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

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	589 AA.
Sequence status	Complete.
Protein existence	Evidence 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. 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.

Ontologies

Keywords
Biological process	Chromosome partition
Cellular component	Centromere Chromosome Cytoplasm
Domain	Repeat
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	chromosome segregation Inferred from sequence or structural similarity. Source: UniProtKB peptidyl-serine dephosphorylation Inferred from direct assay PubMed 12944463. Source: MGI regulation of apoptotic process Inferred from mutant phenotype PubMed 12944463. Source: MGI
Cellular_component	chromosome, centromeric region Inferred from sequence or structural similarity. Source: UniProtKB cytosol Inferred from direct assay PubMed 12885400. Source: MGI protein phosphatase type 2A complex Inferred from direct assay PubMed 16717086. Source: MGI
Molecular_function	antigen binding Inferred from electronic annotation. Source: Compara protein serine/threonine phosphatase activity Inferred from direct assay PubMed 12944463. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 589

589

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

PRO_0000071401

Regions

Repeat

8 – 46

39

HEAT 1

Repeat

47 – 84

38

HEAT 2

Repeat

85 – 123

39

HEAT 3

Repeat

124 – 161

38

HEAT 4

Repeat

162 – 200

39

HEAT 5

Repeat

201 – 239

39

HEAT 6

Repeat

240 – 278

39

HEAT 7

Repeat

279 – 321

43

HEAT 8

Repeat

322 – 360

39

HEAT 9

Repeat

361 – 399

39

HEAT 10

Repeat

400 – 438

39

HEAT 11

Repeat

439 – 477

39

HEAT 12

Repeat

478 – 516

39

HEAT 13

Repeat

517 – 555

39

HEAT 14

Repeat

556 – 589

34

HEAT 15

Amino acid modifications

Modified residue

280

1

N6-acetyllysine By similarity

Secondary structure

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589

Helix Strand Turn

Details...

Helix

11 – 21

11

Helix

25 – 33

9

Helix

35 – 41

7

Helix

44 – 49

6

Helix

51 – 56

6

Helix

63 – 73

11

Turn

77 – 81

5

Helix

83 – 85

3

Helix

86 – 89

4

Helix

90 – 98

9

Helix

102 – 116

15

Helix

121 – 126

6

Helix

128 – 136

9

Helix

141 – 147

7

Turn

148 – 150

3

Helix

151 – 154

4

Helix

155 – 157

3

Helix

160 – 174

15

Helix

179 – 187

9

Helix

189 – 193

5

Helix

198 – 213

16

Helix

218 – 232

15

Helix

237 – 242

6

Helix

244 – 251

8

Helix

257 – 265

9

Helix

267 – 274

8

Helix

276 – 291

16

Helix

296 – 303

8

Helix

306 – 311

6

Turn

315 – 317

3

Helix

318 – 324

7

Helix

327 – 334

8

Helix

339 – 346

8

Helix

349 – 352

4

Helix

353 – 373

21

Helix

378 – 385

8

Helix

386 – 388

3

Helix

389 – 394

6

Helix

397 – 403

7

Helix

405 – 411

7

Helix

417 – 424

8

Helix

427 – 434

8

Helix

436 – 442

7

Helix

444 – 451

8

Helix

456 – 473

18

Helix

475 – 481

7

Helix

483 – 488

6

Helix

489 – 491

3

Helix

495 – 520

26

Helix

522 – 528

7

Helix

534 – 547

14

Helix

548 – 550

3

Helix

553 – 558

6

Helix

560 – 568

9

Beta strand

569 – 571

3

Helix

573 – 585

13

Sequences

	Sequence		Length	Mass (Da)
	Q76MZ3 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 5175409E4D50A366	FASTA	589	65,323
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
+	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.

IPI

IPI00310091.

RefSeq

NP_058587.1. NM_016891.3.

UniGene

Mm.294138.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IAE	X-ray	3.50	A/D	1-589	[»]
2PF4	X-ray	3.10	A/B/C/D	1-589	[»]
3FGA	X-ray	2.70	A	2-589	[»]

ProteinModelPortal

Q76MZ3.

SMR

Q76MZ3. Positions 2-589.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29429N.

IntAct

Q76MZ3. 40 interactions.

MINT

MINT-135926.

STRING

10090.ENSMUSP00000007708.

PTM databases

PhosphoSite

Q76MZ3.

2D gel databases

REPRODUCTION-2DPAGE

Q76MZ3.

Proteomic databases

PaxDb

Q76MZ3.

PRIDE

Q76MZ3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000007708; ENSMUSP00000007708; ENSMUSG00000007564.

GeneID

51792.

KEGG

mmu:51792.

UCSC

uc008aqi.1. mouse.

Organism-specific databases

CTD

5518.

MGI

MGI:1926334. Ppp2r1a.

Phylogenomic databases

eggNOG

NOG247268.

GeneTree

ENSGT00670000097819.

HOGENOM

HOG000078539.

HOVERGEN

HBG000011.

InParanoid

Q76MZ3.

KO

K03456.

OMA

TCLFCIN.

OrthoDB

EOG45MN4X.

Gene expression databases

ArrayExpress

Q76MZ3.

Bgee

Q76MZ3.

Genevestigator

Q76MZ3.

GermOnline

ENSMUSG00000007564. Mus musculus.

Family and domain databases

Gene3D

1.25.10.10. 1 hit.

InterPro

IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR021133. HEAT_type_2.
[Graphical view]

Pfam

PF02985. HEAT. 2 hits.
[Graphical view]

SUPFAM

SSF48371. ARM-type_fold. 1 hit.

PROSITE

PS50077. HEAT_REPEAT. 11 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

Q76MZ3.

ChEMBL

CHEMBL3557.

ChiTaRS

PPP2R1A. mouse.

EvolutionaryTrace

Q76MZ3.

NextBio

308024.

SOURCE

Search...

Entry information

Entry name

2AAA_MOUSE

Accession

Primary (citable) accession number: Q76MZ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 27, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 80 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program