AFAP1
entrez
60312
canonical
uniprot
Q8N556
canonical
ensembl
ENSG00000196526
resolver
ensp
ENSP00000351245
resolver
ensp
ENSP00000353402
resolver
ensp
ENSP00000371983
resolver
ensp
ENSP00000410689
resolver
ensp
ENSP00000604908
resolver
ensp
ENSP00000728826
resolver
genesymbol
AFAP1
resolver
genesymbol_syn
AFAP
resolver
hgnc
HGNC:24017
resolver
uniprot
A8K442
resolver
uniprot
B4DMU2
resolver
uniprot
E9PDT7
resolver
uniprot
Q59EY5
resolver
uniprot
Q6ZRV0
resolver
uniprot
Q9HBY1
resolver
uniprot_entry
AFAP1_HUMAN
resolver
uniprot_entry
Q6ZRV0_HUMAN
resolver
uniprot_sec
A8K442
resolver
uniprot_sec
B4DMU2
resolver
uniprot_sec
E9PDT7
resolver
uniprot_sec
Q59EY5
resolver
uniprot_sec
Q9HBY1
resolver
amino_acid_sequence
MEELIVELRLFLELLDHEYLTSTVREKKAVITNILLRIQSSKGFDVKDHAQKQETANSLPAPPQMPLPEIPQPWLPPDSGPPPLPTSSLPEGYYEEAVPLSPGKAPEYITSNYDSDAMSSSYESYDEEEEDGKGKKTRHQWPSEEASMDLVKDAKICAFLLRKKRFGQWTKLLCVIKDTKLLCYKSSKDQQPQMELPLQGCNITYIPKDSKKKKHELKITQQGTDPLVLAVQSKEQAEQWLKVIKEAYSGCSGPVDSECPPPPSSPVHKAELEKKLSSERPSSDGEGVVENGITTCNGKEQVKRKKSSKSEAKGTVSKVTGKKITKIISLGKKKPSTDEQTSSAEEDVPTCGYLNVLSNSRWRERWCRVKDNKLIFHKDRTDLKTHIVSIPLRGCEVIPGLDSKHPLTFRLLRNGQEVAVLEASSSEDMGRWIGILLAETGSSTDPEALHYDYIDVEMSASVIQTAKQTFCFMNRRVISANPYLGGTSNGYAHPSGTALHYDDVPCINGSLKGKKPPVASNGVTGKGKTLSSQPKKADPAAVVKRTGSNAAQYKYGKNRVEADAKRLQTKEEELLKRKEALRNRLAQLRKERKDLRAAIEVNAGRKPQAILEEKLKQLEEECRQKEAERVSLELELTEVKESLKKALAGGVTLGLAIEPKSGTSSPQSPVFRHRTLENSPISSCDTSDTEGPVPVNSAAVLKKSQAAPGSSPCRGHVLRKAKEWELKNGT
uniprot
proteins
function
FUNCTION: Can cross-link actin filaments into both network and bundle structures (By similarity). May modulate changes in actin filament integrity and induce lamellipodia formation. May function as an adapter molecule that links other proteins, such as SRC and PKC to the actin cytoskeleton. Seems to play a role in the development and progression of prostate adenocarcinoma by regulating cell-matrix adhesions and migration in the cancer cells. {ECO:0000250, ECO:0000269|PubMed:15485829}.
uniprot
proteins
mass_dalton
80725
uniprot
proteins
mutagenesis
MUTAGEN 71; /note="P->A: Decreased tyrosine phosphorylation."; /evidence="ECO:0000269|PubMed:15485829"; MUTAGEN 77; /note="P->A: No effect on tyrosine phosphorylation."; /evidence="ECO:0000269|PubMed:15485829"; MUTAGEN 93; /note="Y->F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-94; F-125; F-451 and F-453."; /evidence="ECO:0000269|PubMed:15485829"; MUTAGEN 94; /note="Y->F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-125; F-451 and F-453."; /evidence="ECO:0000269|PubMed:15485829"; MUTAGEN 125; /note="Y->F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-451 and F-453."; /evidence="ECO:0000269|PubMed:15485829"; MUTAGEN 451; /note="Y->F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-453."; /evidence="ECO:0000269|PubMed:15485829"; MUTAGEN 453; /note="Y->F: Reduces phosphorylation and phosphorylation of SRC at Y-416; when associated with F-93; F-94; F-125 and F-451."; /evidence="ECO:0000269|PubMed:15485829
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on tyrosine residues by SRC. {ECO:0000269|PubMed:15485829}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15485829
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17520695
uniprot
proteins
pubmed
17885682
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
730
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, stress fiber {ECO:0000269|PubMed:15485829}.
uniprot
proteins