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O60346

- PHLP1_HUMAN

UniProt

O60346 - PHLP1_HUMAN

Protein

PH domain leucine-rich repeat-containing protein phosphatase 1

Gene

PHLPP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 3 (07 Jun 2005)
      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 suppression of tumor growth. Controls the phosphorylation of AKT2 and AKT3 more efficiently than that of AKT1. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Inhibits cancer cell proliferation and may act as a tumor suppressor. May act as a negative regulator of K-Ras signaling in membrane rafts.4 Publications

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.1 Publication

    Cofactori

    Binds 2 manganese ions per subunit.By similarity

    Enzyme regulationi

    Insensitive to okadaic acid.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1210 – 12101Manganese 1By similarity
    Metal bindingi1210 – 12101Manganese 2By similarity
    Metal bindingi1211 – 12111Manganese 1; via carbonyl oxygenBy similarity
    Metal bindingi1374 – 13741Manganese 2By similarity
    Metal bindingi1413 – 14131Manganese 2By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. entrainment of circadian clock Source: Ensembl
    3. epidermal growth factor receptor signaling pathway Source: Reactome
    4. Fc-epsilon receptor signaling pathway Source: Reactome
    5. fibroblast growth factor receptor signaling pathway Source: Reactome
    6. innate immune response Source: Reactome
    7. neurotrophin TRK receptor signaling pathway Source: Reactome
    8. phosphatidylinositol-mediated signaling Source: Reactome

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Apoptosis

    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 1 (EC:3.1.3.16)
    Alternative name(s):
    Pleckstrin homology domain-containing family E member 1
    Short name:
    PH domain-containing family E member 1
    Suprachiasmatic nucleus circadian oscillatory protein
    Short name:
    hSCOP
    Gene namesi
    Name:PHLPP1
    Synonyms:KIAA0606, PHLPP, PLEKHE1, SCOP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:20610. PHLPP1.

    Subcellular locationi

    Cytoplasm. Membrane; Peripheral membrane protein. Nucleus
    Note: In colorectal cancer tissue, expression is concentrated at the lateral membrane of epithelial cells.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. membrane Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1715 – 17173Missing: Loss of function in vivo, but does not abolishes intrinsic phosphatase activity. 1 Publication

    Keywords - Diseasei

    Tumor suppressor

    Organism-specific databases

    PharmGKBiPA165429055.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17171717PH domain leucine-rich repeat-containing protein phosphatase 1PRO_0000057781Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiO60346.
    PaxDbiO60346.
    PeptideAtlasiO60346.
    PRIDEiO60346.

    PTM databases

    PhosphoSiteiO60346.

    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 78% of tested tumors (at protein level). Ubiquitously expressed in non-cancerous tissues.2 Publications

    Gene expression databases

    BgeeiO60346.
    CleanExiHS_PHLPP.
    GenevestigatoriO60346.

    Organism-specific databases

    HPAiHPA020200.

    Interactioni

    Subunit structurei

    Interacts with the nucleotide free form of K-Ras (KRAS) via its LRR repeats By similarity. Interacts with AKT2, AKT3 and PRKCB isoform beta-II.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PRKCBP05771-25EBI-2511516,EBI-5774511
    SCRIBQ141602EBI-2511516,EBI-357345
    ScribQ80U722EBI-2511516,EBI-1766028From a different organism.

    Protein-protein interaction databases

    BioGridi116843. 23 interactions.
    IntActiO60346. 20 interactions.
    MINTiMINT-2796653.
    STRINGi9606.ENSP00000393405.

