Q8BXA7 (PHLP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Phlpp2
Synonyms:	Phlppl

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1320 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	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 activity	A phosphoprotein + H2O = a protein + phosphate.
Cofactor	Binds 2 manganese ions per subunit By similarity.
Subunit structure	Interacts with AKT1, AKT3 and PRKCB By similarity.
Subcellular location	Cytoplasm. Membrane; Peripheral membrane protein. Nucleus By similarity.
Sequence similarities	Contains 22 LRR (leucine-rich) repeats. Contains 1 PH domain. Contains 1 PP2C-like domain.
Sequence caution	The sequence BAC33347.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane Nucleus
Disease	Tumor suppressor
Domain	Leucine-rich repeat Repeat
Ligand	Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	metabolic process Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1320	1320	PH domain leucine-rich repeat-containing protein phosphatase 2		PRO_0000057785
Regions
	Domain	147 – 245	99	PH
	Repeat	247 – 268	22	LRR 1
	Repeat	270 – 293	24	LRR 2
	Repeat	297 – 318	22	LRR 3
	Repeat	320 – 341	22	LRR 4
	Repeat	343 – 364	22	LRR 5
	Repeat	366 – 388	23	LRR 6
	Repeat	389 – 409	21	LRR 7
	Repeat	413 – 434	22	LRR 8
	Repeat	437 – 457	21	LRR 9
	Repeat	458 – 477	20	LRR 10
	Repeat	478 – 499	22	LRR 11
	Repeat	500 – 521	22	LRR 12
	Repeat	523 – 544	22	LRR 13
	Repeat	546 – 567	22	LRR 14
	Repeat	568 – 589	22	LRR 15
	Repeat	592 – 613	22	LRR 16
	Repeat	618 – 641	24	LRR 17
	Repeat	642 – 663	22	LRR 18
	Repeat	666 – 687	22	LRR 19
	Repeat	689 – 710	22	LRR 20
	Repeat	711 – 732	22	LRR 21
	Repeat	734 – 755	22	LRR 22
	Domain	772 – 1028	257	PP2C-like
	Compositional bias	40 – 47	8	Poly-Thr
	Compositional bias	48 – 57	10	Poly-Ser
	Compositional bias	1068 – 1071	4	Poly-Ser
Sites
	Metal binding	817	1	Manganese 1 By similarity
	Metal binding	817	1	Manganese 2 By similarity
	Metal binding	818	1	Manganese 1; via carbonyl oxygen By similarity
	Metal binding	982	1	Manganese 2 By similarity
	Metal binding	1021	1	Manganese 2 By similarity
Experimental info
	Sequence conflict	67	1	E → Q in BAC33288. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8BXA7 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 302407C231BD539B	FASTA	1,320	145,947
	10 20 30 40 50 60 MKHNGSRTCL NRRSRFGSRE RDWLREDVKR GCVYLYGADT TTATTTTSSS SSSSSSSDLH 70 80 90 100 110 120 LVLCTVETPA SEICAGEGRE SLYLQLHGDL VRRLEPSERP LQIVYDYLSR LGFEDPVRIQ 130 140 150 160 170 180 EEATNPDLSC MIRFYGEKPC QMDHLDRILL SGIYNVRKGK TQLHKWAERL VVLCGTCLIV 190 200 210 220 230 240 SSVKDCQTGK MHILPLVGGK IEEVKRRQHS LAFSSAGAQA QTYHVSFETL AEYQRWQRQA 250 260 270 280 290 300 SKVVSQRMST VDLSCYSLEE VPEHLFYSQD ITYLNLRHNF MQLERPGGLD TLHKFSQLKG 310 320 330 340 350 360 LNLSHNKLGL FPVLLCEIST LTELSLSCNG FHDLPSQIGK LLNLQTLSLD GNGLTALPDE 370 380 390 400 410 420 LGNLRQLTSL GISFNDFRHI PEVLEKLTML DKVAMAGNRL EVLNLGALTR MSQVKHVDLR 430 440 450 460 470 480 MNHLKTVITE NMEGNKHITH MDLRDNQLTD LDLSSLCSLE QLHCERNQLR ELTLSGFSLR 490 500 510 520 530 540 TLYASWNRLT AVNVYPVPSL LTSLELSQNL LECVPDWACE AKKLEILDIS HNLLTEVPMR 550 560 570 580 590 600 ILSSLSLRKL MVGHNHIHVL PALVEHIPLE VLDIQHNTLS RLPDTLFSKA LNLRYLNASA 610 620 630 640 650 660 NSLESLPSAC AGEESLSVLQ LLYLTSNLLT DQCIPVLVGH PHLRVLHLAN NQLQTFPASK 670 680 690 700 710 720 LNKLEQLEEL NLSGNKLTAI PTTIANCKRL HTLVAHANNI SIFPEILQLP QIQFVDLSCN 730 740 750 760 770 780 DLTEILIPEA LPATLQDLDL TGNTNLVLEH KTLDMFSHIT ALKIDQKPLP ATDSAVTSTF 790 800 810 820 830 840 WSHGLAEMAG QRNKLCVSAL AMDNFAEGVG AVYGMFDGDR NEELPRLLQC TMADVLLEEV 850 860 870 880 890 900 QHSTNDTVFM TNTFLVSHRK LGMAGQKLGS SALLCYIRPD TADPTSSFSL TVANVGMCQA 910 920 930 940 950 960 VLCRGGKPVP LSKVFSLEHD PEEAQRVKDQ KAIITEDNKV NGVTCCTRLL GCTYLYPWIL 970 980 990 1000 1010 1020 PKPHIASTPL TIQDELLILG NKALWEHLSY LEAVNAVRHV QDPLAAAKKL CTLAQSYGCQ 1030 1040 1050 1060 1070 1080 DNVGAMVVYL NIGEEGCTCE MNGLTLPGPV GFASTAALKD TPKPTTPSSS SGIASEFSSE 1090 1100 1110 1120 1130 1140 MSTSEVSSEV GSTASDEHNT VGLEASLLPR PERRCSLHPA SSAGVFQRQP SCATFSSNQS 1150 1160 1170 1180 1190 1200 DNGLDSDDDQ PVEGVITNGS RVEVEVDIHC CRGREPESSP PLPKNSSNAC SEERARGAGF 1210 1220 1230 1240 1250 1260 GIRRQNSVNS GILLPANRDK MELQKSPSTS CLYGKKLSNG SIVPLEDSLN LIEVATEAPK 1270 1280 1290 1300 1310 1320 RKTGYFAAPT QLEPEDQFVV PRDLEEEVKE QMKQHQEGRP EPEPRGEERT EPLEEFDTAL

