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Protein

PH domain leucine-rich repeat-containing protein phosphatase 2

Gene

PHLPP2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 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

Mn2+By similarityNote: 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
Complete GO annotation...

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
Complete GO annotation...

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

DEPODiQ6ZVD8.
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

BgeeiQ6ZVD8.
CleanExiHS_PHLPPL.
ExpressionAtlasiQ6ZVD8. baseline and differential.
GenevestigatoriQ6ZVD8.

Organism-specific databases

HPAiHPA048598.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ6ZVD8.
SMRiQ6ZVD8. Positions 222-1033.
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.
GeneTreeiENSGT00440000037833.
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

        10         20         30         40         50
MKRNGSRNCL NRRSRFGSRE RDWLREDVKR GCVYLYGADT TTATTTTTTS
60 70 80 90 100
SSSSSSSSSS DLHLVLCTVE TPASEICAGE GRESLYLQLH GDLVRRLEPT
110 120 130 140 150
ERPLQIVYDY LSRLGFDDPV RIQEEATNPD LGCMIRFYGE KPCHMDRLDR
160 170 180 190 200
ILLSGIYNVR KGKTQLHKWA ERLVVLCGTC LIVSSVKDCQ TGKMHILPLV
210 220 230 240 250
GGKIEEVKRR QYSLAFSSAG AQAQTYHVSF ETLAEYQRWQ RQASKVVSQR
260 270 280 290 300
ISTVDLSCYS LEEVPEHLFY SQDITYLNLR HNFMQLERPG GLDTLYKFSQ
310 320 330 340 350
LKGLNLSHNK LGLFPILLCE ISTLTELNLS CNGFHDLPSQ IGNLLNLQTL
360 370 380 390 400
CLDGNFLTTL PEELGNLQQL SSLGISFNNF SQIPEVYEKL TMLDRVVMAG
410 420 430 440 450
NCLEVLNLGV LNRMNHIKHV DLRMNHLKTM VIENLEGNKH ITHVDLRDNR
460 470 480 490 500
LTDLDLSSLC SLEQLHCGRN QLRELTLSGF SLRTLYASSN RLTAVNVYPV
510 520 530 540 550
PSLLTFLDLS RNLLECVPDW ACEAKKIEVL DVSYNLLTEV PVRILSSLSL
560 570 580 590 600
RKLMLGHNHV QNLPTLVEHI PLEVLDLQHN ALTRLPDTLF SKALNLRYLN
610 620 630 640 650
ASANSLESLP SACTGEESLS MLQLLYLTNN LLTDQCIPVL VGHLHLRILH
660 670 680 690 700
LANNQLQTFP ASKLNKLEQL EELNLSGNKL KTIPTTIANC KRLHTLVAHS
710 720 730 740 750
NNISIFPEIL QLPQIQFVDL SCNDLTEILI PEALPATLQD LDLTGNTNLV
760 770 780 790 800
LEHKTLDIFS HITTLKIDQK PLPTTDSTVT STFWSHGLAE MAGQRNKLCV
810 820 830 840 850
SALAMDSFAE GVGAVYGMFD GDRNEELPRL LQCTMADVLL EEVQQSTNDT
860 870 880 890 900
VFMANTFLVS HRKLGMAGQK LGSSALLCYI RPDTADPASS FSLTVANVGT
910 920 930 940 950
CQAVLCRGGK PVPLSKVFSL EQDPEEAQRV KDQKAIITED NKVNGVTCCT
960 970 980 990 1000
RMLGCTYLYP WILPKPHISS TPLTIQDELL ILGNKALWEH LSYTEAVNAV
1010 1020 1030 1040 1050
RHVQDPLAAA KKLCTLAQSY GCQDNVGAMV VYLNIGEEGC TCEMNGLTLP
1060 1070 1080 1090 1100
GPVGFASTTT IKDAPKPATP SSSSGIASEF SSEMSTSEVS SEVGSTASDE
1110 1120 1130 1140 1150
HNAGGLDTAL LPRPERRCSL HPTPTSGLFQ RQPSSATFSS NQSDNGLDSD
1160 1170 1180 1190 1200
DDQPVEGVIT NGSKVEVEVD IHCCRGRDLE NSPPLIESSP TLCSEEHARG
1210 1220 1230 1240 1250
SCFGIRRQNS VNSGMLLPMS KDRMELQKSP STSCLYGKKL SNGSIVPLED
1260 1270 1280 1290 1300
SLNLIEVATE VPKRKTGYFA APTQMEPEDQ FVVPHDLEEE VKEQMKQHQD
1310 1320
SRLEPEPHEE DRTEPPEEFD TAL
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. Curated
The sequence BAA91943.1 differs from that shown. Reason: Erroneous initiation. Curated

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:
EMBLi
GenBanki
DDBJi
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]
CCDS73910.1. [Q6ZVD8-3]
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:
EMBLi
GenBanki
DDBJi
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]
CCDS73910.1. [Q6ZVD8-3]
RefSeqiNP_001275932.1. NM_001289003.1. [Q6ZVD8-3]
NP_055835.2. NM_015020.3. [Q6ZVD8-1]
UniGeneiHs.709458.

3D structure databases

ProteinModelPortaliQ6ZVD8.
SMRiQ6ZVD8. Positions 222-1033.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

BindingDBiQ6ZVD8.
ChEMBLiCHEMBL1275209.

PTM databases

DEPODiQ6ZVD8.
PhosphoSiteiQ6ZVD8.

Polymorphism databases

DMDMi116242711.

Proteomic databases

MaxQBiQ6ZVD8.
PaxDbiQ6ZVD8.
PRIDEiQ6ZVD8.

Protocols and materials databases

DNASUi23035.
Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi23035.
GeneCardsiGC16M071674.
H-InvDBHIX0013215.
HIX0173315.
HGNCiHGNC:29149. PHLPP2.
HPAiHPA048598.
MIMi611066. gene.
neXtProtiNX_Q6ZVD8.
PharmGKBiPA165450496.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00440000037833.
HOGENOMiHOG000115529.
InParanoidiQ6ZVD8.
KOiK16340.
PhylomeDBiQ6ZVD8.
TreeFamiTF315993.

Enzyme and pathway databases

ReactomeiREACT_12447. Negative regulation of the PI3K/AKT network.

Miscellaneous databases

ChiTaRSiPHLPP2. human.
GeneWikiiPHLPPL.
GenomeRNAii23035.
NextBioi44034.
PROiQ6ZVD8.
SOURCEiSearch...

Gene expression databases

BgeeiQ6ZVD8.
CleanExiHS_PHLPPL.
ExpressionAtlasiQ6ZVD8. baseline and differential.
GenevestigatoriQ6ZVD8.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: January 7, 2015
This is version 112 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.