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O60346

- PHLP1_HUMAN

UniProt

O60346 - PHLP1_HUMAN

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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

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

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
Complete GO annotation...

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-KW
  3. nucleus Source: UniProtKB-KW
Complete GO annotation...

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. 25 interactions.
IntActiO60346. 20 interactions.
MINTiMINT-2796653.
STRINGi9606.ENSP00000393405.

Structurei

3D structure databases

ProteinModelPortaliO60346.
SMRiO60346. Positions 630-1160, 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.
GeneTreeiENSGT00440000037833.
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

« Hide

        10         20         30         40         50
MEPAAAATVQ RLPELGREDR ASAPAAAAAA AAAAAAAAAA LAAAAGGGRS
60 70 80 90 100
PEPALTPAAP SGGNGSGSGA REEAPGEAPP GPLPGRAGGA GRRRRRGAPQ
110 120 130 140 150
PIAGGAAPVP GAGGGANSLL LRRGRLKRNL SAAAAAASSS SSSSAAAASH
160 170 180 190 200
SPGAAGLPAS CSASASLCTR SLDRKTLLLK HRQTLQLQPS DRDWVRHQLQ
210 220 230 240 250
RGCVHVFDRH MASTYLRPVL CTLDTTAGEV AARLLQLGHK GGGVVKVLGQ
260 270 280 290 300
GPGAAAAREP AEPPPEAGPR LAPPEPRDSE VPPARSAPGA FGGPPRAPPA
310 320 330 340 350
DLPLPVGGPG GWSRRASPAP SDSSPGEPFV GGPVSSPRAP RPVVSDTESF
360 370 380 390 400
SLSPSAESVS DRLDPYSSGG GSSSSSEELE ADAASAPTGV PGQPRRPGHP
410 420 430 440 450
AQPLPLPQTA SSPQPQQKAP RAIDSPGGAV REGSCEEKAA AAVAPGGLQS
460 470 480 490 500
TPGRSGVTAE KAPPPPPPPT LYVQLHGETT RRLEAEEKPL QIQNDYLFQL
510 520 530 540 550
GFGELWRVQE EGMDSEIGCL IRFYAGKPHS TGSSERIQLS GMYNVRKGKM
560 570 580 590 600
QLPVNRWTRR QVILCGTCLI VSSVKDSLTG KMHVLPLIGG KVEEVKKHQH
610 620 630 640 650
CLAFSSSGPQ SQTYYICFDT FTEYLRWLRQ VSKVASQRIS SVDLSCCSLE
660 670 680 690 700
HLPANLFYSQ DLTHLNLKQN FLRQNPSLPA ARGLNELQRF TKLKSLNLSN
710 720 730 740 750
NHLGDFPLAV CSIPTLAELN VSCNALRSVP AAVGVMHNLQ TFLLDGNFLQ
760 770 780 790 800
SLPAELENMK QLSYLGLSFN EFTDIPEVLE KLTAVDKLCM SGNCVETLRL
810 820 830 840 850
QALRKMPHIK HVDLRLNVIR KLIADEVDFL QHVTQLDLRD NKLGDLDAMI
860 870 880 890 900
FNNIEVLHCE RNQLVTLDIC GYFLKALYAS SNELVQLDVY PVPNYLSYMD
910 920 930 940 950
VSRNRLENVP EWVCESRKLE VLDIGHNQIC ELPARLFCNS SLRKLLAGHN
960 970 980 990 1000
QLARLPERLE RTSVEVLDVQ HNQLLELPPN LLMKADSLRF LNASANKLES
1010 1020 1030 1040 1050
LPPATLSEET NSILQELYLT NNSLTDKCVP LLTGHPHLKI LHMAYNRLQS
1060 1070 1080 1090 1100
FPASKMAKLE ELEEIDLSGN KLKAIPTTIM NCRRMHTVIA HSNCIEVFPE
1110 1120 1130 1140 1150
VMQLPEIKCV DLSCNELSEV TLPENLPPKL QELDLTGNPR LVLDHKTLEL
1160 1170 1180 1190 1200
LNNIRCFKID QPSTGDASGA PAVWSHGYTE ASGVKNKLCV AALSVNNFCD
1210 1220 1230 1240 1250
NREALYGVFD GDRNVEVPYL LQCTMSDILA EELQKTKNEE EYMVNTFIVM
1260 1270 1280 1290 1300
QRKLGTAGQK LGGAAVLCHI KHDPVDPGGS FTLTSANVGK CQTVLCRNGK
1310 1320 1330 1340 1350
PLPLSRSYIM SCEEELKRIK QHKAIITEDG KVNGVTESTR ILGYTFLHPS
1360 1370 1380 1390 1400
VVPRPHVQSV LLTPQDEFFI LGSKGLWDSL SVEEAVEAVR NVPDALAAAK
1410 1420 1430 1440 1450
KLCTLAQSYG CHDSISAVVV QLSVTEDSFC CCELSAGGAV PPPSPGIFPP
1460 1470 1480 1490 1500
SVNMVIKDRP SDGLGVPSSS SGMASEISSE LSTSEMSSEV GSTASDEPPP
1510 1520 1530 1540 1550
GALSENSPAY PSEQRCMLHP ICLSNSFQRQ LSSATFSSAF SDNGLDSDDE
1560 1570 1580 1590 1600
EPIEGVFTNG SRVEVEVDIH CSRAKEKEKQ QHLLQVPAEA SDEGIVISAN
1610 1620 1630 1640 1650
EDEPGLPRKA DFSAVGTIGR RRANGSVAPQ ERSHNVIEVA TDAPLRKPGG
1660 1670 1680 1690 1700
YFAAPAQPDP DDQFIIPPEL EEEVKEIMKH HQEQQQQQQP PPPPQLQPQL
1710
PRHYQLDQLP DYYDTPL
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 630-1160, 1205-1422.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116843. 25 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.
GeneTreei ENSGT00440000037833.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 138 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