References

[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00890064.
RefSeq	NP_001116066.2. NM_001122594.2.
UniGene	Mm.23494.
3D structure databases
ProteinModelPortal	Q8BXA7.
SMR	Q8BXA7. Positions 248-769, 783-1030.
ModBase	Search...
PTM databases
PhosphoSite	Q8BXA7.
Proteomic databases
PaxDb	Q8BXA7.
PRIDE	Q8BXA7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000034175; ENSMUSP00000034175; ENSMUSG00000031732.
GeneID	244650.
KEGG	mmu:244650.
Organism-specific databases
CTD	23035.
MGI	MGI:2444928. Phlpp2.
Phylogenomic databases
eggNOG	COG4886.
GeneTree	ENSGT00440000037833.
HOGENOM	HOG000115529.
HOVERGEN	HBG062748.
InParanoid	Q148U6.
KO	K16340.
OrthoDB	EOG48PMJB.
Gene expression databases
Bgee	Q8BXA7.
Genevestigator	Q8BXA7.
GermOnline	ENSMUSG00000031732. Mus musculus.
Family and domain databases
Gene3D	2.30.29.30. 1 hit. 3.60.40.10. 1 hit.
InterPro	IPR001611. Leu-rich_rpt. IPR025875. Leu-rich_rpt_4. IPR003591. Leu-rich_rpt_typical-subtyp. IPR011993. PH_like_dom. IPR001932. PP2C-like. [Graphical view]
Pfam	PF00560. LRR_1. 1 hit. PF12799. LRR_4. 1 hit. PF00481. PP2C. 1 hit. [Graphical view]
SMART	SM00369. LRR_TYP. 1 hit. SM00332. PP2Cc. 1 hit. [Graphical view]
SUPFAM	SSF81606. PP2C-related. 1 hit.
PROSITE	PS51450. LRR. 17 hits. PS50003. PH_DOMAIN. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	PHLPP2. mouse.
NextBio	386351.
SOURCE	Search...

Entry information

Entry name

PHLP2_MOUSE

Accession

Primary (citable) accession number: Q8BXA7
Secondary accession number(s): Q148U6, Q8BX96

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program