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PH domain leucine-rich repeat-containing protein phosphatase 1 (EC 3.1.3.16) (Pleckstrin homology domain-containing family E member 1) (PH domain-containing family E member 1) (Suprachiasmatic nucleus circadian oscillatory protein) (hSCOP)

 PHLP1_HUMAN             Reviewed;        1717 AA.
O60346; A1A4F5; Q641Q7; Q6P4C4; Q6PJI6; Q86TN6; Q96FK2; Q9NUY1;
07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
07-JUN-2005, sequence version 3.
25-OCT-2017, entry version 166.
RecName: Full=PH domain leucine-rich repeat-containing protein phosphatase 1;
EC=3.1.3.16;
AltName: Full=Pleckstrin homology domain-containing family E member 1;
Short=PH domain-containing family E member 1;
AltName: Full=Suprachiasmatic nucleus circadian oscillatory protein;
Short=hSCOP;
Name=PHLPP1; Synonyms=KIAA0606, PHLPP, PLEKHE1, SCOP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 349-1717.
TISSUE=Brain;
PubMed=9628581; DOI=10.1093/dnares/5.1.31;
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
Ohara O.;
"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.";
DNA Res. 5:31-39(1998).
[3]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 475-1717.
TISSUE=Cerebellum, Hippocampus, Lymphoma, Melanoma, and
Retinoblastoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 495-1233.
TISSUE=Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[6]
FUNCTION, ENZYME ACTIVITY, COFACTOR, ENZYME REGULATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF 1715-THR--LEU-1717.
PubMed=15808505; DOI=10.1016/j.molcel.2005.03.008;
Gao T., Furnari F., Newton A.C.;
"PHLPP: a phosphatase that directly dephosphorylates Akt, promotes
apoptosis, and suppresses tumor growth.";
Mol. Cell 18:13-24(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND INTERACTION
WITH AKT2 AND AKT3.
PubMed=17386267; DOI=10.1016/j.molcel.2007.02.017;
Brognard J., Sierecki E., Gao T., Newton A.C.;
"PHLPP and a second isoform, PHLPP2, differentially attenuate the
amplitude of Akt signaling by regulating distinct Akt isoforms.";
Mol. Cell 25:917-931(2007).
[9]
FUNCTION, AND INTERACTION WITH PRKCB.
PubMed=18162466; DOI=10.1074/jbc.M707319200;
Gao T., Brognard J., Newton A.C.;
"The phosphatase PHLPP controls the cellular levels of protein kinase
C.";
J. Biol. Chem. 283:6300-6311(2008).
[10]
INTERACTION WITH FKBP5; AKT2 AND AKT3.
PubMed=19732725; DOI=10.1016/j.ccr.2009.07.016;
Pei H., Li L., Fridley B.L., Jenkins G.D., Kalari K.R., Lingle W.,
Petersen G., Lou Z., Wang L.;
"FKBP51 affects cancer cell response to chemotherapy by negatively
regulating Akt.";
Cancer Cell 16:259-266(2009).
[11]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=19079341; DOI=10.1038/onc.2008.450;
Liu J., Weiss H.L., Rychahou P., Jackson L.N., Evers B.M., Gao T.;
"Loss of PHLPP expression in colon cancer: role in proliferation and
tumorigenesis.";
Oncogene 28:994-1004(2009).
[12]
FUNCTION, AND INTERACTION WITH STK4.
PubMed=20513427; DOI=10.1016/j.molcel.2010.03.017;
Qiao M., Wang Y., Xu X., Lu J., Dong Y., Tao W., Stein J., Stein G.S.,
Iglehart J.D., Shi Q., Pardee A.B.;
"Mst1 is an interacting protein that mediates PHLPPs' induced
apoptosis.";
Mol. Cell 38:512-523(2010).
[13]
INTERACTION WITH SCRIB.
PubMed=21701506; DOI=10.1038/embor.2011.106;
Li X., Yang H., Liu J., Schmidt M.D., Gao T.;
"Scribble-mediated membrane targeting of PHLPP1 is required for its
negative regulation of Akt.";
EMBO Rep. 12:818-824(2011).
[14]
FUNCTION, AND INTERACTION WITH RPS6KB1.
PubMed=21986499; DOI=10.1128/MCB.05799-11;
Liu J., Stevens P.D., Li X., Schmidt M.D., Gao T.;
"PHLPP-mediated dephosphorylation of S6K1 inhibits protein translation
and cell growth.";
Mol. Cell. Biol. 31:4917-4927(2011).
[15]
INTERACTION WITH SLC9A3R1.
PubMed=21804599; DOI=10.1038/onc.2011.324;
Molina J.R., Agarwal N.K., Morales F.C., Hayashi Y., Aldape K.D.,
Cote G., Georgescu M.M.;
"PTEN, NHERF1 and PHLPP form a tumor suppressor network that is
disabled in glioblastoma.";
Oncogene 31:1264-1274(2012).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[17]
INTERACTION WITH WDR48 AND USP12, AND ENZYME REGULATION.
PubMed=24145035; DOI=10.1074/jbc.M113.503383;
Gangula N.R., Maddika S.;
"WD repeat protein WDR48 in complex with deubiquitinase USP12
suppresses Akt-dependent cell survival signaling by stabilizing PH
domain leucine-rich repeat protein phosphatase 1 (PHLPP1).";
J. Biol. Chem. 288:34545-34554(2013).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-317 AND SER-412, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
PubMed=24892992; DOI=10.1021/bi500428j;
Sierecki E., Newton A.C.;
"Biochemical characterization of the phosphatase domain of the tumor
suppressor PH domain leucine-rich repeat protein phosphatase.";
Biochemistry 53:3971-3981(2014).
[20]
FUNCTION, AND INTERACTION WITH RAF1.
PubMed=24530606; DOI=10.1053/j.gastro.2014.02.003;
Li X., Stevens P.D., Liu J., Yang H., Wang W., Wang C., Zeng Z.,
Schmidt M.D., Yang M., Lee E.Y., Gao T.;
"PHLPP is a negative regulator of RAF1, which reduces colorectal
cancer cell motility and prevents tumor progression in mice.";
Gastroenterology 146:1301-1310(2014).
[21]
INTERACTION WITH BRAP.
PubMed=25820252; DOI=10.1038/srep09459;
Fatima S., Wagstaff K.M., Loveland K.L., Jans D.A.;
"Interactome of the negative regulator of nuclear import BRCA1-binding
protein 2.";
Sci. Rep. 5:9459-9459(2015).
-!- FUNCTION: Protein phosphatase involved in regulation of Akt and
PKC signaling. Mediates dephosphorylation in the C-terminal domain
hydrophobic motif of members of the AGC Ser/Thr protein kinase
family; specifically acts on 'Ser-473' of AKT2 and AKT3, 'Ser-660'
of PRKCB and 'Ser-657' of PRKCA (PubMed:15808505, PubMed:17386267,
PubMed:18162466). Isoform 2 seems to have a major role in
regulating Akt signaling in hippocampal neurons (By similarity).
Akt 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 Akt triggers apoptosis and
suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB
leads to their destabilization and degradation (PubMed:18162466).
Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and
apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is
involved in regulation of cap-dependent translation
(PubMed:21986499). Inhibits cancer cell proliferation and may act
as a tumor suppressor (PubMed:19079341). Dephosphorylates RAF1
inhibiting its kinase activity (PubMed:24530606). May act as a
negative regulator of K-Ras signaling in membrane rafts (By
similarity). Involved in the hippocampus-dependent long-term
memory formation (By similarity). Involved in circadian control by
regulating the consolidation of circadian periodicity after
resetting (By similarity). Involved in development and function of
regulatory T-cells (By similarity). {ECO:0000250|UniProtKB:Q8CHE4,
ECO:0000250|UniProtKB:Q9WTR8, ECO:0000269|PubMed:15808505,
ECO:0000269|PubMed:17386267, ECO:0000269|PubMed:18162466,
ECO:0000269|PubMed:19079341, ECO:0000269|PubMed:21986499,
ECO:0000269|PubMed:24530606}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:15808505, ECO:0000269|PubMed:24892992}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
Note=Binds 2 manganese ions per subunit (By similarity). Mn(2+) is
inhibitory below pH 8 and activating above pH 8 (PubMed:24892992).
