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Q9NY27

- PP4R2_HUMAN

UniProt

Q9NY27 - PP4R2_HUMAN

Protein

Serine/threonine-protein phosphatase 4 regulatory subunit 2

Gene

PPP4R2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 90 (01 Oct 2014)
      Sequence version 3 (11 Sep 2007)
      Previous versions | rss
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    Functioni

    Regulatory subunit of serine/threonine-protein phosphatase 4 (PP4). May regulate the activity of PPP4C at centrosomal microtubule organizing centers. Its interaction with the SMN complex leads to enhance the temporal localization of snRNPs, suggesting a role of PPP4C in maturation of spliceosomal snRNPs. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AFX phosphorylated on 'Ser-140' (gamma-H2AFX) generated during DNA replication and required for DNA double strand break repair. Mediates RPA2 dephosphorylation by recruiting PPP4C to RPA2 in a DNA damage-dependent manner. RPA2 dephosphorylation is required for the efficient RPA2-mediated recruitment of RAD51 to chromatin following double strand breaks, an essential step for DNA repair.4 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein binding, bridging Source: UniProtKB
    3. protein phosphatase type 4 regulator activity Source: UniProtKB

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. mRNA processing Source: UniProtKB-KW
    3. regulation of catalytic activity Source: GOC
    4. regulation of double-strand break repair via homologous recombination Source: UniProtKB
    5. RNA splicing Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein phosphatase 4 regulatory subunit 2
    Gene namesi
    Name:PPP4R2
    ORF Names:SBBI57
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:18296. PPP4R2.

    Subcellular locationi

    Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Nucleus
    Note: Ionizing radiation induces relocalization to nuclear foci and colocalization with RPA2.

    GO - Cellular componenti

    1. centrosome Source: ProtInc
    2. cytoplasm Source: UniProtKB-KW
    3. nucleus Source: UniProtKB
    4. protein phosphatase 4 complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi99 – 991F → A: No effect on RPA2-binding; decrease in PPP4C-binding. 1 Publication
    Mutagenesisi103 – 1031R → A: No effect on RPA2-binding; loss of PPP4C-binding. 1 Publication
    Mutagenesisi106 – 1061E → A: No effect on RPA2-binding, nor on PPP4C-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA38520.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 417417Serine/threonine-protein phosphatase 4 regulatory subunit 2PRO_0000299365Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei159 – 1591Phosphoserine4 Publications
    Modified residuei226 – 2261Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9NY27.
    PaxDbiQ9NY27.
    PRIDEiQ9NY27.

    PTM databases

    PhosphoSiteiQ9NY27.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ9NY27.
    BgeeiQ9NY27.
    CleanExiHS_PPP4R2.
    GenevestigatoriQ9NY27.

    Organism-specific databases

    HPAiHPA034695.

    Interactioni

    Subunit structurei

    Serine/threonine-protein phosphatase 4 (PP4) occurs in different assemblies of the catalytic and one or more regulatory subunits. Component of the PP4 complexes PPP4C-PPP4R2, PPP4C-PPP4R2-PPP4R3A and PPP4C-PPP4R2-PPP4R3B. The PPP4C-PPP4R2 complex appears to be a tetramer composed of 2 molecules of PPP4C and 2 molecules of PPP4R2. Interacts with DDX20/GEMIN3 and GEMIN4. Interacts with RPA2; this DNA damage-dependent interaction recruits PPP4C leading to RPA2 dephosphorylation.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP4CP605108EBI-1048740,EBI-1046072

    Protein-protein interaction databases

    BioGridi127414. 25 interactions.
    IntActiQ9NY27. 4 interactions.
    MINTiMINT-8214437.
    STRINGi9606.ENSP00000349124.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9NY27.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi298 – 415118Glu-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PPP4R2 family.Curated

    Phylogenomic databases

    eggNOGiNOG240518.
    HOGENOMiHOG000060339.
    HOVERGENiHBG101227.
    InParanoidiQ9NY27.
    KOiK15425.
    OMAiPVKNKHS.
    OrthoDBiEOG74XS92.
    PhylomeDBiQ9NY27.
    TreeFamiTF105561.

