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Protein

Phosphoinositide 3-kinase adapter protein 1

Gene

Pik3ap1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Signaling adapter that contributes to B-cell development by linking B-cell receptor (BCR) signaling to the phosphoinositide 3-kinase (PI3K)-Akt signaling pathway. Has a complementary role to the BCR coreceptor CD19, coupling BCR and PI3K activation by providing a docking site for the PI3K subunit PIK3R1. Alternatively, links Toll-like receptor (TLR) signaling to PI3K activation, a process preventing excessive inflammatory cytokine production. Also involved in the activation of PI3K in natural killer cells. May be involved in the survival of mature B-cells via activation of REL.7 Publications

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB

GO - Biological processi

  • negative regulation of toll-like receptor signaling pathway Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
  • positive regulation of toll-like receptor signaling pathway Source: UniProtKB
  • regulation of inflammatory response Source: UniProtKB
  • toll-like receptor 2 signaling pathway Source: UniProtKB
  • toll-like receptor 4 signaling pathway Source: UniProtKB
  • toll-like receptor 7 signaling pathway Source: UniProtKB
  • toll-like receptor 9 signaling pathway Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoinositide 3-kinase adapter protein 1
Alternative name(s):
B-cell adapter for phosphoinositide 3-kinase
B-cell phosphoinositide 3-kinase adapter protein 1
Gene namesi
Name:Pik3ap1
Synonyms:Bcap
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:1933177. Pik3ap1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice lacking Pik3ap1 display altered B-cell maturation and impaired immune function. Pik3ap1 depletion has an opposite effect in NK cells by promoting their maturation. Mice lacking Pik3ap1 and Cd19 have severe defects in generation of immature and mature B-cells. Moreover, mice lacking Pik3ap1 display increased IL-10, Il-12 and TNF proinflammatory cytokine secretion upon activation of the Toll-like receptors TLR4, TLR7 and TLR9.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi264 – 2641Y → F: Fails to bind PIK3R1 in a BCR-signaling dependent manner; when associated with Y-420; Y-445 and Y-460. Loss of regulatory function in Toll-like receptor signaling probably due to loss of interaction with PIK3R1; when associated with Y-420; Y-445 and Y-460. Impairs mature B-cell generation; when associated with Y-420; Y-445 and Y-460. 1 Publication
Mutagenesisi420 – 4201Y → F: Fails to bind PIK3R1 in a BCR-signaling dependent manner; when associated with Y-264; Y-445 and Y-460. Loss of regulatory function in Toll-like receptor signaling probably due to loss of interaction with PIK3R1; when associated with Y-264; Y-445 and Y-460. Impairs mature B-cell generation; when associated with Y-264; Y-445 and Y-460. 1 Publication
Mutagenesisi445 – 4451Y → F: Fails to bind PIK3R1 in a BCR-signaling dependent manner; when associated with Y-264; Y-420 and Y-460. Loss of regulatory function in Toll-like receptor signaling probably due to loss of interaction with PIK3R1; when associated with Y-264; Y-420 and Y-460. Impairs mature B-cell generation; when associated with Y-264; Y-420 and Y-460. 1 Publication
Mutagenesisi460 – 4601Y → F: Fails to bind PIK3R1 in a BCR-signaling dependent manner; when associated with Y-264; Y-420 and Y-445. Loss of regulatory function in Toll-like receptor signaling probably due to loss of interaction with PIK3R1; when associated with Y-264; Y-420 and Y-445. Impairs mature B-cell generation; when associated with Y-264; Y-420 and Y-445. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 811811Phosphoinositide 3-kinase adapter protein 1PRO_0000341274Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei264 – 2641Phosphotyrosine2 Publications
Modified residuei420 – 4201Phosphotyrosine; by SYK3 Publications
Modified residuei445 – 4451Phosphotyrosine; by SYK3 Publications
Modified residuei460 – 4601Phosphotyrosine; by SYK3 Publications
Modified residuei513 – 5131Phosphotyrosine; by ABL1By similarity
Modified residuei553 – 5531Phosphotyrosine; by ABL1By similarity
Modified residuei570 – 5701Phosphotyrosine; by ABL1By similarity
Modified residuei594 – 5941Phosphotyrosine; by ABL1By similarity
Modified residuei694 – 6941Phosphotyrosine; by ABL1By similarity
Modified residuei718 – 7181PhosphoserineBy similarity

