Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

APC membrane recruitment protein 1

Gene

Amer1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

  • adipose tissue development Source: MGI
  • bone development Source: MGI
  • kidney development Source: MGI
  • mesenchymal cell differentiation involved in kidney development Source: MGI
  • negative regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  • positive regulation of cellular protein catabolic process Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • 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

ReactomeiR-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-196299. Beta-catenin phosphorylation cascade.
R-MMU-4641262. 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
Gene namesi
Name:Amer1
Synonyms:Fam123b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1919595. Amer1.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Nucleus By similarity

  • 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 (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11321132APC membrane recruitment protein 1PRO_0000281888Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ7TS75.
PaxDbiQ7TS75.
PeptideAtlasiQ7TS75.
PRIDEiQ7TS75.

PTM databases

iPTMnetiQ7TS75.
PhosphoSiteiQ7TS75.

Expressioni

Tissue specificityi

Expressed in kidney.1 Publication

Developmental stagei

In embryos, it is highly expressed in the neonatal brain and kidney and then declines substantially in the mature organs. Also expressed in lung and spleen. Expressed in the condensing metanephric mesenchyme and in early epithelial structures that are precursors to glomeruli.1 Publication

Gene expression databases

BgeeiQ7TS75.
GenevisibleiQ7TS75. MM.

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 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000109502.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi375 – 3817Poly-Asp
Compositional biasi382 – 42746Glu-richAdd
BLAST
Compositional biasi756 – 76611Poly-GluAdd
BLAST
Compositional biasi934 – 9429Poly-Glu

Sequence similaritiesi

Belongs to the Amer family.Curated

Phylogenomic databases

eggNOGiENOG410IJHD. Eukaryota.
ENOG410XU7Y. LUCA.
GeneTreeiENSGT00530000063529.
HOGENOMiHOG000049188.
HOVERGENiHBG107863.
InParanoidiQ7TS75.
KOiK19407.
OMAiRDGEGKC.
OrthoDBiEOG7ZKS9T.
PhylomeDBiQ7TS75.
TreeFamiTF333006.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q7TS75-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESQQDEAVQ TKGASTSSDA QDQGAEKGAK NKTTEATEGP TSEPPLSGPG
60 70 80 90 100
RLKKTAMKLF GGKKGICTLP SFFGGGRSKG SGKVSSKKSL NKSKTHDGLS
110 120 130 140 150
EASQGPEDVV IEETDLSTPL SKSSAQFPSS QSANGALEIG SKHKTSGTEA
160 170 180 190 200
IEKAGVEKVP SVHKPKKSLK SFFSSIRRHR KGKTSGADQS VPGAKELEGA
210 220 230 240 250
RTRSHEHVSS ISLPSSEEIF RDTRKENAKP QDAPGPKMSP AQVHFSPTTE
260 270 280 290 300
KAACKNPEKL TRTCASEFMQ PKPVLEGGSL EEPHTSETEG KVVAGEVNPP
310 320 330 340 350
NGPVGDQLSL LFGDVTSLKS FDSLTGCGDI IAEQDMDSMT DSMASGGQRA
360 370 380 390 400
NRDGTKRSSC LVTYQGGGEE MALPDDDDND DEEEEEEEEE EEEEEEEEEE
410 420 430 440 450
EEEEEEEEEL LEDEEEVKDG EENDDLEYLW ASAQIYPRFN MNLGYHTAIS
460 470 480 490 500
PSHQGYMLLD PVQSYPNLGL GELLTPQSDQ QESAPNSDEG YYDSTTPGFE
510 520 530 540 550
DDSGEALGLA HRDCLPRDSY SGDALYEFYE PDDSLEHSPP GDDCLYDLRG
560 570 580 590 600
RNSEMLDPFL NLEPFSSRPP GAMETEEERL VTIQKQLLYW ELRREQREAQ
610 620 630 640 650
EACAREAHAR EAYARDTHTR ESYGRNVRAR ETQALEAHSQ EGRVQETKVR
660 670 680 690 700
QEKPALEYQM RPLGPSVMGL VAGTSGGSQT SHRGTTSAFP ATSSSEPDWR
710 720 730 740 750
DFRPLEKRFE GTCSKKDQST CLMQLFQSDA MFEPDMQEAN FGGSPRKAYP
760 770 780 790 800
SYSPPEEPEE EEEEKEGNAT VSFSQALVEF TSNGNLFTSM SYSSDSDSSF
810 820 830 840 850
TQNLPELPPM VTFDIADVER DGEGKCEENP EFNNDEDLTA SLEAFELGYY
860 870 880 890 900
HKHAFNSYHS RFYQGLPWGV SSLPRYLGLP GVHPRPPPAA MALNRRSRSL
910 920 930 940 950
DNAESLELEL SSSHLAQGYM ESDELQAHQE DSDEEGEEEE GEWGRDSPLS
960 970 980 990 1000
LYTEPPGVYD WPPWAHCPLP VGPGLAWMSP NQLYEPFNQS SYVQATCCVP
1010 1020 1030 1040 1050
PVAMPVSVPG RTPGDSVSQL ARPSHLPLPM GPCYNLQSQA SQSGRAKPRD
1060 1070 1080 1090 1100
VLLPVDEPSC SSISGANSQS QAKPVGITHG IPQLPRVRPE PFQLQPNHYR
1110 1120 1130
ASNLDLSKER GEQGASLSTS YSSTAMNGNL AK
Length:1,132
Mass (Da):124,164
Last modified:March 21, 2012 - v3
Checksum:i7039226488581FCC
GO

