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Protein

APC membrane recruitment protein 1

Gene

AMER1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

  • beta-catenin binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: UniProtKB

GO - Biological processi

  • adipose tissue development Source: Ensembl
  • bone development Source: Ensembl
  • mesenchymal cell differentiation involved in kidney development Source: Ensembl
  • negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • regulation of canonical Wnt signaling pathway Source: UniProtKB
  • Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

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_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.

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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:26837. AMER1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleus Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Involvement in diseasei

Osteopathia striata with cranial sclerosis (OSCS)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:300373

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.

Polymorphism and mutation databases

BioMutaiAMER1.
DMDMi142984753.

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.
GenevisibleiQ5JTC6. HS.

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. 16 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.
GeneTreeiENSGT00530000063529.
HOGENOMiHOG000049188.
HOVERGENiHBG107863.
InParanoidiQ5JTC6.
OMAiRDGEGKC.
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. AlignAdd to basket

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

        10         20         30         40         50
METQKDEAAQ AKGAAASGST REQTAEKGAK NKAAEATEGP TSEPSSSGPG
60 70 80 90 100
RLKKTAMKLF GGKKGICTLP SFFGGGRSKG SGKGSSKKGL SKSKTHDGLS
110 120 130 140 150
EAAHGPEDVV SEGTGFSLPL PELPCQFPSS QSAHGALETG SRCKTSVAGA
160 170 180 190 200
TEKAVAEKFP SMPKPKKGLK GFFSSIRRHR KSKVTGAEQS EPGAKGPERV
210 220 230 240 250
RARPHEHVSS APQVPCFEET FQAPRKENAN PQDAPGPKVS PTPEPSPPAT
260 270 280 290 300
EKMACKDPEK PMEACASAHV QPKPAPEASS LEEPHSPETG EKVVAGEVNP
310 320 330 340 350
PNGPVGDPLS LLFGDVTSLK SFDSLTGCGD IIAEQDMDSM TDSMASGGQR
360 370 380 390 400
ANRDGTKRSS CLVTYQGGGE EMALPDDDDE EEEEEEEVEL EEEEEEVKEE
410 420 430 440 450
EEDDDLEYLW ETAQMYPRPN MNLGYHPTTS PGHHGYMLLD PVRSYPGLAP
460 470 480 490 500
GELLTPQSDQ QESAPNSDEG YYDSTTPGFE DDSGEALGLV RRDCLPRDSY
510 520 530 540 550
SGDALYEFYE PDDSLENSPP GDDCLYDLHG RSSEMFDPFL NFEPFLSSRP
560 570 580 590 600
PGAMETEEER LVTIQKQLLY WELRREQLEA QEARAREAHA REAHAREAYT
610 620 630 640 650
REAYGREAYA REAHTWEAHG REARTREAQA REVRCRETQV RETQARQEKP
660 670 680 690 700
VLEYQMRPLG PSVMGLAAGV SGTSQISHRG ITSAFPTTAS SEPDWRDFRP
710 720 730 740 750
LEKRYEGTCS KKDQSTCLMQ LFQSDAMFEP DMQEANFGGS PRRAYPTYSP
760 770 780 790 800
PEDPEEEEVE KEGNATVSFS QALVEFTSNG NLFSSMSCSS DSDSSFTQNL
810 820 830 840 850
PELPPMVTFD IADVERDGEG KCEENPEFHN DEDLAASLEA FELGYYHKHA
860 870 880 890 900
FNNYHSRFYQ GLPWGVSSLP RYLGLPGLHP RPPPAAMALN RRSRSLDTAE
910 920 930 940 950
TLEMELSNSH LVQGYLESDE LQAQQEDSDE EDEEEEEGEW SRDSPLSLYT
960 970 980 990 1000
EPPGAYDWPA WAPCPLPVGP GPAWISPNQL DRPSSQSPYR QATCCIPPMT
1010 1020 1030 1040 1050
MSISLSVPES RAPGESGPQL ARPSHLHLPM GPCYNLQPQA SQSMRARPRD
1060 1070 1080 1090 1100
VLLPVDEPSC SSSSGGFSPS PLPQAKPVGI THGIPQLPRV RPEHPQPQPT
1110 1120 1130
HYGPSSLDLS KERAEQGASL ATSYSSTAMN GNLAK
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:
EMBLi
GenBanki
DDBJi
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]
XP_011529160.1. XM_011530858.1. [Q5JTC6-1]
UniGeneiHs.314225.

Genome annotation databases

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

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:
EMBLi
GenBanki
DDBJi
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]
XP_011529160.1. XM_011530858.1. [Q5JTC6-1]
UniGeneiHs.314225.

3D structure databases

ProteinModelPortaliQ5JTC6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi126556. 16 interactions.
IntActiQ5JTC6. 6 interactions.
STRINGi9606.ENSP00000329117.

PTM databases

PhosphoSiteiQ5JTC6.

Polymorphism and mutation databases

BioMutaiAMER1.
DMDMi142984753.

Proteomic databases

MaxQBiQ5JTC6.
PaxDbiQ5JTC6.
PRIDEiQ5JTC6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi139285.
GeneCardsiGC0XM063406.
HGNCiHGNC:26837. AMER1.
MIMi300373. phenotype.
300647. gene.
neXtProtiNX_Q5JTC6.
Orphaneti2780. Osteopathia striata - cranial sclerosis.
PharmGKBiPA145148904.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG45581.
GeneTreeiENSGT00530000063529.
HOGENOMiHOG000049188.
HOVERGENiHBG107863.
InParanoidiQ5JTC6.
OMAiRDGEGKC.
OrthoDBiEOG7ZKS9T.
PhylomeDBiQ5JTC6.
TreeFamiTF333006.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_11065. Beta-catenin phosphorylation cascade.
REACT_263893. truncations of AMER1 destabilize the destruction complex.
REACT_263992. APC truncation mutants have impaired AXIN binding.
REACT_264030. AXIN missense mutants destabilize the destruction complex.
REACT_264034. disassembly of the destruction complex and recruitment of AXIN to the membrane.
REACT_264092. misspliced GSK3beta mutants stabilize beta-catenin.
REACT_264127. T41 mutants of beta-catenin aren't phosphorylated.
REACT_264295. S45 mutants of beta-catenin aren't phosphorylated.
REACT_264581. S33 mutants of beta-catenin aren't phosphorylated.
REACT_264636. S37 mutants of beta-catenin aren't phosphorylated.

Miscellaneous databases

GenomeRNAii139285.
NextBioi83932.
PROiQ5JTC6.
SOURCEiSearch...

Gene expression databases

BgeeiQ5JTC6.
CleanExiHS_FAM123B.
GenevisibleiQ5JTC6. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: July 22, 2015
This is version 91 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.