BIN1
entrez
274
canonical
uniprot
O00499
canonical
ensembl
ENSG00000136717
resolver
ensp
ENSP00000259237
resolver
ensp
ENSP00000259238
resolver
ensp
ENSP00000315284
resolver
ensp
ENSP00000315388
resolver
ensp
ENSP00000315411
resolver
ensp
ENSP00000316779
resolver
ensp
ENSP00000350654
resolver
ensp
ENSP00000365281
resolver
ensp
ENSP00000376760
resolver
ensp
ENSP00000376761
resolver
ensp
ENSP00000386797
resolver
ensp
ENSP00000575693
resolver
ensp
ENSP00000575694
resolver
ensp
ENSP00000618086
resolver
genesymbol
BIN1
resolver
genesymbol_syn
AMPHL
resolver
hgnc
HGNC:1052
resolver
uniprot
B7Z2Z2
resolver
uniprot
B7Z6Y2
resolver
uniprot
O00297
resolver
uniprot
O00545
resolver
uniprot
O43867
resolver
uniprot
O60552
resolver
uniprot
O60553
resolver
uniprot
O60554
resolver
uniprot
O60555
resolver
uniprot
O75514
resolver
uniprot
O75515
resolver
uniprot
O75516
resolver
uniprot
O75517
resolver
uniprot
O75518
resolver
uniprot
Q659B7
resolver
uniprot
Q92944
resolver
uniprot
Q99688
resolver
uniprot
Q9BTH3
resolver
uniprot_entry
B7Z2Z2_HUMAN
resolver
uniprot_entry
B7Z6Y2_HUMAN
resolver
uniprot_entry
BIN1_HUMAN
resolver
uniprot_entry
Q9BTH3_HUMAN
resolver
uniprot_sec
O00297
resolver
uniprot_sec
O00545
resolver
uniprot_sec
O43867
resolver
uniprot_sec
O60552
resolver
uniprot_sec
O60553
resolver
uniprot_sec
O60554
resolver
uniprot_sec
O60555
resolver
uniprot_sec
O75514
resolver
uniprot_sec
O75515
resolver
uniprot_sec
O75516
resolver
uniprot_sec
O75517
resolver
uniprot_sec
O75518
resolver
uniprot_sec
Q659B7
resolver
uniprot_sec
Q92944
resolver
uniprot_sec
Q99688
resolver
amino_acid_sequence
MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAGGATPGATLPKSPSQLRKGPPVPPPPKHTPSKEVKQEQILSLFEDTFVPEISVTTPSQFEAPGPFSEQASLLDLDFDPLPPVTSPVKAPTPSGQSIPWDLWEPTESPAGSLPSGEPSAAEGTFAVSWPSQTAEPGPAQPAEASEVAGGTQPAAGAQEPGETAASEAASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVP
uniprot
proteins
disease_involvement
DISEASE: Myopathy, centronuclear, 2 (CNM2) [MIM:255200]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers. {ECO:0000269|PubMed:17676042, ECO:0000269|PubMed:20142620, ECO:0000269|PubMed:24755653, ECO:0000269|PubMed:29950440}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=BIN1 mutations have been found in families segregating autosomal dominant centronuclear myopathy. Patients show adult-onset, mildly progressive muscle weakness affecting selected proximal muscles and all distal muscles of the lower limbs. {ECO:0000269|PubMed:25260562}.
uniprot
proteins
function
FUNCTION: Is a key player in the control of plasma membrane curvature, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:24755653). Is a negative regulator of endocytosis (By similarity). Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:27179792). In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity). May be involved in the regulation of MYC activity and the control cell proliferation (PubMed:8782822). Has actin bundling activity and stabilizes actin filaments against depolymerization in vitro (PubMed:28893863). {ECO:0000250|UniProtKB:O08839, ECO:0000269|PubMed:24755653, ECO:0000269|PubMed:27179792, ECO:0000269|PubMed:28893863, ECO:0000269|PubMed:8782822}.
uniprot
proteins
mass_dalton
64699
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by protein kinase C. {ECO:0000250}.
uniprot
proteins
pubmed
10903846
uniprot
proteins
pubmed
12668730
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16530520
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17676042
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20142620
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24755653
uniprot
proteins
pubmed
25260562
uniprot
proteins
pubmed
27179792
uniprot
proteins
pubmed
27488240
uniprot
proteins
pubmed
28893863
uniprot
proteins
pubmed
29950440
uniprot
proteins
pubmed
8782822
uniprot
proteins
pubmed
9182667
uniprot
proteins
pubmed
9195986
uniprot
proteins
pubmed
9223448
uniprot
proteins
pubmed
9395479
uniprot
proteins
pubmed
9418903
uniprot
proteins
pubmed
9603201
uniprot
proteins
sequence_length
593
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform BIN1]: Nucleus {ECO:0000269|PubMed:8782822}. Cytoplasm {ECO:0000269|PubMed:9182667}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}.; SUBCELLULAR LOCATION: [Isoform IIA]: Cytoplasm {ECO:0000269|PubMed:9182667}.
uniprot
proteins