    Structurei

    3D structure databases

    ProteinModelPortaliO60346.
    SMRiO60346. Positions 626-1160, 1205-1422.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini536 – 636101PHPROSITE-ProRule annotationAdd
    BLAST
    Repeati638 – 65922LRR 1Add
    BLAST
    Repeati661 – 68222LRR 2Add
    BLAST
    Repeati692 – 71221LRR 3Add
    BLAST
    Repeati715 – 73622LRR 4Add
    BLAST
    Repeati738 – 76023LRR 5Add
    BLAST
    Repeati761 – 78323LRR 6Add
    BLAST
    Repeati784 – 80421LRR 7Add
    BLAST
    Repeati808 – 83124LRR 8Add
    BLAST
    Repeati832 – 85322LRR 9Add
    BLAST
    Repeati873 – 89422LRR 10Add
    BLAST
    Repeati895 – 91622LRR 11Add
    BLAST
    Repeati918 – 93922LRR 12Add
    BLAST
    Repeati941 – 96222LRR 13Add
    BLAST
    Repeati963 – 98422LRR 14Add
    BLAST
    Repeati987 – 100822LRR 15Add
    BLAST
    Repeati1013 – 103321LRR 16Add
    BLAST
    Repeati1037 – 105822LRR 17Add
    BLAST
    Repeati1061 – 108222LRR 18Add
    BLAST
    Repeati1084 – 110522LRR 19Add
    BLAST
    Repeati1106 – 112722LRR 20Add
    BLAST
    Repeati1129 – 115022LRR 21Add
    BLAST
    Domaini1165 – 1420256PP2C-likeAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1715 – 17173PDZ-binding

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 74Poly-Ala
    Compositional biasi21 – 4525Poly-AlaAdd
    BLAST
    Compositional biasi132 – 1376Poly-Ala
    Compositional biasi138 – 1447Poly-Ser
    Compositional biasi145 – 1484Poly-Ala
    Compositional biasi254 – 2574Poly-Ala
    Compositional biasi463 – 4697Poly-Pro
    Compositional biasi1682 – 16898Poly-Gln

    Domaini

    The PH domain is required for interaction with PRKCB and its dephosphorylation.

    Sequence similaritiesi

    Contains 21 LRR (leucine-rich) repeats.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 PP2C-like domain.Curated

    Keywords - Domaini

    Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG4886.
    InParanoidiO60346.
    KOiK16340.
    OMAiFTNGSRV.
    OrthoDBiEOG7RFTGK.
    PhylomeDBiO60346.
    TreeFamiTF315993.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.60.40.10. 1 hit.
    InterProiIPR001611. Leu-rich_rpt.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001932. PP2C-like_dom.
    [Graphical view]
    PfamiPF00560. LRR_1. 2 hits.
    PF13855. LRR_8. 2 hits.
    PF00481. PP2C. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 1 hit.
    PROSITEiPS51450. LRR. 17 hits.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O60346-1 [UniParc]FASTAAdd to Basket

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    MEPAAAATVQ RLPELGREDR ASAPAAAAAA AAAAAAAAAA LAAAAGGGRS     50
    PEPALTPAAP SGGNGSGSGA REEAPGEAPP GPLPGRAGGA GRRRRRGAPQ 100
    PIAGGAAPVP GAGGGANSLL LRRGRLKRNL SAAAAAASSS SSSSAAAASH 150
    SPGAAGLPAS CSASASLCTR SLDRKTLLLK HRQTLQLQPS DRDWVRHQLQ 200
    RGCVHVFDRH MASTYLRPVL CTLDTTAGEV AARLLQLGHK GGGVVKVLGQ 250
    GPGAAAAREP AEPPPEAGPR LAPPEPRDSE VPPARSAPGA FGGPPRAPPA 300
    DLPLPVGGPG GWSRRASPAP SDSSPGEPFV GGPVSSPRAP RPVVSDTESF 350
    SLSPSAESVS DRLDPYSSGG GSSSSSEELE ADAASAPTGV PGQPRRPGHP 400
    AQPLPLPQTA SSPQPQQKAP RAIDSPGGAV REGSCEEKAA AAVAPGGLQS 450
    TPGRSGVTAE KAPPPPPPPT LYVQLHGETT RRLEAEEKPL QIQNDYLFQL 500
    GFGELWRVQE EGMDSEIGCL IRFYAGKPHS TGSSERIQLS GMYNVRKGKM 550
    QLPVNRWTRR QVILCGTCLI VSSVKDSLTG KMHVLPLIGG KVEEVKKHQH 600
    CLAFSSSGPQ SQTYYICFDT FTEYLRWLRQ VSKVASQRIS SVDLSCCSLE 650
    HLPANLFYSQ DLTHLNLKQN FLRQNPSLPA ARGLNELQRF TKLKSLNLSN 700
    NHLGDFPLAV CSIPTLAELN VSCNALRSVP AAVGVMHNLQ TFLLDGNFLQ 750
    SLPAELENMK QLSYLGLSFN EFTDIPEVLE KLTAVDKLCM SGNCVETLRL 800
    QALRKMPHIK HVDLRLNVIR KLIADEVDFL QHVTQLDLRD NKLGDLDAMI 850
    FNNIEVLHCE RNQLVTLDIC GYFLKALYAS SNELVQLDVY PVPNYLSYMD 900
    VSRNRLENVP EWVCESRKLE VLDIGHNQIC ELPARLFCNS SLRKLLAGHN 950
    QLARLPERLE RTSVEVLDVQ HNQLLELPPN LLMKADSLRF LNASANKLES 1000
    LPPATLSEET NSILQELYLT NNSLTDKCVP LLTGHPHLKI LHMAYNRLQS 1050
    FPASKMAKLE ELEEIDLSGN KLKAIPTTIM NCRRMHTVIA HSNCIEVFPE 1100
    VMQLPEIKCV DLSCNELSEV TLPENLPPKL QELDLTGNPR LVLDHKTLEL 1150
    LNNIRCFKID QPSTGDASGA PAVWSHGYTE ASGVKNKLCV AALSVNNFCD 1200
    NREALYGVFD GDRNVEVPYL LQCTMSDILA EELQKTKNEE EYMVNTFIVM 1250
    QRKLGTAGQK LGGAAVLCHI KHDPVDPGGS FTLTSANVGK CQTVLCRNGK 1300
    PLPLSRSYIM SCEEELKRIK QHKAIITEDG KVNGVTESTR ILGYTFLHPS 1350
    VVPRPHVQSV LLTPQDEFFI LGSKGLWDSL SVEEAVEAVR NVPDALAAAK 1400
    KLCTLAQSYG CHDSISAVVV QLSVTEDSFC CCELSAGGAV PPPSPGIFPP 1450
    SVNMVIKDRP SDGLGVPSSS SGMASEISSE LSTSEMSSEV GSTASDEPPP 1500
    GALSENSPAY PSEQRCMLHP ICLSNSFQRQ LSSATFSSAF SDNGLDSDDE 1550
    EPIEGVFTNG SRVEVEVDIH CSRAKEKEKQ QHLLQVPAEA SDEGIVISAN 1600
    EDEPGLPRKA DFSAVGTIGR RRANGSVAPQ ERSHNVIEVA TDAPLRKPGG 1650
    YFAAPAQPDP DDQFIIPPEL EEEVKEIMKH HQEQQQQQQP PPPPQLQPQL 1700
    PRHYQLDQLP DYYDTPL 1717
    Length:1,717
    Mass (Da):184,672
    Last modified:June 7, 2005 - v3
    Checksum:iA4AB53F334EA8AB6
    GO

    Sequence cautioni

    The sequence AAH82244.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence AAH14927.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAI26278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA91980.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti691 – 6911T → A in BAA91980. (PubMed:14702039)Curated
    Sequence conflicti1062 – 10621L → F in AAH47653. (PubMed:15489334)Curated
    Sequence conflicti1083 – 10831R → S in BAA25532. (PubMed:9628581)Curated
    Sequence conflicti1227 – 12271D → V in BAA91980. (PubMed:14702039)Curated
    Sequence conflicti1490 – 14901V → M in AAH47653. (PubMed:15489334)Curated
    Sequence conflicti1580 – 15801Missing in AAH63519. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti1118 – 11181S → T.
    Corresponds to variant rs9950585 [ dbSNP | Ensembl ].
    VAR_056725

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC015989 Genomic DNA. No translation available.
    AC022046 Genomic DNA. No translation available.
    AC027553 Genomic DNA. No translation available.
    AB011178 mRNA. Translation: BAA25532.2.
    BC010706 mRNA. Translation: AAH10706.1.
    BC014927 mRNA. Translation: AAH14927.3. Different initiation.
    BC047653 mRNA. Translation: AAH47653.1.
    BC063519 mRNA. Translation: AAH63519.1.
    BC082244 mRNA. Translation: AAH82244.1. Sequence problems.
    BC126277 mRNA. Translation: AAI26278.1. Different initiation.
    AK001924 mRNA. Translation: BAA91980.1. Different initiation.
    CCDSiCCDS45881.2.
    PIRiT00258.
    RefSeqiNP_919431.2. NM_194449.3.
    UniGeneiHs.465337.

