Asap1
entrez
13196
canonical
uniprot
Q9QWY8
canonical
ensembl
ENSMUSG00000022377
resolver
ensp
ENSMUSP00000105742
resolver
ensp
ENSMUSP00000134825
resolver
ensp
ENSMUSP00000134877
resolver
ensp
ENSMUSP00000135172
resolver
ensp
ENSMUSP00000135190
resolver
ensp
ENSMUSP00000135346
resolver
ensp
ENSMUSP00000135359
resolver
ensp
ENSMUSP00000135643
resolver
ensp
ENSMUSP00000135718
resolver
enst
ENSMUST00000175799
resolver
enst
ENSMUST00000176014
resolver
enst
ENSMUST00000177035
resolver
enst
ENSMUST00000177083
resolver
enst
ENSMUST00000177371
resolver
genesymbol
Asap1
resolver
genesymbol_syn
Ddef1
resolver
genesymbol_syn
Kiaa1249
resolver
genesymbol_syn
Shag1
resolver
uniprot
E9QMJ1
resolver
uniprot
H3BJY2
resolver
uniprot
H3BKD4
resolver
uniprot
H3BKE6
resolver
uniprot
H3BL41
resolver
uniprot
O08612
resolver
uniprot
Q3TXY1
resolver
uniprot
Q3UJA5
resolver
uniprot
Q505F0
resolver
uniprot
Q80TG8
resolver
uniprot
Q80UV6
resolver
uniprot
Q99LV8
resolver
uniprot
Q9Z2B6
resolver
uniprot_entry
ASAP1_MOUSE
resolver
uniprot_entry
E9QMJ1_MOUSE
resolver
uniprot_entry
H3BJY2_MOUSE
resolver
uniprot_entry
H3BKD4_MOUSE
resolver
uniprot_entry
H3BKE6_MOUSE
resolver
uniprot_entry
H3BL41_MOUSE
resolver
uniprot_entry
Q3TXY1_MOUSE
resolver
uniprot_entry
Q3UJA5_MOUSE
resolver
uniprot_sec
O08612
resolver
uniprot_sec
Q505F0
resolver
uniprot_sec
Q80TG8
resolver
uniprot_sec
Q80UV6
resolver
uniprot_sec
Q99LV8
resolver
uniprot_sec
Q9Z2B6
resolver
activity_regulation
ACTIVITY REGULATION: Activity stimulated by phosphatidylinositol 4,5-bisphosphate (PIP2).
uniprot
proteins
amino_acid_sequence
MRSSASRLSSFSSRDSLWNRMPDQISVSEFIAETTEDYNSPTTSSFTTRLHNCRNTVTLLEEALDQDRTALQKVKKSVKAIYNSGQDHVQNEENYAQVLDKFGSNFLSRDNPDLGTAFVKFSTLTKELSTLLKNLLQGLSHNVIFTLDSLLKGDLKGVKGDLKKPFDKAWKDYETKFTKIEKEKREHAKQHGMIRTEITGAEIAEEMEKERRLFQLQMCEYLIKVNEIKTKKGVDLLQNLIKYYHAQCNFFQDGLKTADKLKQYIEKLAADLYNIKQTQDEEKKQLTALRDLIKSSLQLDPKEVGGLYVASRANSSRRDSQSRQGGYSMHQLQGNKEYGSEKKGFLLKKSDGIRKVWQRRKCAVKNGILTISHATSNRQPAKLNLLTCQVKPNAEDKKSFDLISHNRTYHFQAEDEQDYIAWISVLTNSKEEALTMAFRGEQSTGENSLEDLTKAIIEDVQRLPGNDICCDCGSSEPTWLSTNLGILTCIECSGIHREMGVHISRIQSLELDKLGTSELLLAKNVGNNSFNDIMEANLPSPSPKPTPSSDMTVRKEYITAKYVDHRFSRKTCASSSAKLNELLEAIKSRDLLALIQVYAEGVELMEPLLEPGQELGETALHLAVRTADQTSLHLVDFLVQNCGNLDKQTSVGNTVLHYCSMYGKPECLKLLLRSKPTVDIVNQNGETALDIAKRLKATQCEDLLSQAKSGKFNPHVHVEYEWNLRQDEMDESDDDLDDKPSPIKKERSPRPQSFCHSSSISPQDKLALPGFSTPRDKQRLSYGAFTNQIFASTSTDLPTSPTSEAPPLPPRNAGKGPTGPPSTLPLGTQTSSGSSTLSKKRPPPPPPGHKRTLSDPPSPLPHGPPNKGAIPWGNDVGPLSSSKTANKFEGLSQQASTSSAKTALGPRVLPKLPQKVALRKTETSHHLSLDRTNIPPETFQKSSQLTELPQKPPLGELPPKPVELAPKPQVGELPPKPGELPPKPQLGDLPPKPQLSDLPPKPQMKDLPPKPQLGDLLAKSQAGDVSAKVQPPSEVTQRSHTGDLSPNVQSRDAIQKQASEDSNDLTPTLPETPVPLPRKINTGKNKVRRVKTIYDCQADNDDELTFIEGEVIIVTGEEDQEWWIGHIEGQPERKGVFPVSFVHILSD
uniprot
proteins
function
FUNCTION: May function as a signal transduction protein involved in the differentiation of fibroblasts into adipocytes and possibly other cell types. Possesses phosphatidylinositol 4,5-bisphosphate-dependent GTPase-activating protein activity for ARF1 (ADP ribosylation factor 1) and ARF5 and a lesser activity towards ARF6. May coordinate membrane trafficking with cell growth or actin cytoskeleton remodeling by binding to both SRC and PIP2. Part of the ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, RAB11FIP3 and ARF4, which direct preciliary vesicle trafficking to mother centriole and ciliogenesis initiation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9ULH1}.
uniprot
proteins
mass_dalton
127421
uniprot
proteins
mutagenesis
MUTAGEN 811; /note="R->A: Significant reduction in binding to SRC and CRK and loss of phosphorylation. Loss of binding and phosphorylation; when associated with A-910 and A-913."; /evidence="ECO:0000269|PubMed:9819391"; MUTAGEN 910; /note="P->A: Significant reduction in binding to SRC and CRK and decrease in phosphorylation; when associated with A-913. Loss of binding and phosphorylation; when associated with A-811 and A-913."; /evidence="ECO:0000269|PubMed:9819391"; MUTAGEN 913; /note="P->A: Significant reduction in binding to SRC and CRK and decrease in phosphorylation; when associated with A-910. Loss of binding and phosphorylation; when associated with A-811 and A-910."; /evidence="ECO:0000269|PubMed:9819391
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues by SRC. {ECO:0000269|PubMed:12771146}.
uniprot
proteins
pubmed
10022919
uniprot
proteins
pubmed
12149250
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
12771146
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
18685082
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
9126384
uniprot
proteins
pubmed
9819391
uniprot
proteins
sequence_length
1147
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Membrane. Golgi apparatus {ECO:0000250|UniProtKB:Q9ULH1}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9ULH1}. Note=Predominantly cytoplasmic. Partially membrane-associated.
uniprot
proteins