BCAP_MOUSE
ID BCAP_MOUSE Reviewed; 811 AA.
AC Q9EQ32; Q2KHL6; Q3TBW6; Q3TC39; Q3U5J3; Q8BN25; Q8C2Y4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Phosphoinositide 3-kinase adapter protein 1;
DE AltName: Full=B-cell adapter for phosphoinositide 3-kinase;
DE AltName: Full=B-cell phosphoinositide 3-kinase adapter protein 1;
GN Name=Pik3ap1; Synonyms=Bcap;
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] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION
RP WITH PIK3R1, AND PHOSPHORYLATION AT TYR-264; TYR-420; TYR-445 AND TYR-460.
RX PubMed=11163197; DOI=10.1016/s1074-7613(00)00079-0;
RA Okada T., Maeda A., Iwamatsu A., Gotoh K., Kurosaki T.;
RT "BCAP: the tyrosine kinase substrate that connects B cell receptor to
RT phosphoinositide 3-kinase activation.";
RL Immunity 13:817-827(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Ovary, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [4]
RP FUNCTION, AND TYROSINE PHOSPHORYLATION (ISOFORMS 1 AND 2).
RX PubMed=11781242; DOI=10.1182/blood.v99.2.584;
RA Inabe K., Kurosaki T.;
RT "Tyrosine phosphorylation of B-cell adaptor for phosphoinositide 3-kinase
RT is required for Akt activation in response to CD19 engagement.";
RL Blood 99:584-589(2002).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11877477; DOI=10.1084/jem.20011751;
RA Yamazaki T., Takeda K., Gotoh K., Takeshima H., Akira S., Kurosaki T.;
RT "Essential immunoregulatory role for BCAP in B cell development and
RT function.";
RL J. Exp. Med. 195:535-545(2002).
RN [6]
RP HOMOOLIGOMERIZATION, AND DBB DOMAIN.
RX PubMed=12767830; DOI=10.1016/s0022-2836(03)00489-3;
RA Battersby A., Csiszar A., Leptin M., Wilson R.;
RT "Isolation of proteins that interact with the signal transduction molecule
RT Dof and identification of a functional domain conserved between Dof and
RT vertebrate BCAP.";
RL J. Mol. Biol. 329:479-493(2003).
RN [7]
RP FUNCTION.
RX PubMed=12833156; DOI=10.1038/ni949;
RA Yamazaki T., Kurosaki T.;
RT "Contribution of BCAP to maintenance of mature B cells through c-Rel.";
RL Nat. Immunol. 4:780-786(2003).
RN [8]
RP FUNCTION, INTERACTION WITH PIK3R1, PHOSPHORYLATION AT TYR-264; TYR-420;
RP TYR-445 AND TYR-460, MUTAGENESIS OF TYR-264; TYR-420; TYR-445 AND TYR-460,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=18025150; DOI=10.1182/blood-2007-08-109769;
RA Aiba Y., Kameyama M., Yamazaki T., Tedder T.F., Kurosaki T.;
RT "Regulation of B-cell development by BCAP and CD19 through their binding to
RT phosphoinositide 3-kinase.";
RL Blood 111:1497-1503(2008).
RN [9]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18337558; DOI=10.1182/blood-2007-08-107847;
RA Macfarlane A.W. IV, Yamazaki T., Fang M., Sigal L.J., Kurosaki T.,
RA Campbell K.S.;
RT "Enhanced NK cell development and function in BCAP-deficient mice.";
RL Blood 112:131-140(2008).
RN [10]
RP FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING (ISOFORMS 1 AND 2), AND
RP PHOSPHORYLATION AT TYR-420; TYR-445 AND TYR-460 BY SYK.
