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Q8BXA7

- PHLP2_MOUSE

UniProt

Q8BXA7 - PHLP2_MOUSE

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Protein
PH domain leucine-rich repeat-containing protein phosphatase 2
Gene
Phlpp2, Phlppl
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Protein phosphatase that mediates dephosphorylation of 'Ser-473' of AKT1, 'Ser-660' of PRKCB 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 By similarity.

Catalytic activityi

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

Cofactori

Binds 2 manganese ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi817 – 8171Manganese 1 By similarity
Metal bindingi817 – 8171Manganese 2 By similarity
Metal bindingi818 – 8181Manganese 1; via carbonyl oxygen By similarity
Metal bindingi982 – 9821Manganese 2 By similarity
Metal bindingi1021 – 10211Manganese 2 By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. phosphoprotein phosphatase activity Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_214733. 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:Phlppl
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:2444928. Phlpp2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. membrane Source: UniProtKB-SubCell
  3. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Keywords - Diseasei

Tumor suppressor

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13201320PH domain leucine-rich repeat-containing protein phosphatase 2
PRO_0000057785Add
BLAST

Proteomic databases

MaxQBiQ8BXA7.
PaxDbiQ8BXA7.
PRIDEiQ8BXA7.

PTM databases

PhosphoSiteiQ8BXA7.

Expressioni

Gene expression databases

ArrayExpressiQ8BXA7.
BgeeiQ8BXA7.
GenevestigatoriQ8BXA7.

Interactioni

Subunit structurei

Interacts with AKT1, AKT3 and PRKCB By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ8BXA7.
SMRiQ8BXA7. Positions 248-763, 810-1030.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 24599PH
Add
BLAST
Repeati247 – 26822LRR 1
Add
BLAST
Repeati270 – 29324LRR 2
Add
BLAST
Repeati297 – 31822LRR 3
Add
BLAST
Repeati320 – 34122LRR 4
Add
BLAST
Repeati343 – 36422LRR 5
Add
BLAST
Repeati366 – 38823LRR 6
Add
BLAST
Repeati389 – 40921LRR 7
Add
BLAST
Repeati413 – 43422LRR 8
Add
BLAST
Repeati437 – 45721LRR 9
Add
BLAST
Repeati458 – 47720LRR 10
Add
BLAST
Repeati478 – 49922LRR 11
Add
BLAST
Repeati500 – 52122LRR 12
Add
BLAST
Repeati523 – 54422LRR 13
Add
BLAST
Repeati546 – 56722LRR 14
Add
BLAST
Repeati568 – 58922LRR 15
Add
BLAST
Repeati592 – 61322LRR 16
Add
BLAST
Repeati618 – 64124LRR 17
Add
BLAST
Repeati642 – 66322LRR 18
Add
BLAST
Repeati666 – 68722LRR 19
Add
BLAST
Repeati689 – 71022LRR 20
Add
BLAST
Repeati711 – 73222LRR 21
Add
BLAST
Repeati734 – 75522LRR 22
Add
BLAST
Domaini772 – 1028257PP2C-like
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi40 – 478Poly-Thr
Compositional biasi48 – 5710Poly-Ser
Compositional biasi1068 – 10714Poly-Ser

Sequence similaritiesi

Contains 1 PH domain.
Contains 1 PP2C-like domain.

Keywords - Domaini

Leucine-rich repeat, Repeat

Phylogenomic databases

eggNOGiCOG4886.
GeneTreeiENSGT00440000037833.
HOGENOMiHOG000115529.
HOVERGENiHBG062748.
InParanoidiQ148U6.
KOiK16340.
OrthoDBiEOG7RFTGK.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.60.40.10. 1 hit.
InterProiIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR011993. PH_like_dom.
IPR001932. PP2C-like_dom.
[Graphical view]
PfamiPF12799. LRR_4. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 3 hits.
PF00481. PP2C. 1 hit.
[Graphical view]
SMARTiSM00369. LRR_TYP. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]
SUPFAMiSSF81606. SSF81606. 1 hit.
PROSITEiPS51450. LRR. 17 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BXA7-1 [UniParc]FASTAAdd to Basket

« Hide

MKHNGSRTCL NRRSRFGSRE RDWLREDVKR GCVYLYGADT TTATTTTSSS     50
SSSSSSSDLH LVLCTVETPA SEICAGEGRE SLYLQLHGDL VRRLEPSERP 100
LQIVYDYLSR LGFEDPVRIQ EEATNPDLSC MIRFYGEKPC QMDHLDRILL 150
SGIYNVRKGK TQLHKWAERL VVLCGTCLIV SSVKDCQTGK MHILPLVGGK 200
IEEVKRRQHS LAFSSAGAQA QTYHVSFETL AEYQRWQRQA SKVVSQRMST 250
VDLSCYSLEE VPEHLFYSQD ITYLNLRHNF MQLERPGGLD TLHKFSQLKG 300
LNLSHNKLGL FPVLLCEIST LTELSLSCNG FHDLPSQIGK LLNLQTLSLD 350
GNGLTALPDE LGNLRQLTSL GISFNDFRHI PEVLEKLTML DKVAMAGNRL 400
EVLNLGALTR MSQVKHVDLR MNHLKTVITE NMEGNKHITH MDLRDNQLTD 450
LDLSSLCSLE QLHCERNQLR ELTLSGFSLR TLYASWNRLT AVNVYPVPSL 500
LTSLELSQNL LECVPDWACE AKKLEILDIS HNLLTEVPMR ILSSLSLRKL 550
MVGHNHIHVL PALVEHIPLE VLDIQHNTLS RLPDTLFSKA LNLRYLNASA 600
NSLESLPSAC AGEESLSVLQ LLYLTSNLLT DQCIPVLVGH PHLRVLHLAN 650
NQLQTFPASK LNKLEQLEEL NLSGNKLTAI PTTIANCKRL HTLVAHANNI 700
SIFPEILQLP QIQFVDLSCN DLTEILIPEA LPATLQDLDL TGNTNLVLEH 750
KTLDMFSHIT ALKIDQKPLP ATDSAVTSTF WSHGLAEMAG QRNKLCVSAL 800
AMDNFAEGVG AVYGMFDGDR NEELPRLLQC TMADVLLEEV QHSTNDTVFM 850
TNTFLVSHRK LGMAGQKLGS SALLCYIRPD TADPTSSFSL TVANVGMCQA 900
VLCRGGKPVP LSKVFSLEHD PEEAQRVKDQ KAIITEDNKV NGVTCCTRLL 950
GCTYLYPWIL PKPHIASTPL TIQDELLILG NKALWEHLSY LEAVNAVRHV 1000
QDPLAAAKKL CTLAQSYGCQ DNVGAMVVYL NIGEEGCTCE MNGLTLPGPV 1050
GFASTAALKD TPKPTTPSSS SGIASEFSSE MSTSEVSSEV GSTASDEHNT 1100
VGLEASLLPR PERRCSLHPA SSAGVFQRQP SCATFSSNQS DNGLDSDDDQ 1150
PVEGVITNGS RVEVEVDIHC CRGREPESSP PLPKNSSNAC SEERARGAGF 1200
GIRRQNSVNS GILLPANRDK MELQKSPSTS CLYGKKLSNG SIVPLEDSLN 1250
LIEVATEAPK RKTGYFAAPT QLEPEDQFVV PRDLEEEVKE QMKQHQEGRP 1300
EPEPRGEERT EPLEEFDTAL 1320
Length:1,320
Mass (Da):145,947
Last modified:July 27, 2011 - v3
Checksum:i302407C231BD539B
GO

Sequence cautioni

The sequence BAC33347.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti67 – 671E → Q in BAC33288. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC122807 Genomic DNA. No translation available.
BC117961 mRNA. Translation: AAI17962.1.
BC117962 mRNA. Translation: AAI17963.1.
AK048260 mRNA. Translation: BAC33288.1.
AK048472 mRNA. Translation: BAC33347.2. Different initiation.
RefSeqiNP_001116066.2. NM_001122594.2.
UniGeneiMm.23494.

Genome annotation databases

EnsembliENSMUST00000034175; ENSMUSP00000034175; ENSMUSG00000031732.
GeneIDi244650.
KEGGimmu:244650.
UCSCiuc009njn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AC122807 Genomic DNA. No translation available.
BC117961 mRNA. Translation: AAI17962.1 .
BC117962 mRNA. Translation: AAI17963.1 .
AK048260 mRNA. Translation: BAC33288.1 .
AK048472 mRNA. Translation: BAC33347.2 . Different initiation.
RefSeqi NP_001116066.2. NM_001122594.2.
UniGenei Mm.23494.

3D structure databases

ProteinModelPortali Q8BXA7.
SMRi Q8BXA7. Positions 248-763, 810-1030.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q8BXA7.

Proteomic databases

MaxQBi Q8BXA7.
PaxDbi Q8BXA7.
PRIDEi Q8BXA7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034175 ; ENSMUSP00000034175 ; ENSMUSG00000031732 .
GeneIDi 244650.
KEGGi mmu:244650.
UCSCi uc009njn.2. mouse.

Organism-specific databases

CTDi 23035.
MGIi MGI:2444928. Phlpp2.

Phylogenomic databases

eggNOGi COG4886.
GeneTreei ENSGT00440000037833.
HOGENOMi HOG000115529.
HOVERGENi HBG062748.
InParanoidi Q148U6.
KOi K16340.
OrthoDBi EOG7RFTGK.

Enzyme and pathway databases

Reactomei REACT_214733. Negative regulation of the PI3K/AKT network.

Miscellaneous databases

ChiTaRSi PHLPP2. mouse.
NextBioi 386351.
PROi Q8BXA7.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BXA7.
Bgeei Q8BXA7.
Genevestigatori Q8BXA7.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.60.40.10. 1 hit.
InterProi IPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR011993. PH_like_dom.
IPR001932. PP2C-like_dom.
[Graphical view ]
Pfami PF12799. LRR_4. 1 hit.
PF13504. LRR_7. 1 hit.
PF13855. LRR_8. 3 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. 17 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "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].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1259.
    Strain: C57BL/6J.
    Tissue: Head.
  4. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiPHLP2_MOUSE
AccessioniPrimary (citable) accession number: Q8BXA7
Secondary accession number(s): Q148U6, Q8BX96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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