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UniProtKB/Swiss-Prot entry P30153


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name 2AAA_HUMAN
Primary accession number P30153
Secondary accession numbers Q13773 Q6ICQ3 Q96DH3
Integrated into Swiss-Prot on April 1, 1993
Sequence was last modified on April 3, 2007 (Sequence version 4)
Annotations were last modified on    November 25, 2008 (Entry version 86)
Name and origin of the protein
Protein name Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Synonyms PP2A, subunit A, PR65-alpha isoform
PP2A, subunit A, R1-alpha isoform
Medium tumor antigen-associated 61 kDa protein
Gene name
Name: PPP2R1A
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
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).
[2]
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).
[3]
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.
[4]
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).
[5]
PROTEIN SEQUENCE OF 34-46, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[6]
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).
[7]
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).
[8]
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).
[9]
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).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M31786; AAA35531.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J02902; AAA36399.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR450340; CAG29336.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001537; AAH01537.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A34541; A34541.
RefSeq NP_055040.2; -.
UniGene Hs.467192
3D structure databases
PDB
1B3U; X-ray; 2.30 A; A=1-589, B=2-589.[ExPASy / RCSB / EBI]
2IE3; X-ray; 2.80 A; A=1-589.[ExPASy / RCSB / EBI]
2IE4; X-ray; 2.60 A; A=1-589.[ExPASy / RCSB / EBI]
2NPP; X-ray; 3.30 A; A/D=1-589.[ExPASy / RCSB / EBI]
2NYL; X-ray; 3.80 A; A/D=8-589.[ExPASy / RCSB / EBI]
2NYM; X-ray; 3.60 A; A/D=8-589.[ExPASy / RCSB / EBI]
2PKG; X-ray; 3.30 A; A/B=10-589.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1B3U; -.
2IE3; -.
2IE4; -.
2NPP; -.
2NYL; -.
2NYM; -.
2PKG; -.
ModBase P30153.
Protein-protein interaction databases
IntAct P30153; -.
PTM databases
PhosphoSite P30153; -.
Enzyme and pathway databases
Reactome REACT_11045; Signaling by Wnt.
REACT_1505; Integration of energy metabolism.
2D gel databases
OGP P30153; -.
REPRODUCTION-2DPAGE IPI00554737; -.
Organism-specific databases
HGNC HGNC:9302; PPP2R1A.
GenAtlas PPP2R1A.
HPA CAB018599; -.
MIM 605983; gene. [NCBI / EBI]
PharmGKB PA33666; -.
GeneCards P30153.
Gene expression databases
ArrayExpress P30153; -.
CleanEx HS_PPP2R1A; -.
GermOnline ENSG00000105568; Homo sapiens.
Ontologies
GO
GO:0005829; Cellular component: cytosol (traceable author statement from UniProtKB).
GO:0016020; Cellular component: membrane (non-traceable author statement from UniProtKB).
GO:0015630; Cellular component: microtubule cytoskeleton (non-traceable author statement from UniProtKB).
GO:0005739; Cellular component: mitochondrion (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (non-traceable author statement from UniProtKB).
GO:0000159; Cellular component: protein phosphatase type 2A complex (traceable author statement from UniProtKB).
GO:0005625; Cellular component: soluble fraction (non-traceable author statement from UniProtKB).
GO:0003823; Molecular function: antigen binding (inferred from physical interaction from UniProtKB).
GO:0046982; Molecular function: protein heterodimerization activity (inferred from physical interaction from UniProtKB).
GO:0008601; Molecular function: protein phosphatase type 2A regulator activity (traceable author statement from UniProtKB).
GO:0006672; Biological process: ceramide metabolic process (non-traceable author statement from UniProtKB).
GO:0000188; Biological process: inactivation of MAPK activity (non-traceable author statement from UniProtKB).
GO:0006917; Biological process: induction of apoptosis (traceable author statement from UniProtKB).
GO:0030308; Biological process: negative regulation of cell growth (non-traceable author statement from UniProtKB).
GO:0042518; Biological process: negative regulation of tyrosine phosphorylation of Stat3 protein (non-traceable author statement from UniProtKB).
GO:0006470; Biological process: protein amino acid dephosphorylation (traceable author statement from UniProtKB).