RX PubMed=20728433; DOI=10.1016/j.bbrc.2010.08.055;
RA Matsumura T., Oyama M., Kozuka-Hata H., Ishikawa K., Inoue T., Muta T.,
RA Semba K., Inoue J.;
RT "Identification of BCAP-(L) as a negative regulator of the TLR signaling-
RT induced production of IL-6 and IL-10 in macrophages by tyrosine
RT phosphoproteomics.";
RL Biochem. Biophys. Res. Commun. 400:265-270(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Lung, Pancreas, 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 [12]
RP FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, DISRUPTION PHENOTYPE,
RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=22187458; DOI=10.1073/pnas.1111957108;
RA Ni M., MacFarlane A.W. IV, Toft M., Lowell C.A., Campbell K.S.,
RA Hamerman J.A.;
RT "B-cell adaptor for PI3K (BCAP) negatively regulates Toll-like receptor
RT signaling through activation of PI3K.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:267-272(2012).
RN [13]
RP FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, INTERACTION WITH MYD88 AND TIRAP,
RP AND PHOSPHORYLATION.
RX PubMed=22187460; DOI=10.1073/pnas.1118579109;
RA Troutman T.D., Hu W., Fulenchek S., Yamazaki T., Kurosaki T., Bazan J.F.,
RA Pasare C.;
RT "Role for B-cell adapter for PI3K (BCAP) as a signaling adapter linking
RT Toll-like receptors (TLRs) to serine/threonine kinases PI3K/Akt.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:273-278(2012).
CC -!- FUNCTION: Signaling adapter that contributes to B-cell development by
CC linking B-cell receptor (BCR) signaling to the phosphoinositide 3-
CC kinase (PI3K)-Akt signaling pathway. Has a complementary role to the
CC BCR coreceptor CD19, coupling BCR and PI3K activation by providing a
CC docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-
CC like receptor (TLR) signaling to PI3K activation, a process preventing
CC excessive inflammatory cytokine production. Also involved in the
CC activation of PI3K in natural killer cells. May be involved in the
CC survival of mature B-cells via activation of REL.
CC {ECO:0000269|PubMed:11781242, ECO:0000269|PubMed:11877477,
CC ECO:0000269|PubMed:12833156, ECO:0000269|PubMed:18025150,
CC ECO:0000269|PubMed:18337558, ECO:0000269|PubMed:22187458,
CC ECO:0000269|PubMed:22187460}.
CC -!- SUBUNIT: Homooligomer (Probable). Interacts (phosphorylated on tyrosine
CC residues within YXXM motifs) with PIK3R1 (via SH2 domain); required for
CC BCR- and TLR-mediated activation of phosphoinositide 3-kinase.
CC Interacts (via polyproline C-terminal region) with ABI1 (via SH3
CC domain); the interaction promotes phosphorylation of PIK3AP1 by ABL1
CC (By similarity). May interact with MYD88 and TIRAP. {ECO:0000250,
CC ECO:0000269|PubMed:11163197, ECO:0000269|PubMed:18025150,
CC ECO:0000269|PubMed:22187460, ECO:0000305}.
CC -!- INTERACTION:
CC Q9EQ32; P22366: Myd88; NbExp=2; IntAct=EBI-643949, EBI-525108;
CC Q9EQ32; Q9EQ32: Pik3ap1; NbExp=3; IntAct=EBI-643949, EBI-643949;
CC Q9EQ32; Q99JY1: Tirap; NbExp=2; IntAct=EBI-643949, EBI-6559589;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22187458}. Cell
CC membrane {ECO:0000305|PubMed:22187458}; Peripheral membrane protein
CC {ECO:0000305|PubMed:22187458}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=BCAP-L;
CC IsoId=Q9EQ32-1; Sequence=Displayed;
CC Name=2; Synonyms=BCAP-S;
CC IsoId=Q9EQ32-2; Sequence=VSP_034241;
CC Name=3;
CC IsoId=Q9EQ32-3; Sequence=VSP_034242, VSP_034243;
CC -!- TISSUE SPECIFICITY: Predominantly expressed in spleen (at protein
CC level). Expressed at lower levels in thymus, liver and lung. Expressed
CC in B-cells, macrophages and natural killer (NK) cells.