Sequence cautioni

The sequence AAH53442.1 differs from that shown.Contaminating sequence. Potential poly-A sequence.Curated
The sequence BAC25373.1 differs from that shown. Reason: Frameshift at positions 235 and 284. Curated
The sequence BAC33914.1 differs from that shown. Reason: Erroneous termination at position 4. Translated as Gln.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL671765 Genomic DNA. Translation: CAM13296.1.
AK049774 mRNA. Translation: BAC33914.1. Sequence problems.
AK012651 mRNA. Translation: BAC25373.1. Frameshift.
BC053442 mRNA. Translation: AAH53442.1. Sequence problems.
CCDSiCCDS41067.1.
RefSeqiNP_780388.2. NM_175179.4.
UniGeneiMm.182867.

Genome annotation databases

EnsembliENSMUST00000084535; ENSMUSP00000109502; ENSMUSG00000050332.
GeneIDi72345.
KEGGimmu:72345.
UCSCiuc009ttx.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL671765 Genomic DNA. Translation: CAM13296.1.
AK049774 mRNA. Translation: BAC33914.1. Sequence problems.
AK012651 mRNA. Translation: BAC25373.1. Frameshift.
BC053442 mRNA. Translation: AAH53442.1. Sequence problems.
CCDSiCCDS41067.1.
RefSeqiNP_780388.2. NM_175179.4.
UniGeneiMm.182867.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000109502.

PTM databases

iPTMnetiQ7TS75.
PhosphoSiteiQ7TS75.

Proteomic databases

MaxQBiQ7TS75.
PaxDbiQ7TS75.
PeptideAtlasiQ7TS75.
PRIDEiQ7TS75.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084535; ENSMUSP00000109502; ENSMUSG00000050332.
GeneIDi72345.
KEGGimmu:72345.
UCSCiuc009ttx.2. mouse.

Organism-specific databases

CTDi139285.
MGIiMGI:1919595. Amer1.

Phylogenomic databases

eggNOGiENOG410IJHD. Eukaryota.
ENOG410XU7Y. LUCA.
GeneTreeiENSGT00530000063529.
HOGENOMiHOG000049188.
HOVERGENiHBG107863.
InParanoidiQ7TS75.
KOiK19407.
OMAiRDGEGKC.
OrthoDBiEOG7ZKS9T.
PhylomeDBiQ7TS75.
TreeFamiTF333006.

Enzyme and pathway databases

ReactomeiR-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-196299. Beta-catenin phosphorylation cascade.
R-MMU-4641262. Disassembly of the destruction complex and recruitment of AXIN to the membrane.

Miscellaneous databases

PROiQ7TS75.
SOURCEiSearch...

Gene expression databases

BgeeiQ7TS75.
GenevisibleiQ7TS75. MM.

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 [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-387.
    Strain: C57BL/6J.
    Tissue: Spinal cord.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-389.
    Tissue: Embryo.
  4. Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiAMER1_MOUSE
AccessioniPrimary (citable) accession number: Q7TS75
Secondary accession number(s): B1AUM2, Q8BT92, Q8C7P7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: March 21, 2012
Last modified: July 6, 2016
This is version 79 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.