PHLB2_MOUSE
ID PHLB2_MOUSE Reviewed; 1249 AA.
AC Q8K1N2; Q3TNI3; Q80Y16; Q8BKV3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Pleckstrin homology-like domain family B member 2;
DE AltName: Full=Protein LL5-beta;
GN Name=Phldb2; Synonyms=Ll5b;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=BALB/cJ;
RA Guo J.H., Yu L.;
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-793 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Spleen;
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 PROTEIN SEQUENCE OF 570-579 AND 698-705, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15851520; DOI=10.1083/jcb.200411012;
RA Kishi M., Kummer T.T., Eglen S.J., Sanes J.R.;
RT "LL5beta: a regulator of postsynaptic differentiation identified in a
RT screen for synaptically enriched transcripts at the neuromuscular
RT junction.";
RL J. Cell Biol. 169:355-366(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510 AND THR-546, AND
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465 AND SER-510, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203; SER-241; SER-244;
RP SER-329; SER-333; SER-347; SER-380; SER-383; SER-389; SER-465; SER-486;
RP SER-510 AND THR-546, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
CC -!- FUNCTION: Seems to be involved in the assembly of the postsynaptic
CC apparatus. May play a role in acetyl-choline receptor (AChR)
CC aggregation in the postsynaptic membrane.
CC {ECO:0000269|PubMed:15851520}.
CC -!- SUBUNIT: Interacts with FLNC. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Note=Translocates to the
CC plasma membrane at high levels of PtdIns(3,4,5)P3. At low levels of
CC PtdIns(3,4,5)P3 is translocated to vesicular compartments (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K1N2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K1N2-2; Sequence=VSP_016746;
CC -!- TISSUE SPECIFICITY: Expressed at postsynaptic membranes of skeletal
CC neuromuscular junctions (at protein level).
CC {ECO:0000269|PubMed:15851520}.
CC -!- DEVELOPMENTAL STAGE: In synapses, is expressed at embryonic day 15 and
CC colocalizes with acetyl-choline receptor at prenatal day 4. Expression
CC decreases in adult. {ECO:0000269|PubMed:15851520}.
CC -!- DOMAIN: The PH domain mediates the binding to phosphoinositides.
CC {ECO:0000250}.
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DR EMBL; AF506821; AAM33635.1; -; mRNA.
DR EMBL; BC050915; AAH50915.1; -; mRNA.
DR EMBL; BC060683; AAH60683.1; -; mRNA.
DR EMBL; AK049595; BAC33833.1; -; mRNA.
DR EMBL; AK165251; BAE38105.1; -; mRNA.
DR CCDS; CCDS28202.1; -. [Q8K1N2-1]
DR CCDS; CCDS57031.1; -. [Q8K1N2-2]
DR RefSeq; NP_001239371.1; NM_001252442.1. [Q8K1N2-2]
DR RefSeq; NP_700461.2; NM_153412.4. [Q8K1N2-1]
DR AlphaFoldDB; Q8K1N2; -.
DR SMR; Q8K1N2; -.
DR BioGRID; 228960; 3.
DR IntAct; Q8K1N2; 3.
DR STRING; 10090.ENSMUSP00000046496; -.
DR iPTMnet; Q8K1N2; -.
DR PhosphoSitePlus; Q8K1N2; -.
DR jPOST; Q8K1N2; -.
DR MaxQB; Q8K1N2; -.
DR PaxDb; Q8K1N2; -.
DR PeptideAtlas; Q8K1N2; -.
DR PRIDE; Q8K1N2; -.
DR ProteomicsDB; 287710; -. [Q8K1N2-1]
DR ProteomicsDB; 287711; -. [Q8K1N2-2]
DR Antibodypedia; 34806; 45 antibodies from 12 providers.
DR DNASU; 208177; -.
DR Ensembl; ENSMUST00000036355; ENSMUSP00000046496; ENSMUSG00000033149. [Q8K1N2-1]
DR Ensembl; ENSMUST00000076333; ENSMUSP00000075672; ENSMUSG00000033149. [Q8K1N2-2]
DR GeneID; 208177; -.
DR KEGG; mmu:208177; -.
DR UCSC; uc007zjb.3; mouse. [Q8K1N2-2]
DR UCSC; uc012agj.2; mouse. [Q8K1N2-1]
DR CTD; 90102; -.
DR MGI; MGI:2444981; Phldb2.
DR VEuPathDB; HostDB:ENSMUSG00000033149; -.
DR eggNOG; ENOG502QUWG; Eukaryota.
DR GeneTree; ENSGT00940000156371; -.
DR HOGENOM; CLU_003180_3_0_1; -.
DR InParanoid; Q8K1N2; -.
DR OMA; XEKVKLD; -.
DR OrthoDB; 70229at2759; -.
DR PhylomeDB; Q8K1N2; -.
DR TreeFam; TF329165; -.
DR BioGRID-ORCS; 208177; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Phldb2; mouse.
DR PRO; PR:Q8K1N2; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q8K1N2; protein.
DR Bgee; ENSMUSG00000033149; Expressed in undifferentiated genital tubercle and 224 other tissues.
DR ExpressionAtlas; Q8K1N2; baseline and differential.
DR Genevisible; Q8K1N2; MM.
DR GO; GO:0045180; C:basal cortex; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0051895; P:negative regulation of focal adhesion assembly; ISO:MGI.
DR GO; GO:0051497; P:negative regulation of stress fiber assembly; ISO:MGI.
DR GO; GO:1903690; P:negative regulation of wound healing, spreading of epidermal cells; ISO:MGI.
DR GO; GO:1904261; P:positive regulation of basement membrane assembly involved in embryonic body morphogenesis; ISO:MGI.
DR GO; GO:0010717; P:regulation of epithelial to mesenchymal transition; ISO:MGI.
DR GO; GO:0010470; P:regulation of gastrulation; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISO:MGI.
DR CDD; cd14673; PH_PHLDB1_2; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037810; PHLDB1/2/3_PH.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Direct protein sequencing;
KW Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1..1249
FT /note="Pleckstrin homology-like domain family B member 2"
FT /id="PRO_0000053895"
FT DOMAIN 1139..1242
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 64..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 866..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 580..692
FT /evidence="ECO:0000255"
FT COILED 718..803
FT /evidence="ECO:0000255"
FT COILED 1028..1094
FT /evidence="ECO:0000255"
FT COMPBIAS 128..143
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..233
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..893
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ0"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ0"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ0"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 329
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 347
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ0"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ0"
FT MOD_RES 465
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 486
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079"
FT MOD_RES 546
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ0"
FT MOD_RES 894
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q86SQ0"
FT VAR_SEQ 866..873
FT /note="VSQPQSSE -> HRTAVYSGFMSPSTLSPSVTEPSSATWPEVMTTSVDPFPL
FT NDTPPPLPAKKHRRQQPQEQQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016746"
FT CONFLICT 112
FT /note="S -> I (in Ref. 2; AAH50915/AAH60683)"
FT /evidence="ECO:0000305"
FT CONFLICT 504
FT /note="R -> M (in Ref. 1; AAM33635)"
FT /evidence="ECO:0000305"
FT CONFLICT 634
FT /note="A -> S (in Ref. 3; BAE38105)"
FT /evidence="ECO:0000305"
FT CONFLICT 807
FT /note="Y -> D (in Ref. 1; AAM33635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1127
FT /note="H -> P (in Ref. 1; AAM33635)"
FT /evidence="ECO:0000305"
FT CONFLICT 1138
FT /note="T -> P (in Ref. 1; AAM33635)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1249 AA; 141486 MW; 3875492F043ACFAB CRC64;
MAEDSHMQKQ LEFQNGSLEE GFVVRSLENE PQNMMESLSP RKYSSSLKFK ANGDYSGSYL
TLSQPVSAKR SPSPMGTSVR SSPSLAKIQG SKQFCDGIDK NISMKPPISF LSSAASLGGY
PLGKADLDHY TGRDSERSTR LSEKPPYSRY SSRNKSHDSV YFLGGLEGRK TSGSLLTMWN
GNSLSCTGSS PISRSGAASM PSSPKQVRKM NLQDHSTLQP RLSRHKEPAS ENVSVRTRKY
SGSSLSNMGA YSRSLPRLYK ATDNQMSPLS LPPRSSLGNS RRGQLGEKDL PHSLVDSDNY
LNFSSLSSGA SPYKTCLSEG NPYVSSALSV PASPRVARKM LLASTSSDDF DRASYSGTSP
SHSFISGEPD RVLVARRNFS CGSMELDDSD LESLRQSSET PQPVLRERKS SISSISGRDD
LMDYHRRQRE ERLREQEMER LERQRLETIL SLCAEYTKPE GRRLSAGTTV ADVQKINKEL
EKLQLSDEES VFEDALVCPD ARYRCHRKGS LQDVDVAGFG NLGHSASFLA PRGSRSDELL
GDLTRTPPSS SAAFLKATNE SSYLSILPKT PEDIGEEQRT QELAAMEDAR MVILNNLEEL
EQKIKDINDQ MDESSRELDM ECALLDGEQK SETAELMKEK EILDHLNRKI TELEKNIVGE
KTKEKVKLDA EREKLERLQE LYSEQKTQLD NCPESMREQL QQQLKRDADL LDVESKHFED
LEFQQLEHES RLDEEKENLT QQLLREVAEY QRNIVARKEK ISALKKQASH IVQQAQREQD
HFVKEKNNLI MMLQREKENL CNLEKKYSSL TGGKGFPINP NTLKEGYISV NEINESCGNS
TNLSPSTQFP ADADAAVTEP ALAVPVSQPQ SSEHFRSLEE RKKQHKEGLY LSDTLPRKKT
TPSLSPHFSS ATMGRSTTPK AHLPLGQSNS CGSVLPHSLA TMTKDSESRR MLRGYNHQQM
SEGQRQKPEF YSRTASESNV YLNSFHYPDR SYKDQAYDTL SLDSSDSMET SISACSPDNI
SSASTSNIAR IEEMERLLKQ AHAEKTRLLE SREREMEAKK RALEEEKRRR EILEKRLQEE
TSQRQKLIEK EVKIREKQRA QARPLTRYLP VRKEDFDLRS HVETAGHNID TCFHVSITEK
TCRGYLIKMG GKIKTWKKRW FVFDRNKRTF SYYADKHEAK LKGVIYFQAI EEVYYDHLKN
ANKSPNPLLT FSVKTHDRIY YMVAPSPEAM RIWMDVIVTG AEGYTHFLL
