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Q6ZVD8

- PHLP2_HUMAN

UniProt

Q6ZVD8 - PHLP2_HUMAN

Protein

PH domain leucine-rich repeat-containing protein phosphatase 2

Gene

PHLPP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Protein phosphatase that mediates dephosphorylation of 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II 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.3 Publications

    Catalytic activityi

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

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Kineticsi

    1. KM=4.13 mM for p-nitrophenyl phosphate

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi820 – 8201Manganese 1By similarity
    Metal bindingi820 – 8201Manganese 2By similarity
    Metal bindingi821 – 8211Manganese 1; via carbonyl oxygenBy similarity
    Metal bindingi985 – 9851Manganese 2By similarity
    Metal bindingi1024 – 10241Manganese 2By similarity

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. protein serine/threonine phosphatase activity Source: Ensembl

    GO - Biological processi

    1. epidermal growth factor receptor signaling pathway Source: Reactome
    2. Fc-epsilon receptor signaling pathway Source: Reactome
    3. fibroblast growth factor receptor signaling pathway Source: Reactome
    4. innate immune response Source: Reactome
    5. neurotrophin TRK receptor signaling pathway Source: Reactome
    6. phosphatidylinositol-mediated signaling Source: Reactome
    7. protein dephosphorylation Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_12447. 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:KIAA0931, PHLPPL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:29149. PHLPP2.

    Subcellular locationi

    Cytoplasm. Membrane; Peripheral membrane protein. Nucleus
    Note: In colorectal cancer tissue, expression is concentrated in the cytoplasm and nucleus.

    GO - Cellular componenti

    1. cytoplasm Source: LIFEdb
    2. cytosol Source: Reactome
    3. nucleus Source: UniProtKB-SubCell
    4. photoreceptor inner segment Source: Ensembl
    5. photoreceptor outer segment membrane Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA165450496.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13231323PH domain leucine-rich repeat-containing protein phosphatase 2PRO_0000057784Add
    BLAST

    Proteomic databases

    MaxQBiQ6ZVD8.
    PaxDbiQ6ZVD8.
    PRIDEiQ6ZVD8.

    PTM databases

    PhosphoSiteiQ6ZVD8.

    Expressioni

    Tissue specificityi

    In colorectal cancer tissue, expression is highest in the surface epithelium of normal colonic mucosa adjacent to the cancer tissue but is largely excluded from the crypt bases. Expression is lost or significantly decreased in 80% of tested tumors (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ6ZVD8.
    BgeeiQ6ZVD8.
    CleanExiHS_PHLPPL.
    GenevestigatoriQ6ZVD8.

    Organism-specific databases

    HPAiHPA048598.

    Interactioni

    Subunit structurei

    Interacts with AKT1, AKT3 and PRKCB isoform beta-II.2 Publications

    Protein-protein interaction databases

    BioGridi116674. 13 interactions.
    DIPiDIP-53556N.
    IntActiQ6ZVD8. 14 interactions.
    MINTiMINT-4781843.
    STRINGi9606.ENSP00000348611.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6ZVD8.
    SMRiQ6ZVD8. Positions 251-773, 797-1033.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini150 – 24899PHAdd
    BLAST
    Repeati250 – 27122LRR 1Add
    BLAST
    Repeati273 – 29624LRR 2Add
    BLAST
    Repeati300 – 32122LRR 3Add
    BLAST
    Repeati323 – 34422LRR 4Add
    BLAST
    Repeati346 – 36823LRR 5Add
    BLAST
    Repeati369 – 39022LRR 6Add
    BLAST
    Repeati392 – 41221LRR 7Add
    BLAST
    Repeati416 – 43924LRR 8Add
    BLAST
    Repeati440 – 46021LRR 9Add
    BLAST
    Repeati461 – 48020LRR 10Add
    BLAST
    Repeati481 – 50222LRR 11Add
    BLAST
    Repeati503 – 52422LRR 12Add
    BLAST
    Repeati526 – 54722LRR 13Add
    BLAST
    Repeati549 – 57022LRR 14Add
    BLAST
    Repeati571 – 59222LRR 15Add
    BLAST
    Repeati595 – 61622LRR 16Add
    BLAST
    Repeati621 – 64424LRR 17Add
    BLAST
    Repeati645 – 66622LRR 18Add
    BLAST
    Repeati669 – 69022LRR 19Add
    BLAST
    Repeati692 – 71322LRR 20Add
    BLAST
    Repeati714 – 73522LRR 21Add
    BLAST
    Repeati737 – 75822LRR 22Add
    BLAST
    Domaini775 – 1031257PP2C-likeAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi40 – 4910Poly-Thr
    Compositional biasi50 – 6011Poly-SerAdd
    BLAST
    Compositional biasi1071 – 10744Poly-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.
    HOGENOMiHOG000115529.
    InParanoidiQ6ZVD8.
    KOiK16340.
    PhylomeDBiQ6ZVD8.
    TreeFamiTF315993.

    Family and domain databases

    Gene3Di3.60.40.10. 1 hit.
    InterProiIPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR001932. PP2C-like_dom.
    [Graphical view]
    PfamiPF00560. LRR_1. 2 hits.
    PF13855. LRR_8. 2 hits.
    PF00481. PP2C. 1 hit.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 1 hit.
    PROSITEiPS51450. LRR. 18 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6ZVD8-1) [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

    MKRNGSRNCL NRRSRFGSRE RDWLREDVKR GCVYLYGADT TTATTTTTTS     50
    SSSSSSSSSS DLHLVLCTVE TPASEICAGE GRESLYLQLH GDLVRRLEPT 100
    ERPLQIVYDY LSRLGFDDPV RIQEEATNPD LGCMIRFYGE KPCHMDRLDR 150
    ILLSGIYNVR KGKTQLHKWA ERLVVLCGTC LIVSSVKDCQ TGKMHILPLV 200
    GGKIEEVKRR QYSLAFSSAG AQAQTYHVSF ETLAEYQRWQ RQASKVVSQR 250
    ISTVDLSCYS LEEVPEHLFY SQDITYLNLR HNFMQLERPG GLDTLYKFSQ 300
    LKGLNLSHNK LGLFPILLCE ISTLTELNLS CNGFHDLPSQ IGNLLNLQTL 350
    CLDGNFLTTL PEELGNLQQL SSLGISFNNF SQIPEVYEKL TMLDRVVMAG 400
    NCLEVLNLGV LNRMNHIKHV DLRMNHLKTM VIENLEGNKH ITHVDLRDNR 450
    LTDLDLSSLC SLEQLHCGRN QLRELTLSGF SLRTLYASSN RLTAVNVYPV 500
    PSLLTFLDLS RNLLECVPDW ACEAKKIEVL DVSYNLLTEV PVRILSSLSL 550
    RKLMLGHNHV QNLPTLVEHI PLEVLDLQHN ALTRLPDTLF SKALNLRYLN 600
    ASANSLESLP SACTGEESLS MLQLLYLTNN LLTDQCIPVL VGHLHLRILH 650
    LANNQLQTFP ASKLNKLEQL EELNLSGNKL KTIPTTIANC KRLHTLVAHS 700
    NNISIFPEIL QLPQIQFVDL SCNDLTEILI PEALPATLQD LDLTGNTNLV 750
    LEHKTLDIFS HITTLKIDQK PLPTTDSTVT STFWSHGLAE MAGQRNKLCV 800
    SALAMDSFAE GVGAVYGMFD GDRNEELPRL LQCTMADVLL EEVQQSTNDT 850
    VFMANTFLVS HRKLGMAGQK LGSSALLCYI RPDTADPASS FSLTVANVGT 900
    CQAVLCRGGK PVPLSKVFSL EQDPEEAQRV KDQKAIITED NKVNGVTCCT 950
    RMLGCTYLYP WILPKPHISS TPLTIQDELL ILGNKALWEH LSYTEAVNAV 1000
    RHVQDPLAAA KKLCTLAQSY GCQDNVGAMV VYLNIGEEGC TCEMNGLTLP 1050
    GPVGFASTTT IKDAPKPATP SSSSGIASEF SSEMSTSEVS SEVGSTASDE 1100
    HNAGGLDTAL LPRPERRCSL HPTPTSGLFQ RQPSSATFSS NQSDNGLDSD 1150
    DDQPVEGVIT NGSKVEVEVD IHCCRGRDLE NSPPLIESSP TLCSEEHARG 1200
    SCFGIRRQNS VNSGMLLPMS KDRMELQKSP STSCLYGKKL SNGSIVPLED 1250
    SLNLIEVATE VPKRKTGYFA APTQMEPEDQ FVVPHDLEEE VKEQMKQHQD 1300
    SRLEPEPHEE DRTEPPEEFD TAL 1323
    Length:1,323
    Mass (Da):146,751
    Last modified:October 17, 2006 - v3
    Checksum:i04FC8550C2E22A6D
    GO
    Isoform 2 (identifier: Q6ZVD8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         940-956: DNKVNGVTCCTRMLGCT → NWVLNQKHLQDFPGEDK
         957-1323: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:956
    Mass (Da):107,079
    Checksum:iD639027D022AFED9
    GO
    Isoform 3 (identifier: Q6ZVD8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         596-662: Missing.

    Show »
    Length:1,256
    Mass (Da):139,394
    Checksum:iDC706C3744570432
    GO

    Sequence cautioni

    The sequence BAA76775.2 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA91943.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti147 – 1471R → C in BX647823. (PubMed:17974005)Curated
    Sequence conflicti542 – 5421V → L(PubMed:15616553)Curated
    Sequence conflicti766 – 7661K → E in BX647823. (PubMed:17974005)Curated
    Sequence conflicti896 – 8961A → G in BAA91943. (PubMed:14702039)Curated
    Sequence conflicti978 – 9781E → G in BX647823. (PubMed:17974005)Curated
    Sequence conflicti1016 – 10161L → S in BX647823. (PubMed:17974005)Curated
    Sequence conflicti1312 – 13121R → Q in AAI29928. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei596 – 66267Missing in isoform 3. 1 PublicationVSP_017265Add
    BLAST
    Alternative sequencei940 – 95617DNKVN…MLGCT → NWVLNQKHLQDFPGEDK in isoform 2. 1 PublicationVSP_014056Add
    BLAST
    Alternative sequencei957 – 1323367Missing in isoform 2. 1 PublicationVSP_014057Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023148 mRNA. Translation: BAA76775.2. Different initiation.
    BX647823 mRNA. No translation available.
    AC009097 Genomic DNA. No translation available.
    BC129927 mRNA. Translation: AAI29928.1.
    AK001854 mRNA. Translation: BAA91943.1. Different initiation.
    AK124678 mRNA. Translation: BAC85924.1.
    CCDSiCCDS32479.1. [Q6ZVD8-1]
    RefSeqiNP_001275932.1. NM_001289003.1. [Q6ZVD8-3]
    NP_055835.2. NM_015020.3. [Q6ZVD8-1]
    UniGeneiHs.709458.

    Genome annotation databases

    EnsembliENST00000393524; ENSP00000377159; ENSG00000040199. [Q6ZVD8-3]
    ENST00000568954; ENSP00000457991; ENSG00000040199. [Q6ZVD8-1]
    GeneIDi23035.
    KEGGihsa:23035.
    UCSCiuc002fax.3. human. [Q6ZVD8-1]
    uc010cgf.3. human. [Q6ZVD8-3]

    Polymorphism databases

    DMDMi116242711.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB023148 mRNA. Translation: BAA76775.2 . Different initiation.
    BX647823 mRNA. No translation available.
    AC009097 Genomic DNA. No translation available.
    BC129927 mRNA. Translation: AAI29928.1 .
    AK001854 mRNA. Translation: BAA91943.1 . Different initiation.
    AK124678 mRNA. Translation: BAC85924.1 .
    CCDSi CCDS32479.1. [Q6ZVD8-1 ]
    RefSeqi NP_001275932.1. NM_001289003.1. [Q6ZVD8-3 ]
    NP_055835.2. NM_015020.3. [Q6ZVD8-1 ]
    UniGenei Hs.709458.

    3D structure databases

    ProteinModelPortali Q6ZVD8.
    SMRi Q6ZVD8. Positions 251-773, 797-1033.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116674. 13 interactions.
    DIPi DIP-53556N.
    IntActi Q6ZVD8. 14 interactions.
    MINTi MINT-4781843.
    STRINGi 9606.ENSP00000348611.

    Chemistry

    BindingDBi Q6ZVD8.
    ChEMBLi CHEMBL1275209.

    PTM databases

    PhosphoSitei Q6ZVD8.

    Polymorphism databases

    DMDMi 116242711.

    Proteomic databases

    MaxQBi Q6ZVD8.
    PaxDbi Q6ZVD8.
    PRIDEi Q6ZVD8.

    Protocols and materials databases

    DNASUi 23035.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000393524 ; ENSP00000377159 ; ENSG00000040199 . [Q6ZVD8-3 ]
    ENST00000568954 ; ENSP00000457991 ; ENSG00000040199 . [Q6ZVD8-1 ]
    GeneIDi 23035.
    KEGGi hsa:23035.
    UCSCi uc002fax.3. human. [Q6ZVD8-1 ]
    uc010cgf.3. human. [Q6ZVD8-3 ]

    Organism-specific databases

    CTDi 23035.
    GeneCardsi GC16M071674.
    H-InvDB HIX0013215.
    HIX0173315.
    HGNCi HGNC:29149. PHLPP2.
    HPAi HPA048598.
    MIMi 611066. gene.
    neXtProti NX_Q6ZVD8.
    PharmGKBi PA165450496.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000115529.
    InParanoidi Q6ZVD8.
    KOi K16340.
    PhylomeDBi Q6ZVD8.
    TreeFami TF315993.

    Enzyme and pathway databases

    Reactomei REACT_12447. Negative regulation of the PI3K/AKT network.

    Miscellaneous databases

    GeneWikii PHLPPL.
    GenomeRNAii 23035.
    NextBioi 44034.
    PROi Q6ZVD8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6ZVD8.
    Bgeei Q6ZVD8.
    CleanExi HS_PHLPPL.
    Genevestigatori Q6ZVD8.

    Family and domain databases

    Gene3Di 3.60.40.10. 1 hit.
    InterProi IPR001611. Leu-rich_rpt.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR001932. PP2C-like_dom.
    [Graphical view ]
    Pfami PF00560. LRR_1. 2 hits.
    PF13855. LRR_8. 2 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. 18 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 6:63-70(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Brain.
    2. Ohara O., Nagase T., Kikuno R.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Retina.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      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).
    6. "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] OF 1-423 (ISOFORMS 1/2/3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 639-1323 (ISOFORM 2).
      Tissue: Amygdala and Placenta.
    7. "PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms."
      Brognard J., Sierecki E., Gao T., Newton A.C.
      Mol. Cell 25:917-931(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH AKT1 AND AKT3.
    8. "The phosphatase PHLPP controls the cellular levels of protein kinase C."
      Gao T., Brognard J., Newton A.C.
      J. Biol. Chem. 283:6300-6311(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PRKCB.
    9. "Loss of PHLPP expression in colon cancer: role in proliferation and tumorigenesis."
      Liu J., Weiss H.L., Rychahou P., Jackson L.N., Evers B.M., Gao T.
      Oncogene 28:994-1004(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPHLP2_HUMAN
    AccessioniPrimary (citable) accession number: Q6ZVD8
    Secondary accession number(s): A1L374, Q9NV17, Q9Y2E3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: October 17, 2006
    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
    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 16
      Human chromosome 16: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3