AMER1_HUMAN
ID AMER1_HUMAN Reviewed; 1135 AA.
AC Q5JTC6; A2IB86; Q8N885;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=APC membrane recruitment protein 1;
DE Short=Amer1;
DE AltName: Full=Protein FAM123B;
DE AltName: Full=Wilms tumor gene on the X chromosome protein;
GN Name=AMER1; Synonyms=FAM123B, WTX;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-292, AND INACTIVATION
RP IN WILMS TUMOR.
RX PubMed=17204608; DOI=10.1126/science.1137509;
RA Rivera M.N., Kim W.J., Wells J., Driscoll D.R., Brannigan B.W., Han M.,
RA Kim J.C., Feinberg A.P., Gerald W.L., Vargas S.O., Chin L., Iafrate A.J.,
RA Bell D.W., Haber D.A.;
RT "An X chromosome gene, WTX, is commonly inactivated in Wilms tumor.";
RL Science 315:642-645(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP INTERACTION WITH CTNNB1; KEAP1; AXIN1; APC; FBXW11 AND BTRC.
RX PubMed=17510365; DOI=10.1126/science/1141515;
RA Major M.B., Camp N.D., Berndt J.D., Yi X., Goldenberg S.J., Hubbert C.,
RA Biechele T.L., Gingras A.-C., Zheng N., Maccoss M.J., Angers S., Moon R.T.;
RT "Wilms tumor suppressor WTX negatively regulates WNT/beta-catenin
RT signaling.";
RL Science 316:1043-1046(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP INVOLVEMENT IN OSCS.
RX PubMed=19079258; DOI=10.1038/ng.270;
RA Jenkins Z.A., van Kogelenberg M., Morgan T., Jeffs A., Fukuzawa R.,
RA Pearl E., Thaller C., Hing A.V., Porteous M.E., Garcia-Minaur S.,
RA Bohring A., Lacombe D., Stewart F., Fiskerstrand T., Bindoff L.,
RA Berland S., Ades L.C., Tchan M., David A., Wilson L.C., Hennekam R.C.,
RA Donnai D., Mansour S., Cormier-Daire V., Robertson S.P.;
RT "Germline mutations in WTX cause a sclerosing skeletal dysplasia but do not
RT predispose to tumorigenesis.";
RL Nat. Genet. 41:95-100(2009).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, PTDINS(4,5)P2-BINDING, AND INTERACTION WITH
RP APC.
RX PubMed=17925383; DOI=10.1242/jcs.011320;
RA Grohmann A., Tanneberger K., Alzner A., Schneikert J., Behrens J.;
RT "AMER1 regulates the distribution of the tumor suppressor APC between
RT microtubules and the plasma membrane.";
RL J. Cell Sci. 120:3738-3747(2007).
RN [9]
RP FUNCTION, ALTERNATIVE SPLICING, INTERACTION WITH WT1, SUBCELLULAR LOCATION,
RP AND TISSUE SPECIFICITY.
RX PubMed=19416806; DOI=10.1073/pnas.0811349106;
RA Rivera M.N., Kim W.J., Wells J., Stone A., Burger A., Coffman E.J.,
RA Zhang J., Haber D.A.;
RT "The tumor suppressor WTX shuttles to the nucleus and modulates WT1
RT activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8338-8343(2009).
RN [10]
RP GENE FAMILY.
RX PubMed=20843316; DOI=10.1186/1471-2148-10-280;
RA Boutet A., Comai G., Schedl A.;
RT "The WTX/AMER1 gene family: evolution, signature and function.";
RL BMC Evol. Biol. 10:280-280(2010).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, PTDINS(4,5)P2-BINDING, INTERACTION WITH
RP LRP6, AND MUTAGENESIS OF LYS-54; LYS-58; LYS-79; LYS-83; LYS-166; LYS-181
RP AND LYS-183.
RX PubMed=21304492; DOI=10.1038/emboj.2011.28;
RA Tanneberger K., Pfister A.S., Brauburger K., Schneikert J.,
RA Hadjihannas M.V., Kriz V., Schulte G., Bryja V., Behrens J.;
RT "Amer1/WTX couples Wnt-induced formation of PtdIns(4,5)P2 to LRP6
RT phosphorylation.";
RL EMBO J. 30:1433-1443(2011).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1.
RX PubMed=21498506; DOI=10.1074/jbc.m111.224881;
RA Tanneberger K., Pfister A.S., Kriz V., Bryja V., Schambony A., Behrens J.;
RT "Structural and functional characterization of the Wnt inhibitor APC
RT membrane recruitment 1 (Amer1).";
RL J. Biol. Chem. 286:19204-19214(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP VARIANT CYS-178.
RX PubMed=23092983; DOI=10.1038/tp.2012.102;
RA Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B., Cohen D.,
RA Faudet A., Bouteiller D., Gilleron M., Jacquette A., Whalen S., Afenjar A.,
RA Perisse D., Laurent C., Dupuits C., Gautier C., Gerard M., Huguet G.,
RA Caillet S., Leheup B., Leboyer M., Gillberg C., Delorme R., Bourgeron T.,
RA Brice A., Depienne C.;
RT "Analysis of the chromosome X exome in patients with autism spectrum
RT disorders identified novel candidate genes, including TMLHE.";
RL Transl. Psychiatry 2:E179-E179(2012).
CC -!- FUNCTION: Regulator of the canonical Wnt signaling pathway. Acts by
CC specifically binding phosphatidylinositol 4,5-bisphosphate
CC (PtdIns(4,5)P2), translocating to the cell membrane and interacting
CC with key regulators of the canonical Wnt signaling pathway, such as
CC components of the beta-catenin destruction complex. Acts both as a
CC positive and negative regulator of the Wnt signaling pathway, depending
CC on the context: acts as a positive regulator by promoting LRP6
CC phosphorylation. Also acts as a negative regulator by acting as a
CC scaffold protein for the beta-catenin destruction complex and promoting
CC stabilization of Axin at the cell membrane. Promotes CTNNB1
CC ubiquitination and degradation. Involved in kidney development.
CC {ECO:0000269|PubMed:17510365, ECO:0000269|PubMed:17925383,
CC ECO:0000269|PubMed:19416806, ECO:0000269|PubMed:21304492,
CC ECO:0000269|PubMed:21498506}.
CC -!- SUBUNIT: Interacts with CTNNB1, AXIN1, LRP6, KEAP1, APC and BTRC.
CC Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein
CC ligase complexes containing BTRC and/or FBXW11. Identified in the beta-
CC catenin destruction complex containing CTNNB1, APC, AXIN1 and AXIN2.
CC Interacts with WT1. {ECO:0000269|PubMed:17510365,
CC ECO:0000269|PubMed:17925383, ECO:0000269|PubMed:19416806,
CC ECO:0000269|PubMed:21304492, ECO:0000269|PubMed:21498506}.
CC -!- INTERACTION:
CC Q5JTC6; Q8N944: AMER3; NbExp=4; IntAct=EBI-6169747, EBI-8869590;
CC Q5JTC6; P25054: APC; NbExp=4; IntAct=EBI-6169747, EBI-727707;
CC Q5JTC6; O15169: AXIN1; NbExp=7; IntAct=EBI-6169747, EBI-710484;
CC Q5JTC6; Q9Y297: BTRC; NbExp=5; IntAct=EBI-6169747, EBI-307461;
CC Q5JTC6; P35222: CTNNB1; NbExp=9; IntAct=EBI-6169747, EBI-491549;
CC Q5JTC6; Q9UKB1: FBXW11; NbExp=4; IntAct=EBI-6169747, EBI-355189;
CC Q5JTC6; Q14145: KEAP1; NbExp=2; IntAct=EBI-6169747, EBI-751001;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane
CC protein; Cytoplasmic side. Nucleus. Note=Shuttles between nucleus and
CC cytoplasm. Detected in nuclear paraspeckles that are found close to
CC splicing speckles. Translocates to the cell membrane following binding
CC to PtdIns(4,5)P2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Amer1-S1;
CC IsoId=Q5JTC6-1; Sequence=Displayed;
CC Name=2; Synonyms=Amer1-S2, Short;
CC IsoId=Q5JTC6-2; Sequence=VSP_024091, VSP_024092;
CC -!- TISSUE SPECIFICITY: Detected in fetal and adult kidney, brain and
CC spleen. {ECO:0000269|PubMed:19416806}.