{ECO:0000250, ECO:0000269|PubMed:24892992};
-!- ENZYME REGULATION: Insensitive to okadaic acid (PubMed:15808505).
Deubiquitination by WDR48-USP12 complex positively regulates
PHLPP1 stability (PubMed:24145035). {ECO:0000269|PubMed:15808505,
ECO:0000269|PubMed:24145035}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.5 mM for p-nitrophenyl phosphate
{ECO:0000269|PubMed:24892992};
-!- SUBUNIT: Interacts with the nucleotide free form of K-Ras (KRAS)
via its LRR repeats (By similarity). Interacts with AKT2, AKT3,
PRKCB isoform beta-II, STK4, RPS6KB1, RAF1 (PubMed:17386267,
PubMed:18162466, PubMed:19732725, PubMed:21986499,
PubMed:24530606). Isoform 1 (predominantly) and isoform 2 interact
with BRAP (PubMed:25820252). Interacts with FKBP5; FKBP5 acts as a
scaffold for PHLPP1 and Akt (PubMed:19732725). Interacts with
SCRIB; SCRIB acts as a scaffold for PHLPP1 and Akt
(PubMed:21701506). Interacts with SLC9A3R1; SLC9A3R1 scaffolds a
heterotrimeric complex with PTEN at the plasma membrane
(PubMed:21804599). Interacts with WDR48 and USP12
(PubMed:24145035). {ECO:0000250|UniProtKB:Q9WTR8,
ECO:0000269|PubMed:17386267, ECO:0000269|PubMed:18162466,
ECO:0000269|PubMed:19732725, ECO:0000269|PubMed:20513427,
ECO:0000269|PubMed:21701506, ECO:0000269|PubMed:21804599,
ECO:0000269|PubMed:21986499, ECO:0000269|PubMed:24145035,
ECO:0000269|PubMed:24530606, ECO:0000269|PubMed:25820252}.
-!- INTERACTION:
P05771-2:PRKCB; NbExp=5; IntAct=EBI-2511516, EBI-5774511;
Q14160:SCRIB; NbExp=2; IntAct=EBI-2511516, EBI-357345;
Q80U72:Scrib (xeno); NbExp=2; IntAct=EBI-2511516, EBI-1766028;
O14745:SLC9A3R1; NbExp=5; IntAct=EBI-11165225, EBI-349787;
-!- SUBCELLULAR LOCATION: Cytoplasm. Membrane; Peripheral membrane
protein. Nucleus. Note=In colorectal cancer tissue, expression is
concentrated at the lateral membrane of epithelial cells.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane
{ECO:0000269|PubMed:21804599}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=beta;
IsoId=O60346-1; Sequence=Displayed;
Name=2; Synonyms=alpha;
IsoId=O60346-2; Sequence=VSP_057809;
-!- TISSUE SPECIFICITY: 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. {ECO:0000269|PubMed:15808505,
ECO:0000269|PubMed:19079341}.
-!- DOMAIN: The PH domain is required for interaction with PRKCB and
its dephosphorylation.
-!- SEQUENCE CAUTION:
Sequence=AAH14927.3; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH82244.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAI26278.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAA91980.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PHLPP1ID44544ch18q21.html";
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EMBL; AC015989; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC022046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC027553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB011178; BAA25532.2; -; mRNA.
EMBL; BC010706; AAH10706.1; -; mRNA.
EMBL; BC014927; AAH14927.3; ALT_INIT; mRNA.
