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Q00005

- 2ABB_HUMAN

UniProt

Q00005 - 2ABB_HUMAN

Protein

Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform

Gene

PPP2R2B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    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. Within the PP2A holoenzyme complex, isoform 2 is required to promote proapoptotic activity By similarity. Isoform 2 regulates neuronal survival through the mitochondrial fission and fusion balance By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein phosphatase type 2A regulator activity Source: ProtInc

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. regulation of catalytic activity Source: GOC
    3. signal transduction Source: InterPro

    Keywords - Biological processi

    Apoptosis

    Enzyme and pathway databases

    SignaLinkiQ00005.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
    Alternative name(s):
    PP2A subunit B isoform B55-beta
    PP2A subunit B isoform PR55-beta
    PP2A subunit B isoform R2-beta
    PP2A subunit B isoform beta
    Gene namesi
    Name:PPP2R2B
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:9305. PPP2R2B.

    Subcellular locationi

    Isoform 1 : Cytoplasm By similarity. Cytoplasmcytoskeleton By similarity. Membrane By similarity
    Isoform 2 : Cytoplasm By similarity. Mitochondrion By similarity. Mitochondrion outer membrane By similarity
    Note: Under basal conditions, localizes to both cytosolic and mitochondrial compartments. Relocalizes from the cytosolic to the mitochondrial compartment during apoptosis. Its targeting to the outer mitochondrial membrane (OMM) involves an association with import receptors of the TOM complex and is required to promote proapoptotic activity By similarity.By similarity

    GO - Cellular componenti

    1. cytoskeleton Source: UniProtKB-SubCell
    2. mitochondrial outer membrane Source: UniProtKB
    3. mitochondrion Source: UniProtKB
    4. protein phosphatase type 2A complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Membrane, Mitochondrion, Mitochondrion outer membrane

    Pathology & Biotechi

    Involvement in diseasei

    Spinocerebellar ataxia 12 (SCA12) [MIM:604326]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA12 is an autosomal dominant cerebellar ataxia (ADCA).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Neurodegeneration, Spinocerebellar ataxia

    Organism-specific databases

    MIMi604326. phenotype.
    Orphaneti98762. Spinocerebellar ataxia type 12.
    PharmGKBiPA33669.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 443443Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoformPRO_0000071421Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei275 – 2751PhosphoserineBy similarity
    Modified residuei295 – 2951PhosphotyrosineBy similarity
    Modified residuei298 – 2981PhosphothreonineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ00005.
    PRIDEiQ00005.

    PTM databases

    PhosphoSiteiQ00005.

    Expressioni

    Tissue specificityi

    Brain.

    Gene expression databases

    ArrayExpressiQ00005.
    BgeeiQ00005.
    CleanExiHS_PPP2R2B.
    GenevestigatoriQ00005.

    Organism-specific databases

    HPAiHPA038118.

    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.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PDPK1O155308EBI-1052159,EBI-717097
    PPP2R1AP301535EBI-1052159,EBI-302388
    RPS6KB1P234432EBI-1052159,EBI-1775921

    Protein-protein interaction databases

    BioGridi111513. 45 interactions.
    IntActiQ00005. 167 interactions.
    MINTiMINT-6631022.
    STRINGi9606.ENSP00000336591.

    Structurei

    3D structure databases

    ProteinModelPortaliQ00005.
    SMRiQ00005. Positions 23-442.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati22 – 6140WD 1Add
    BLAST
    Repeati87 – 12842WD 2Add
    BLAST
    Repeati171 – 20939WD 3Add
    BLAST
    Repeati220 – 26041WD 4Add
    BLAST
    Repeati279 – 31739WD 5Add
    BLAST
    Repeati334 – 37542WD 6Add
    BLAST
    Repeati410 – 44233WD 7Add
    BLAST

    Domaini

    The N-terminal 26 residues of isoform 2 constitute a cryptic mitochondrial matrix import signal with critical basic and hydrophobic residues, that is necessary and sufficient for targeting the PP2A holoenzyme to the outer mitochondrial membrane (OMM) and does not affect holoenzyme formation or catalytic activity.By similarity
    The last WD repeat of isoform 2 constitutes a mitochondrial stop-transfer domain that confers resistance to the unfolding step process required for import and therefore prevents PPP2R2B matrix translocation and signal sequence cleavage.By similarity

    Sequence similaritiesi

    Contains 7 WD repeats.Curated

    Keywords - Domaini

    Repeat, WD repeat

    Phylogenomic databases

    eggNOGiCOG5170.
    HOVERGENiHBG000012.
    InParanoidiQ00005.
    KOiK04354.
    OMAiRLRDPSM.
    OrthoDBiEOG7Q5HCZ.
    PhylomeDBiQ00005.
    TreeFamiTF105553.

    Family and domain databases

    Gene3Di2.130.10.10. 3 hits.
    InterProiIPR000009. PP2A_PR55.
    IPR018067. PP2A_PR55_CS.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view]
    PANTHERiPTHR11871. PTHR11871. 1 hit.
    PIRSFiPIRSF037309. PP2A_PR55. 1 hit.
    PRINTSiPR00600. PP2APR55.
    SMARTiSM00320. WD40. 6 hits.
    [Graphical view]
    SUPFAMiSSF50978. SSF50978. 3 hits.
    PROSITEiPS01024. PR55_1. 1 hit.
    PS01025. PR55_2. 1 hit.
    PS00678. WD_REPEATS_1. 1 hit.
    [Graphical view]

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q00005-1) [UniParc]FASTAAdd to Basket

    Also known as: Bbeta, Bbeta1

    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

    MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI    50
    FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ 100
    QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV 150
    PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN 200
    FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC 250
    DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD 300
    YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD 350
    SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR 400
    KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN 443

    Note: Conserved additional ATG codons are found 5' of the putative initiator codon in transcripts supporting isoform 1. They may initiate the translation of upstream short open reading frames altering the expression of that isoform as described in PubMed:1849734.

    Length:443
    Mass (Da):51,710
    Last modified:April 1, 1993 - v1
    Checksum:iC383C834B2852B8F
    GO
    Isoform 2 (identifier: Q00005-2) [UniParc]FASTAAdd to Basket

    Also known as: Bbeta2

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MEEDIDTRKINNSFLRDHSYA → MKCFSRYLPYIFRPPNTILSSSCH

    Note: Contains a cryptic mitochondrial transit peptide at positions 1-26.By similarity

    Show »
    Length:446
    Mass (Da):52,017
    Checksum:iD5BDD8D10F79CF0B
    GO
    Isoform 3 (identifier: Q00005-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-21: MEEDIDTRKINNSFLRDHSYA → MIPGIGTLTQDTLWCFSQVKGTIEIGT

    Show »
    Length:449
    Mass (Da):52,066
    Checksum:i6773D04E733403B1
    GO
    Isoform 4 (identifier: Q00005-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVLQPSERHYRDWNHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLSM

    Show »
    Length:501
    Mass (Da):58,171
    Checksum:i3FE3DD278143364A
    GO
    Isoform 5 (identifier: Q00005-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLLSLPALHLQTSEHHPFFQLPHRRLGPWCSPTGSPAPLSCETGCGEGSWILVCRLLVPTQVSLLSM

    Show »
    Length:509
    Mass (Da):58,897
    Checksum:iD47AFC5DD1629FDB
    GO
    Isoform 6 (identifier: Q00005-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-23: MEEDIDTRKINNSFLRDHSYATE → MNYPDENTYGNK

    Show »
    Length:432
    Mass (Da):50,371
    Checksum:iB63F511DEF9670CA
    GO
    Isoform 7 (identifier: Q00005-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MHQPPPASCS...VPTQVSLLSM

    Note: No experimental confirmation available.

