Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q5JTC6

- AMER1_HUMAN

UniProt

Q5JTC6 - AMER1_HUMAN

Protein

APC membrane recruitment protein 1

Gene

AMER1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 2 (03 Apr 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.5 Publications

    GO - Molecular functioni

    1. beta-catenin binding Source: UniProtKB
    2. phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. adipose tissue development Source: Ensembl
    2. bone development Source: Ensembl
    3. mesenchymal cell differentiation involved in kidney development Source: Ensembl
    4. negative regulation of canonical Wnt signaling pathway Source: UniProtKB
    5. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    6. regulation of canonical Wnt signaling pathway Source: UniProtKB
    7. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    Lipid-binding

    Enzyme and pathway databases

    ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    APC membrane recruitment protein 1
    Short name:
    Amer1
    Alternative name(s):
    Protein FAM123B
    Wilms tumor gene on the X chromosome protein
    Gene namesi
    Name:AMER1
    Synonyms:FAM123B, WTX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:26837. AMER1.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. nucleus Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi54 – 541K → 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. 1 Publication
    Mutagenesisi58 – 581K → 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. 1 Publication
    Mutagenesisi79 – 791K → 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. 1 Publication
    Mutagenesisi83 – 831K → 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. 1 Publication
    Mutagenesisi166 – 1661K → 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. 1 Publication
    Mutagenesisi181 – 1811K → 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. 1 Publication
    Mutagenesisi183 – 1831K → 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. 1 Publication

    Organism-specific databases

    MIMi300373. phenotype.
    Orphaneti2780. Osteopathia striata - cranial sclerosis.
    PharmGKBiPA145148904.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11351135APC membrane recruitment protein 1PRO_0000281887Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei246 – 2461Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ5JTC6.
    PaxDbiQ5JTC6.
    PRIDEiQ5JTC6.

    PTM databases

    PhosphoSiteiQ5JTC6.

    Expressioni

    Tissue specificityi

    Detected in fetal and adult kidney, brain and spleen.1 Publication

    Gene expression databases

    BgeeiQ5JTC6.
    CleanExiHS_FAM123B.
    GenevestigatoriQ5JTC6.

    Interactioni

    Subunit structurei

    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 WT1.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AMER3Q8N9444EBI-6169747,EBI-8869590

    Protein-protein interaction databases

    BioGridi126556. 8 interactions.
    IntActiQ5JTC6. 6 interactions.
    STRINGi9606.ENSP00000329117.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5JTC6.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi370 – 41142Glu-richAdd
    BLAST
    Compositional biasi755 – 7628Poly-Glu
    Compositional biasi930 – 93910Poly-Glu
    Compositional biasi952 – 1104153Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Amer family.Curated

    Phylogenomic databases

    eggNOGiNOG45581.
    HOGENOMiHOG000049188.
    HOVERGENiHBG107863.
    InParanoidiQ5JTC6.
    OMAiDMDSMTD.
    OrthoDBiEOG7ZKS9T.
    PhylomeDBiQ5JTC6.
    TreeFamiTF333006.

    Family and domain databases

    InterProiIPR019003. Uncharacterised_FAM123.
    [Graphical view]
    PfamiPF09422. WTX. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5JTC6-1) [UniParc]FASTAAdd to Basket

    Also known as: Amer1-S1

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    METQKDEAAQ AKGAAASGST REQTAEKGAK NKAAEATEGP TSEPSSSGPG     50
    RLKKTAMKLF GGKKGICTLP SFFGGGRSKG SGKGSSKKGL SKSKTHDGLS 100
    EAAHGPEDVV SEGTGFSLPL PELPCQFPSS QSAHGALETG SRCKTSVAGA 150
    TEKAVAEKFP SMPKPKKGLK GFFSSIRRHR KSKVTGAEQS EPGAKGPERV 200
    RARPHEHVSS APQVPCFEET FQAPRKENAN PQDAPGPKVS PTPEPSPPAT 250
    EKMACKDPEK PMEACASAHV QPKPAPEASS LEEPHSPETG EKVVAGEVNP 300
    PNGPVGDPLS LLFGDVTSLK SFDSLTGCGD IIAEQDMDSM TDSMASGGQR 350
    ANRDGTKRSS CLVTYQGGGE EMALPDDDDE EEEEEEEVEL EEEEEEVKEE 400
    EEDDDLEYLW ETAQMYPRPN MNLGYHPTTS PGHHGYMLLD PVRSYPGLAP 450
    GELLTPQSDQ QESAPNSDEG YYDSTTPGFE DDSGEALGLV RRDCLPRDSY 500
    SGDALYEFYE PDDSLENSPP GDDCLYDLHG RSSEMFDPFL NFEPFLSSRP 550
    PGAMETEEER LVTIQKQLLY WELRREQLEA QEARAREAHA REAHAREAYT 600
    REAYGREAYA REAHTWEAHG REARTREAQA REVRCRETQV RETQARQEKP 650
    VLEYQMRPLG PSVMGLAAGV SGTSQISHRG ITSAFPTTAS SEPDWRDFRP 700
    LEKRYEGTCS KKDQSTCLMQ LFQSDAMFEP DMQEANFGGS PRRAYPTYSP 750
    PEDPEEEEVE KEGNATVSFS QALVEFTSNG NLFSSMSCSS DSDSSFTQNL 800
    PELPPMVTFD IADVERDGEG KCEENPEFHN DEDLAASLEA FELGYYHKHA 850
    FNNYHSRFYQ GLPWGVSSLP RYLGLPGLHP RPPPAAMALN RRSRSLDTAE 900
    TLEMELSNSH LVQGYLESDE LQAQQEDSDE EDEEEEEGEW SRDSPLSLYT 950
    EPPGAYDWPA WAPCPLPVGP GPAWISPNQL DRPSSQSPYR QATCCIPPMT 1000
    MSISLSVPES RAPGESGPQL ARPSHLHLPM GPCYNLQPQA SQSMRARPRD 1050
    VLLPVDEPSC SSSSGGFSPS PLPQAKPVGI THGIPQLPRV RPEHPQPQPT 1100
    HYGPSSLDLS KERAEQGASL ATSYSSTAMN GNLAK 1135
    Length:1,135
    Mass (Da):124,029
    Last modified:April 3, 2007 - v2
    Checksum:i7C77EF692A0F60D3
    GO
    Isoform 2 (identifier: Q5JTC6-2) [UniParc]FASTAAdd to Basket

    Also known as: Amer1-S2, Short

    The sequence of this isoform differs from the canonical sequence as follows:
         786-804: MSCSSDSDSSFTQNLPELP → IRCPGTEDKRQVTQACGTW
         805-1135: Missing.

    Show »
    Length:804
    Mass (Da):87,823
    Checksum:i3DDEF91694003622
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Isoform 2 (identifier: Q5JTC6-2)
    Sequence conflicti786 – 7861I → R in BAC04964. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti159 – 1591F → L.
    Corresponds to variant rs34677493 [ dbSNP | Ensembl ].
    VAR_053870
    Natural varianti278 – 2781A → S.
    Corresponds to variant rs35718712 [ dbSNP | Ensembl ].
    VAR_053871
    Natural varianti292 – 2921K → N.1 Publication
    VAR_031304

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei786 – 80419MSCSS…LPELP → IRCPGTEDKRQVTQACGTW in isoform 2. 1 PublicationVSP_024091Add
    BLAST
    Alternative sequencei805 – 1135331Missing in isoform 2. 1 PublicationVSP_024092Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF186024 mRNA. Translation: ABM60755.1.
    AK097146 mRNA. Translation: BAC04964.1.
    AL355852 Genomic DNA. Translation: CAI40637.1.
    AL355852 Genomic DNA. Translation: CAO03539.1.
    CCDSiCCDS14377.2. [Q5JTC6-1]
    RefSeqiNP_689637.3. NM_152424.3. [Q5JTC6-1]
    UniGeneiHs.314225.

    Genome annotation databases

    EnsembliENST00000330258; ENSP00000329117; ENSG00000184675. [Q5JTC6-1]
    ENST00000374869; ENSP00000364003; ENSG00000184675. [Q5JTC6-2]
    GeneIDi139285.
    KEGGihsa:139285.
    UCSCiuc004dvo.3. human. [Q5JTC6-1]

    Polymorphism databases

    DMDMi142984753.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    EF186024 mRNA. Translation: ABM60755.1 .
    AK097146 mRNA. Translation: BAC04964.1 .
    AL355852 Genomic DNA. Translation: CAI40637.1 .
    AL355852 Genomic DNA. Translation: CAO03539.1 .
    CCDSi CCDS14377.2. [Q5JTC6-1 ]
    RefSeqi NP_689637.3. NM_152424.3. [Q5JTC6-1 ]
    UniGenei Hs.314225.

    3D structure databases

    ProteinModelPortali Q5JTC6.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 126556. 8 interactions.
    IntActi Q5JTC6. 6 interactions.
    STRINGi 9606.ENSP00000329117.

    PTM databases

    PhosphoSitei Q5JTC6.

    Polymorphism databases

    DMDMi 142984753.

    Proteomic databases

    MaxQBi Q5JTC6.
    PaxDbi Q5JTC6.
    PRIDEi Q5JTC6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330258 ; ENSP00000329117 ; ENSG00000184675 . [Q5JTC6-1 ]
    ENST00000374869 ; ENSP00000364003 ; ENSG00000184675 . [Q5JTC6-2 ]
    GeneIDi 139285.
    KEGGi hsa:139285.
    UCSCi uc004dvo.3. human. [Q5JTC6-1 ]

    Organism-specific databases

    CTDi 139285.
    GeneCardsi GC0XM063406.
    HGNCi HGNC:26837. AMER1.
    MIMi 300373. phenotype.
    300647. gene.
    neXtProti NX_Q5JTC6.
    Orphaneti 2780. Osteopathia striata - cranial sclerosis.
    PharmGKBi PA145148904.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG45581.
    HOGENOMi HOG000049188.
    HOVERGENi HBG107863.
    InParanoidi Q5JTC6.
    OMAi DMDSMTD.
    OrthoDBi EOG7ZKS9T.
    PhylomeDBi Q5JTC6.
    TreeFami TF333006.

    Enzyme and pathway databases

    Reactomei REACT_11063. Degradation of beta-catenin by the destruction complex.
    REACT_11065. Beta-catenin phosphorylation cascade.
    REACT_200610. disassembly of the destruction complex and recruitment of AXIN to the membrane.

    Miscellaneous databases

    GenomeRNAii 139285.
    NextBioi 83932.
    PROi Q5JTC6.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q5JTC6.
    CleanExi HS_FAM123B.
    Genevestigatori Q5JTC6.

    Family and domain databases

    InterProi IPR019003. Uncharacterised_FAM123.
    [Graphical view ]
    Pfami PF09422. WTX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-292, INACTIVATION IN WILMS TUMOR.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Spleen.
    3. "The DNA sequence of the human X chromosome."
      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.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CTNNB1; KEAP1; AXIN1; APC; FBXW11 AND BTRC.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. Cited for: INVOLVEMENT IN OSCS.
    8. "AMER1 regulates the distribution of the tumor suppressor APC between microtubules and the plasma membrane."
      Grohmann A., Tanneberger K., Alzner A., Schneikert J., Behrens J.
      J. Cell Sci. 120:3738-3747(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PTDINS(4,5)P2-BINDING, INTERACTION WITH APC.
    9. "The tumor suppressor WTX shuttles to the nucleus and modulates WT1 activity."
      Rivera M.N., Kim W.J., Wells J., Stone A., Burger A., Coffman E.J., Zhang J., Haber D.A.
      Proc. Natl. Acad. Sci. U.S.A. 106:8338-8343(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING, INTERACTION WITH WT1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    10. "The WTX/AMER1 gene family: evolution, signature and function."
      Boutet A., Comai G., Schedl A.
      BMC Evol. Biol. 10:280-280(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY.
    11. "Amer1/WTX couples Wnt-induced formation of PtdIns(4,5)P2 to LRP6 phosphorylation."
      Tanneberger K., Pfister A.S., Brauburger K., Schneikert J., Hadjihannas M.V., Kriz V., Schulte G., Bryja V., Behrens J.
      EMBO J. 30:1433-1443(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, PTDINS(4,5)P2-BINDING, INTERACTION WITH LRP6, MUTAGENESIS OF LYS-54; LYS-58; LYS-79; LYS-83; LYS-166; LYS-181 AND LYS-183.
    12. "Structural and functional characterization of the Wnt inhibitor APC membrane recruitment 1 (Amer1)."
      Tanneberger K., Pfister A.S., Kriz V., Bryja V., Schambony A., Behrens J.
      J. Biol. Chem. 286:19204-19214(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CTNNB1.
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAMER1_HUMAN
    AccessioniPrimary (citable) accession number: Q5JTC6
    Secondary accession number(s): A2IB86, Q8N885
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 3, 2007
    Last sequence update: April 3, 2007
    Last modified: October 1, 2014
    This is version 83 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Inactivated in approximately one-third of Wilms tumors.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3