FNBP1
entrez
23048
canonical
uniprot
Q96RU3
canonical
ensembl
ENSG00000187239
resolver
ensp
ENSP00000347907
resolver
ensp
ENSP00000413625
resolver
ensp
ENSP00000415602
resolver
ensp
ENSP00000514403
resolver
ensp
ENSP00000515358
resolver
ensp
ENSP00000515359
resolver
ensp
ENSP00000515374
resolver
ensp
ENSP00000515375
resolver
ensp
ENSP00000515376
resolver
ensp
ENSP00000577798
resolver
ensp
ENSP00000577799
resolver
ensp
ENSP00000577800
resolver
ensp
ENSP00000577801
resolver
ensp
ENSP00000577802
resolver
ensp
ENSP00000588103
resolver
ensp
ENSP00000616073
resolver
ensp
ENSP00000676056
resolver
ensp
ENSP00000676057
resolver
ensp
ENSP00000676059
resolver
ensp
ENSP00000676060
resolver
ensp
ENSP00000676061
resolver
ensp
ENSP00000676063
resolver
ensp
ENSP00000716231
resolver
ensp
ENSP00000716232
resolver
ensp
ENSP00000716233
resolver
ensp
ENSP00000716234
resolver
ensp
ENSP00000780558
resolver
ensp
ENSP00000783475
resolver
enst
ENST00000449089
resolver
enst
ENST00000699492
resolver
enst
ENST00000703533
resolver
enst
ENST00000703559
resolver
genesymbol
FNBP1
resolver
genesymbol_syn
FBP17
resolver
genesymbol_syn
KIAA0554
resolver
hgnc
HGNC:17069
resolver
uniprot
A0A8V8TQ35
resolver
uniprot
A0A994J3U5
resolver
uniprot
A0A994J3V8
resolver
uniprot
B7ZL12
resolver
uniprot
B7ZL13
resolver
uniprot
B7ZL14
resolver
uniprot
E7EPB7
resolver
uniprot
E9PGQ4
resolver
uniprot
H0Y7W6
resolver
uniprot
O60301
resolver
uniprot
Q3MIN8
resolver
uniprot
Q5TC87
resolver
uniprot
Q5TC88
resolver
uniprot
Q6P658
resolver
uniprot
Q7LGG2
resolver
uniprot
Q9H8H8
resolver
uniprot
Q9NWD1
resolver
uniprot_entry
A0A8V8TQ35_HUMAN
resolver
uniprot_entry
A0A994J3U5_HUMAN
resolver
uniprot_entry
A0A994J3V8_HUMAN
resolver
uniprot_entry
B7ZL13_HUMAN
resolver
uniprot_entry
B7ZL14_HUMAN
resolver
uniprot_entry
FNBP1_HUMAN
resolver
uniprot_entry
H0Y7W6_HUMAN
resolver
uniprot_sec
B7ZL12
resolver
uniprot_sec
E7EPB7
resolver
uniprot_sec
E9PGQ4
resolver
uniprot_sec
O60301
resolver
uniprot_sec
Q3MIN8
resolver
uniprot_sec
Q5TC87
resolver
uniprot_sec
Q5TC88
resolver
uniprot_sec
Q6P658
resolver
uniprot_sec
Q7LGG2
resolver
uniprot_sec
Q9H8H8
resolver
uniprot_sec
Q9NWD1
resolver
amino_acid_sequence
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRHQMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDELNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLAEVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVCLDKNAKDS
uniprot
proteins
disease_involvement
DISEASE: Note=A chromosomal aberration involving FNBP1 is found in acute leukemias. Translocation t(9;11)(q34;q23) with KMT2A/MLL1. The relatively low incidence of the KMT2A/MLL1-FNBP1 fusion protein in acute leukemia may reflect the marginal capacity of this fusion protein to induce cellular transformation.
uniprot
proteins
function
FUNCTION: May act as a link between RND2 signaling and regulation of the actin cytoskeleton (By similarity). Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL. {ECO:0000250, ECO:0000269|PubMed:15252009, ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391, ECO:0000269|PubMed:16418535, ECO:0000269|PubMed:17512409}.
uniprot
proteins
mass_dalton
71307
uniprot
proteins
mutagenesis
MUTAGEN 7; /note="L->E: Impairs membrane tubulation but does not affect lipid-binding."; /evidence="ECO:0000269|PubMed:16326391"; MUTAGEN 33; /note="K->E: Abolishes membrane invagination."; /evidence="ECO:0000269|PubMed:16418535, ECO:0000269|PubMed:17512409"; MUTAGEN 33; /note="K->Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-35."; /evidence="ECO:0000269|PubMed:16418535, ECO:0000269|PubMed:17512409"; MUTAGEN 35; /note="R->Q: Impairs lipid-binding and induction of membrane tubulation; when associated with Q-33."; /evidence="ECO:0000269|PubMed:16418535"; MUTAGEN 51..52; /note="KK->QQ: Impairs lipid-binding and induction of membrane tubulation."; /evidence="ECO:0000269|PubMed:16418535"; MUTAGEN 113..114; /note="RK->QQ: Impairs lipid-binding and induction of membrane tubulation."; /evidence="ECO:0000269|PubMed:16418535"; MUTAGEN 165; /note="T->A: Abolishes membrane invagination."; /evidence="ECO:0000269|PubMed:17512409"; MUTAGEN 166; /note="K->A: Abolishes membrane invagination."; /evidence="ECO:0000269|PubMed:17512409"; MUTAGEN 168; /note="D->A,N,R: No significant effect."; /evidence="ECO:0000269|PubMed:17512409"; MUTAGEN 210; /note="P->A: Disrupts helix kink and moderately increases diameter of the induced tubular membrane."; /evidence="ECO:0000269|PubMed:17512409"; MUTAGEN 515..520; /note="Missing: Abrogates interaction with TNKS."; /evidence="ECO:0000269|PubMed:14596906"; MUTAGEN 515; /note="R->A: Impairs interaction with TNKS."; /evidence="ECO:0000269|PubMed:14596906"; MUTAGEN 519; /note="D->A: Impairs interaction with TNKS; when associated with A-515."; /evidence="ECO:0000269|PubMed:14596906"; MUTAGEN 602; /note="P->L: Abrogates interaction with DNM1, DNM2 and DNM3."; /evidence="ECO:0000269|PubMed:15252009
uniprot
proteins
protein_family
FNBP1 family
uniprot
proteins
pubmed
11431473
uniprot
proteins
pubmed
11438682
uniprot
proteins
pubmed
12023017
uniprot
proteins
pubmed
14596906
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15047863
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15252009
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16318909
uniprot
proteins
pubmed
16326391
uniprot
proteins
pubmed
16418535
uniprot
proteins
pubmed
16630611
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
17512409
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19367720
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
9628581
uniprot
proteins
sequence_length
617
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Cytoplasmic vesicle. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-coated pit. Note=Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes.
uniprot
proteins