EMBL; BC047653; AAH47653.1; -; mRNA.
EMBL; BC063519; AAH63519.1; -; mRNA.
EMBL; BC082244; AAH82244.1; ALT_SEQ; mRNA.
EMBL; BC126277; AAI26278.1; ALT_INIT; mRNA.
EMBL; AK001924; BAA91980.1; ALT_INIT; mRNA.
CCDS; CCDS45881.2; -. [O60346-1]
PIR; T00258; T00258.
RefSeq; NP_919431.2; NM_194449.3. [O60346-1]
UniGene; Hs.465337; -.
ProteinModelPortal; O60346; -.
BioGrid; 116843; 45.
CORUM; O60346; -.
IntAct; O60346; 32.
MINT; MINT-2796653; -.
STRING; 9606.ENSP00000262719; -.
BindingDB; O60346; -.
ChEMBL; CHEMBL3414405; -.
DEPOD; O60346; -.
iPTMnet; O60346; -.
PhosphoSitePlus; O60346; -.
BioMuta; PHLPP1; -.
EPD; O60346; -.
MaxQB; O60346; -.
PaxDb; O60346; -.
PeptideAtlas; O60346; -.
PRIDE; O60346; -.
Ensembl; ENST00000262719; ENSP00000262719; ENSG00000081913. [O60346-1]
GeneID; 23239; -.
KEGG; hsa:23239; -.
UCSC; uc021ule.2; human. [O60346-1]
CTD; 23239; -.
DisGeNET; 23239; -.
EuPathDB; HostDB:ENSG00000081913.13; -.
GeneCards; PHLPP1; -.
H-InvDB; HIX0014494; -.
H-InvDB; HIX0174202; -.
HGNC; HGNC:20610; PHLPP1.
HPA; HPA020200; -.
MIM; 609396; gene.
neXtProt; NX_O60346; -.
OpenTargets; ENSG00000081913; -.
PharmGKB; PA165429055; -.
eggNOG; KOG0619; Eukaryota.
eggNOG; COG0631; LUCA.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00440000037833; -.
InParanoid; O60346; -.
KO; K16340; -.
OMA; MSCEEEL; -.
OrthoDB; EOG091G03A3; -.
PhylomeDB; O60346; -.
TreeFam; TF315993; -.
Reactome; R-HSA-199418; Negative regulation of the PI3K/AKT network.
SIGNOR; O60346; -.
ChiTaRS; PHLPP1; human.
GeneWiki; PHLPP_(gene); -.
GenomeRNAi; 23239; -.
PRO; PR:O60346; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000081913; -.
CleanEx; HS_PHLPP; -.
ExpressionAtlas; O60346; baseline and differential.
Genevisible; O60346; HS.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0031965; C:nuclear membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0009649; P:entrainment of circadian clock; IEA:Ensembl.
GO; GO:0051898; P:negative regulation of protein kinase B signaling; IMP:UniProtKB.
GO; GO:0042981; P:regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0046328; P:regulation of JNK cascade; IDA:UniProtKB.
GO; GO:0043408; P:regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:1900744; P:regulation of p38MAPK cascade; IDA:UniProtKB.
GO; GO:0090036; P:regulation of protein kinase C signaling; IBA:GO_Central.
GO; GO:0002667; P:regulation of T cell anergy; IEA:Ensembl.
CDD; cd00143; PP2Cc; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.60.40.10; -; 1.
Gene3D; 3.80.10.10; -; 5.
InterPro; IPR032675; L_dom-like.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR011993; PH_dom-like.
InterPro; IPR001849; PH_domain.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
Pfam; PF13516; LRR_6; 2.
Pfam; PF13855; LRR_8; 2.
Pfam; PF00169; PH; 1.
Pfam; PF00481; PP2C; 1.
SMART; SM00369; LRR_TYP; 10.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF50729; SSF50729; 2.