    Genome annotation databases

    EnsembliENST00000262719; ENSP00000262719; ENSG00000081913.
    GeneIDi23239.
    KEGGihsa:23239.
    UCSCiuc021ule.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AC015989 Genomic DNA. No translation available.
    AC022046 Genomic DNA. No translation available.
    AC027553 Genomic DNA. No translation available.
    AB011178 mRNA. Translation: BAA25532.2 .
    BC010706 mRNA. Translation: AAH10706.1 .
    BC014927 mRNA. Translation: AAH14927.3 . Different initiation.
    BC047653 mRNA. Translation: AAH47653.1 .
    BC063519 mRNA. Translation: AAH63519.1 .
    BC082244 mRNA. Translation: AAH82244.1 . Sequence problems.
    BC126277 mRNA. Translation: AAI26278.1 . Different initiation.
    AK001924 mRNA. Translation: BAA91980.1 . Different initiation.
    CCDSi CCDS45881.2.
    PIRi T00258.
    RefSeqi NP_919431.2. NM_194449.3.
    UniGenei Hs.465337.

    3D structure databases

    ProteinModelPortali O60346.
    SMRi O60346. Positions 626-1160, 1205-1422.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116843. 23 interactions.
    IntActi O60346. 20 interactions.
    MINTi MINT-2796653.
    STRINGi 9606.ENSP00000393405.

    PTM databases

    PhosphoSitei O60346.

    Proteomic databases

    MaxQBi O60346.
    PaxDbi O60346.
    PeptideAtlasi O60346.
    PRIDEi O60346.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262719 ; ENSP00000262719 ; ENSG00000081913 .
    GeneIDi 23239.
    KEGGi hsa:23239.
    UCSCi uc021ule.1. human.

    Organism-specific databases

    CTDi 23239.
    GeneCardsi GC18P060382.
    H-InvDB HIX0014494.
    HIX0174202.
    HGNCi HGNC:20610. PHLPP1.
    HPAi HPA020200.
    MIMi 609396. gene.
    neXtProti NX_O60346.
    PharmGKBi PA165429055.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    InParanoidi O60346.
    KOi K16340.
    OMAi FTNGSRV.
    OrthoDBi EOG7RFTGK.
    PhylomeDBi O60346.
    TreeFami TF315993.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi PHLPP1. human.
    GeneWikii PHLPP_(gene).
    GenomeRNAii 23239.
    NextBioi 44894.
    PROi O60346.
    SOURCEi Search...

    Gene expression databases

    Bgeei O60346.
    CleanExi HS_PHLPP.
    Genevestigatori O60346.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.60.40.10. 1 hit.
    InterProi IPR001611. Leu-rich_rpt.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR001932. PP2C-like_dom.
    [Graphical view ]
    Pfami PF00560. LRR_1. 2 hits.
    PF13855. LRR_8. 2 hits.
    PF00481. PP2C. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81606. SSF81606. 1 hit.
    PROSITEi PS51450. LRR. 17 hits.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    2. "Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-1717.
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. "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] OF 475-1717.
      Tissue: Cerebellum, Hippocampus, Lymphoma, Melanoma and Retinoblastoma.
    5. "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 495-1233.
      Tissue: Placenta.
    6. "PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth."
      Gao T., Furnari F., Newton A.C.
      Mol. Cell 18:13-24(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, COFACTOR, ENZYME REGULATION, TISSUE SPECIFICITY, MUTAGENESIS OF 1715-THR--LEU-1717.
    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. "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 AKT2 AND AKT3.
    9. "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.
    10. "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.
    11. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPHLP1_HUMAN
    AccessioniPrimary (citable) accession number: O60346
    Secondary accession number(s): A1A4F5
    , Q641Q7, Q6P4C4, Q6PJI6, Q86TN6, Q96FK2, Q9NUY1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 137 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 18
      Human chromosome 18: 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