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Q6ZUJ8 (BCAP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:PIK3AP1
Synonyms:BCAP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length805 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.5

Subunit structure

Homooligomer By similarity. 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. May interact with MYD88 and TIRAP By similarity. Ref.5 Ref.6

Subcellular location

Cytoplasm By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity.

Tissue specificity

Expressed in natural killer (NK) cells. Ref.6

Domain

The DBB domain is required for dimerization By similarity.

Post-translational modification

Constitutively phosphorylated. Phosphorylated on tyrosine residues in C-terminal region by ABL1. Phosphorylated on tyrosine residues within the YXXM motifs by BTK and SYK By similarity. Isoform 1 and isoform 2 are phosphorylated on tyrosine residues, most likely within the YXXM motifs, via CD19 activation By similarity. Toll-like receptor activation induces appearance of a phosphorylated form associated with membranes By similarity. Ref.5

Sequence similarities

Contains 1 DBB domain.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processnegative regulation of toll-like receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of toll-like receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

toll-like receptor 2 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

toll-like receptor 4 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

toll-like receptor 7 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

toll-like receptor 9 signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytosol

Inferred from sequence or structural similarity. Source: UniProtKB

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionphosphatidylinositol 3-kinase regulatory subunit binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6ZUJ8-1)

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.
Isoform 2 (identifier: Q6ZUJ8-2)

Also known as: BCAP-S;

The sequence of this isoform differs from the canonical sequence as follows:
     1-178: Missing.
Isoform 3 (identifier: Q6ZUJ8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: MAASGVPRGC...GPEASFSAED → MRFFTSVACY...TGAKHVPGSS
     58-458: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 805805Phosphoinositide 3-kinase adapter protein 1
PRO_0000341273

Regions

Domain181 – 317137DBB
Region10 – 144135Necessary and sufficent to mediate inhibition of NF-kappa-B downstream of activated TLRs; may mediate interaction with MYD88 and TIRAP By similarity
Coiled coil645 – 66723 Potential
Compositional bias760 – 80243Pro-rich

Amino acid modifications

Modified residue2631Phosphotyrosine By similarity
Modified residue4191Phosphotyrosine; by SYK By similarity
Modified residue4441Phosphotyrosine; by SYK By similarity
Modified residue4591Phosphotyrosine; by SYK By similarity
Modified residue5131Phosphotyrosine; by ABL1 Ref.5
Modified residue5531Phosphotyrosine; by ABL1 Ref.5
Modified residue5701Phosphotyrosine; by ABL1 Ref.5
Modified residue5941Phosphotyrosine; by ABL1 Ref.5
Modified residue6941Phosphotyrosine; by ABL1 Ref.5

Natural variations

Alternative sequence1 – 178178Missing in isoform 2.
VSP_034238
Alternative sequence1 – 5757MAASG…FSAED → MRFFTSVACYGSCLFASELL IRCKDWLKGRPALFTALLAC VLYLCEWTGAKHVPGSS in isoform 3.
VSP_034239
Alternative sequence58 – 458401Missing in isoform 3.
VSP_034240
Natural variant211E → K. Ref.1
Corresponds to variant rs17112076 [ dbSNP | Ensembl ].
VAR_044035
Natural variant831A → S. Ref.2
Corresponds to variant rs3748229 [ dbSNP | Ensembl ].
VAR_044036
Natural variant5511E → K.
Corresponds to variant rs3748233 [ dbSNP | Ensembl ].
VAR_044037
Natural variant6381K → R.
Corresponds to variant rs12784975 [ dbSNP | Ensembl ].
VAR_044038

Experimental info

Sequence conflict7261T → P in BAC03996. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BCAP-L) [UniParc].

Last modified July 22, 2008. Version 2.
Checksum: DF1025A37905AEA7

FASTA80590,398
        10         20         30         40         50         60 
MAASGVPRGC DILIVYSPDA EEWCQYLQTL FLSSRQVRSQ KILTHRLGPE ASFSAEDLSL 

        70         80         90        100        110        120 
FLSTRCVVVL LSAELVQHFH KPALLPLLQR AFHPPHRVVR LLCGVRDSEE FLDFFPDWAH 

       130        140        150        160        170        180 
WQELTCDDEP ETYVAAVKKA ISEDSGCDSV TDTEPEDEKV VSYSKQQNLP TVTSPGNLMV 

       190        200        210        220        230        240 
VQPDRIRCGA ETTVYVIVRC KLDDRVATEA EFSPEDSPSV RMEAKVENEY TISVKAPNLS 

       250        260        270        280        290        300 
SGNVSLKIYS GDLVVCETVI SYYTDMEEIG NLLSNAANPV EFMCQAFKIV PYNTETLDKL 

       310        320        330        340        350        360 
LTESLKNNIP ASGLHLFGIN QLEEEDMMTN QRDEELPTLL HFAAKYGLKN LTALLLTCPG 

       370        380        390        400        410        420 
ALQAYSVANK HGHYPNTIAE KHGFRDLRQF IDEYVETVDM LKSHIKEELM HGEEADAVYE 

       430        440        450        460        470        480 
SMAHLSTDLL MKCSLNPGCD EDLYESMAAF VPAATEDLYV EMLQASTSNP IPGDGFSRAT 

       490        500        510        520        530        540 
KDSMIRKFLE GNSMGMTNLE RDQCHLGQEE DVYHTVDDDE AFSVDLASRP PVPVPRPETT 

       550        560        570        580        590        600 
APGAHQLPDN EPYIFKVFAE KSQERPGNFY VSSESIRKGP PVRPWRDRPQ SSIYDPFAGM 

       610        620        630        640        650        660 
KTPGQRQLIT LQEQVKLGIV NVDEAVLHFK EWQLNQKKRS ESFRFQQENL KRLRDSITRR 

       670        680        690        700        710        720 
QREKQKSGKQ TDLEITVPIR HSQHLPAKVE FGVYESGPRK SVIPPRTELR RGDWKTDSTS 

       730        740        750        760        770        780 
STASSTSNRS STRSLLSVSS GMEGDNEDNE VPEVTRSRSP GPPQVDGTPT MSLERPPRVP 

       790        800 
PRAASQRPPT RETFHPPPPV PPRGR 

« Hide

Isoform 2 (BCAP-S) [UniParc].

Checksum: A2D7C2496537C129
Show »

FASTA62770,412
Isoform 3 [UniParc].

Checksum: EDBB28E0023875E9
Show »

FASTA40445,484

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT LYS-21.
Tissue: Spleen and Synovium.
[2]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT SER-83.
Tissue: Fetal liver.
[3]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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 3).
Tissue: Brain.
[5]"Identification of B cell adaptor for PI3-kinase (BCAP) as an Abl interactor 1-regulated substrate of Abl kinases."
Maruoka M., Suzuki J., Kawata S., Yoshida K., Hirao N., Sato S., Goff S.P., Takeya T., Tani K., Shishido T.
FEBS Lett. 579:2986-2990(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ABI1, PHOSPHORYLATION AT TYR-513; TYR-553; TYR-570; TYR-594 AND TYR-694.
[6]"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: INTERACTION WITH PIK3R1, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK092883 mRNA. Translation: BAC03996.1.
AK125635 mRNA. Translation: BAC86227.1.
BX648550 mRNA. No translation available.
AL358235, AL138765, AL591364 Genomic DNA. Translation: CAH71154.2.
AL591364, AL358235, AL138765 Genomic DNA. Translation: CAH73440.2.
AL591364, AL358235, AL138765 Genomic DNA. Translation: CAH73441.2.
AL138765, AL591364 Genomic DNA. Translation: CAI13579.2.
AL138765, AL358235, AL591364 Genomic DNA. Translation: CAI13581.2.
AL138765 Genomic DNA. Translation: CAI13586.1.
BC029917 mRNA. Translation: AAH29917.1.
CCDSCCDS31259.1. [Q6ZUJ8-1]
RefSeqNP_689522.2. NM_152309.2. [Q6ZUJ8-1]
XP_005269555.1. XM_005269498.1. [Q6ZUJ8-2]
XP_005269556.1. XM_005269499.1. [Q6ZUJ8-2]
UniGeneHs.310456.

3D structure databases

ProteinModelPortalQ6ZUJ8.
SMRQ6ZUJ8. Positions 338-393.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125621. 5 interactions.
IntActQ6ZUJ8. 5 interactions.
MINTMINT-7009152.
STRING9606.ENSP00000339826.

PTM databases

PhosphoSiteQ6ZUJ8.

Polymorphism databases

DMDM205830907.

Proteomic databases

MaxQBQ6ZUJ8.
PaxDbQ6ZUJ8.
PRIDEQ6ZUJ8.

Protocols and materials databases

DNASU118788.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000339364; ENSP00000339826; ENSG00000155629. [Q6ZUJ8-1]
ENST00000371109; ENSP00000360150; ENSG00000155629. [Q6ZUJ8-3]
ENST00000371110; ENSP00000360151; ENSG00000155629. [Q6ZUJ8-2]
GeneID118788.
KEGGhsa:118788.
UCSCuc001kmo.3. human. [Q6ZUJ8-3]
uc001kmp.3. human. [Q6ZUJ8-1]

Organism-specific databases

CTD118788.
GeneCardsGC10M098343.
H-InvDBHIX0201490.
HGNCHGNC:30034. PIK3AP1.
HPACAB026136.
MIM607942. gene.
neXtProtNX_Q6ZUJ8.
PharmGKBPA134979629.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG70048.
HOGENOMHOG000095183.
HOVERGENHBG104426.
InParanoidQ6ZUJ8.
KOK12230.
OMAPGKVEFG.
OrthoDBEOG77DJ53.
PhylomeDBQ6ZUJ8.
TreeFamTF328570.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeQ6ZUJ8.
CleanExHS_PIK3AP1.
GenevestigatorQ6ZUJ8.

Family and domain databases

InterProIPR017893. DBB_domain.
[Graphical view]
PfamPF14545. DBB. 1 hit.
[Graphical view]
PROSITEPS51376. DBB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPIK3AP1.
GenomeRNAi118788.
NextBio80340.
PROQ6ZUJ8.
SOURCESearch...

Entry information

Entry nameBCAP_HUMAN
AccessionPrimary (citable) accession number: Q6ZUJ8
Secondary accession number(s): Q5TB56 expand/collapse secondary AC list , Q5VXJ9, Q8N6J6, Q8NAC8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: July 22, 2008
Last modified: July 9, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM