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Q8BXA7

- PHLP2_MOUSE

UniProt

Q8BXA7 - PHLP2_MOUSE

Protein

PH domain leucine-rich repeat-containing protein phosphatase 2

Gene

Phlpp2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Protein phosphatase that mediates dephosphorylation of 'Ser-473' of AKT1, 'Ser-660' of PRKCB and 'Ser-657' of PRKCA. AKT1 regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of AKT1 triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Inhibits cancer cell proliferation and may act as a tumor suppressor By similarity.By similarity

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi817 – 8171Manganese 1By similarity
    Metal bindingi817 – 8171Manganese 2By similarity
    Metal bindingi818 – 8181Manganese 1; via carbonyl oxygenBy similarity
    Metal bindingi982 – 9821Manganese 2By similarity
    Metal bindingi1021 – 10211Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. phosphoprotein phosphatase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_214733. Negative regulation of the PI3K/AKT network.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    PH domain leucine-rich repeat-containing protein phosphatase 2 (EC:3.1.3.16)
    Alternative name(s):
    PH domain leucine-rich repeat-containing protein phosphatase-like
    Short name:
    PHLPP-like
    Gene namesi
    Name:Phlpp2
    Synonyms:Phlppl
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:2444928. Phlpp2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. membrane Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13201320PH domain leucine-rich repeat-containing protein phosphatase 2PRO_0000057785Add
    BLAST

    Proteomic databases

    MaxQBiQ8BXA7.
    PaxDbiQ8BXA7.
    PRIDEiQ8BXA7.

    PTM databases

    PhosphoSiteiQ8BXA7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8BXA7.
    BgeeiQ8BXA7.
    GenevestigatoriQ8BXA7.

    Interactioni

    Subunit structurei

    Interacts with AKT1, AKT3 and PRKCB.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BXA7.
    SMRiQ8BXA7. Positions 248-763, 810-1030.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini147 – 24599PHAdd
    BLAST
    Repeati247 – 26822LRR 1Add
    BLAST
    Repeati270 – 29324LRR 2Add
    BLAST
    Repeati297 – 31822LRR 3Add
    BLAST
    Repeati320 – 34122LRR 4Add
    BLAST
    Repeati343 – 36422LRR 5Add
    BLAST
    Repeati366 – 38823LRR 6Add
    BLAST
    Repeati389 – 40921LRR 7Add
    BLAST
    Repeati413 – 43422LRR 8Add
    BLAST
    Repeati437 – 45721LRR 9Add
    BLAST
    Repeati458 – 47720LRR 10Add
    BLAST
    Repeati478 – 49922LRR 11Add
    BLAST
    Repeati500 – 52122LRR 12Add
    BLAST
    Repeati523 – 54422LRR 13Add
    BLAST
    Repeati546 – 56722LRR 14Add
    BLAST
    Repeati568 – 58922LRR 15Add
    BLAST
    Repeati592 – 61322LRR 16Add
    BLAST
    Repeati618 – 64124LRR 17Add
    BLAST
    Repeati642 – 66322LRR 18Add
    BLAST
    Repeati666 – 68722LRR 19Add
    BLAST
    Repeati689 – 71022LRR 20Add
    BLAST
    Repeati711 – 73222LRR 21Add
    BLAST
    Repeati734 – 75522LRR 22Add
    BLAST
    Domaini772 – 1028257PP2C-likeAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi40 – 478Poly-Thr
    Compositional biasi48 – 5710Poly-Ser
    Compositional biasi1068 – 10714Poly-Ser

    Sequence similaritiesi

    Contains 22 LRR (leucine-rich) repeats.Curated
    Contains 1 PH domain.Curated
    Contains 1 PP2C-like domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG4886.
    GeneTreeiENSGT00440000037833.
    HOGENOMiHOG000115529.
    HOVERGENiHBG062748.
    InParanoidiQ148U6.
    KOiK16340.
    OrthoDBiEOG7RFTGK.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.60.40.10. 1 hit.
    InterProiIPR001611. Leu-rich_rpt.
    IPR025875. Leu-rich_rpt_4.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR011993. PH_like_dom.
    IPR001932. PP2C-like_dom.
    [Graphical view]
    PfamiPF12799. LRR_4. 1 hit.
    PF13504. LRR_7. 1 hit.
    PF13855. LRR_8. 3 hits.
    PF00481. PP2C. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 1 hit.
    PROSITEiPS51450. LRR. 17 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q8BXA7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKHNGSRTCL NRRSRFGSRE RDWLREDVKR GCVYLYGADT TTATTTTSSS     50
    SSSSSSSDLH LVLCTVETPA SEICAGEGRE SLYLQLHGDL VRRLEPSERP 100
    LQIVYDYLSR LGFEDPVRIQ EEATNPDLSC MIRFYGEKPC QMDHLDRILL 150
    SGIYNVRKGK TQLHKWAERL VVLCGTCLIV SSVKDCQTGK MHILPLVGGK 200
    IEEVKRRQHS LAFSSAGAQA QTYHVSFETL AEYQRWQRQA SKVVSQRMST 250
    VDLSCYSLEE VPEHLFYSQD ITYLNLRHNF MQLERPGGLD TLHKFSQLKG 300
    LNLSHNKLGL FPVLLCEIST LTELSLSCNG FHDLPSQIGK LLNLQTLSLD 350
    GNGLTALPDE LGNLRQLTSL GISFNDFRHI PEVLEKLTML DKVAMAGNRL 400
    EVLNLGALTR MSQVKHVDLR MNHLKTVITE NMEGNKHITH MDLRDNQLTD 450
    LDLSSLCSLE QLHCERNQLR ELTLSGFSLR TLYASWNRLT AVNVYPVPSL 500
    LTSLELSQNL LECVPDWACE AKKLEILDIS HNLLTEVPMR ILSSLSLRKL 550
    MVGHNHIHVL PALVEHIPLE VLDIQHNTLS RLPDTLFSKA LNLRYLNASA 600
    NSLESLPSAC AGEESLSVLQ LLYLTSNLLT DQCIPVLVGH PHLRVLHLAN 650
    NQLQTFPASK LNKLEQLEEL NLSGNKLTAI PTTIANCKRL HTLVAHANNI 700
    SIFPEILQLP QIQFVDLSCN DLTEILIPEA LPATLQDLDL TGNTNLVLEH 750
    KTLDMFSHIT ALKIDQKPLP ATDSAVTSTF WSHGLAEMAG QRNKLCVSAL 800
    AMDNFAEGVG AVYGMFDGDR NEELPRLLQC TMADVLLEEV QHSTNDTVFM 850
    TNTFLVSHRK LGMAGQKLGS SALLCYIRPD TADPTSSFSL TVANVGMCQA 900
    VLCRGGKPVP LSKVFSLEHD PEEAQRVKDQ KAIITEDNKV NGVTCCTRLL 950
    GCTYLYPWIL PKPHIASTPL TIQDELLILG NKALWEHLSY LEAVNAVRHV 1000
    QDPLAAAKKL CTLAQSYGCQ DNVGAMVVYL NIGEEGCTCE MNGLTLPGPV 1050
    GFASTAALKD TPKPTTPSSS SGIASEFSSE MSTSEVSSEV GSTASDEHNT 1100
    VGLEASLLPR PERRCSLHPA SSAGVFQRQP SCATFSSNQS DNGLDSDDDQ 1150
    PVEGVITNGS RVEVEVDIHC CRGREPESSP PLPKNSSNAC SEERARGAGF 1200
    GIRRQNSVNS GILLPANRDK MELQKSPSTS CLYGKKLSNG SIVPLEDSLN 1250
    LIEVATEAPK RKTGYFAAPT QLEPEDQFVV PRDLEEEVKE QMKQHQEGRP 1300
    EPEPRGEERT EPLEEFDTAL 1320
    Length:1,320
    Mass (Da):145,947
    Last modified:July 27, 2011 - v3
    Checksum:i302407C231BD539B
    GO

    Sequence cautioni

    The sequence BAC33347.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671E → Q in BAC33288. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC122807 Genomic DNA. No translation available.
    BC117961 mRNA. Translation: AAI17962.1.
    BC117962 mRNA. Translation: AAI17963.1.
    AK048260 mRNA. Translation: BAC33288.1.
    AK048472 mRNA. Translation: BAC33347.2. Different initiation.
    RefSeqiNP_001116066.2. NM_001122594.2.
    UniGeneiMm.23494.

    Genome annotation databases

    EnsembliENSMUST00000034175; ENSMUSP00000034175; ENSMUSG00000031732.
    GeneIDi244650.
    KEGGimmu:244650.
    UCSCiuc009njn.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC122807 Genomic DNA. No translation available.
    BC117961 mRNA. Translation: AAI17962.1 .
    BC117962 mRNA. Translation: AAI17963.1 .
    AK048260 mRNA. Translation: BAC33288.1 .
    AK048472 mRNA. Translation: BAC33347.2 . Different initiation.
    RefSeqi NP_001116066.2. NM_001122594.2.
    UniGenei Mm.23494.

    3D structure databases

    ProteinModelPortali Q8BXA7.
    SMRi Q8BXA7. Positions 248-763, 810-1030.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q8BXA7.

    Proteomic databases

    MaxQBi Q8BXA7.
    PaxDbi Q8BXA7.
    PRIDEi Q8BXA7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034175 ; ENSMUSP00000034175 ; ENSMUSG00000031732 .
    GeneIDi 244650.
    KEGGi mmu:244650.
    UCSCi uc009njn.2. mouse.

    Organism-specific databases

    CTDi 23035.
    MGIi MGI:2444928. Phlpp2.

    Phylogenomic databases

    eggNOGi COG4886.
    GeneTreei ENSGT00440000037833.
    HOGENOMi HOG000115529.
    HOVERGENi HBG062748.
    InParanoidi Q148U6.
    KOi K16340.
    OrthoDBi EOG7RFTGK.

    Enzyme and pathway databases

    Reactomei REACT_214733. Negative regulation of the PI3K/AKT network.

    Miscellaneous databases

    ChiTaRSi PHLPP2. mouse.
    NextBioi 386351.
    PROi Q8BXA7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8BXA7.
    Bgeei Q8BXA7.
    Genevestigatori Q8BXA7.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.60.40.10. 1 hit.
    InterProi IPR001611. Leu-rich_rpt.
    IPR025875. Leu-rich_rpt_4.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR011993. PH_like_dom.
    IPR001932. PP2C-like_dom.
    [Graphical view ]
    Pfami PF12799. LRR_4. 1 hit.
    PF13504. LRR_7. 1 hit.
    PF13855. LRR_8. 3 hits.
    PF00481. PP2C. 1 hit.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81606. SSF81606. 1 hit.
    PROSITEi PS51450. LRR. 17 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    2. "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].
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1259.
      Strain: C57BL/6J.
      Tissue: Head.
    4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiPHLP2_MOUSE
    AccessioniPrimary (citable) accession number: Q8BXA7
    Secondary accession number(s): Q148U6, Q8BX96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 109 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3