Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q15172 (2A5A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
Alternative name(s):
PP2A B subunit isoform B'-alpha
PP2A B subunit isoform B56-alpha
PP2A B subunit isoform PR61-alpha
Short name=PR61alpha
PP2A B subunit isoform R5-alpha
Gene names
Name:PPP2R5A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length486 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment.

Subunit structure

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 SGOL1. Ref.8

Subcellular location

Cytoplasm. Nucleus. Chromosomecentromere. Note: From mitotic prophase to metaphase, localizes at the inner centromere between a pair of sister kinetochores. Decreased expression at the onset of anaphase. Ref.7 Ref.8

Tissue specificity

Widely expressed with the highest expression in heart and skeletal muscle.

Post-translational modification

Phosphorylated on serine residues. Ref.7

Sequence similarities

Belongs to the phosphatase 2A regulatory subunit B56 family.

Ontologies

Keywords
   Cellular componentCentromere
Chromosome
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of establishment of protein localization to plasma membrane

Inferred from mutant phenotype PubMed 21075214. Source: BHF-UCL

negative regulation of lipid kinase activity

Inferred from mutant phenotype PubMed 21075214. Source: BHF-UCL

positive regulation of protein dephosphorylation

Inferred from mutant phenotype PubMed 21075214. Source: BHF-UCL

signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentM band

Inferred from sequence or structural similarity PubMed 18782775. Source: BHF-UCL

Z disc

Inferred from electronic annotation. Source: Ensembl

chromosome, centromeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 21075214. Source: BHF-UCL

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

protein phosphatase type 2A complex

Inferred from direct assay PubMed 17245430. Source: UniProtKB

   Molecular_functionkinase binding

Inferred from physical interaction PubMed 21075214. Source: BHF-UCL

protein binding

Inferred from physical interaction PubMed 9847399. Source: UniProtKB

protein phosphatase type 2A regulator activity

Traceable author statement Ref.7. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q15172-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q15172-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: MSSSSPPAGAASAAISASEKVDGFTRKSVRKAQRQKRSQGSSQFRSQGSQAELHPLPQLKD → MIMN
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.13
Chain2 – 486485Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
PRO_0000071448

Regions

Compositional bias2 – 54Poly-Ser

Amino acid modifications

Modified residue21N-acetylserine Ref.13
Modified residue411Phosphoserine Ref.9 Ref.10 Ref.12
Modified residue421Phosphoserine Ref.9 Ref.10 Ref.12

Natural variations

Alternative sequence1 – 6161MSSSS…PQLKD → MIMN in isoform 2.
VSP_042889

Experimental info

Sequence conflict521E → F AA sequence Ref.6
Sequence conflict541H → S AA sequence Ref.6
Sequence conflict1761Q → R in AAH22474. Ref.5
Sequence conflict3891D → N in AAH22474. Ref.5
Sequence conflict4511R → E AA sequence Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D31407F7032A6D44

FASTA48656,194
        10         20         30         40         50         60 
MSSSSPPAGA ASAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ AELHPLPQLK 

        70         80         90        100        110        120 
DATSNEQQEL FCQKLQQCCI LFDFMDSVSD LKSKEIKRAT LNELVEYVST NRGVIVESAY 

       130        140        150        160        170        180 
SDIVKMISAN IFRTLPPSDN PDFDPEEDEP TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA 

       190        200        210        220        230        240 
KRYIDQKFVQ QLLELFDSED PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET 

       250        260        270        280        290        300 
EHFNGVAELL EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL 

       310        320        330        340        350        360 
EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE PLFKQISKCV 

       370        380        390        400        410        420 
SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY KISKEHWNPT IVALVYNVLK 

       430        440        450        460        470        480 
TLMEMNGKLF DDLTSSYKAE RQREKKKELE REELWKKLEE LKLKKALEKQ NSAYNMHSIL 


SNTSAE 

« Hide

Isoform 2 [UniParc].

Checksum: 8DF4B7962741F179
Show »

FASTA42950,244

References

« Hide 'large scale' references
[1]"Identification of a new family of protein phosphatase 2A regulatory subunits."
McCright B., Virshup D.M.
J. Biol. Chem. 270:26123-26128(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Mammary cancer.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Testis and Tongue.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Hippocampus and Testis.
[6]"The variable subunit associated with protein phosphatase 2A0 defines a novel multimember family of regulatory subunits."
Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., Merlevede W., Goris J., Hemmings B.A.
Biochem. J. 317:187-194(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 47-56; 129-132; 347-354; 448-462 AND 471-480.
Tissue: Brain.
[7]"The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm."
McCright B., Rivers A.M., Audlin S., Virshup D.M.
J. Biol. Chem. 271:22081-22089(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION.
[8]"Shugoshin collaborates with protein phosphatase 2A to protect cohesin."
Kitajima T.S., Sakuno T., Ishiguro K., Iemura S., Natsume T., Kawashima S.A., Watanabe Y.
Nature 441:46-52(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SGOL1.
[9]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-41 AND SER-42, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L42373 mRNA. Translation: AAC37601.1.
AK302202 mRNA. Translation: BAH13648.1.
AK312530 mRNA. Translation: BAG35429.1.
AL451060, AL360091 Genomic DNA. Translation: CAH71821.1.
AL360091, AL451060 Genomic DNA. Translation: CAH73229.1.
CH471100 Genomic DNA. Translation: EAW93392.1.
CH471100 Genomic DNA. Translation: EAW93393.1.
BC022474 mRNA. Translation: AAH22474.1.
BC110883 mRNA. Translation: AAI10884.1.
CCDSCCDS1503.1. [Q15172-1]
CCDS55686.1. [Q15172-2]
PIRI55449.
RefSeqNP_001186685.1. NM_001199756.1. [Q15172-2]
NP_006234.1. NM_006243.3. [Q15172-1]
UniGeneHs.744012.

3D structure databases

ProteinModelPortalQ15172.
SMRQ15172. Positions 66-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111517. 21 interactions.
DIPDIP-459N.
IntActQ15172. 21 interactions.
MINTMINT-88251.
STRING9606.ENSP00000261461.

Chemistry

BindingDBQ15172.
ChEMBLCHEMBL4763.

PTM databases

PhosphoSiteQ15172.

Polymorphism databases

DMDM7387496.

2D gel databases

OGPQ15172.

Proteomic databases

MaxQBQ15172.
PaxDbQ15172.
PeptideAtlasQ15172.
PRIDEQ15172.

Protocols and materials databases

DNASU5525.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261461; ENSP00000261461; ENSG00000066027. [Q15172-1]
ENST00000537030; ENSP00000442866; ENSG00000066027. [Q15172-2]
GeneID5525.
KEGGhsa:5525.
UCSCuc001hjb.3. human. [Q15172-1]
uc010ptd.2. human. [Q15172-2]

Organism-specific databases

CTD5525.
GeneCardsGC01P212458.
HGNCHGNC:9309. PPP2R5A.
MIM601643. gene.
neXtProtNX_Q15172.
PharmGKBPA33672.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG264925.
HOGENOMHOG000067326.
HOVERGENHBG000009.
InParanoidQ15172.
KOK11584.
OMADLFCQKL.
OrthoDBEOG7C2R2S.
PhylomeDBQ15172.
TreeFamTF105556.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_115566. Cell Cycle.
REACT_21300. Mitotic M-M/G1 phases.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkQ15172.

Gene expression databases

BgeeQ15172.
CleanExHS_PPP2R5A.
GenevestigatorQ15172.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR002554. PP2A_B56.
[Graphical view]
PANTHERPTHR10257. PTHR10257. 1 hit.
PfamPF01603. B56. 1 hit.
[Graphical view]
PIRSFPIRSF028043. PP2A_B56. 1 hit.
SUPFAMSSF48371. SSF48371. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPPP2R5A. human.
GeneWikiPPP2R5A.
GenomeRNAi5525.
NextBio21392.
PROQ15172.
SOURCESearch...

Entry information

Entry name2A5A_HUMAN
AccessionPrimary (citable) accession number: Q15172
Secondary accession number(s): B2R6D2 expand/collapse secondary AC list , B7Z7L2, D3DT99, Q2NL72, Q5VVB2, Q8TBI9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM