ARAP1
entrez
116985
canonical
uniprot
Q96P48
canonical
ensembl
ENSG00000186635
resolver
ensp
ENSP00000335506
resolver
ensp
ENSP00000377233
resolver
ensp
ENSP00000392264
resolver
ensp
ENSP00000403127
resolver
enst
ENST00000426523
resolver
genesymbol
ARAP1
resolver
genesymbol_syn
CENTD2
resolver
genesymbol_syn
KIAA0782
resolver
hgnc
HGNC:16925
resolver
uniprot
A3KLL7
resolver
uniprot
B2RTS2
resolver
uniprot
E7EU13
resolver
uniprot
O94879
resolver
uniprot
Q4LDD5
resolver
uniprot
Q59FI7
resolver
uniprot
Q6PHS3
resolver
uniprot
Q8WU51
resolver
uniprot
Q96HP6
resolver
uniprot
Q96L71
resolver
uniprot_entry
ARAP1_HUMAN
resolver
uniprot_entry
E7EU13_HUMAN
resolver
uniprot_sec
A3KLL7
resolver
uniprot_sec
B2RTS2
resolver
uniprot_sec
O94879
resolver
uniprot_sec
Q4LDD5
resolver
uniprot_sec
Q59FI7
resolver
uniprot_sec
Q6PHS3
resolver
uniprot_sec
Q8WU51
resolver
uniprot_sec
Q96HP6
resolver
uniprot_sec
Q96L71
resolver
amino_acid_sequence
MAEAGDAALSVAEWLRALHLEQYTGLFEQHGLVWATECQGLSDTRLMDMGMLLPGHRRRILAGLLRAHTSPAPAPRPTPRPVPMKRHIFRSPPVPATPPEPLPTTTEDEGLPAAPPIPPRRSCLPPTCFTTPSTAAPDPVLPPLPAKRHLAELSVPPVPPRTGPPRLLVSLPTKEEESLLPSLSSPPQPQSEEPLSTLPQGPPQPPSPPPCPPEIPPKPVRLFPEFDDSDYDEVPEEGPGAPARVMTKKEEPPPSRVPRAVRVASLLSEGEELSGDDQGDEEEDDHAYEGVPNGGWHTSSLSLSLPSTIAAPHPMDGPPGGSTPVTPVIKAGWLDKNPPQGSYIYQKRWVRLDTDHLRYFDSNKDAYSKRFISVACISHVAAIGDQKFEVITNNRTFAFRAESDVERKEWMQALQQAMAEQRARARLSSAYLLGVPGSEQPDRAGSLELRGFKNKLYVAVVGDKVQLYKNLEEYHLGIGITFIDMSVGNVKEVDRRSFDLTTPYRIFSFSADSELEKEQWLEAMQGAIAEALSTSEVAERIWAAAPNRFCADCGAPQPDWASINLCVVICKRCAGEHRGLGAGVSKVRSLKMDRKVWTETLIELFLQLGNGAGNRFWAANVPPSEALQPSSSPSTRRCHLEAKYREGKYRRYHPLFGNQEELDKALCAAVTTTDLAETQALLGCGAGINCFSGDPEAPTPLALAEQAGQTLQMEFLRNNRTTEVPRLDSMKPLEKHYSVVLPTVSHSGFLYKTASAGKLLQDRRAREEFSRRWCVLGDGVLSYFENERAVTPNGEIRASEIVCLAVPPPDTHGFEHTFEVYTEGERLYLFGLESAEQAHEWVKCIAKAFVPPLAEDLLARDFERLGRLPYKAGLSLQRAQEGWFSLSGSELRAVFPEGPCEEPLQLRKLQELSIQGDSENQVLVLVERRRTLYIQGERRLDFMGWLGAIQKAAASMGDTLSEQQLGDSDIPVIVYRCVDYITQCGLTSEGIYRKCGQTSKTQRLLESLRQDARSVHLKEGEQHVDDVSSALKRFLRDLPDGLFTRAQRLTWLEASEIEDEEEKVSRYRELLVRLPPVNRATVKALISHLYCVQCFSDTNQMNVHNLAIVFGPTLFQTDGQDYKAGRVVEDLINHYVVVFSVDEEELRKQREEITAIVKMRVAGTASGTQHAGDFICTVYLEEKKAETEQHIKVPASMTAEELTLEILDRRNVGIREKDYWTCFEVNEREEAERPLHFAEKVLPILHGLGTDSHLVVKKHQAMEAMLLYLASRVGDTKHGMMKFREDRSLLGLGLPSGGFHDRYFILNSSCLRLYKEVRSQRPWSGAPETSHRPEKEWPIKSLKVYLGVKKKLRPPTCWGFTVVHETEKHEKQQWYLCCDTQMELREWFATFLFVQHDGLVWPSEPSRVSRAVPEVRLGSVSLIPLRGSENEMRRSVAAFTADPLSLLRNV
uniprot
proteins
function
FUNCTION: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members (PubMed:11804590, PubMed:19666464). Activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding and, to a lesser extent, by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) binding (PubMed:11804590). Has a preference for ARF1 and ARF5 (PubMed:11804590, PubMed:19666464). Positively regulates the ring size of circular dorsal ruffles and promotes macropinocytosis (PubMed:22573888). Acts as a bridging factor in osteoclasts to control actin and membrane dynamics (By similarity). Regulates the condensing of osteoclast podosomes into sealing zones which segregate the bone-facing membrane from other membrane domains and are required for osteoclast resorption activity (By similarity). Also regulates recruitment of the AP-3 complex to endosomal membranes and trafficking of lysosomal membrane proteins to the ruffled membrane border of osteoclasts to modulate bone resorption (By similarity). Regulates the endocytic trafficking of EGFR (PubMed:18764928, PubMed:18939958, PubMed:21275903). Regulates the incorporation of CD63 and CD9 into multivesicular bodies (PubMed:38682696). Required in the retinal pigment epithelium (RPE) for photoreceptor survival due to its role in promoting RPE phagocytosis (By similarity). {ECO:0000250|UniProtKB:Q4LDD4, ECO:0000269|PubMed:11804590, ECO:0000269|PubMed:18764928, ECO:0000269|PubMed:18939958, ECO:0000269|PubMed:19666464, ECO:0000269|PubMed:21275903, ECO:0000269|PubMed:22573888, ECO:0000269|PubMed:38682696}.
uniprot
proteins
mass_dalton
162192
uniprot
proteins
mutagenesis
MUTAGEN 23; /note="Y->F: No effect on phosphorylation by PTK6."; /evidence="ECO:0000269|PubMed:20554524"; MUTAGEN 81..86; /note="PVPMKR->AVAMKA: Reduced interaction with SH3KBP1."; /evidence="ECO:0000269|PubMed:21275903"; MUTAGEN 81; /note="P->A: Slightly reduced interaction with SH3KBP1."; /evidence="ECO:0000269|PubMed:21275903"; MUTAGEN 86..90; /note="RHIFR->AHIFA: Reduced interaction with SH3KBP1."; /evidence="ECO:0000269|PubMed:21275903"; MUTAGEN 231; /note="Y->F: Abolishes phosphorylation by PTK6."; /evidence="ECO:0000269|PubMed:20554524"; MUTAGEN 288; /note="Y->F: No effect on phosphorylation by PTK6."; /evidence="ECO:0000269|PubMed:20554524"; MUTAGEN 578; /note="R->K: Abolishes effect on circular dorsal ruffle size."; /evidence="ECO:0000269|PubMed:22573888"; MUTAGEN 993; /note="R->K: No effect on regulation of circular dorsal ruffle size."; /evidence="ECO:0000269|PubMed:22573888
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PTK6 following EGF stimulation which enhances EGFR signaling by delaying EGFR down-regulation; the interaction is mediated by the SH2 domain of PTK6 (PubMed:20554524). Phosphorylation promotes association with the Golgi apparatus and endosomes (PubMed:18939958). {ECO:0000269|PubMed:18939958, ECO:0000269|PubMed:20554524}.
uniprot
proteins
pubmed
11804590
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18165900
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18764928
uniprot
proteins
pubmed
18939958
uniprot
proteins
pubmed
19666464
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20554524
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21275903
uniprot
proteins
pubmed
22573888
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
38682696
uniprot
proteins
pubmed
9872452
uniprot
proteins
sequence_length
1450
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11804590}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:18939958}. Golgi apparatus, Golgi stack {ECO:0000269|PubMed:11804590, ECO:0000269|PubMed:18764928, ECO:0000269|PubMed:18939958}. Cell membrane {ECO:0000269|PubMed:18165900, ECO:0000269|PubMed:18939958, ECO:0000269|PubMed:22573888}; Peripheral membrane protein {ECO:0000305}. Endosome, multivesicular body {ECO:0000269|PubMed:18939958}. Cell projection, ruffle {ECO:0000269|PubMed:22573888}. Cell projection, podosome {ECO:0000250|UniProtKB:Q4LDD4}. Early endosome {ECO:0000250|UniProtKB:Q4LDD4}. Note=Associated with Golgi stacks in resting cells (PubMed:11804590). Throughout the cytoplasm and in surface protrusions in cells that are in the process of attaching to a surface and spreading (PubMed:11804590). Localizes to actin-rich podosomes, sealing zones and early endosomes in osteoclasts (By similarity). {ECO:0000250|UniProtKB:Q4LDD4, ECO:0000269|PubMed:11804590}.
uniprot
proteins