[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 242-255.
TISSUE=Placenta;
PubMed=2554323 [NCBI, ExPASy, EBI, Israel, Japan]
Walter G.,
Ferre F.,
Espiritu O.,
Carbone-Wiley A.;
"Molecular cloning and sequence of cDNA encoding polyoma medium tumor antigen-associated 61-kDa protein.";
Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1021/bi00465a002; PubMed=2159327 [NCBI, ExPASy, EBI, Israel, Japan]
Hemmings B.A.,
Adams-Pearson C.,
Maurer F.,
Mueller P.,
Goris J.,
Merlevede W.,
Hofsteenge J.,
Stone S.R.;
"Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure.";
Biochemistry 29:3166-3173(1990).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L.,
Schick M.,
Neubert P.,
Schatten R.,
Henze S.,
Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
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[4]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[5]
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PROTEIN SEQUENCE OF 34-46, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G.,
Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
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[6]
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PROTEIN SEQUENCE OF 204-214; 261-272 AND 521-527.
PubMed=8694763 [NCBI, ExPASy, EBI, Israel, Japan]
Zolnierowicz S.,
van Hoof C.,
Andjelkovic N.,
Cron P.,
Stevens I.,
Merlevede W.,
Goris J.,
Hemmings B.A.;
"The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits.";
Biochem. J. 317:187-194(1996).
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[7]
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BINDING DOMAINS.
PubMed=8254721 [NCBI, ExPASy, EBI, Israel, Japan]
Ruediger R.,
Hentz M.,
Fait J.,
Mumby M.,
Walter G.;
"Molecular model of the A subunit of protein phosphatase 2A: interaction with other subunits and tumor antigens.";
J. Virol. 68:123-129(1994).
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[8]
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INTERACTION WITH IPO9.
DOI=10.1016/S0006-291X(03)00434-0; PubMed=12670497 [NCBI, ExPASy, EBI, Israel, Japan]
Lubert E.J.,
Sarge K.D.;
"Interaction between protein phosphatase 2A and members of the importin beta superfamily.";
Biochem. Biophys. Res. Commun. 303:908-913(2003).
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[9]
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1016/S0092-8674(00)80963-0; PubMed=9989501 [NCBI, ExPASy, EBI, Israel, Japan]
Groves M.R.,
Hanlon N.,
Turowski P.,
Hemmings B.A.,
Barford D.;
"The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs.";
Cell 96:99-110(1999).
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- 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.
- SUBUNIT: PP2A consists of a common heterodimeric core enzyme, composed of a 36 kDa catalytic subunit (subunit C) and 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.
- INTERACTION:
P03081:- (xeno); NbExp=1; IntAct=EBI-302388, EBI-1266256;
Q9NSA3:CTNNBIP1; NbExp=1; IntAct=EBI-302388, EBI-747082;
P53816:HRASLS3; NbExp=3; IntAct=EBI-302388, EBI-746318;
Q14164:IKBKE; NbExp=1; IntAct=EBI-302388, EBI-307369;
Q8TCG1:KIAA1524; NbExp=2; IntAct=EBI-302388, EBI-1379376;
P23508:MCC; NbExp=1; IntAct=EBI-302388, EBI-307531;
P67775:PPP2CA; NbExp=1; IntAct=EBI-302388, EBI-712311;
Q13362-1:PPP2R5C; NbExp=1; IntAct=EBI-302388, EBI-1266170;
Q13362-2:PPP2R5C; NbExp=1; IntAct=EBI-302388, EBI-1266173;
Q60996-3:Ppp2r5c (xeno); NbExp=1; IntAct=EBI-302388, EBI-1369292;
P60510:PPP4C; NbExp=1; IntAct=EBI-302388, EBI-1046072;
Q5T5B3:STK24; NbExp=1; IntAct=EBI-302388, EBI-1054809;
- 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.
- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit A family.
- SIMILARITY: Contains 15 HEAT repeats.
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