Post-translational modificationi

Constitutively phosphorylated. Phosphorylated on tyrosine residues in C-terminal region by ABL1 (By similarity). Phosphorylated on tyrosine residues within the YXXM motifs by BTK and SYK. Isoform 1 and isoform 2 are phosphorylated on tyrosine residues, most likely within the YXXM motifs, via CD19 activation. Toll-like receptor activation induces appearance of a phosphorylated form associated with membranes.By similarity5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9EQ32.
MaxQBiQ9EQ32.
PaxDbiQ9EQ32.
PRIDEiQ9EQ32.

PTM databases

iPTMnetiQ9EQ32.
PhosphoSiteiQ9EQ32.

Expressioni

Tissue specificityi

Predominantly expressed in spleen (at protein level). Expressed at lower levels in thymus, liver and lung. Expressed in B-cells, macrophages and natural killer (NK) cells.2 Publications

Gene expression databases

BgeeiQ9EQ32.
GenevisibleiQ9EQ32. MM.

Interactioni

Subunit structurei

Homooligomer (Probable). Interacts (phosphorylated on tyrosine residues within YXXM motifs) with PIK3R1 (via SH2 domain); required for BCR- and TLR-mediated activation of phosphoinositide 3-kinase. Interacts (via polyproline C-terminal region) with ABI1 (via SH3 domain); the interaction promotes phosphorylation of PIK3AP1 by ABL1 (By similarity). May interact with MYD88 and TIRAP.By similarityCurated3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-643949,EBI-643949
Myd88P223662EBI-643949,EBI-525108
TirapQ99JY12EBI-643949,EBI-6559589

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • phosphatidylinositol 3-kinase regulatory subunit binding Source: UniProtKB

Protein-protein interaction databases

BioGridi219934. 1 interaction.
IntActiQ9EQ32. 7 interactions.
MINTiMINT-1612514.
STRINGi10090.ENSMUSP00000052777.

Structurei

3D structure databases

ProteinModelPortaliQ9EQ32.
SMRiQ9EQ32. Positions 334-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini182 – 318137DBBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni10 – 145136Necessary and sufficent to mediate inhibition of NF-kappa-B downstream of activated TLRs; may mediate interaction with MYD88 and TIRAPAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi760 – 80849Pro-richAdd
BLAST

Domaini

The DBB domain is required for dimerization.

Sequence similaritiesi

Contains 1 DBB domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IKKC. Eukaryota.
ENOG4110NCP. LUCA.
GeneTreeiENSGT00390000008787.
HOVERGENiHBG104426.
InParanoidiQ9EQ32.
KOiK12230.
OMAiVRCKLDE.
OrthoDBiEOG77DJ53.
PhylomeDBiQ9EQ32.
TreeFamiTF328570.

Family and domain databases

InterProiIPR017893. DBB_domain.
[Graphical view]
PfamiPF14545. DBB. 1 hit.
[Graphical view]
SMARTiSM01282. DBB. 1 hit.
[Graphical view]
PROSITEiPS51376. DBB. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9EQ32-1) [UniParc]FASTAAdd to basket