SUPFAM; SSF52058; SSF52058; 2.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS51450; LRR; 17.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Apoptosis; Cell membrane;
Complete proteome; Cytoplasm; Hydrolase; Leucine-rich repeat;
Manganese; Membrane; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Protein phosphatase; Reference proteome; Repeat;
Tumor suppressor.
CHAIN 1 1717 PH domain leucine-rich repeat-containing
protein phosphatase 1.
/FTId=PRO_0000057781.
DOMAIN 536 636 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
REPEAT 638 659 LRR 1.
REPEAT 661 682 LRR 2.
REPEAT 692 712 LRR 3.
REPEAT 715 736 LRR 4.
REPEAT 738 760 LRR 5.
REPEAT 761 783 LRR 6.
REPEAT 784 804 LRR 7.
REPEAT 808 831 LRR 8.
REPEAT 832 853 LRR 9.
REPEAT 873 894 LRR 10.
REPEAT 895 916 LRR 11.
REPEAT 918 939 LRR 12.
REPEAT 941 962 LRR 13.
REPEAT 963 984 LRR 14.
REPEAT 987 1008 LRR 15.
REPEAT 1013 1033 LRR 16.
REPEAT 1037 1058 LRR 17.
REPEAT 1061 1082 LRR 18.
REPEAT 1084 1105 LRR 19.
REPEAT 1106 1127 LRR 20.
REPEAT 1129 1150 LRR 21.
DOMAIN 1175 1422 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
REGION 1076 1205 Interaction with SLC9A3R1.
{ECO:0000269|PubMed:21804599}.
MOTIF 1715 1717 PDZ-binding; required for interaction
with SLC9A3R1.
{ECO:0000269|PubMed:21804599}.
COMPBIAS 4 7 Poly-Ala.
COMPBIAS 21 45 Poly-Ala.
COMPBIAS 132 137 Poly-Ala.
COMPBIAS 138 144 Poly-Ser.
COMPBIAS 145 148 Poly-Ala.
COMPBIAS 254 257 Poly-Ala.
COMPBIAS 463 469 Poly-Pro.
COMPBIAS 1682 1689 Poly-Gln.
METAL 1210 1210 Manganese 1.
{ECO:0000250|UniProtKB:P35813}.
METAL 1210 1210 Manganese 2.
{ECO:0000250|UniProtKB:P35813}.
METAL 1211 1211 Manganese 1; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P35813}.
METAL 1374 1374 Manganese 2.
{ECO:0000250|UniProtKB:P35813}.
METAL 1413 1413 Manganese 2.
{ECO:0000250|UniProtKB:P35813}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 317 317 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 412 412 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 512 Missing (in isoform 2).
/FTId=VSP_057809.
VARIANT 1118 1118 S -> T (in dbSNP:rs9950585).
/FTId=VAR_056725.
MUTAGEN 1715 1717 Missing: Loss of function in vivo, but
does not abolishes intrinsic phosphatase
activity. {ECO:0000269|PubMed:15808505}.
CONFLICT 691 691 T -> A (in Ref. 5; BAA91980).
{ECO:0000305}.
CONFLICT 1062 1062 L -> F (in Ref. 4; AAH47653).
{ECO:0000305}.
CONFLICT 1083 1083 R -> S (in Ref. 2; BAA25532).
{ECO:0000305}.
CONFLICT 1227 1227 D -> V (in Ref. 5; BAA91980).
{ECO:0000305}.
CONFLICT 1490 1490 V -> M (in Ref. 4; AAH47653).
{ECO:0000305}.
CONFLICT 1580 1580 Missing (in Ref. 4; AAH63519).
{ECO:0000305}.