    Show »
    Length:549
    Mass (Da):62,505
    Checksum:iDFACDC3C235450D7
    GO

    Sequence cautioni

    The sequence AAH31790.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG51642.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAG51642.1 differs from that shown. Reason: Erroneous termination at position 116. Translated as Lys.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti22 – 221T → A in BAH11838. (PubMed:14702039)Curated
    Sequence conflicti62 – 621H → N in BI669304. (PubMed:15489334)Curated
    Sequence conflicti109 – 1091S → F in BAH12040. (PubMed:14702039)Curated
    Sequence conflicti163 – 1631T → S in BI490027. 1 PublicationCurated
    Sequence conflicti164 – 1641P → S in BAF82406. (PubMed:14702039)Curated
    Sequence conflicti292 – 2921S → R in BAH12040. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361G → V.
    Corresponds to variant rs11547494 [ dbSNP | Ensembl ].
    VAR_051738

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2323MEEDI…SYATE → MNYPDENTYGNK in isoform 6. 1 PublicationVSP_044923Add
    BLAST
    Alternative sequencei1 – 2121MEEDI…DHSYA → MKCFSRYLPYIFRPPNTILS SSCH in isoform 2. 1 PublicationVSP_037976Add
    BLAST
    Alternative sequencei1 – 2121MEEDI…DHSYA → MIPGIGTLTQDTLWCFSQVK GTIEIGT in isoform 3. 1 PublicationVSP_037977Add
    BLAST
    Alternative sequencei1 – 11M → MVLQPSERHYRDWNHRRLGP WCSPTGSPAPLSCETGCGEG SWILVCRLLVPTQVSLLSM in isoform 4. 1 PublicationVSP_037978
    Alternative sequencei1 – 11M → MLLSLPALHLQTSEHHPFFQ LPHRRLGPWCSPTGSPAPLS CETGCGEGSWILVCRLLVPT QVSLLSM in isoform 5. 1 PublicationVSP_037979
    Alternative sequencei1 – 11M → MHQPPPASCSSSSSSSSSSC ECARVGVRVSALAPAAAPCP APRQLPYPRLPEPPSRGTST LIPARLGPWCSPTGSPAPLS CETGCGEGSWILVCRLLVPT QVSLLSM in isoform 7. 1 PublicationVSP_045748

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64930 mRNA. Translation: AAA36493.1.
    AK056192 mRNA. Translation: BAG51642.1. Sequence problems.
    AK289717 mRNA. Translation: BAF82406.1.
    AK294659 mRNA. Translation: BAH11838.1.
    AK295347 mRNA. Translation: BAH12040.1.
    AC008728 Genomic DNA. No translation available.
    AC009186 Genomic DNA. No translation available.
    AC010251 Genomic DNA. No translation available.
    AC011386 Genomic DNA. No translation available.
    AC011357 Genomic DNA. No translation available.
    AC091919 Genomic DNA. No translation available.
    AC091924 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61829.1.
    CH471062 Genomic DNA. Translation: EAW61831.1.
    CH471062 Genomic DNA. Translation: EAW61832.1.
    CH471062 Genomic DNA. Translation: EAW61833.1.
    CH471062 Genomic DNA. Translation: EAW61834.1.
    CH471062 Genomic DNA. Translation: EAW61835.1.
    BC031790 mRNA. Translation: AAH31790.1. Different initiation.
    BI490027 mRNA. No translation available.
    BI669304 mRNA. No translation available.
    CCDSiCCDS4283.1. [Q00005-2]
    CCDS4284.2. [Q00005-5]
    CCDS43380.1. [Q00005-6]
    CCDS64281.1. [Q00005-4]
    CCDS64282.1. [Q00005-3]
    PIRiB38351.
    RefSeqiNP_001258828.1. NM_001271899.1. [Q00005-3]
    NP_001258829.1. NM_001271900.1. [Q00005-4]
    NP_001258877.1. NM_001271948.1. [Q00005-6]
    NP_858060.2. NM_181674.2. [Q00005-5]
    NP_858061.2. NM_181675.3. [Q00005-7]
    NP_858062.1. NM_181676.2. [Q00005-2]
    NP_858063.1. NM_181677.2.
    NP_858064.1. NM_181678.2. [Q00005-6]
    UniGeneiHs.627618.
    Hs.655213.

    Genome annotation databases

    EnsembliENST00000336640; ENSP00000336591; ENSG00000156475. [Q00005-2]
    ENST00000394409; ENSP00000377931; ENSG00000156475. [Q00005-4]
    ENST00000394411; ENSP00000377933; ENSG00000156475. [Q00005-1]
    ENST00000394413; ENSP00000377935; ENSG00000156475. [Q00005-1]
    ENST00000394414; ENSP00000377936; ENSG00000156475. [Q00005-5]
    ENST00000453001; ENSP00000398779; ENSG00000156475. [Q00005-1]
    ENST00000504198; ENSP00000421396; ENSG00000156475. [Q00005-3]
    ENST00000508545; ENSP00000431320; ENSG00000156475. [Q00005-6]
    GeneIDi5521.
    KEGGihsa:5521.
    UCSCiuc003loe.4. human. [Q00005-1]
    uc003log.5. human. [Q00005-4]
    uc003loh.5. human. [Q00005-5]
    uc003loi.5. human. [Q00005-2]
    uc003lok.5. human.
    uc011dbu.3. human. [Q00005-3]

    Polymorphism databases

    DMDMi231446.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64930 mRNA. Translation: AAA36493.1 .
    AK056192 mRNA. Translation: BAG51642.1 . Sequence problems.
    AK289717 mRNA. Translation: BAF82406.1 .
    AK294659 mRNA. Translation: BAH11838.1 .
    AK295347 mRNA. Translation: BAH12040.1 .
    AC008728 Genomic DNA. No translation available.
    AC009186 Genomic DNA. No translation available.
    AC010251 Genomic DNA. No translation available.
    AC011386 Genomic DNA. No translation available.
    AC011357 Genomic DNA. No translation available.
    AC091919 Genomic DNA. No translation available.
    AC091924 Genomic DNA. No translation available.
    CH471062 Genomic DNA. Translation: EAW61829.1 .
    CH471062 Genomic DNA. Translation: EAW61831.1 .
    CH471062 Genomic DNA. Translation: EAW61832.1 .
    CH471062 Genomic DNA. Translation: EAW61833.1 .
    CH471062 Genomic DNA. Translation: EAW61834.1 .
    CH471062 Genomic DNA. Translation: EAW61835.1 .
    BC031790 mRNA. Translation: AAH31790.1 . Different initiation.
    BI490027 mRNA. No translation available.
    BI669304 mRNA. No translation available.
    CCDSi CCDS4283.1. [Q00005-2 ]
    CCDS4284.2. [Q00005-5 ]
    CCDS43380.1. [Q00005-6 ]
    CCDS64281.1. [Q00005-4 ]
    CCDS64282.1. [Q00005-3 ]
    PIRi B38351.
    RefSeqi NP_001258828.1. NM_001271899.1. [Q00005-3 ]
    NP_001258829.1. NM_001271900.1. [Q00005-4 ]
    NP_001258877.1. NM_001271948.1. [Q00005-6 ]
    NP_858060.2. NM_181674.2. [Q00005-5 ]
    NP_858061.2. NM_181675.3. [Q00005-7 ]
    NP_858062.1. NM_181676.2. [Q00005-2 ]
    NP_858063.1. NM_181677.2.
    NP_858064.1. NM_181678.2. [Q00005-6 ]
    UniGenei Hs.627618.
    Hs.655213.

    3D structure databases

    ProteinModelPortali Q00005.
    SMRi Q00005. Positions 23-442.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111513. 45 interactions.
    IntActi Q00005. 167 interactions.
    MINTi MINT-6631022.
    STRINGi 9606.ENSP00000336591.

    PTM databases

    PhosphoSitei Q00005.

    Polymorphism databases

    DMDMi 231446.

    Proteomic databases

    PaxDbi Q00005.
    PRIDEi Q00005.

    Protocols and materials databases

    DNASUi 5521.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000336640 ; ENSP00000336591 ; ENSG00000156475 . [Q00005-2 ]
    ENST00000394409 ; ENSP00000377931 ; ENSG00000156475 . [Q00005-4 ]
    ENST00000394411 ; ENSP00000377933 ; ENSG00000156475 . [Q00005-1 ]
    ENST00000394413 ; ENSP00000377935 ; ENSG00000156475 . [Q00005-1 ]
    ENST00000394414 ; ENSP00000377936 ; ENSG00000156475 . [Q00005-5 ]
    ENST00000453001 ; ENSP00000398779 ; ENSG00000156475 . [Q00005-1 ]
    ENST00000504198 ; ENSP00000421396 ; ENSG00000156475 . [Q00005-3 ]
    ENST00000508545 ; ENSP00000431320 ; ENSG00000156475 . [Q00005-6 ]
    GeneIDi 5521.
    KEGGi hsa:5521.
    UCSCi uc003loe.4. human. [Q00005-1 ]
    uc003log.5. human. [Q00005-4 ]
    uc003loh.5. human. [Q00005-5 ]
    uc003loi.5. human. [Q00005-2 ]
    uc003lok.5. human.
    uc011dbu.3. human. [Q00005-3 ]

    Organism-specific databases

    CTDi 5521.
    GeneCardsi GC05M145969.
    GeneReviewsi PPP2R2B.
    HGNCi HGNC:9305. PPP2R2B.
    HPAi HPA038118.
    MIMi 604325. gene.
    604326. phenotype.
    neXtProti NX_Q00005.
    Orphaneti 98762. Spinocerebellar ataxia type 12.
    PharmGKBi PA33669.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5170.
    HOVERGENi HBG000012.
    InParanoidi Q00005.
    KOi K04354.
    OMAi RLRDPSM.
    OrthoDBi EOG7Q5HCZ.
    PhylomeDBi Q00005.
    TreeFami TF105553.

    Enzyme and pathway databases

    SignaLinki Q00005.

    Miscellaneous databases

    ChiTaRSi PPP2R2B. human.
    GeneWikii PPP2R2B.
    GenomeRNAii 5521.
    NextBioi 21356.
    PROi Q00005.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q00005.
    Bgeei Q00005.
    CleanExi HS_PPP2R2B.
    Genevestigatori Q00005.

    Family and domain databases

    Gene3Di 2.130.10.10. 3 hits.
    InterProi IPR000009. PP2A_PR55.
    IPR018067. PP2A_PR55_CS.
    IPR015943. WD40/YVTN_repeat-like_dom.
    IPR001680. WD40_repeat.
    IPR019775. WD40_repeat_CS.
    IPR017986. WD40_repeat_dom.
    [Graphical view ]
    PANTHERi PTHR11871. PTHR11871. 1 hit.
    PIRSFi PIRSF037309. PP2A_PR55. 1 hit.
    PRINTSi PR00600. PP2APR55.
    SMARTi SM00320. WD40. 6 hits.
    [Graphical view ]
    SUPFAMi SSF50978. SSF50978. 3 hits.
    PROSITEi PS01024. PR55_1. 1 hit.
    PS01025. PR55_2. 1 hit.
    PS00678. WD_REPEATS_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the 55-kDa regulatory subunit of protein phosphatase 2A: evidence for a neuronal-specific isoform."
      Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., Merlevede W., Hofsteenge J., Hemmings B.A.
      Biochemistry 30:3589-3597(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal brain.
    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.
      , 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; 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-433 (ISOFORM 7).
      Tissue: Brain and Corpus callosum.
    3. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. 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 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-131 (ISOFORM 6).
      Tissue: Brain and Hypothalamus.
    6. Strausberg R.L.
      Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-197 (ISOFORM 2).
    7. Cited for: INVOLVEMENT IN SCA12.

    Entry informationi

    Entry namei2ABB_HUMAN
    AccessioniPrimary (citable) accession number: Q00005
    Secondary accession number(s): A6NEJ2
    , A8K102, B3KPD0, B7Z2F2, B7Z304, D3DQF7, D3DQF8, G3V149
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 151 of the entry and version 1 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 5
      Human chromosome 5: 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