Q61315
uniprot
Q61315
canonical
amino_acid_sequence
MAAASYDQLLKQVEALKMENSNLRQELEDNSNHLTKLETEASNMKEVLKQLQGSIEDETMTSGQIDLLERLKEFNLDSNFPGVKLRSKMSLRSYGSREGSVSSRSGECSPVPMGSFPRRTFVNGSRESTGYLEELEKERSLLLADLDKEEKEKDWYYAQLQNLTKRIDSLPLTENFSLQTDMTRRQLEYEARQIRAAMEEQLGTCQDMEKRAQRRIARIQQIEKDILRVRQLLQSQAAEAERSSQSRHDAASHEAGRQHEGHGVAESNTAASSSGQSPATRVDHETASVLSSSGTHSAPRRLTSHLGTKVEMVYSLLSMLGTHDKDDMSRTLLAMSSSQDSCISMRQSGCLPLLIQLLHGNDKDSVLLGNSRGSKEARARASAALHNIIHSQPDDKRGRREIRVLHLLEQIRAYCETCWEWQEAHEQGMDQDKNPMPAPVEHQICPAVCVLMKLSFDEEHRHAMNELGGLQAIAELLQVDCEMYGLTNDHYSVTLRRYAGMALTNLTFGDVANKATLCSMKGCMRALVAQLKSESEDLQQVIASVLRNLSWRADVNSKKTLREVGSVKALMECALEVKKESTLKSVLSALWNLSAHCTENKADICAVDGALAFLVGTLTYRSQTNTLAIIESGGGILRNVSSLIATNEDHRQILRENNCLQTLLQHLKSHSLTIVSNACGTLWNLSARNPKDQEALWDMGAVSMLKNLIHSKHKMIAMGSAAALRNLMANRPAKYKDANIMSPGSSLPSLHVRKQKALEAELDAQHLSETFDNIDNLSPKASHRSKQRHKQNLYGDYAFDANRHDDSRSDNFNTGNMTVLSPYLNTTVLPSSSSSRGSLDSSRSEKDRSLERERGIGLSAYHPTTENAGTSSKRGLQITTTAAQIAKVMEEVSAIHTSQDDRSSASTTEFHCVADDRSAARRSSASHTHSNTYNFTKSENSNRTCSMPYAKVEYKRSSNDSLNSVTSSDGYGKRGQMKPSVESYSEDDESKFCSYGQYPADLAHKIHSANHMDDNDGELDTPINYSLKYSDEQLNSGRQSPSQNERWARPKHVIEDEIKQNEQRQARSQNTSYPVYSENTDDKHLKFQPHFGQQECVSPYRSRGTSGSETNRMGSSHAINQNVNQSLCQEDDYEDDKPTNYSERYSEEEQHEEEEERPTNYSIKYNEEKHHVDQPIDYSLKYATDISSSQKPSFSFSKNSSAQSTKPEHLSPSSENTAVPPSNAKRQNQLRPSSAQRNGQTQKGTTCKVPSINQETIQTYCVEDTPICFSRCSSLSSLSSADDEIGCDQTTQEADSANTLQTAEVKENDVTRSAEDPATEVPAVSQNARAKPSRLQASGLSSESTRHNKAVEFSSGAKSPSKSGAQTPKSPPEHYVQETPLVFSRCTSVSSLDSFESRSIASSVQSEPCSGMVSGIISPSDLPDSPGQTMPPSRSKTPPPPPQTVQAKREVPKSKVPAAEKRESGPKQTAVNAAVQRVQVLPDVDTLLHFATESTPDGFSCSSSLSALSLDEPFIQKDVELRIMPPVQENDNGNETESEQPEESNENQDKEVEKPDSEKDLLDDSDDDDIEILEECIISAMPTKSSRKAKKLAQTASKLPPPVARKPSQLPVYKLLPAQNRLQAQKHVSFTPGDDVPRVYCVEGTPINFSTATSLSDLTIESPPNELATGDGVRAGIQSGEFEKRDTIPTEGRSTDDAQRGKISSIVTPDLDDNKAEEGDILAECINSAMPKGKSHKPFRVKKIMDQVQQASSTSSGANKNQVDTKKKKPTSPVKPMPQNTEYRTRVRKNTDSKVNVNTEETFSDNKDSKKPSLQTNAKAFNEKLPNNEDRVRGTFALDSPHHYTPIEGTPYCFSRNDSLSSLDFDDDDVDLSREKAELRKGKESKDSEAKVTCRPEPNSSQQAASKSQASIKHPANRAQSKPVLQKQPTFPQSSKDGPDRGAATDEKLQNLAIENTPVCFSRNSSLSSLSDIDQENNNNKESEPIKEAEPANSQGEPSKPQASGYAPKSFHVEDTPVCFSRNSSLSSLSIDSEDDLLQECISSAMPKKKRPSRLKSESEKQSPRKVGGILAEDLTLDLKDLQRPDSEHAFSPGSENFDWKAIQEGANSIVSSLHQAAAAAACLSRQASSDSDSILSLKSGISLGSPFHLTPDQEEKPFTSNKGPRILKPGEKSTLEAKKIESENKGIKGGKKVYKSLITGKIRSNSEISSQMKQPLPTNMPSISRGRTMIHIPGLRNSSSSTSPVSKKGPPLKTPASKSPSEGPGATTSPRGTKPAGKSELSPITRQTSQISGSNKGSSRSGSRDSTPSRPTQQPLSRPMQSPGRNSISPGRNGISPPNKLSQLPRTSSPSTASTKSSGSGKMSYTSPGRQLSQQNLTKQASLSKNASSIPRSESASKGLNQMSNGNGSNKKVELSRMSSTKSSGSESDSSERPALVRQSTFIKEAPSPTLRRKLEESASFESLSPSSRPDSPTRSQAQTPVLSPSLPDMSLSTHPSVQAGGWRKLPPNLSPTIEYNDGRPTKRHDIARSHSESPSRLPINRAGTWKREHSKHSSSLPRVSTWRRTGSSSSILSASSESSEKAKSEDERHVSSMPAPRQMKENQVPTKGTWRKIKESDISPTGMASQSASSGAASGAESKPLIYQMAPPVSKTEDVWVRIEDCPINNPRSGRSPTGNTPPVIDSVSEKGSSSIKDSKDSKDTHGKQSVGSGSPVQTVGLETRLNSFVQVEAPEQKGTEAKPGQSNPVSIAETAETCIAERTPFSSSSSSKHSSPSGTVAARVTPFNYNPSPRKSSADSTSARPSQIPTPVSTNTKKRDSKTDITESSGAQSPKRHSGSYLVTSV
uniprot
proteins
function
FUNCTION: Tumor suppressor. Promotes rapid degradation of CTNNB1 and participates in Wnt signaling as a negative regulator. APC activity is correlated with its phosphorylation state. Activates the GEF activity of SPATA13 and ARHGEF4. Plays a role in hepatocyte growth factor (HGF)-induced cell migration (By similarity). Required for MMP9 up-regulation via the JNK signaling pathway in colorectal tumor cells (PubMed:19893577). Associates with both microtubules and actin filaments, components of the cytoskeleton (By similarity). Plays a role in mediating the organization of F-actin into ordered bundles (By similarity). Functions downstream of Rho GTPases and DIAPH1 to selectively stabilize microtubules (PubMed:15311282). Acts as a mediator of ERBB2-dependent stabilization of microtubules at the cell cortex. It is required for the localization of MACF1 to the cell membrane and this localization of MACF1 is critical for its function in microtubule stabilization (By similarity). {ECO:0000250|UniProtKB:P25054, ECO:0000269|PubMed:15311282, ECO:0000269|PubMed:19893577}.
uniprot
proteins
mass_dalton
311089
uniprot
proteins
post_translational_modification
PTM: Phosphorylated; phosphorylation enhances the F-actin bundling activity (By similarity). Phosphorylated by GSK3B. {ECO:0000250, ECO:0000250|UniProtKB:P25054}.; PTM: Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is facilitated by Axin. Deubiquitinated by ZRANB1/TRABID (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
Adenomatous polyposis coli (APC) family
uniprot
proteins
pubmed
1350108
uniprot
proteins
pubmed
15311282
uniprot
proteins
pubmed
16611247
uniprot
proteins
pubmed
19893577
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8242607
uniprot
proteins
sequence_length
2845
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:P25054}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P25054}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P25054}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P25054}. Cytoplasm {ECO:0000250|UniProtKB:P25054}. Cell membrane {ECO:0000250|UniProtKB:P25054}. Note=Associated with the microtubule network at the growing distal tip of microtubules. MAPRE1 may be required for targeting to the growing microtubule plus ends. Accumulates in the lamellipodium and ruffle membrane in response to hepatocyte growth factor (HGF) treatment. The MEMO1-RHOA-DIAPH1 signaling pathway controls localization of the phosphorylated form to the cell membrane. {ECO:0000250|UniProtKB:P25054}.
uniprot
proteins