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P30154

- 2AAB_HUMAN

UniProt

P30154 - 2AAB_HUMAN

Protein

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

Gene

PPP2R1B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    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.

    GO - Molecular functioni

    1. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process involved in morphogenesis Source: UniProtKB
    2. positive regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_12436. ERKs are inactivated.
    REACT_12599. ERK/MAPK targets.
    REACT_1383. Glycolysis.
    REACT_150182. MASTL Facilitates Mitotic Progression.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_1505. Integration of energy metabolism.
    REACT_15334. DARPP-32 events.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_23879. Platelet sensitization by LDL.
    REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_682. Mitotic Prometaphase.
    REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
    REACT_821. Cyclin D associated events in G1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
    Alternative name(s):
    PP2A subunit A isoform PR65-beta
    PP2A subunit A isoform R1-beta
    Gene namesi
    Name:PPP2R1B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:9303. PPP2R1B.

    Subcellular locationi

    GO - Cellular componenti

    1. membrane raft Source: UniProtKB

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA33667.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 601600Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoformPRO_0000071403Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30154.
    PaxDbiP30154.
    PRIDEiP30154.

    PTM databases

    PhosphoSiteiP30154.

    Expressioni

    Gene expression databases

    ArrayExpressiP30154.
    BgeeiP30154.
    CleanExiHS_PPP2R1B.
    GenevestigatoriP30154.

    Organism-specific databases

    HPAiCAB004034.
    HPA018908.

    Interactioni

    Subunit structurei

    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. Interacts with SGOL1. Interacts with RAF1.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ClockO087852EBI-357094,EBI-79859From a different organism.
    PPP2CAP677757EBI-357094,EBI-712311
    PPP2R2AP631512EBI-357094,EBI-1048931
    PPP2R5AQ151722EBI-357094,EBI-641666
    PPP2R5CQ133622EBI-357094,EBI-1266156
    PPP2R5DQ147382EBI-357094,EBI-396563
    PPP2R5EQ165373EBI-357094,EBI-968374
    RALAP112336EBI-357094,EBI-1036803
    Unc5bO087224EBI-357094,EBI-4404185From a different organism.

    Protein-protein interaction databases

    BioGridi111511. 56 interactions.
    IntActiP30154. 64 interactions.
    MINTiMINT-1150161.
    STRINGi9606.ENSP00000311344.

    Structurei

    3D structure databases

    ProteinModelPortaliP30154.
    SMRiP30154. Positions 19-601.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati20 – 5839HEAT 1Add
    BLAST
    Repeati59 – 9638HEAT 2Add
    BLAST
    Repeati97 – 13539HEAT 3Add
    BLAST
    Repeati136 – 17338HEAT 4Add
    BLAST
    Repeati174 – 21239HEAT 5Add
    BLAST
    Repeati213 – 25139HEAT 6Add
    BLAST
    Repeati252 – 29039HEAT 7Add
    BLAST
    Repeati291 – 33343HEAT 8Add
    BLAST
    Repeati334 – 37239HEAT 9Add
    BLAST
    Repeati373 – 41139HEAT 10Add
    BLAST
    Repeati412 – 45039HEAT 11Add
    BLAST
    Repeati451 – 48939HEAT 12Add
    BLAST
    Repeati490 – 52839HEAT 13Add
    BLAST
    Repeati529 – 56739HEAT 14Add
    BLAST
    Repeati568 – 60134HEAT 15Add
    BLAST

    Domaini

    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 similaritiesi

    Contains 15 HEAT repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG247268.
    HOGENOMiHOG000078539.
    HOVERGENiHBG000011.
    KOiK03456.
    OMAiNREQIIM.
    OrthoDBiEOG764722.
    PhylomeDBiP30154.
    TreeFamiTF105552.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000357. HEAT.
    IPR021133. HEAT_type_2.
    [Graphical view]
    PfamiPF02985. HEAT. 2 hits.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50077. HEAT_REPEAT. 12 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P30154-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAGASELGTG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI    50
    ALALGVERTR SELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC 100
    LLPPLENLAT VEETVVRDKA VESLRQISQE HTPVALEAYF VPLVKRLASG 150
    DWFTSRTSAC GLFSVCYPRA SNAVKAEIRQ QFRSLCSDDT PMVRRAAASK 200
    LGEFAKVLEL DSVKSEIVPL FTSLASDEQD SVRLLAVEAC VSIAQLLSQD 250
    DLETLVMPTL RQAAEDKSWR VRYMVADRFS ELQKAMGPKI TLNDLIPAFQ 300
    NLLKDCEAEV RAAAAHKVKE LGENLPIEDR ETIIMNQILP YIKELVSDTN 350
    QHVKSALASV IMGLSTILGK ENTIEHLLPL FLAQLKDECP DVRLNIISNL 400
    DCVNEVIGIR QLSQSLLPAI VELAEDAKWR VRLAIIEYMP LLAGQLGVEF 450
    FDEKLNSLCM AWLVDHVYAI REAATNNLMK LVQKFGTEWA QNTIVPKVLV 500
    MANDPNYLHR MTTLFCINAL SEACGQEITT KQMLPIVLKM AGDQVANVRF 550
    NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL 600
    A 601
    Length:601
    Mass (Da):66,214
    Last modified:October 17, 2006 - v3
    Checksum:i86AB20D7505210B0
    GO
    Isoform 2 (identifier: P30154-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD

    Show »
    Length:667
    Mass (Da):73,585
    Checksum:i726EA8A8FB0DEB23
    GO
    Isoform 3 (identifier: P30154-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         39-102: Missing.
         598-601: LALA → VAQRLRKLEFPVKDSGEPSVPRADKNHFPRPTVPGEDMGKGPVYQLRGDTRDTLAQLGIAELVHFSQSTD

    Note: No experimental confirmation available.

    Show »
    Length:603
    Mass (Da):66,617
    Checksum:i3FB011FD47C65810
    GO
    Isoform 4 (identifier: P30154-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         344-388: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:556
    Mass (Da):61,314
    Checksum:i1FFAFBC9A8C38FA2
    GO
    Isoform 5 (identifier: P30154-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         103-229: Missing.

    Show »
    Length:474
    Mass (Da):52,214
    Checksum:i6F8EEB7D9779BFB1
    GO

    Sequence cautioni

    The sequence AAA59983.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence BAG59103.1 differs from that shown. Reason: Frameshift at position 540.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741E → V in AAA59983. (PubMed:2159327)Curated
    Sequence conflicti178 – 1781I → T in AAC63525. (PubMed:9795170)Curated
    Sequence conflicti178 – 1781I → T in AAG39644. (PubMed:11313745)Curated
    Sequence conflicti178 – 1781I → T in AAA59983. (PubMed:2159327)Curated
    Sequence conflicti211 – 2111D → G in BAG57867. (PubMed:14702039)Curated
    Sequence conflicti411 – 4111Q → R in AAA59983. (PubMed:2159327)Curated
    Sequence conflicti503 – 5031N → S in BAG57867. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti8 – 81G → R in a lung cancer patient. 1 Publication
    Corresponds to variant rs142771326 [ dbSNP | Ensembl ].
    VAR_022895
    Natural varianti15 – 151G → A in a colorectal cancer patient. 1 Publication
    VAR_022896
    Natural varianti65 – 651P → S in a lung cancer patient. 1 Publication
    VAR_022897
    Natural varianti90 – 901G → D in a lung cancer patient. 3 Publications
    Corresponds to variant rs1805076 [ dbSNP | Ensembl ].
    VAR_006384
    Natural varianti101 – 1011L → P in a colon adenocarcinoma. 1 Publication
    VAR_022898
    Natural varianti343 – 3431K → E in a lung cancer patient. 1 Publication
    VAR_022899
    Natural varianti365 – 3651S → P in a colorectal cancer patient. 1 Publication
    VAR_022900
    Natural varianti448 – 4481V → A in a colon adenocarcinoma. 1 Publication
    VAR_022901
    Natural varianti498 – 4981V → E in a colorectal cancer patient. 1 Publication
    VAR_022902
    Natural varianti499 – 4991L → I in a colorectal cancer patient. 1 Publication
    VAR_022903
    Natural varianti500 – 5001V → G in a colorectal cancer patient. 1 Publication
    VAR_022904
    Natural varianti504 – 5041D → G in a lung cancer patient. 1 Publication
    VAR_022905
    Natural varianti545 – 5451V → A in a colon adenocarcinoma. 1 Publication
    VAR_022906

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei39 – 10264Missing in isoform 3. 1 PublicationVSP_043379Add
    BLAST
    Alternative sequencei103 – 229127Missing in isoform 5. 1 PublicationVSP_046684Add
    BLAST
    Alternative sequencei344 – 38845Missing in isoform 4. 1 PublicationVSP_045275Add
    BLAST
    Alternative sequencei598 – 6014LALA → VAQRLRKLEFPVKDSGEPSV PRADKNHFPRPTVPGEDMGK GPVYQLRGDTRDTLAQLGIA ELVHFSQSTD in isoform 2 and isoform 3. 2 PublicationsVSP_036460

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF083439
    , AF083425, AF083426, AF083427, AF083428, AF083429, AF083430, AF083431, AF083432, AF083433, AF083434, AF083435, AF083436, AF083437, AF083438 Genomic DNA. Translation: AAC63525.1.
    AF087438 mRNA. Translation: AAC69624.1.
    AF163473 mRNA. Translation: AAG39644.1.
    AK294716 mRNA. Translation: BAG57867.1.
    AK296455 mRNA. Translation: BAG59103.1. Frameshift.
    AK301705 mRNA. Translation: BAG63177.1.
    EF445011 Genomic DNA. Translation: ACA06046.1.
    EF445011 Genomic DNA. Translation: ACA06047.1.
    AP000925 Genomic DNA. No translation available.
    AP001781 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67150.1.
    CH471065 Genomic DNA. Translation: EAW67151.1.
    BC027596 mRNA. Translation: AAH27596.1.
    M65254 mRNA. Translation: AAA59983.1. Sequence problems.
    CCDSiCCDS53706.1. [P30154-3]
    CCDS53707.1. [P30154-5]
    CCDS53708.1. [P30154-4]
    CCDS8348.1. [P30154-2]
    CCDS8349.1. [P30154-1]
    PIRiB34541.
    RefSeqiNP_001171033.1. NM_001177562.1. [P30154-4]
    NP_001171034.1. NM_001177563.1. [P30154-5]
    NP_002707.3. NM_002716.4. [P30154-1]
    NP_859050.1. NM_181699.2. [P30154-2]
    NP_859051.1. NM_181700.1. [P30154-3]
    UniGeneiHs.269128.
    Hs.584790.

    Genome annotation databases

    EnsembliENST00000311129; ENSP00000311344; ENSG00000137713. [P30154-2]
    ENST00000341980; ENSP00000343317; ENSG00000137713. [P30154-4]
    ENST00000393055; ENSP00000376775; ENSG00000137713. [P30154-5]
    ENST00000426998; ENSP00000410671; ENSG00000137713. [P30154-3]
    ENST00000527614; ENSP00000437193; ENSG00000137713. [P30154-1]
    GeneIDi5519.
    KEGGihsa:5519.
    UCSCiuc001plw.1. human. [P30154-2]
    uc001plx.1. human. [P30154-1]
    uc010rwi.1. human. [P30154-3]

    Polymorphism databases

    DMDMi116241236.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF083439
    , AF083425 , AF083426 , AF083427 , AF083428 , AF083429 , AF083430 , AF083431 , AF083432 , AF083433 , AF083434 , AF083435 , AF083436 , AF083437 , AF083438 Genomic DNA. Translation: AAC63525.1 .
    AF087438 mRNA. Translation: AAC69624.1 .
    AF163473 mRNA. Translation: AAG39644.1 .
    AK294716 mRNA. Translation: BAG57867.1 .
    AK296455 mRNA. Translation: BAG59103.1 . Frameshift.
    AK301705 mRNA. Translation: BAG63177.1 .
    EF445011 Genomic DNA. Translation: ACA06046.1 .
    EF445011 Genomic DNA. Translation: ACA06047.1 .
    AP000925 Genomic DNA. No translation available.
    AP001781 Genomic DNA. No translation available.
    CH471065 Genomic DNA. Translation: EAW67150.1 .
    CH471065 Genomic DNA. Translation: EAW67151.1 .
    BC027596 mRNA. Translation: AAH27596.1 .
    M65254 mRNA. Translation: AAA59983.1 . Sequence problems.
    CCDSi CCDS53706.1. [P30154-3 ]
    CCDS53707.1. [P30154-5 ]
    CCDS53708.1. [P30154-4 ]
    CCDS8348.1. [P30154-2 ]
    CCDS8349.1. [P30154-1 ]
    PIRi B34541.
    RefSeqi NP_001171033.1. NM_001177562.1. [P30154-4 ]
    NP_001171034.1. NM_001177563.1. [P30154-5 ]
    NP_002707.3. NM_002716.4. [P30154-1 ]
    NP_859050.1. NM_181699.2. [P30154-2 ]
    NP_859051.1. NM_181700.1. [P30154-3 ]
    UniGenei Hs.269128.
    Hs.584790.

    3D structure databases

    ProteinModelPortali P30154.
    SMRi P30154. Positions 19-601.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111511. 56 interactions.
    IntActi P30154. 64 interactions.
    MINTi MINT-1150161.
    STRINGi 9606.ENSP00000311344.

    PTM databases

    PhosphoSitei P30154.

    Polymorphism databases

    DMDMi 116241236.

    Proteomic databases

    MaxQBi P30154.
    PaxDbi P30154.
    PRIDEi P30154.

    Protocols and materials databases

    DNASUi 5519.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000311129 ; ENSP00000311344 ; ENSG00000137713 . [P30154-2 ]
    ENST00000341980 ; ENSP00000343317 ; ENSG00000137713 . [P30154-4 ]
    ENST00000393055 ; ENSP00000376775 ; ENSG00000137713 . [P30154-5 ]
    ENST00000426998 ; ENSP00000410671 ; ENSG00000137713 . [P30154-3 ]
    ENST00000527614 ; ENSP00000437193 ; ENSG00000137713 . [P30154-1 ]
    GeneIDi 5519.
    KEGGi hsa:5519.
    UCSCi uc001plw.1. human. [P30154-2 ]
    uc001plx.1. human. [P30154-1 ]
    uc010rwi.1. human. [P30154-3 ]

    Organism-specific databases

    CTDi 5519.
    GeneCardsi GC11M111642.
    HGNCi HGNC:9303. PPP2R1B.
    HPAi CAB004034.
    HPA018908.
    MIMi 603113. gene.
    neXtProti NX_P30154.
    PharmGKBi PA33667.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247268.
    HOGENOMi HOG000078539.
    HOVERGENi HBG000011.
    KOi K03456.
    OMAi NREQIIM.
    OrthoDBi EOG764722.
    PhylomeDBi P30154.
    TreeFami TF105552.

    Enzyme and pathway databases

    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_12436. ERKs are inactivated.
    REACT_12599. ERK/MAPK targets.
    REACT_1383. Glycolysis.
    REACT_150182. MASTL Facilitates Mitotic Progression.
    REACT_150425. Resolution of Sister Chromatid Cohesion.
    REACT_150471. Separation of Sister Chromatids.
    REACT_1505. Integration of energy metabolism.
    REACT_15334. DARPP-32 events.
    REACT_1857. Cyclin A/B1 associated events during G2/M transition.
    REACT_19405. CTLA4 inhibitory signaling.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.
    REACT_23879. Platelet sensitization by LDL.
    REACT_329. Inhibition of replication initiation of damaged DNA by RB1/E2F1.
    REACT_682. Mitotic Prometaphase.
    REACT_705. PP2A-mediated dephosphorylation of key metabolic factors.
    REACT_821. Cyclin D associated events in G1.

