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

Last modified November 16, 2011. Version 70. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.

Subcellular location

Cytoplasm By similarity. Chromosome › centromere 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.

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 By similarity

Secondary structure

1 ................................................................................................................ 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: 10100624] [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: 16141072] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
+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.
IPIIPI00310091.
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...

Protein-protein interaction databases

DIPDIP-29429N.
IntActQ76MZ3. 39 interactions.
MINTMINT-135926.
STRINGQ76MZ3.

PTM databases

PhosphoSiteQ76MZ3.

2D gel databases

REPRODUCTION-2DPAGEQ76MZ3.

Proteomic databases

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

eggNOGroNOG07248.
HOGENOMHBG526812.
HOVERGENHBG000011.
InParanoidQ76MZ3.
OMALFLIQLK.
OrthoDBEOG45MN4X.
PhylomeDBQ76MZ3.

Gene expression databases

ArrayExpressQ76MZ3.
BgeeQ76MZ3.
GenevestigatorQ76MZ3.
GermOnlineENSMUSG00000007564. Mus musculus.

Family and domain databases

InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]
Gene3DG3DSA:1.25.10.10. ARM-like. 1 hit.
KOK03456.
PfamPF02985. HEAT. 2 hits.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
PROSITEPS50077. HEAT_REPEAT. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio308024.
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: November 16, 2011
This is version 70 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents