Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

APC membrane recruitment protein 1 (Amer1) (Protein FAM123B) (Wilms tumor gene on the X chromosome protein)

 AMER1_HUMAN             Reviewed;        1135 AA.
Q5JTC6; A2IB86; Q8N885;
03-APR-2007, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
22-NOV-2017, entry version 111.
RecName: Full=APC membrane recruitment protein 1;
Short=Amer1;
AltName: Full=Protein FAM123B;
AltName: Full=Wilms tumor gene on the X chromosome protein;
Name=AMER1; Synonyms=FAM123B, WTX;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-292, AND
INACTIVATION IN WILMS TUMOR.
PubMed=17204608; DOI=10.1126/science.1137509;
Rivera M.N., Kim W.J., Wells J., Driscoll D.R., Brannigan B.W.,
Han M., Kim J.C., Feinberg A.P., Gerald W.L., Vargas S.O., Chin L.,
Iafrate A.J., Bell D.W., Haber D.A.;
"An X chromosome gene, WTX, is commonly inactivated in Wilms tumor.";
Science 315:642-645(2007).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
AND INTERACTION WITH CTNNB1; KEAP1; AXIN1; APC; FBXW11 AND BTRC.
PubMed=17510365; DOI=10.1126/science/1141515;
Major M.B., Camp N.D., Berndt J.D., Yi X., Goldenberg S.J.,
Hubbert C., Biechele T.L., Gingras A.-C., Zheng N., Maccoss M.J.,
Angers S., Moon R.T.;
"Wilms tumor suppressor WTX negatively regulates WNT/beta-catenin
signaling.";
Science 316:1043-1046(2007).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[7]
INVOLVEMENT IN OSCS.
PubMed=19079258; DOI=10.1038/ng.270;
Jenkins Z.A., van Kogelenberg M., Morgan T., Jeffs A., Fukuzawa R.,
Pearl E., Thaller C., Hing A.V., Porteous M.E., Garcia-Minaur S.,
Bohring A., Lacombe D., Stewart F., Fiskerstrand T., Bindoff L.,
Berland S., Ades L.C., Tchan M., David A., Wilson L.C., Hennekam R.C.,
Donnai D., Mansour S., Cormier-Daire V., Robertson S.P.;
"Germline mutations in WTX cause a sclerosing skeletal dysplasia but
do not predispose to tumorigenesis.";
Nat. Genet. 41:95-100(2009).
[8]
FUNCTION, SUBCELLULAR LOCATION, PTDINS(4,5)P2-BINDING, AND INTERACTION
WITH APC.
PubMed=17925383; DOI=10.1242/jcs.011320;
Grohmann A., Tanneberger K., Alzner A., Schneikert J., Behrens J.;
"AMER1 regulates the distribution of the tumor suppressor APC between
microtubules and the plasma membrane.";
J. Cell Sci. 120:3738-3747(2007).
[9]
FUNCTION, ALTERNATIVE SPLICING, INTERACTION WITH WT1, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=19416806; DOI=10.1073/pnas.0811349106;
Rivera M.N., Kim W.J., Wells J., Stone A., Burger A., Coffman E.J.,
Zhang J., Haber D.A.;
"The tumor suppressor WTX shuttles to the nucleus and modulates WT1
activity.";
Proc. Natl. Acad. Sci. U.S.A. 106:8338-8343(2009).
[10]
GENE FAMILY.
PubMed=20843316; DOI=10.1186/1471-2148-10-280;
Boutet A., Comai G., Schedl A.;
"The WTX/AMER1 gene family: evolution, signature and function.";
BMC Evol. Biol. 10:280-280(2010).
[11]
FUNCTION, SUBCELLULAR LOCATION, PTDINS(4,5)P2-BINDING, INTERACTION
WITH LRP6, AND MUTAGENESIS OF LYS-54; LYS-58; LYS-79; LYS-83; LYS-166;
LYS-181 AND LYS-183.
PubMed=21304492; DOI=10.1038/emboj.2011.28;
Tanneberger K., Pfister A.S., Brauburger K., Schneikert J.,
Hadjihannas M.V., Kriz V., Schulte G., Bryja V., Behrens J.;
"Amer1/WTX couples Wnt-induced formation of PtdIns(4,5)P2 to LRP6
phosphorylation.";
EMBO J. 30:1433-1443(2011).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CTNNB1.
PubMed=21498506; DOI=10.1074/jbc.M111.224881;
Tanneberger K., Pfister A.S., Kriz V., Bryja V., Schambony A.,
Behrens J.;
"Structural and functional characterization of the Wnt inhibitor APC
membrane recruitment 1 (Amer1).";
J. Biol. Chem. 286:19204-19214(2011).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[16]
VARIANT CYS-178.
PubMed=23092983; DOI=10.1038/tp.2012.102;
Nava C., Lamari F., Heron D., Mignot C., Rastetter A., Keren B.,
Cohen D., Faudet A., Bouteiller D., Gilleron M., Jacquette A.,
Whalen S., Afenjar A., Perisse D., Laurent C., Dupuits C., Gautier C.,
Gerard M., Huguet G., Caillet S., Leheup B., Leboyer M., Gillberg C.,
Delorme R., Bourgeron T., Brice A., Depienne C.;
"Analysis of the chromosome X exome in patients with autism spectrum
disorders identified novel candidate genes, including TMLHE.";
Transl. Psychiatry 2:E179-E179(2012).
-!- 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}.
-!- SUBUNIT: Interacts with CTNNB1, AXIN1, LRP6, KEAP1, APC and BTRC.
Interacts with SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein
ligase complexes containing BTRC and/or FBXW11. Identified in the
beta-catenin destruction complex containing CTNNB1, APC, AXIN1 and
AXIN2. Interacts with WT1. {ECO:0000269|PubMed:17510365,
ECO:0000269|PubMed:17925383, ECO:0000269|PubMed:19416806,
ECO:0000269|PubMed:21304492, ECO:0000269|PubMed:21498506}.
-!- INTERACTION:
Q8N944:AMER3; NbExp=4; IntAct=EBI-6169747, EBI-8869590;
P25054:APC; NbExp=4; IntAct=EBI-6169747, EBI-727707;
O15169:AXIN1; NbExp=7; IntAct=EBI-6169747, EBI-710484;
Q9Y297:BTRC; NbExp=5; IntAct=EBI-6169747, EBI-307461;
P35222:CTNNB1; NbExp=9; IntAct=EBI-6169747, EBI-491549;
Q9UKB1:FBXW11; NbExp=4; IntAct=EBI-6169747, EBI-355189;
Q14145:KEAP1; NbExp=2; IntAct=EBI-6169747, EBI-751001;
-!- 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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Amer1-S1;
IsoId=Q5JTC6-1; Sequence=Displayed;
Name=2; Synonyms=Amer1-S2, Short;
IsoId=Q5JTC6-2; Sequence=VSP_024091, VSP_024092;
Note=Ref.2 (BAC04964) sequence is in conflict in position:
786:I->R. {ECO:0000305};
-!- TISSUE SPECIFICITY: Detected in fetal and adult kidney, brain and
spleen. {ECO:0000269|PubMed:19416806}.
-!- 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 mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Inactivated in approximately one-third of Wilms
tumors.
-!- SIMILARITY: Belongs to the Amer family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FAM123BID44119chXq11.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; EF186024; ABM60755.1; -; mRNA.
EMBL; AK097146; BAC04964.1; -; mRNA.
EMBL; AL355852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS14377.2; -. [Q5JTC6-1]
RefSeq; NP_689637.3; NM_152424.3. [Q5JTC6-1]
UniGene; Hs.314225; -.
PDB; 4YJE; X-ray; 1.90 A; B=325-335.
PDB; 4YJL; X-ray; 2.10 A; G/H/I/J/K/L=496-508.
PDB; 4YK6; X-ray; 1.70 A; B=365-375.
PDBsum; 4YJE; -.
PDBsum; 4YJL; -.
PDBsum; 4YK6; -.
ProteinModelPortal; Q5JTC6; -.
SMR; Q5JTC6; -.
BioGrid; 126556; 26.
ELM; Q5JTC6; -.
IntAct; Q5JTC6; 16.
STRING; 9606.ENSP00000329117; -.
iPTMnet; Q5JTC6; -.
PhosphoSitePlus; Q5JTC6; -.
BioMuta; AMER1; -.
DMDM; 142984753; -.
EPD; Q5JTC6; -.
MaxQB; Q5JTC6; -.
PaxDb; Q5JTC6; -.
PeptideAtlas; Q5JTC6; -.
PRIDE; Q5JTC6; -.
Ensembl; ENST00000330258; ENSP00000329117; ENSG00000184675. [Q5JTC6-1]
Ensembl; ENST00000374869; ENSP00000364003; ENSG00000184675. [Q5JTC6-2]
GeneID; 139285; -.
KEGG; hsa:139285; -.
UCSC; uc004dvo.3; human. [Q5JTC6-1]
CTD; 139285; -.
DisGeNET; 139285; -.
EuPathDB; HostDB:ENSG00000184675.9; -.
GeneCards; AMER1; -.
HGNC; HGNC:26837; AMER1.
HPA; HPA065214; -.
HPA; HPA065265; -.
MalaCards; AMER1; -.
MIM; 300373; phenotype.
MIM; 300647; gene.
neXtProt; NX_Q5JTC6; -.
OpenTargets; ENSG00000184675; -.
Orphanet; 2780; Osteopathia striata - cranial sclerosis.
PharmGKB; PA145148904; -.
eggNOG; ENOG410IJHD; Eukaryota.
eggNOG; ENOG410XU7Y; LUCA.
GeneTree; ENSGT00530000063529; -.
HOGENOM; HOG000049188; -.
HOVERGEN; HBG107863; -.
InParanoid; Q5JTC6; -.
KO; K19407; -.
OMA; RDGEGKC; -.
OrthoDB; EOG091G08AF; -.
PhylomeDB; Q5JTC6; -.
TreeFam; TF333006; -.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-196299; Beta-catenin phosphorylation cascade.
Reactome; R-HSA-4641262; Disassembly of the destruction complex and recruitment of AXIN to the membrane.
Reactome; R-HSA-5339716; Misspliced GSK3beta mutants stabilize beta-catenin.
Reactome; R-HSA-5358747; S33 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358749; S37 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358751; S45 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5358752; T41 mutants of beta-catenin aren't phosphorylated.
Reactome; R-HSA-5467337; APC truncation mutants have impaired AXIN binding.
Reactome; R-HSA-5467340; AXIN missense mutants destabilize the destruction complex.
Reactome; R-HSA-5467348; Truncations of AMER1 destabilize the destruction complex.
SIGNOR; Q5JTC6; -.
GenomeRNAi; 139285; -.
PRO; PR:Q5JTC6; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000184675; -.
CleanEx; HS_FAM123B; -.
Genevisible; Q5JTC6; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
GO; GO:1904713; F:beta-catenin destruction complex binding; IPI:ParkinsonsUK-UCL.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0060612; P:adipose tissue development; IEA:Ensembl.
GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
GO; GO:1904885; P:beta-catenin destruction complex assembly; TAS:Reactome.
GO; GO:1904886; P:beta-catenin destruction complex disassembly; TAS:Reactome.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0072161; P:mesenchymal cell differentiation involved in kidney development; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:1903364; P:positive regulation of cellular protein catabolic process; IDA:ParkinsonsUK-UCL.
GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; IMP:UniProtKB.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
InterPro; IPR019003; Uncharacterised_FAM123.
Pfam; PF09422; WTX; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell membrane;
Complete proteome; Cytoplasm; Lipid-binding; Membrane; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome;
Wnt signaling pathway.
CHAIN 1 1135 APC membrane recruitment protein 1.
/FTId=PRO_0000281887.
COMPBIAS 370 411 Glu-rich.
COMPBIAS 755 762 Poly-Glu.
COMPBIAS 930 939 Poly-Glu.
COMPBIAS 952 1104 Pro-rich.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 246 246 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 786 804 MSCSSDSDSSFTQNLPELP -> IRCPGTEDKRQVTQACGT
W (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_024091.
VAR_SEQ 805 1135 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_024092.
VARIANT 159 159 F -> L (in dbSNP:rs34677493).
/FTId=VAR_053870.
VARIANT 178 178 R -> C (in dbSNP:rs376626895).
{ECO:0000269|PubMed:23092983}.
/FTId=VAR_076268.
VARIANT 278 278 A -> S (in dbSNP:rs35718712).
/FTId=VAR_053871.
VARIANT 292 292 K -> N (in dbSNP:rs138948924).
{ECO:0000269|PubMed:17204608}.
/FTId=VAR_031304.
MUTAGEN 54 54 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.
{ECO:0000269|PubMed:21304492}.
MUTAGEN 58 58 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.
{ECO:0000269|PubMed:21304492}.
MUTAGEN 79 79 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.
{ECO:0000269|PubMed:21304492}.
MUTAGEN 83 83 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.
{ECO:0000269|PubMed:21304492}.
MUTAGEN 166 166 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.
{ECO:0000269|PubMed:21304492}.
MUTAGEN 181 181 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.
{ECO:0000269|PubMed:21304492}.
MUTAGEN 183 183 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.
{ECO:0000269|PubMed:21304492}.
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


Related products :

Catalog number Product name Quantity
EIAAB13652 FAM123B,Homo sapiens,Human,Protein FAM123B,Wilms tumor gene on the X chromosome protein,WTX
A024894 Rabbit Anti-FAM123B per AMER1 per Wilms tumor on the X Ab 100ul
EIAAB46373 Homo sapiens,Human,Putative Wilms tumor upstream neighbor 1 gene protein,Wilms tumor-associated antisense RNA,WIT1,WIT-1,WT1-AS
F123B_MOUSE ELISA Kit FOR Protein FAM123B; organism: Mouse; gene name: Fam123b 96T
F123B_HUMAN ELISA Kit FOR Protein FAM123B; organism: Human; gene name: FAM123B 96T
WIT1_HUMAN ELISA Kit FOR Putative Wilms tumor upstream neighbor 1 gene protein; organism: Human; gene name: WT1-AS 96T
WT1_RAT ELISA Kit FOR Wilms tumor protein homolog; organism: Rat; gene name: Wt1 96T
EIAAB26474 1A13B,Cell migration-inducing gene 19 protein,Homo sapiens,Human,KIAA0049,M17S2,Membrane component chromosome 17 surface marker 2,MIG19,NBR1,Neighbor of BRCA1 gene 1 protein,Next to BRCA1 gene 1 prote
A020391 Rabbit Anti-FAM123B per AMER1 Ab 200Ul
EIAAB26475 M17s2,Membrane component chromosome 17 surface marker 2 homolog,Mouse,Mus musculus,Nbr1,Neighbor of BRCA1 gene 1 protein,Next to BRCA1 gene 1 protein
E1884d Human ELISA Kit FOR Putative Wilms tumor upstream neighbor 1 gene protein 96T
EIAAB12912 EMP1,EMP-1,Epithelial membrane protein 1,Oryctolagus cuniculus,Rabbit,Squamous cell-specific protein CL-20,Tumor-associated membrane protein
EIAAB12909 B4B,CL-20,EMP1,EMP-1,Epithelial membrane protein 1,Homo sapiens,Human,Protein B4B,TMP,Tumor-associated membrane protein
I2793 Wilms tumor protein 1-interacting protein (WTIP), Human, ELISA Kit 96T
CSB-EL026161MO Mouse Wilms tumor protein 1-interacting protein(WTIP) ELISA kit 96T
CSB-EL026161HU Human Wilms tumor protein 1-interacting protein(WTIP) ELISA kit 96T
I2794 Wilms tumor protein 1-interacting protein (WTIP), Mouse, ELISA Kit 96T
CSB-EL026161HU Human Wilms tumor protein 1-interacting protein(WTIP) ELISA kit SpeciesHuman 96T
CSB-EL026161MO Mouse Wilms tumor protein 1-interacting protein(WTIP) ELISA kit SpeciesMouse 96T
EH2071 Wilms tumor protein 1-interacting protein Elisa Kit 96T
EIAAB46469 Homo sapiens,Human,Wilms tumor protein 1-interacting protein,WT1-interacting protein,WTIP
10-288-22286F Wilms' tumor 1-associating protein - WT1-associated protein; Putative pre-mRNA-splicing regulator female-lethal(2D) homolog 0.05 mg
10-288-22286F Wilms' tumor 1-associating protein - WT1-associated protein; Putative pre-mRNA-splicing regulator female-lethal(2D) homolog 0.1 mg
5204 Protein,Wilms' tumor 1_associating protein 0.05 mg
5204 Protein,Wilms' tumor 1_associating protein 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur