PKHA2_MOUSE
ID PKHA2_MOUSE Reviewed; 425 AA.
AC Q9ERS5; Q8BY29;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Pleckstrin homology domain-containing family A member 2;
DE Short=PH domain-containing family A member 2;
DE AltName: Full=PH domain-containing adaptor PHAD47;
DE AltName: Full=Tandem PH domain-containing protein 2;
DE Short=TAPP-2;
GN Name=Plekha2; Synonyms=Tapp2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11001876; DOI=10.1042/0264-6021:3510019;
RA Dowler S.J., Currie R.A., Campbell D.G., Deak M., Kular G., Downes C.P.,
RA Alessi D.R.;
RT "Identification of pleckstrin-homology-domain-containing proteins with
RT novel phosphoinositide-binding specificities.";
RL Biochem. J. 351:19-31(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=BALB/cJ;
RX PubMed=12101241; DOI=10.1128/mcb.22.15.5479-5491.2002;
RA Marshall A.J., Krahn A.K., Ma K., Duronio V., Hou S.;
RT "TAPP1 and TAPP2 are targets of phosphatidylinositol 3-kinase signaling in
RT B cells: sustained plasma membrane recruitment triggered by the B-cell
RT antigen receptor.";
RL Mol. Cell. Biol. 22:5479-5491(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Olfactory bulb, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH MPDZ.
RX PubMed=11802782; DOI=10.1042/0264-6021:3610525;
RA Kimber W.A., Trinkle-Mulcahy L., Cheung P.C.F., Deak M., Marsden L.J.,
RA Kieloch A., Watt S., Javier R.T., Gray A., Downes C.P., Lucocq J.M.,
RA Alessi D.R.;
RT "Evidence that the tandem-pleckstrin-homology-domain-containing protein
RT TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein
RT MUPP1 in vivo.";
RL Biochem. J. 361:525-536(2002).
RN [6]
RP INTERACTION WITH PTPN13, AND FUNCTION.
RX PubMed=14516276; DOI=10.1042/bj20031154;
RA Kimber W.A., Deak M., Prescott A.R., Alessi D.R.;
RT "Interaction of the protein tyrosine phosphatase PTPL1 with the
RT PtdIns(3,4)P2-binding adaptor protein TAPP1.";
RL Biochem. J. 376:525-535(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP STRUCTURE BY NMR OF 1-113.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the N-terminal pleckstrin homology domain of TAPP2
RT from mouse.";
RL Submitted (MAY-2004) to the PDB data bank.
CC -!- FUNCTION: Binds specifically to phosphatidylinositol 3,4-diphosphate
CC (PtdIns3,4P2), but not to other phosphoinositides. May recruit other
CC proteins to the plasma membrane. {ECO:0000269|PubMed:12101241,
CC ECO:0000269|PubMed:14516276}.
CC -!- SUBUNIT: Binds MPDZ and PTPN13.
CC -!- INTERACTION:
CC Q9ERS5; O75970: MPDZ; Xeno; NbExp=5; IntAct=EBI-8079166, EBI-821405;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12101241}. Cell
CC membrane {ECO:0000269|PubMed:12101241}; Peripheral membrane protein
CC {ECO:0000269|PubMed:12101241}. Nucleus {ECO:0000269|PubMed:12101241}.
CC Note=Locates to the plasma membrane after treatments that stimulate the
CC production of PtdIns3,4P2.
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DR EMBL; AF286161; AAG15198.1; -; mRNA.
DR EMBL; AF418551; AAL57436.1; -; mRNA.
DR EMBL; AK042324; BAC31224.2; -; mRNA.
DR EMBL; AK078212; BAC37176.1; -; mRNA.
DR EMBL; AK088395; BAC40325.1; -; mRNA.
DR EMBL; BC010215; AAH10215.1; -; mRNA.
DR CCDS; CCDS22198.1; -.
DR RefSeq; NP_112547.1; NM_031257.3.
DR RefSeq; XP_006509290.1; XM_006509227.2.
DR RefSeq; XP_006509291.1; XM_006509228.3.
DR RefSeq; XP_006509293.1; XM_006509230.2.
DR PDB; 1V5P; NMR; -; A=1-113.
DR PDBsum; 1V5P; -.
DR AlphaFoldDB; Q9ERS5; -.
DR BMRB; Q9ERS5; -.
DR SMR; Q9ERS5; -.
DR IntAct; Q9ERS5; 2.
DR MINT; Q9ERS5; -.
DR STRING; 10090.ENSMUSP00000122564; -.
DR iPTMnet; Q9ERS5; -.
DR PhosphoSitePlus; Q9ERS5; -.
DR EPD; Q9ERS5; -.
DR jPOST; Q9ERS5; -.
DR MaxQB; Q9ERS5; -.
DR PaxDb; Q9ERS5; -.
DR PRIDE; Q9ERS5; -.
DR ProteomicsDB; 289899; -.
DR Antibodypedia; 1200; 18 antibodies from 9 providers.
DR DNASU; 83436; -.
DR Ensembl; ENSMUST00000064883; ENSMUSP00000066546; ENSMUSG00000031557.
DR Ensembl; ENSMUST00000128715; ENSMUSP00000122564; ENSMUSG00000031557.
DR GeneID; 83436; -.
DR KEGG; mmu:83436; -.
DR UCSC; uc009lfq.3; mouse.
DR CTD; 59339; -.
DR MGI; MGI:1928144; Plekha2.
DR VEuPathDB; HostDB:ENSMUSG00000031557; -.
DR eggNOG; ENOG502QV0M; Eukaryota.
DR GeneTree; ENSGT00940000158064; -.
DR InParanoid; Q9ERS5; -.
DR OMA; QANHLLW; -.
DR OrthoDB; 1513983at2759; -.
DR PhylomeDB; Q9ERS5; -.
DR TreeFam; TF329516; -.
DR Reactome; R-MMU-1660499; Synthesis of PIPs at the plasma membrane.
DR BioGRID-ORCS; 83436; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Plekha2; mouse.
DR EvolutionaryTrace; Q9ERS5; -.
DR PRO; PR:Q9ERS5; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q9ERS5; protein.
DR Bgee; ENSMUSG00000031557; Expressed in peripheral lymph node and 236 other tissues.
DR ExpressionAtlas; Q9ERS5; baseline and differential.
DR Genevisible; Q9ERS5; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001968; F:fibronectin binding; ISO:MGI.
DR GO; GO:0043236; F:laminin binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; IPI:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IDA:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cytoplasm; Isopeptide bond; Lipid-binding;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..425
FT /note="Pleckstrin homology domain-containing family A
FT member 2"
FT /id="PRO_0000053877"
FT DOMAIN 7..113
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 198..298
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 310..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..331
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..425
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB19"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB19"
FT MOD_RES 349
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9HB19"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9HB19"
FT CONFLICT 240
FT /note="R -> H (in Ref. 3; BAC31224)"
FT /evidence="ECO:0000305"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:1V5P"
FT STRAND 25..33
FT /evidence="ECO:0007829|PDB:1V5P"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1V5P"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:1V5P"
FT TURN 46..48
FT /evidence="ECO:0007829|PDB:1V5P"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1V5P"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1V5P"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1V5P"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:1V5P"
FT STRAND 79..85
FT /evidence="ECO:0007829|PDB:1V5P"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:1V5P"
FT HELIX 98..110
FT /evidence="ECO:0007829|PDB:1V5P"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1V5P"
SQ SEQUENCE 425 AA; 47380 MW; 6666F5DB303B2CBA CRC64;
MPYVDRQNRI CGFLDIEDNE NSGKFLRRYF ILDTQANCLL WYMDNPQNLA VGAGAVGSLQ
LTYISKVSIA TPKQKPKTPF CFVINALSQR YFLQANDQKD LKDWVEALNQ ASKITVPKAG
TVPLATEVLK NLTAPPTLEK KPQVAYKTEI IGGVVVQTPI SQNGGDGQEG CEPGTHAFLR
RSQSYIPTSG CRPSTGPPLI KSGYCVKQGN VRKSWKRRFF ALDDFTICYF KCEQDREPLR
TIPLKDVLKT HECLVKSGDL LMRDNLFEII TTSRTFYVQA DSPEDMHSWI EGIGAAVQAL
KCHPREPSFS RSISLTRPGS STLTSAPNSI LSRRRPPAEE KRGLCKAPSV ASSWQPWTPV
PQAEEKPLSV EHAPEDSLFM PNPGESTATG VLASSRVRHR SEPQHPKEKP FVFNLDDENI
RTSDV