SEQUENCE 1717 AA; 184672 MW; A4AB53F334EA8AB6 CRC64;
MEPAAAATVQ RLPELGREDR ASAPAAAAAA AAAAAAAAAA LAAAAGGGRS PEPALTPAAP
SGGNGSGSGA REEAPGEAPP GPLPGRAGGA GRRRRRGAPQ PIAGGAAPVP GAGGGANSLL
LRRGRLKRNL SAAAAAASSS SSSSAAAASH SPGAAGLPAS CSASASLCTR SLDRKTLLLK
HRQTLQLQPS DRDWVRHQLQ RGCVHVFDRH MASTYLRPVL CTLDTTAGEV AARLLQLGHK
GGGVVKVLGQ GPGAAAAREP AEPPPEAGPR LAPPEPRDSE VPPARSAPGA FGGPPRAPPA
DLPLPVGGPG GWSRRASPAP SDSSPGEPFV GGPVSSPRAP RPVVSDTESF SLSPSAESVS
DRLDPYSSGG GSSSSSEELE ADAASAPTGV PGQPRRPGHP AQPLPLPQTA SSPQPQQKAP
RAIDSPGGAV REGSCEEKAA AAVAPGGLQS TPGRSGVTAE KAPPPPPPPT LYVQLHGETT
RRLEAEEKPL QIQNDYLFQL GFGELWRVQE EGMDSEIGCL IRFYAGKPHS TGSSERIQLS
GMYNVRKGKM QLPVNRWTRR QVILCGTCLI VSSVKDSLTG KMHVLPLIGG KVEEVKKHQH
CLAFSSSGPQ SQTYYICFDT FTEYLRWLRQ VSKVASQRIS SVDLSCCSLE HLPANLFYSQ
DLTHLNLKQN FLRQNPSLPA ARGLNELQRF TKLKSLNLSN NHLGDFPLAV CSIPTLAELN
VSCNALRSVP AAVGVMHNLQ TFLLDGNFLQ SLPAELENMK QLSYLGLSFN EFTDIPEVLE
KLTAVDKLCM SGNCVETLRL QALRKMPHIK HVDLRLNVIR KLIADEVDFL QHVTQLDLRD
NKLGDLDAMI FNNIEVLHCE RNQLVTLDIC GYFLKALYAS SNELVQLDVY PVPNYLSYMD
VSRNRLENVP EWVCESRKLE VLDIGHNQIC ELPARLFCNS SLRKLLAGHN QLARLPERLE
RTSVEVLDVQ HNQLLELPPN LLMKADSLRF LNASANKLES LPPATLSEET NSILQELYLT
NNSLTDKCVP LLTGHPHLKI LHMAYNRLQS FPASKMAKLE ELEEIDLSGN KLKAIPTTIM
NCRRMHTVIA HSNCIEVFPE VMQLPEIKCV DLSCNELSEV TLPENLPPKL QELDLTGNPR
LVLDHKTLEL LNNIRCFKID QPSTGDASGA PAVWSHGYTE ASGVKNKLCV AALSVNNFCD
NREALYGVFD GDRNVEVPYL LQCTMSDILA EELQKTKNEE EYMVNTFIVM QRKLGTAGQK
LGGAAVLCHI KHDPVDPGGS FTLTSANVGK CQTVLCRNGK PLPLSRSYIM SCEEELKRIK
QHKAIITEDG KVNGVTESTR ILGYTFLHPS VVPRPHVQSV LLTPQDEFFI LGSKGLWDSL
SVEEAVEAVR NVPDALAAAK KLCTLAQSYG CHDSISAVVV QLSVTEDSFC CCELSAGGAV
PPPSPGIFPP SVNMVIKDRP SDGLGVPSSS SGMASEISSE LSTSEMSSEV GSTASDEPPP
GALSENSPAY PSEQRCMLHP ICLSNSFQRQ LSSATFSSAF SDNGLDSDDE EPIEGVFTNG
SRVEVEVDIH CSRAKEKEKQ QHLLQVPAEA SDEGIVISAN EDEPGLPRKA DFSAVGTIGR
RRANGSVAPQ ERSHNVIEVA TDAPLRKPGG YFAAPAQPDP DDQFIIPPEL EEEVKEIMKH
HQEQQQQQQP PPPPQLQPQL PRHYQLDQLP DYYDTPL


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