    Family and domain databases

    InterProiIPR015267. PPP4R2.
    [Graphical view]
    PfamiPF09184. PPP4R2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9NY27-1) [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

    MDVERLQEAL KDFEKRGKKE VCPVLDQFLC HVAKTGETMI QWSQFKGYFI    50
    FKLEKVMDDF RTSAPEPRGP PNPNVEYIPF DEMKERILKI VTGFNGIPFT 100
    IQRLCELLTD PRRNYTGTDK FLRGVEKNVM VVSCVYPSSE KNNSNSLNRM 150
    NGVMFPGNSP SYTERSNING PGTPRPLNRP KVSLSAPMTT NGLPESTDSK 200
    EANLQQNEEK NHSDSSTSES EVSSVSPLKN KHPDEDAVEA EGHEVKRLRF 250
    DKEGEVRETA SQTTSSEISS VMVGETEASS SSQDKDKDSR CTRQHCTEED 300
    EEEDEEEEEE SFMTSREMIP ERKNQEKESD DALTVNEETS EENNQMEESD 350
    VSQAEKDLLH SEGSENEGPV SSSSSDCRET EELVGSNSSK TGEILSESSM 400
    ENDDEATEVT DEPMEQD 417
    Length:417
    Mass (Da):46,898
    Last modified:September 11, 2007 - v3
    Checksum:i75298CD34A202F40
    GO
    Isoform 2 (identifier: Q9NY27-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         39-96: MIQWSQFKGYFIFKLEKVMDDFRTSAPEPRGPPNPNVEYIPFDEMKERILKIVTGFNG → I

    Note: No experimental confirmation available.

    Show »
    Length:360
    Mass (Da):40,175
    Checksum:i8008773931775213
    GO
    Isoform 3 (identifier: Q9NY27-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-56: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:361
    Mass (Da):40,249
    Checksum:i3B1868993A26757A
    GO

    Sequence cautioni

    The sequence AAI00282.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence CAB93534.2 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti174 – 1741P → L.
    Corresponds to variant rs2306983 [ dbSNP | Ensembl ].
    VAR_051749
    Natural varianti282 – 2821S → C.
    Corresponds to variant rs34742137 [ dbSNP | Ensembl ].
    VAR_034811

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5656Missing in isoform 3. 1 PublicationVSP_027612Add
    BLAST
    Alternative sequencei39 – 9658MIQWS…TGFNG → I in isoform 2. 1 PublicationVSP_027613Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271448 mRNA. Translation: CAB93534.2. Different initiation.
    AF327345 mRNA. Translation: AAL56006.1.
    AK289901 mRNA. Translation: BAF82590.1.
    CH471055 Genomic DNA. Translation: EAW65530.1.
    BC100281 mRNA. Translation: AAI00282.1. Sequence problems.
    BC110889 mRNA. Translation: AAI10890.1.
    BC128136 mRNA. Translation: AAI28137.1.
    BC128137 mRNA. Translation: AAI28138.1.
    CCDSiCCDS2917.1. [Q9NY27-1]
    RefSeqiNP_777567.1. NM_174907.2. [Q9NY27-1]
    UniGeneiHs.431092.

    Genome annotation databases

    EnsembliENST00000356692; ENSP00000349124; ENSG00000163605. [Q9NY27-1]
    GeneIDi151987.
    KEGGihsa:151987.
    UCSCiuc003dph.1. human. [Q9NY27-1]
    uc003dpi.1. human. [Q9NY27-2]

    Polymorphism databases

    DMDMi158564082.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ271448 mRNA. Translation: CAB93534.2 . Different initiation.
    AF327345 mRNA. Translation: AAL56006.1 .
    AK289901 mRNA. Translation: BAF82590.1 .
    CH471055 Genomic DNA. Translation: EAW65530.1 .
    BC100281 mRNA. Translation: AAI00282.1 . Sequence problems.
    BC110889 mRNA. Translation: AAI10890.1 .
    BC128136 mRNA. Translation: AAI28137.1 .
    BC128137 mRNA. Translation: AAI28138.1 .
    CCDSi CCDS2917.1. [Q9NY27-1 ]
    RefSeqi NP_777567.1. NM_174907.2. [Q9NY27-1 ]
    UniGenei Hs.431092.

    3D structure databases

    ProteinModelPortali Q9NY27.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 127414. 25 interactions.
    IntActi Q9NY27. 4 interactions.
    MINTi MINT-8214437.
    STRINGi 9606.ENSP00000349124.

    PTM databases

    PhosphoSitei Q9NY27.

    Polymorphism databases

    DMDMi 158564082.

    Proteomic databases

    MaxQBi Q9NY27.
    PaxDbi Q9NY27.
    PRIDEi Q9NY27.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356692 ; ENSP00000349124 ; ENSG00000163605 . [Q9NY27-1 ]
    GeneIDi 151987.
    KEGGi hsa:151987.
    UCSCi uc003dph.1. human. [Q9NY27-1 ]
    uc003dpi.1. human. [Q9NY27-2 ]

    Organism-specific databases

    CTDi 151987.
    GeneCardsi GC03P073045.
    HGNCi HGNC:18296. PPP4R2.
    HPAi HPA034695.
    MIMi 613822. gene.
    neXtProti NX_Q9NY27.
    PharmGKBi PA38520.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG240518.
    HOGENOMi HOG000060339.
    HOVERGENi HBG101227.
    InParanoidi Q9NY27.
    KOi K15425.
    OMAi PVKNKHS.
    OrthoDBi EOG74XS92.
    PhylomeDBi Q9NY27.
    TreeFami TF105561.

    Miscellaneous databases

    ChiTaRSi PPP4R2. human.
    GenomeRNAii 151987.
    NextBioi 86831.
    PROi Q9NY27.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9NY27.
    Bgeei Q9NY27.
    CleanExi HS_PPP4R2.
    Genevestigatori Q9NY27.

    Family and domain databases

    InterProi IPR015267. PPP4R2.
    [Graphical view ]
    Pfami PF09184. PPP4R2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel 50 kDa protein forms complexes with protein phosphatase 4 and is located at centrosomal microtubule organizing centres."
      Hastie C.J., Carnegie G.K., Morrice N., Cohen P.T.W.
      Biochem. J. 347:845-855(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION.
    2. Zhang W., Li N., Wan T., Cao X.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "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] (ISOFORM 1).
      Tissue: Corpus callosum.
    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] (ISOFORMS 1; 2 AND 3).
      Tissue: Uterus.
    6. "Protein phosphatase 4 interacts with the survival of motor neurons complex and enhances the temporal localisation of snRNPs."
      Carnegie G.K., Sleeman J.E., Morrice N., Hastie C.J., Peggie M.W., Philp A., Lamond A.I., Cohen P.T.W.
      J. Cell Sci. 116:1905-1913(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH PPP4C; DDX20 AND GEMIN4.
    7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA replication."
      Chowdhury D., Xu X., Zhong X., Ahmed F., Zhong J., Liao J., Dykxhoorn D.M., Weinstock D.M., Pfeifer G.P., Lieberman J.
      Mol. Cell 31:33-46(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3A COMPLEX, IDENTIFICATION IN THE PPP4C-PPP4R2-PPP4R3B COMPLEX, FUNCTION OF THE PPP4C-PPP4R2-PPP4R3A COMPLEX.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-159 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "A PP4 phosphatase complex dephosphorylates RPA2 to facilitate DNA repair via homologous recombination."
      Lee D.H., Pan Y., Kanner S., Sung P., Borowiec J.A., Chowdhury D.
      Nat. Struct. Mol. Biol. 17:365-372(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH RPA2, SUBCELLULAR LOCATION, MUTAGENESIS OF PHE-99; ARG-103 AND GLU-106.
    13. "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-159 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "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-159 AND SER-226, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPP4R2_HUMAN
    AccessioniPrimary (citable) accession number: Q9NY27
    Secondary accession number(s): A8K1I6
    , Q2TAJ9, Q498B8, Q8WXX6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: September 11, 2007
    Last modified: October 1, 2014
    This is version 90 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 3
      Human chromosome 3: 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