Also known as: BCAP-L

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAASGWGRGC DILIFYSPDA EEWCQYLQDL FVSCRQVRSQ KTQTYRLVPD
60 70 80 90 100
ASFSAQDLWV FRDARCVLVL LSAGLVGCFG QPGLLPMLQR ACHPPQRVVR
110 120 130 140 150
LLCGVQPGDE DFQAFFPDWA HWQEMTCDDE PETYLAAVRK AISEDSGCDS
160 170 180 190 200
VTDTEPEDER ELPFSKQTNL PPEISPGNLM VVQPDRIRCG AETTVYIIVR
210 220 230 240 250
CKLDEKVSTE AEFSPEDSPS IRVEGTLENE YTVSVKAPDL SSGNVSLKVY
260 270 280 290 300
SGDLVVCETT VSYYTDMEEI GNLLSSAANP VEFMCQAFKI VPYNTETLDK
310 320 330 340 350
LLTESLKNNI PASGLHLFGI NQLEEDDMMT NQRDEELPTL LHFAAKYGLK
360 370 380 390 400
NLTALLLTCP GALQAYSVAN KHGHYPNTIA EKHGFRDLRQ FIDEYVETVD
410 420 430 440 450
MLKTHIKEEL MQGEEADDVY ESMAHLSTDL LMKCSLNPGC DDELYESMAA
460 470 480 490 500
FAPAATEDLY VEMLQASAGN PVSGESFSRP TKDSMIRKFL EGNSVKPASW
510 520 530 540 550
EREQHHPYGE ELYHIVDEDE TFSVDLANRP PVPVPRPEAS APGPPPPPDN
560 570 580 590 600
EPYISKVFAE KSQERLGNFY VSSESIRKEP LVRPWRDRPP SSIYDPFAGM
610 620 630 640 650
KTPGQRQLIT LQEQVKLGIV NVDEAVLHFK EWQLNQKKRS ESFRFQQENL
660 670 680 690 700
KRLRESITRR RKEKPKSGKH TDLEITVPIR HSQHLPEKVE FGVYESGPRK
710 720 730 740 750
SVLPARTELR RGDWKTDSMS STASSTSNRS STRSLLSVSS GMEGDNEDNE
760 770 780 790 800
IPEITRSRGP GPTQVDGAPV VTGTPVGTLE RPPRVPPRAA SQRPLTRESF
810
HPPPPVPPRG R
Length:811
Mass (Da):90,928
Last modified:March 1, 2001 - v1
Checksum:i3268E89B5C73F218
GO
Isoform 2 (identifier: Q9EQ32-2) [UniParc]FASTAAdd to basket

Also known as: BCAP-S

The sequence of this isoform differs from the canonical sequence as follows:
     1-179: Missing.

Show »
Length:632
Mass (Da):70,809
Checksum:i4F0FE6801E34684A
GO
Isoform 3 (identifier: Q9EQ32-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     493-517: NSVKPASWEREQHHPYGEELYHIVD → KLSLIREAETLVFKGQVATDMACDD
     518-811: Missing.

Show »
Length:517
Mass (Da):57,643
Checksum:i38B3FFBB3B556AC5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061K → N in BAE42191 (PubMed:16141072).Curated
Sequence conflicti414 – 4141E → G in BAE41584 (PubMed:16141072).Curated
Sequence conflicti414 – 4141E → G in BAE42118 (PubMed:16141072).Curated
Sequence conflicti509 – 5091G → GE in AAI13142 (PubMed:15489334).Curated
Sequence conflicti768 – 7681A → AP in BAC40962 (PubMed:16141072).Curated
Sequence conflicti768 – 7681A → AP in BAE42191 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 179179Missing in isoform 2. 1 PublicationVSP_034241Add
BLAST
Alternative sequencei493 – 51725NSVKP…YHIVD → KLSLIREAETLVFKGQVATD MACDD in isoform 3. 1 PublicationVSP_034242Add
BLAST
Alternative sequencei518 – 811294Missing in isoform 3. 1 PublicationVSP_034243Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293806 mRNA. Translation: AAG48584.1.
AK087722 mRNA. Translation: BAC39980.1.
AK089785 mRNA. Translation: BAC40962.1.
AK150114 mRNA. Translation: BAE29318.1.
AK153548 mRNA. Translation: BAE32085.1.
AK170130 mRNA. Translation: BAE41584.1.
AK170925 mRNA. Translation: BAE42118.1.
AK171021 mRNA. Translation: BAE42191.1.
BC113141 mRNA. Translation: AAI13142.1.
CCDSiCCDS37987.1. [Q9EQ32-1]
RefSeqiNP_113553.1. NM_031376.3. [Q9EQ32-1]
XP_006527535.1. XM_006527472.2. [Q9EQ32-2]
UniGeneiMm.222266.

Genome annotation databases

EnsembliENSMUST00000059672; ENSMUSP00000052777; ENSMUSG00000025017. [Q9EQ32-1]
GeneIDi83490.
KEGGimmu:83490.
UCSCiuc008hlu.1. mouse. [Q9EQ32-1]
uc008hlv.1. mouse. [Q9EQ32-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF293806 mRNA. Translation: AAG48584.1.
AK087722 mRNA. Translation: BAC39980.1.
AK089785 mRNA. Translation: BAC40962.1.
AK150114 mRNA. Translation: BAE29318.1.
AK153548 mRNA. Translation: BAE32085.1.
AK170130 mRNA. Translation: BAE41584.1.
AK170925 mRNA. Translation: BAE42118.1.
AK171021 mRNA. Translation: BAE42191.1.
BC113141 mRNA. Translation: AAI13142.1.
CCDSiCCDS37987.1. [Q9EQ32-1]
RefSeqiNP_113553.1. NM_031376.3. [Q9EQ32-1]
XP_006527535.1. XM_006527472.2. [Q9EQ32-2]
UniGeneiMm.222266.

3D structure databases

ProteinModelPortaliQ9EQ32.
SMRiQ9EQ32. Positions 334-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219934. 1 interaction.
IntActiQ9EQ32. 7 interactions.
MINTiMINT-1612514.
STRINGi10090.ENSMUSP00000052777.

PTM databases

iPTMnetiQ9EQ32.
PhosphoSiteiQ9EQ32.

Proteomic databases

EPDiQ9EQ32.
MaxQBiQ9EQ32.
PaxDbiQ9EQ32.
PRIDEiQ9EQ32.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059672; ENSMUSP00000052777; ENSMUSG00000025017. [Q9EQ32-1]
GeneIDi83490.
KEGGimmu:83490.
UCSCiuc008hlu.1. mouse. [Q9EQ32-1]
uc008hlv.1. mouse. [Q9EQ32-3]

Organism-specific databases

CTDi118788.
MGIiMGI:1933177. Pik3ap1.

Phylogenomic databases

eggNOGiENOG410IKKC. Eukaryota.
ENOG4110NCP. LUCA.
GeneTreeiENSGT00390000008787.
HOVERGENiHBG104426.
InParanoidiQ9EQ32.
KOiK12230.
OMAiVRCKLDE.
OrthoDBiEOG77DJ53.
PhylomeDBiQ9EQ32.
TreeFamiTF328570.

Enzyme and pathway databases

ReactomeiR-MMU-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.

Miscellaneous databases

NextBioi350600.
PROiQ9EQ32.
SOURCEiSearch...

Gene expression databases

BgeeiQ9EQ32.
GenevisibleiQ9EQ32. MM.

Family and domain databases

InterProiIPR017893. DBB_domain.
[Graphical view]
PfamiPF14545. DBB. 1 hit.
[Graphical view]
SMARTiSM01282. DBB. 1 hit.
[Graphical view]
PROSITEiPS51376. DBB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "BCAP: the tyrosine kinase substrate that connects B cell receptor to phosphoinositide 3-kinase activation."
    Okada T., Maeda A., Iwamatsu A., Gotoh K., Kurosaki T.
    Immunity 13:817-827(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH PIK3R1, PHOSPHORYLATION AT TYR-264; TYR-420; TYR-445 AND TYR-460.
  2. "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] (ISOFORMS 1; 2 AND 3).
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Ovary and Spleen.
  3. "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] (ISOFORM 1).
  4. "Tyrosine phosphorylation of B-cell adaptor for phosphoinositide 3-kinase is required for Akt activation in response to CD19 engagement."
    Inabe K., Kurosaki T.
    Blood 99:584-589(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TYROSINE PHOSPHORYLATION (ISOFORMS 1 AND 2).
  5. "Essential immunoregulatory role for BCAP in B cell development and function."
    Yamazaki T., Takeda K., Gotoh K., Takeshima H., Akira S., Kurosaki T.
    J. Exp. Med. 195:535-545(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Isolation of proteins that interact with the signal transduction molecule Dof and identification of a functional domain conserved between Dof and vertebrate BCAP."
    Battersby A., Csiszar A., Leptin M., Wilson R.
    J. Mol. Biol. 329:479-493(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMOOLIGOMERIZATION, DBB DOMAIN.
  7. "Contribution of BCAP to maintenance of mature B cells through c-Rel."
    Yamazaki T., Kurosaki T.
    Nat. Immunol. 4:780-786(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Regulation of B-cell development by BCAP and CD19 through their binding to phosphoinositide 3-kinase."
    Aiba Y., Kameyama M., Yamazaki T., Tedder T.F., Kurosaki T.
    Blood 111:1497-1503(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PIK3R1, PHOSPHORYLATION AT TYR-264; TYR-420; TYR-445 AND TYR-460, MUTAGENESIS OF TYR-264; TYR-420; TYR-445 AND TYR-460, DISRUPTION PHENOTYPE.
  9. "Enhanced NK cell development and function in BCAP-deficient mice."
    Macfarlane A.W. IV, Yamazaki T., Fang M., Sigal L.J., Kurosaki T., Campbell K.S.
    Blood 112:131-140(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  10. "Identification of BCAP-(L) as a negative regulator of the TLR signaling-induced production of IL-6 and IL-10 in macrophages by tyrosine phosphoproteomics."
    Matsumura T., Oyama M., Kozuka-Hata H., Ishikawa K., Inoue T., Muta T., Semba K., Inoue J.
    Biochem. Biophys. Res. Commun. 400:265-270(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING (ISOFORMS 1 AND 2), PHOSPHORYLATION AT TYR-420; TYR-445 AND TYR-460 BY SYK.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver, Lung, Pancreas and Spleen.
  12. "B-cell adaptor for PI3K (BCAP) negatively regulates Toll-like receptor signaling through activation of PI3K."
    Ni M., MacFarlane A.W. IV, Toft M., Lowell C.A., Campbell K.S., Hamerman J.A.
    Proc. Natl. Acad. Sci. U.S.A. 109:267-272(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, DISRUPTION PHENOTYPE, PHOSPHORYLATION, SUBCELLULAR LOCATION.
  13. "Role for B-cell adapter for PI3K (BCAP) as a signaling adapter linking Toll-like receptors (TLRs) to serine/threonine kinases PI3K/Akt."
    Troutman T.D., Hu W., Fulenchek S., Yamazaki T., Kurosaki T., Bazan J.F., Pasare C.
    Proc. Natl. Acad. Sci. U.S.A. 109:273-278(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TOLL-LIKE RECEPTOR SIGNALING, INTERACTION WITH MYD88 AND TIRAP, PHOSPHORYLATION.

Entry informationi

Entry nameiBCAP_MOUSE
AccessioniPrimary (citable) accession number: Q9EQ32
Secondary accession number(s): Q2KHL6
, Q3TBW6, Q3TC39, Q3U5J3, Q8BN25, Q8C2Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: March 1, 2001
Last modified: May 11, 2016
This is version 96 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.