Baiap2l2
entrez
207495
canonical
uniprot
Q80Y61
canonical
ensembl
ENSMUSG00000018126
resolver
ensp
ENSMUSP00000127816
resolver
genesymbol
Baiap2l2
resolver
uniprot
Q3UP58
resolver
uniprot_entry
BI2L2_MOUSE
resolver
uniprot_sec
Q3UP58
resolver
amino_acid_sequence
MAPEMDQFYRSTMAIYKSIMEQFNPALENLVYLGNNYLRAFHALSEAAEVYFSAIQKIGEQALQSSTSQILGEILVQMSDTQRHLNSDLEVVVQTFHGDLLQHMEKNTKLDMQFIKDSCQHYEIEYRHRAANLEKCMSELWRMERKRDKNAREMKESVNRLHAQMQAFVSESKRAAELEEKRRYRFLAEKHLLLSNTFLQFLGRARGMLQNRVLLWKEQSEASRSPSRAHSPGLLGPALGPPYPSGRLTPTRLDMPPRPLGEYGSPRSRHGSGSYGPEPAEARSASQLEPDRRSLPRTPSASSLYASSTQRSRSNSFGERLGGGGARRVRALVSHSEGANHTLLRFSAGDVVEVLVPEAQNGWLYGKLEGSSASGWFPEAYVKPVEEIPVNPMNPVAPMNSMAPMSPMNELPSRSYPLRGSHSLDDLLDRPGNPTASSEYWDSQSRSRTPSRVPSRAPSPAPPPLPSSRRSSVGSMGAATDVKKLMSWEQNPPELFPRGTNPFATVKLRPTVTNDRSAPLIR
uniprot
proteins
function
FUNCTION: Phosphoinositides-binding protein that induces the formation of planar or gently curved membrane structures. Binds to phosphoinositides, including to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2) headgroups. There seems to be no clear preference for a specific phosphoinositide. {ECO:0000269|PubMed:21743456}.
uniprot
proteins
mass_dalton
58402
uniprot
proteins
mutagenesis
MUTAGEN 109; /note="K->A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-116."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 116; /note="K->A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-109."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 124; /note="I->S: Partially impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 127; /note="R->A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-135."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 135; /note="K->A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-127."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 141; /note="W->S: Deficient in oligomerization (dimerization maintained). Inefficient formation of planar membrane structures. No effect on lipid-binding."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 145; /note="R->A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-146 and A-147."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 146; /note="K->A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-147."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 147; /note="R->A: Impairs lipid-binding activity and hence PtdIns(4,5)P2 clustering; when associated with A-145 and A-146."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 149; /note="K->A: No effect on lipid-binding; when associated with A-152 and A-155."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 152; /note="R->A: No effect on lipid-binding; when associated with A-149 and A-155."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 155; /note="K->A: No effect on lipid-binding; when associated with A-149 and A-152."; /evidence="ECO:0000269|PubMed:21743456"; MUTAGEN 214; /note="L->S: No effect on lipid-binding."; /evidence="ECO:0000269|PubMed:21743456
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21743456
uniprot
proteins
sequence_length
522
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasmic vesicle membrane {ECO:0000250}. Note=Localizes to RAB13-positive vesicles and to the plasma membrane at intercellular contacts. {ECO:0000250}.
uniprot
proteins