMVADKFTEL QKAVGPEITK TDLVPAFQNL MKDCEAEVRA 

       310        320        330        340        350        360 
AASHKVKEFC ENLSADCREN VIMTQILPCI KELVSDANQH VKSALASVIM GLSPILGKDN 

       370        380        390        400        410        420 
TIEHLLPLFL AQLKDECPEV RLNIISNLDC VNEVIGIRQL SQSLLPAIVE LAEDAKWRVR 

       430        440        450        460        470        480 
LAIIEYMPLL AGQLGVEFFD EKLNSLCMAW LVDHVYAIRE AATSNLKKLV EKFGKEWAHA 

       490        500        510        520        530        540 
TIIPKVLAMS GDPNYLHRMT TLFCINVLSE VCGQDITTKH MLPTVLRMAG DPVANVRFNV 

       550        560        570        580 
AKSLQKIGPI LDNSTLQSEV KPILEKLTQD QDVDVKYFAQ EALTVLSLA 

« Hide

References

« Hide 'large scale' references
[1]"Alpha4 protein as a common regulator of type 2A-related serine/threonine protein phosphatases."
Nanahoshi M., Tsujishita Y., Tokunaga C., Inui S., Sakaguchi N., Hara K., Yonezawa K.
FEBS Lett. 446:108-112(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Medulla oblongata and Oviduct.
[3]"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].
Strain: FVB/N.
Tissue: Mammary tumor.
[4]"The B55alpha-containing PP2A holoenzyme dephosphorylates FOXO1 in islet beta-cells under oxidative stress."
Yan L., Guo S., Brault M., Harmon J., Robertson R.P., Hamid R., Stein R., Yang E.
Biochem. J. 444:239-247(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH FOXO1.
[5]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB021743 mRNA. Translation: BAA75478.1.
AK054239 mRNA. Translation: BAC35700.1.
AK078135 mRNA. Translation: BAC37143.1.
BC006606 mRNA. Translation: AAH06606.1.
CCDSCCDS28432.1.
RefSeqNP_058587.1. NM_016891.3.
UniGeneMm.294138.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2IAEX-ray3.50A/D1-589[»]
2PF4X-ray3.10A/B/C/D1-589[»]
3FGAX-ray2.70A2-589[»]
ProteinModelPortalQ76MZ3.
SMRQ76MZ3. Positions 2-589.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid206176. 26 interactions.
DIPDIP-29429N.
IntActQ76MZ3. 46 interactions.
MINTMINT-135926.
STRING10090.ENSMUSP00000007708.

Chemistry

BindingDBQ76MZ3.
ChEMBLCHEMBL3557.

PTM databases

PhosphoSiteQ76MZ3.

2D gel databases

REPRODUCTION-2DPAGEQ76MZ3.

Proteomic databases

MaxQBQ76MZ3.
PaxDbQ76MZ3.
PRIDEQ76MZ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000007708; ENSMUSP00000007708; ENSMUSG00000007564.
GeneID51792.
KEGGmmu:51792.
UCSCuc008aqi.1. mouse.

Organism-specific databases

CTD5518.
MGIMGI:1926334. Ppp2r1a.

Phylogenomic databases

eggNOGNOG247268.
GeneTreeENSGT00730000110944.
HOGENOMHOG000078539.
HOVERGENHBG000011.
InParanoidQ76MZ3.
KOK03456.
OMARNLCQDD.
OrthoDBEOG764722.
PhylomeDBQ76MZ3.
TreeFamTF105552.

Enzyme and pathway databases

ReactomeREACT_188257. Signal Transduction.

Gene expression databases

ArrayExpressQ76MZ3.
BgeeQ76MZ3.
GenevestigatorQ76MZ3.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
PfamPF02985. HEAT. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
PROSITEPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPPP2R1A. mouse.
EvolutionaryTraceQ76MZ3.
NextBio308024.
PROQ76MZ3.
SOURCESearch...

Entry information

Entry name2AAA_MOUSE
AccessionPrimary (citable) accession number: Q76MZ3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 27, 2004
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot