AMER1
entrez
139285
canonical
uniprot
Q5JTC6
canonical
ensembl
ENSG00000184675
resolver
ensp
ENSP00000364003
resolver
genesymbol
AMER1
resolver
genesymbol_syn
FAM123B
resolver
genesymbol_syn
WTX
resolver
hgnc
HGNC:26837
resolver
uniprot
A2IB86
resolver
uniprot
Q8N885
resolver
uniprot_entry
AMER1_HUMAN
resolver
uniprot_sec
A2IB86
resolver
uniprot_sec
Q8N885
resolver
amino_acid_sequence
METQKDEAAQAKGAAASGSTREQTAEKGAKNKAAEATEGPTSEPSSSGPGRLKKTAMKLFGGKKGICTLPSFFGGGRSKGSGKGSSKKGLSKSKTHDGLSEAAHGPEDVVSEGTGFSLPLPELPCQFPSSQSAHGALETGSRCKTSVAGATEKAVAEKFPSMPKPKKGLKGFFSSIRRHRKSKVTGAEQSEPGAKGPERVRARPHEHVSSAPQVPCFEETFQAPRKENANPQDAPGPKVSPTPEPSPPATEKMACKDPEKPMEACASAHVQPKPAPEASSLEEPHSPETGEKVVAGEVNPPNGPVGDPLSLLFGDVTSLKSFDSLTGCGDIIAEQDMDSMTDSMASGGQRANRDGTKRSSCLVTYQGGGEEMALPDDDDEEEEEEEEVELEEEEEEVKEEEEDDDLEYLWETAQMYPRPNMNLGYHPTTSPGHHGYMLLDPVRSYPGLAPGELLTPQSDQQESAPNSDEGYYDSTTPGFEDDSGEALGLVRRDCLPRDSYSGDALYEFYEPDDSLENSPPGDDCLYDLHGRSSEMFDPFLNFEPFLSSRPPGAMETEEERLVTIQKQLLYWELRREQLEAQEARAREAHAREAHAREAYTREAYGREAYAREAHTWEAHGREARTREAQAREVRCRETQVRETQARQEKPVLEYQMRPLGPSVMGLAAGVSGTSQISHRGITSAFPTTASSEPDWRDFRPLEKRYEGTCSKKDQSTCLMQLFQSDAMFEPDMQEANFGGSPRRAYPTYSPPEDPEEEEVEKEGNATVSFSQALVEFTSNGNLFSSMSCSSDSDSSFTQNLPELPPMVTFDIADVERDGEGKCEENPEFHNDEDLAASLEAFELGYYHKHAFNNYHSRFYQGLPWGVSSLPRYLGLPGLHPRPPPAAMALNRRSRSLDTAETLEMELSNSHLVQGYLESDELQAQQEDSDEEDEEEEEGEWSRDSPLSLYTEPPGAYDWPAWAPCPLPVGPGPAWISPNQLDRPSSQSPYRQATCCIPPMTMSISLSVPESRAPGESGPQLARPSHLHLPMGPCYNLQPQASQSMRARPRDVLLPVDEPSCSSSSGGFSPSPLPQAKPVGITHGIPQLPRVRPEHPQPQPTHYGPSSLDLSKERAEQGASLATSYSSTAMNGNLAK
uniprot
proteins
disease_involvement
DISEASE: Osteopathia striata with cranial sclerosis (OSCS) [MIM:300373]: An X-linked dominant sclerosing bone dysplasia that presents in females with macrocephaly, cleft palate, facial palsy, conductive hearing loss, mild learning disabilities, sclerosis of the long bones and skull. Longitudinal striations are visible on radiographs of the long bones, pelvis, and scapulae (osteopathia striata). In males this entity is usually associated with fetal or neonatal lethality. Occasional surviving males have, in addition to hyperostosis, cardiac, intestinal, and genitourinary malformations. {ECO:0000269|PubMed:19079258}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Regulator of the canonical Wnt signaling pathway. Acts by specifically binding phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2), translocating to the cell membrane and interacting with key regulators of the canonical Wnt signaling pathway, such as components of the beta-catenin destruction complex. Acts both as a positive and negative regulator of the Wnt signaling pathway, depending on the context: acts as a positive regulator by promoting LRP6 phosphorylation. Also acts as a negative regulator by acting as a scaffold protein for the beta-catenin destruction complex and promoting stabilization of Axin at the cell membrane. Promotes CTNNB1 ubiquitination and degradation. Involved in kidney development. {ECO:0000269|PubMed:17510365, ECO:0000269|PubMed:17925383, ECO:0000269|PubMed:19416806, ECO:0000269|PubMed:21304492, ECO:0000269|PubMed:21498506}.
uniprot
proteins
mass_dalton
124029
uniprot
proteins
mutagenesis
MUTAGEN 54; /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-58; A-79; A-83; A-166; A-181 and A-183."; /evidence="ECO:0000269|PubMed:21304492"; MUTAGEN 58; /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-79; A-83; A-166; A-181 and A-183."; /evidence="ECO:0000269|PubMed:21304492"; MUTAGEN 79; /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-83; A-166; A-181 and A-183."; /evidence="ECO:0000269|PubMed:21304492"; MUTAGEN 83; /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-79; A-166; A-181 and A-183."; /evidence="ECO:0000269|PubMed:21304492"; MUTAGEN 166; /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-79; A-83; A-181 and A-183."; /evidence="ECO:0000269|PubMed:21304492"; MUTAGEN 181; /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-79; A-83; A-166 and A-183."; /evidence="ECO:0000269|PubMed:21304492"; MUTAGEN 183; /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and cell membrane localization; when associated with A-54; A-58; A-79; A-83; A-166 and A-181."; /evidence="ECO:0000269|PubMed:21304492
uniprot
proteins
protein_family
Amer family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
17204608
uniprot
proteins
pubmed
17510365
uniprot
proteins
pubmed
17925383
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19079258
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19416806
uniprot
proteins
pubmed
20843316
uniprot
proteins
pubmed
21304492
uniprot
proteins
pubmed
21498506
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23092983
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
1135
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus. Note=Shuttles between nucleus and cytoplasm. Detected in nuclear paraspeckles that are found close to splicing speckles. Translocates to the cell membrane following binding to PtdIns(4,5)P2.
uniprot
proteins