CC -!- DISEASE: Osteopathia striata with cranial sclerosis (OSCS)
CC [MIM:300373]: An X-linked dominant sclerosing bone dysplasia that
CC presents in females with macrocephaly, cleft palate, facial palsy,
CC conductive hearing loss, mild learning disabilities, sclerosis of the
CC long bones and skull. Longitudinal striations are visible on
CC radiographs of the long bones, pelvis, and scapulae (osteopathia
CC striata). In males this entity is usually associated with fetal or
CC neonatal lethality. Occasional surviving males have, in addition to
CC hyperostosis, cardiac, intestinal, and genitourinary malformations.
CC {ECO:0000269|PubMed:19079258}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Inactivated in approximately one-third of Wilms tumors.
CC -!- SIMILARITY: Belongs to the Amer family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FAM123BID44119chXq11.html";
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DR EMBL; EF186024; ABM60755.1; -; mRNA.
DR EMBL; AK097146; BAC04964.1; -; mRNA.
DR EMBL; AL355852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS14377.2; -. [Q5JTC6-1]
DR RefSeq; NP_689637.3; NM_152424.3. [Q5JTC6-1]
DR PDB; 4YJE; X-ray; 1.90 A; B=325-335.
DR PDB; 4YJL; X-ray; 2.10 A; G/H/I/J/K/L=496-508.
DR PDB; 4YK6; X-ray; 1.70 A; B=365-375.
DR PDBsum; 4YJE; -.
DR PDBsum; 4YJL; -.
DR PDBsum; 4YK6; -.
DR AlphaFoldDB; Q5JTC6; -.
DR SMR; Q5JTC6; -.
DR BioGRID; 126556; 46.
DR ELM; Q5JTC6; -.
DR IntAct; Q5JTC6; 31.
DR MINT; Q5JTC6; -.
DR STRING; 9606.ENSP00000329117; -.
DR iPTMnet; Q5JTC6; -.
DR PhosphoSitePlus; Q5JTC6; -.
DR BioMuta; AMER1; -.
DR DMDM; 142984753; -.
DR EPD; Q5JTC6; -.
DR jPOST; Q5JTC6; -.
DR MassIVE; Q5JTC6; -.
DR MaxQB; Q5JTC6; -.
DR PaxDb; Q5JTC6; -.
DR PeptideAtlas; Q5JTC6; -.
DR PRIDE; Q5JTC6; -.
DR ProteomicsDB; 63211; -. [Q5JTC6-1]
DR ProteomicsDB; 63212; -. [Q5JTC6-2]
DR Antibodypedia; 43710; 112 antibodies from 27 providers.
DR DNASU; 139285; -.
DR Ensembl; ENST00000374869.8; ENSP00000364003.4; ENSG00000184675.11. [Q5JTC6-1]
DR GeneID; 139285; -.
DR KEGG; hsa:139285; -.
DR MANE-Select; ENST00000374869.8; ENSP00000364003.4; NM_152424.4; NP_689637.3.
DR UCSC; uc004dvo.3; human. [Q5JTC6-1]
DR CTD; 139285; -.
DR DisGeNET; 139285; -.
DR GeneCards; AMER1; -.
DR GeneReviews; AMER1; -.
DR HGNC; HGNC:26837; AMER1.
DR HPA; ENSG00000184675; Tissue enhanced (tongue).
DR MalaCards; AMER1; -.
DR MIM; 300373; phenotype.
DR MIM; 300647; gene.
DR neXtProt; NX_Q5JTC6; -.
DR OpenTargets; ENSG00000184675; -.
DR Orphanet; 2780; Osteopathia striata-cranial sclerosis syndrome.
DR PharmGKB; PA145148904; -.
DR VEuPathDB; HostDB:ENSG00000184675; -.
DR eggNOG; ENOG502QT5W; Eukaryota.
DR GeneTree; ENSGT00530000063529; -.
DR HOGENOM; CLU_009351_2_0_1; -.
DR InParanoid; Q5JTC6; -.
DR OMA; KPIMEYQ; -.
DR OrthoDB; 139922at2759; -.
DR PhylomeDB; Q5JTC6; -.
DR TreeFam; TF333006; -.
DR PathwayCommons; Q5JTC6; -.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
DR Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
DR Reactome; R-HSA-5339716; Signaling by GSK3beta mutants.
DR Reactome; R-HSA-5358747; CTNNB1 S33 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358749; CTNNB1 S37 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358751; CTNNB1 S45 mutants aren't phosphorylated.
DR Reactome; R-HSA-5358752; CTNNB1 T41 mutants aren't phosphorylated.
DR Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
DR Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
DR Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
DR SignaLink; Q5JTC6; -.
DR SIGNOR; Q5JTC6; -.
DR BioGRID-ORCS; 139285; 13 hits in 706 CRISPR screens.
DR ChiTaRS; AMER1; human.
DR GenomeRNAi; 139285; -.
DR Pharos; Q5JTC6; Tbio.
DR PRO; PR:Q5JTC6; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5JTC6; protein.
DR Bgee; ENSG00000184675; Expressed in cortical plate and 105 other tissues.
DR Genevisible; Q5JTC6; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR GO; GO:1904713; F:beta-catenin destruction complex binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0072161; P:mesenchymal cell differentiation involved in kidney development; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IDA:ParkinsonsUK-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR019003; AMER.
DR PANTHER; PTHR22237; PTHR22237; 1.
DR Pfam; PF09422; WTX; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane; Cytoplasm;
KW Lipid-binding; Membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Wnt signaling pathway.
FT CHAIN 1..1135
FT /note="APC membrane recruitment protein 1"
FT /id="PRO_0000281887"
FT REGION 1..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..405
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 736..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 921..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..405
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..940
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1116..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 786..804
FT /note="MSCSSDSDSSFTQNLPELP -> IRCPGTEDKRQVTQACGTW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024091"
FT VAR_SEQ 805..1135
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_024092"
FT VARIANT 159
FT /note="F -> L (in dbSNP:rs34677493)"
FT /id="VAR_053870"
FT VARIANT 178
FT /note="R -> C (in dbSNP:rs376626895)"
FT /evidence="ECO:0000269|PubMed:23092983"
FT /id="VAR_076268"
FT VARIANT 278
FT /note="A -> S (in dbSNP:rs35718712)"
FT /id="VAR_053871"
FT VARIANT 292
FT /note="K -> N (in dbSNP:rs138948924)"
FT /evidence="ECO:0000269|PubMed:17204608"
FT /id="VAR_031304"
FT MUTAGEN 54
FT /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and
FT cell membrane localization; when associated with A-58; A-
FT 79; A-83; A-166; A-181 and A-183."
FT /evidence="ECO:0000269|PubMed:21304492"
FT MUTAGEN 58
FT /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and
FT cell membrane localization; when associated with A-54; A-
FT 79; A-83; A-166; A-181 and A-183."
FT /evidence="ECO:0000269|PubMed:21304492"
FT MUTAGEN 79
FT /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and
FT cell membrane localization; when associated with A-54; A-
FT 58; A-83; A-166; A-181 and A-183."
FT /evidence="ECO:0000269|PubMed:21304492"
FT MUTAGEN 83
FT /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and
FT cell membrane localization; when associated with A-54; A-
FT 58; A-79; A-166; A-181 and A-183."
FT /evidence="ECO:0000269|PubMed:21304492"
FT MUTAGEN 166
FT /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and
FT cell membrane localization; when associated with A-54; A-
FT 58; A-79; A-83; A-181 and A-183."
FT /evidence="ECO:0000269|PubMed:21304492"
FT MUTAGEN 181
FT /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and
FT cell membrane localization; when associated with A-54; A-
FT 58; A-79; A-83; A-166 and A-183."
FT /evidence="ECO:0000269|PubMed:21304492"
FT MUTAGEN 183
FT /note="K->A: Abolishes interaction with PtdIns(4,5)P2 and
FT cell membrane localization; when associated with A-54; A-
FT 58; A-79; A-83; A-166 and A-181."
FT /evidence="ECO:0000269|PubMed:21304492"
FT CONFLICT Q5JTC6-2:786
FT /note="I -> R (in Ref. 2; BAC04964)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1135 AA; 124029 MW; 7C77EF692A0F60D3 CRC64;
METQKDEAAQ AKGAAASGST REQTAEKGAK NKAAEATEGP TSEPSSSGPG RLKKTAMKLF
GGKKGICTLP SFFGGGRSKG SGKGSSKKGL SKSKTHDGLS EAAHGPEDVV SEGTGFSLPL
PELPCQFPSS QSAHGALETG SRCKTSVAGA TEKAVAEKFP SMPKPKKGLK GFFSSIRRHR
KSKVTGAEQS EPGAKGPERV RARPHEHVSS APQVPCFEET FQAPRKENAN PQDAPGPKVS
PTPEPSPPAT EKMACKDPEK PMEACASAHV QPKPAPEASS LEEPHSPETG EKVVAGEVNP
PNGPVGDPLS LLFGDVTSLK SFDSLTGCGD IIAEQDMDSM TDSMASGGQR ANRDGTKRSS
CLVTYQGGGE EMALPDDDDE EEEEEEEVEL EEEEEEVKEE EEDDDLEYLW ETAQMYPRPN
MNLGYHPTTS PGHHGYMLLD PVRSYPGLAP GELLTPQSDQ QESAPNSDEG YYDSTTPGFE
DDSGEALGLV RRDCLPRDSY SGDALYEFYE PDDSLENSPP GDDCLYDLHG RSSEMFDPFL
NFEPFLSSRP PGAMETEEER LVTIQKQLLY WELRREQLEA QEARAREAHA REAHAREAYT
REAYGREAYA REAHTWEAHG REARTREAQA REVRCRETQV RETQARQEKP VLEYQMRPLG
PSVMGLAAGV SGTSQISHRG ITSAFPTTAS SEPDWRDFRP LEKRYEGTCS KKDQSTCLMQ
LFQSDAMFEP DMQEANFGGS PRRAYPTYSP PEDPEEEEVE KEGNATVSFS QALVEFTSNG
NLFSSMSCSS DSDSSFTQNL PELPPMVTFD IADVERDGEG KCEENPEFHN DEDLAASLEA
FELGYYHKHA FNNYHSRFYQ GLPWGVSSLP RYLGLPGLHP RPPPAAMALN RRSRSLDTAE
TLEMELSNSH LVQGYLESDE LQAQQEDSDE EDEEEEEGEW SRDSPLSLYT EPPGAYDWPA
WAPCPLPVGP GPAWISPNQL DRPSSQSPYR QATCCIPPMT MSISLSVPES RAPGESGPQL
ARPSHLHLPM GPCYNLQPQA SQSMRARPRD VLLPVDEPSC SSSSGGFSPS PLPQAKPVGI
THGIPQLPRV RPEHPQPQPT HYGPSSLDLS KERAEQGASL ATSYSSTAMN GNLAK