    Miscellaneous databases

    ChiTaRSi PPP2R1B. human.
    GeneWikii PPP2R1B.
    GenomeRNAii 5519.
    NextBioi 21346.
    PROi P30154.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30154.
    Bgeei P30154.
    CleanExi HS_PPP2R1B.
    Genevestigatori P30154.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000357. HEAT.
    IPR021133. HEAT_type_2.
    [Graphical view ]
    Pfami PF02985. HEAT. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50077. HEAT_REPEAT. 12 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic organization and precise physical location of protein phosphatase 2A regulatory subunit A beta isoform gene on chromosome band 11q23."
      Baysal B.E., Farr J.E., Goss J.R., Devlin B., Richard C.W. III
      Gene 217:107-116(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Alterations of the PPP2R1B gene in human lung and colon cancer."
      Wang S.S., Esplin E.D., Li J.L., Huang L., Gazdar A., Minna J., Evans G.A.
      Science 282:284-287(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ARG-8; SER-65; ASP-90; PRO-101; GLU-343; ALA-448; GLY-504 AND ALA-545.
    3. "A high-resolution integrated map spanning the SDHD gene at 11q23: a 1.1-Mb BAC contig, a partial transcript map and 15 new repeat polymorphisms in a tumour-suppressor region."
      Baysal B.E., Willett-Brozick J.E., Taschner P.E.M., Dauwerse J.G., Devilee P., Devlin B.
      Eur. J. Hum. Genet. 9:121-129(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "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.
      , 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 3; 4 AND 5).
      Tissue: Brain, Testis and Thalamus.
    5. NHLBI resequencing and genotyping service (RS&G)
      Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 2).
      Tissue: Testis.
    9. "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase 2A have a similar 39 amino acid repeating structure."
      Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., Merlevede W., Hofsteenge J., Stone S.R.
      Biochemistry 29:3166-3173(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 31-601 (ISOFORM 1).
    10. "Raf-1-associated protein phosphatase 2A as a positive regulator of kinase activation."
      Abraham D., Podar K., Pacher M., Kubicek M., Welzel N., Hemmings B.A., Dilworth S.M., Mischak H., Kolch W., Baccarini M.
      J. Biol. Chem. 275:22300-22304(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAF1.
    11. "Interaction between protein phosphatase 2A and members of the importin beta superfamily."
      Lubert E.J., Sarge K.D.
      Biochem. Biophys. Res. Commun. 303:908-913(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IPO9.
    12. "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: INTERACTION WITH SGOL1.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    15. "Absence of PPP2R1B gene alterations in primary ovarian cancers."
      Campbell I.G., Manolitsas T.
      Oncogene 18:6367-6369(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-90.
    16. "Alterations of the PPP2R1B gene located at 11q23 in human colorectal cancers."
      Takagi Y., Futamura M., Yamaguchi K., Aoki S., Takahashi T., Saji S.
      Gut 47:268-271(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS ALA-15; PRO-365; GLU-498; ILE-499 AND GLY-500.
    17. "Alterations in the suppressor gene PPP2R1B in parathyroid hyperplasias and adenomas."
      Hemmer S., Wasenius V.M., Haglund C., Zhu Y., Knuutila S., Franssila K., Joensuu H.
      Cancer Genet. Cytogenet. 134:13-17(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ASP-90.

    Entry informationi

    Entry namei2AAB_HUMAN
    AccessioniPrimary (citable) accession number: P30154
    Secondary accession number(s): A8MY67
    , B0YJ69, B4DGQ6, B4DK91, B4DWW5, F8W8G1, O75620, Q8NHV8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 142 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3