GO:0006461; Biological process: protein complex assembly (traceable author statement from UniProtKB).
GO:0030155; Biological process: regulation of cell adhesion (non-traceable author statement from UniProtKB).
GO:0045595; Biological process: regulation of cell differentiation (non-traceable author statement from UniProtKB).
GO:0006275; Biological process: regulation of DNA replication (non-traceable author statement from UniProtKB).
GO:0045449; Biological process: regulation of transcription (non-traceable author statement from UniProtKB).
GO:0030111; Biological process: regulation of Wnt receptor signaling pathway (non-traceable author statement from UniProtKB).
GO:0010033; Biological process: response to organic substance (non-traceable author statement from UniProtKB).
GO:0008380; Biological process: RNA splicing (non-traceable author statement from UniProtKB).
GO:0019932; Biological process: second-messenger-mediated signaling (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR011989; ARM-like.
IPR000357; HEAT.
Graphical view of domain structure.
Gene3D G3DSA:1.25.10.10; ARM-like; 1.
Pfam PF02985; HEAT; 11.
Pfam graphical view of domain structure.
PROSITE PS50077; HEAT_REPEAT; 11.
PROSITE graphical view of domain structure (profiles).
BLOCKS P30153.
ProtoNet P30153.
Genome annotation databases
Ensembl ENSG00000105568; Homo sapiens. [Contig view]
GeneID 5518; -.
KEGG hsa:5518; -.
Phylogenomic databases
HOGENOM P30153; -.
HOVERGEN P30153; -.
Other
NextBio 21342; -.
SOURCE PPP2R1A; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Direct protein sequencing; Polymorphism; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   589  588     Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform. PRO_0000071400
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. 
REGION   8   399  392     PP2A subunit B binding. 
REGION   47   321  275     Polyoma small and medium T antigens Binding. 
REGION   85   239  155     SV40 small T antigen binding. 
REGION   400   589  190     PP2A subunit C binding. 
MOD_RES   2     2        N-acetylalanine. 
VARIANT   87    87  1     H -> R (in lung). VAR_006383 
CONFLICT   130   130        P -> A (in Ref. 1; AAA35531). 
CONFLICT   258   258        R -> A (in Ref. 2; AAA36399). 
CONFLICT   272   272        K -> R (in Ref. 6; AA sequence). 
CONFLICT   551   551        L -> P (in Ref. 3; CAG29336). 
TURN   6     8  3      
HELIX   11    19  9      
HELIX   25    33  9      
HELIX   35    41  7      
HELIX   44    49  6      
HELIX   51    57  7      
HELIX   63    73  11      
HELIX   78    80  3      
HELIX   83    89  7      
HELIX   90    96  7      
HELIX   102   116  15      
HELIX   121   126  6      
HELIX   128   136  9      
HELIX   141   147  7      
HELIX   148   150  3      
HELIX   151   154  4      
TURN   155   157  3      
HELIX   160   174  15      
HELIX   179   194  16      
HELIX   198   203  6      
HELIX   205   213  9      
HELIX   218   221  4      
HELIX   224   234  11      
HELIX   237   239  3      
HELIX   240   243  4      
HELIX   245   252  8      
HELIX   257   265  9      
HELIX   267   274  8      
HELIX   276   281  6      
HELIX   283   291  9      
HELIX   296   311  16      
TURN   315   317  3      
HELIX   318   324  7      
HELIX   326   334  9      
HELIX   339   346  8      
HELIX   349   352  4      
HELIX   353   356  4      
HELIX   358   364  7      
HELIX   366   373  8      
HELIX   378   385  8      
HELIX   389   394  6      
HELIX   397   412  16      
HELIX   417   434  18      
HELIX   436   438  3      
HELIX   441   449  9      
HELIX   450   452  3      
HELIX   456   473  18      
HELIX   475   481  7      
HELIX   483   488  6      
TURN   489   491  3      
HELIX   495   520  26      
HELIX   522   527  6      
HELIX   528   530  3      
HELIX   534   547  14      
HELIX   548   550  3      
HELIX   553   567  15      
HELIX   573   585  13      
Sequence information
Length: 589 AA [This is the length of the unprocessed precursor] Molecular weight: 65309 Da [This is the MW of the unprocessed precursor] CRC64: 5174EBE94D537836 [This is a checksum on the sequence]
        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 VIMSQILPCI 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 

P30153 in FASTA format

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