CC {ECO:0000269|PubMed:11163197, ECO:0000269|PubMed:18337558}.
CC -!- DOMAIN: The DBB domain is required for dimerization.
CC -!- PTM: Constitutively phosphorylated. Phosphorylated on tyrosine residues
CC in C-terminal region by ABL1 (By similarity). Phosphorylated on
CC tyrosine residues within the YXXM motifs by BTK and SYK. Isoform 1 and
CC isoform 2 are phosphorylated on tyrosine residues, most likely within
CC the YXXM motifs, via CD19 activation. Toll-like receptor activation
CC induces appearance of a phosphorylated form associated with membranes.
CC {ECO:0000250, ECO:0000269|PubMed:11163197, ECO:0000269|PubMed:18025150,
CC ECO:0000269|PubMed:20728433, ECO:0000269|PubMed:22187458,
CC ECO:0000269|PubMed:22187460}.
CC -!- DISRUPTION PHENOTYPE: Mice lacking Pik3ap1 display altered B-cell
CC maturation and impaired immune function. Pik3ap1 depletion has an
CC opposite effect in NK cells by promoting their maturation. Mice lacking
CC Pik3ap1 and Cd19 have severe defects in generation of immature and
CC mature B-cells. Moreover, mice lacking Pik3ap1 display increased IL-10,
CC Il-12 and TNF pro-inflammatory cytokine secretion upon activation of
CC the Toll-like receptors TLR4, TLR7 and TLR9.
CC {ECO:0000269|PubMed:11877477, ECO:0000269|PubMed:18025150,
CC ECO:0000269|PubMed:18337558, ECO:0000269|PubMed:22187458}.
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DR EMBL; AF293806; AAG48584.1; -; mRNA.
DR EMBL; AK087722; BAC39980.1; -; mRNA.
DR EMBL; AK089785; BAC40962.1; -; mRNA.
DR EMBL; AK150114; BAE29318.1; -; mRNA.
DR EMBL; AK153548; BAE32085.1; -; mRNA.
DR EMBL; AK170130; BAE41584.1; -; mRNA.
DR EMBL; AK170925; BAE42118.1; -; mRNA.
DR EMBL; AK171021; BAE42191.1; -; mRNA.
DR EMBL; BC113141; AAI13142.1; -; mRNA.
DR CCDS; CCDS37987.1; -. [Q9EQ32-1]
DR RefSeq; NP_113553.1; NM_031376.3. [Q9EQ32-1]
DR RefSeq; XP_006527535.1; XM_006527472.3. [Q9EQ32-2]
DR AlphaFoldDB; Q9EQ32; -.
DR SMR; Q9EQ32; -.
DR BioGRID; 219934; 1.
DR IntAct; Q9EQ32; 7.
DR STRING; 10090.ENSMUSP00000052777; -.
DR iPTMnet; Q9EQ32; -.
DR PhosphoSitePlus; Q9EQ32; -.
DR SwissPalm; Q9EQ32; -.
DR EPD; Q9EQ32; -.
DR jPOST; Q9EQ32; -.
DR MaxQB; Q9EQ32; -.
DR PaxDb; Q9EQ32; -.
DR PeptideAtlas; Q9EQ32; -.
DR PRIDE; Q9EQ32; -.
DR ProteomicsDB; 277187; -. [Q9EQ32-1]
DR ProteomicsDB; 277188; -. [Q9EQ32-2]
DR ProteomicsDB; 277189; -. [Q9EQ32-3]
DR Antibodypedia; 30771; 379 antibodies from 24 providers.
DR DNASU; 83490; -.
DR Ensembl; ENSMUST00000059672; ENSMUSP00000052777; ENSMUSG00000025017. [Q9EQ32-1]
DR GeneID; 83490; -.
DR KEGG; mmu:83490; -.
DR UCSC; uc008hlu.1; mouse. [Q9EQ32-1]
DR UCSC; uc008hlv.1; mouse. [Q9EQ32-3]
DR CTD; 118788; -.
DR MGI; MGI:1933177; Pik3ap1.
DR VEuPathDB; HostDB:ENSMUSG00000025017; -.
DR eggNOG; ENOG502QS94; Eukaryota.
DR GeneTree; ENSGT00390000008787; -.
DR HOGENOM; CLU_012993_0_0_1; -.
DR InParanoid; Q9EQ32; -.
DR OMA; IIMKCKL; -.
DR OrthoDB; 280243at2759; -.
DR PhylomeDB; Q9EQ32; -.
DR TreeFam; TF328570; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 83490; 5 hits in 74 CRISPR screens.
DR ChiTaRS; Pik3ap1; mouse.
DR PRO; PR:Q9EQ32; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q9EQ32; protein.
DR Bgee; ENSMUSG00000025017; Expressed in granulocyte and 101 other tissues.
DR Genevisible; Q9EQ32; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:0034123; P:positive regulation of toll-like receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:UniProtKB.
DR GO; GO:0034134; P:toll-like receptor 2 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034154; P:toll-like receptor 7 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IMP:UniProtKB.
DR Gene3D; 3.40.50.10140; -; 1.
DR InterPro; IPR017893; DBB_domain.
DR InterPro; IPR041340; PIK3AP1_TIR.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR Pfam; PF14545; DBB; 1.
DR Pfam; PF18567; TIR_3; 1.
DR SMART; SM01282; DBB; 1.
DR PROSITE; PS51376; DBB; 1.
DR PROSITE; PS50104; TIR; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..811
FT /note="Phosphoinositide 3-kinase adapter protein 1"
FT /id="PRO_0000341274"
FT DOMAIN 8..146
FT /note="TIR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00204"
FT DOMAIN 182..318
FT /note="DBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00707"
FT REGION 10..145
FT /note="Necessary and sufficient to mediate inhibition of
FT NF-kappa-B downstream of activated TLRs; may mediate
FT interaction with MYD88 and TIRAP"
FT /evidence="ECO:0000269|PubMed:22187460"
FT REGION 146..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:11163197,
FT ECO:0000269|PubMed:18025150"
FT MOD_RES 420
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000305|PubMed:11163197,
FT ECO:0000305|PubMed:18025150, ECO:0000305|PubMed:20728433"
FT MOD_RES 445
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000305|PubMed:11163197,
FT ECO:0000305|PubMed:18025150, ECO:0000305|PubMed:20728433"
FT MOD_RES 460
FT /note="Phosphotyrosine; by SYK"
FT /evidence="ECO:0000305|PubMed:11163197,
FT ECO:0000305|PubMed:18025150, ECO:0000305|PubMed:20728433"
FT MOD_RES 513
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUJ8"
FT MOD_RES 553
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUJ8"
FT MOD_RES 570
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUJ8"
FT MOD_RES 594
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUJ8"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUJ8"
FT MOD_RES 694
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUJ8"
FT MOD_RES 718
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZUJ8"
FT VAR_SEQ 1..179
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034241"
FT VAR_SEQ 493..517
FT /note="NSVKPASWEREQHHPYGEELYHIVD -> KLSLIREAETLVFKGQVATDMAC
FT DD (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034242"
FT VAR_SEQ 518..811
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_034243"
FT MUTAGEN 264
FT /note="Y->F: Fails to bind PIK3R1 in a BCR-signaling
FT dependent manner; when associated with Y-420; Y-445 and Y-
FT 460. Loss of regulatory function in Toll-like receptor
FT signaling probably due to loss of interaction with PIK3R1;
FT when associated with Y-420; Y-445 and Y-460. Impairs mature
FT B-cell generation; when associated with Y-420; Y-445 and Y-
FT 460."
FT /evidence="ECO:0000269|PubMed:18025150"
FT MUTAGEN 420
FT /note="Y->F: Fails to bind PIK3R1 in a BCR-signaling
FT dependent manner; when associated with Y-264; Y-445 and Y-
FT 460. Loss of regulatory function in Toll-like receptor
FT signaling probably due to loss of interaction with PIK3R1;
FT when associated with Y-264; Y-445 and Y-460. Impairs mature
FT B-cell generation; when associated with Y-264; Y-445 and Y-
FT 460."
FT /evidence="ECO:0000269|PubMed:18025150"
FT MUTAGEN 445
FT /note="Y->F: Fails to bind PIK3R1 in a BCR-signaling
FT dependent manner; when associated with Y-264; Y-420 and Y-
FT 460. Loss of regulatory function in Toll-like receptor
FT signaling probably due to loss of interaction with PIK3R1;
FT when associated with Y-264; Y-420 and Y-460. Impairs mature
FT B-cell generation; when associated with Y-264; Y-420 and Y-
FT 460."
FT /evidence="ECO:0000269|PubMed:18025150"
FT MUTAGEN 460
FT /note="Y->F: Fails to bind PIK3R1 in a BCR-signaling
FT dependent manner; when associated with Y-264; Y-420 and Y-
FT 445. Loss of regulatory function in Toll-like receptor
FT signaling probably due to loss of interaction with PIK3R1;
FT when associated with Y-264; Y-420 and Y-445. Impairs mature
FT B-cell generation; when associated with Y-264; Y-420 and Y-
FT 445."
FT /evidence="ECO:0000269|PubMed:18025150"
FT CONFLICT 206
FT /note="K -> N (in Ref. 2; BAE42191)"
FT /evidence="ECO:0000305"
FT CONFLICT 414
FT /note="E -> G (in Ref. 2; BAE41584/BAE42118)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="G -> GE (in Ref. 3; AAI13142)"
FT /evidence="ECO:0000305"
FT CONFLICT 768
FT /note="A -> AP (in Ref. 2; BAC40962/BAE42191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 811 AA; 90928 MW; 3268E89B5C73F218 CRC64;
MAASGWGRGC DILIFYSPDA EEWCQYLQDL FVSCRQVRSQ KTQTYRLVPD ASFSAQDLWV
FRDARCVLVL LSAGLVGCFG QPGLLPMLQR ACHPPQRVVR LLCGVQPGDE DFQAFFPDWA
HWQEMTCDDE PETYLAAVRK AISEDSGCDS VTDTEPEDER ELPFSKQTNL PPEISPGNLM
VVQPDRIRCG AETTVYIIVR CKLDEKVSTE AEFSPEDSPS IRVEGTLENE YTVSVKAPDL
SSGNVSLKVY SGDLVVCETT VSYYTDMEEI GNLLSSAANP VEFMCQAFKI VPYNTETLDK
LLTESLKNNI PASGLHLFGI NQLEEDDMMT NQRDEELPTL LHFAAKYGLK NLTALLLTCP
GALQAYSVAN KHGHYPNTIA EKHGFRDLRQ FIDEYVETVD MLKTHIKEEL MQGEEADDVY
ESMAHLSTDL LMKCSLNPGC DDELYESMAA FAPAATEDLY VEMLQASAGN PVSGESFSRP
TKDSMIRKFL EGNSVKPASW EREQHHPYGE ELYHIVDEDE TFSVDLANRP PVPVPRPEAS
APGPPPPPDN EPYISKVFAE KSQERLGNFY VSSESIRKEP LVRPWRDRPP SSIYDPFAGM
KTPGQRQLIT LQEQVKLGIV NVDEAVLHFK EWQLNQKKRS ESFRFQQENL KRLRESITRR
RKEKPKSGKH TDLEITVPIR HSQHLPEKVE FGVYESGPRK SVLPARTELR RGDWKTDSMS
STASSTSNRS STRSLLSVSS GMEGDNEDNE IPEITRSRGP GPTQVDGAPV VTGTPVGTLE
RPPRVPPRAA SQRPLTRESF HPPPPVPPRG R
