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Protein

APC membrane recruitment protein 2

Gene

AMER2

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

Functioni

Negative regulator of the canonical Wnt signaling pathway involved in neuroectodermal patterning. 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.1 Publication

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Wnt signaling pathway

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
APC membrane recruitment protein 2
Short name:
Amer2
Alternative name(s):
Protein FAM123A
Gene namesi
Name:AMER2
Synonyms:FAM123A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:26360. AMER2.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145148898.

Polymorphism and mutation databases

BioMutaiAMER2.
DMDMi338817901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 671671APC membrane recruitment protein 2PRO_0000281885Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei162 – 1621PhosphoserineBy similarity
Modified residuei229 – 2291PhosphoserineBy similarity
Modified residuei233 – 2331PhosphoserineBy similarity
Modified residuei355 – 3551PhosphoserineBy similarity
Modified residuei358 – 3581PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ8N7J2.
PeptideAtlasiQ8N7J2.
PRIDEiQ8N7J2.

PTM databases

iPTMnetiQ8N7J2.
PhosphoSiteiQ8N7J2.

Expressioni

Gene expression databases

BgeeiQ8N7J2.
CleanExiHS_FAM123A.
GenevisibleiQ8N7J2. HS.

Organism-specific databases

HPAiHPA039458.

Interactioni

Subunit structurei

Interacts with APC.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8N7J2. 1 interaction.
STRINGi9606.ENSP00000426528.

Structurei

3D structure databases

ProteinModelPortaliQ8N7J2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 150143Gly-richAdd
BLAST

Sequence similaritiesi

Belongs to the Amer family.Curated

Phylogenomic databases

eggNOGiENOG410IM10. Eukaryota.
ENOG410ZHFV. LUCA.
GeneTreeiENSGT00530000063529.
HOGENOMiHOG000168235.
HOVERGENiHBG107862.
InParanoidiQ8N7J2.
OMAiLECVKEE.
OrthoDBiEOG77T14C.
PhylomeDBiQ8N7J2.
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: Q8N7J2-1) [UniParc]FASTAAdd to basket

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
METSRSRGGG GAVSERGGAG ASVGVCRRKA EAGAGTGTLA ADMDLHCDCA
60 70 80 90 100
AETPAAEPPS GKINKAAFKL FKKRKSGGTM PSIFGVKNKG DGKSSGPTGL
110 120 130 140 150
VRSRTHDGLA EVLVLESGRK EEPRGGGDSG GGGGGRPNPG PPRAAGPGGG
160 170 180 190 200
SLASSSVAKS HSFFSLLKKN GRSENGKGEP VDASKAGGKQ KRGLRGLFSG
210 220 230 240 250
MRWHRKDKRA KAEAAEGRAP GGGLILPGSL TASLECVKEE TPRAAREPEE
260 270 280 290 300
PSQDAPRDPA GEPAGGEEVP APADRAPARS CREAEGLAHP GDTGARGEDA
310 320 330 340 350
AGHRRAEPGP GEVRTAEDAS RTGAVPVKTV PLVDSEGGSG RAPAAPDPAS
360 370 380 390 400
VDPPSDPSAD RICLMFSDVT SLKSFDSLTG CGDIIADQEE EAGPSCDKHV
410 420 430 440 450
PGPGKPALSK KNPGVVAYQG GGEEMASPDE VDDTYLQEFW DMLSQTEEQG
460 470 480 490 500
PEPQEGAAKV AAALETKVVP ETPKDTRCVE AAKDASSVKR RRLNRIPIEP
510 520 530 540 550
HPKEEPKHPE KEQQEGVPNS DEGYWDSTTP GPEEDSSSSG KKAGIPRDSY
560 570 580 590 600
SGDALYDLYA DPDGSPATLP GGKDNEETSS LSRLKPVSPG TITCPLRTPG
610 620 630 640 650
SLLKDSKIPI SIKHLTNLPS SHPVVHQQPS RSEMPRTKIP VSKVLVRRVS
660 670
NRGLAGTTIR ATACHDSAKK L
Length:671
Mass (Da):69,507
Last modified:June 28, 2011 - v3
Checksum:i0640CCCCD03E0334
GO
Isoform 2 (identifier: Q8N7J2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     261-379: Missing.

Show »
Length:552
Mass (Da):57,583
Checksum:iDD5279E3144D7CB1
GO

Sequence cautioni

The sequence AAH32653.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAH41392.1 differs from that shown. Reason: Frameshift at positions 421 and 485. Curated
The sequence BAC05288.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201K → E in BAB70845 (PubMed:14702039).Curated
Sequence conflicti142 – 1421P → S in AAH41392 (PubMed:15489334).Curated
Sequence conflicti265 – 2651G → V in BAC05288 (PubMed:14702039).Curated
Sequence conflicti290 – 2901P → A in AAH41392 (PubMed:15489334).Curated
Sequence conflicti442 – 4421M → V in BAB70845 (PubMed:14702039).Curated
Sequence conflicti511 – 5111K → E in AAH41392 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti457 – 4571A → T in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036448
Natural varianti659 – 6591I → M.
Corresponds to variant rs2282406 [ dbSNP | Ensembl ].
VAR_031303

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei261 – 379119Missing in isoform 2. 2 PublicationsVSP_024089Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055049 mRNA. Translation: BAB70845.1.
AK098343 mRNA. Translation: BAC05288.1. Different initiation.
AL359757 Genomic DNA. Translation: CAH70807.1.
BC032653 mRNA. Translation: AAH32653.2. Different initiation.
BC041392 mRNA. Translation: AAH41392.1. Frameshift.
CCDSiCCDS53859.1. [Q8N7J2-1]
CCDS9312.1. [Q8N7J2-2]
RefSeqiNP_689917.2. NM_152704.3. [Q8N7J2-1]
NP_954589.1. NM_199138.2. [Q8N7J2-2]
XP_005266336.1. XM_005266279.2. [Q8N7J2-1]
XP_005266337.1. XM_005266280.2. [Q8N7J2-1]
XP_006719833.1. XM_006719770.2. [Q8N7J2-2]
UniGeneiHs.528335.
Hs.731897.

Genome annotation databases

EnsembliENST00000357816; ENSP00000350469; ENSG00000165566. [Q8N7J2-2]
ENST00000515384; ENSP00000426528; ENSG00000165566. [Q8N7J2-1]
GeneIDi219287.
KEGGihsa:219287.
UCSCiuc001uqb.5. human. [Q8N7J2-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK055049 mRNA. Translation: BAB70845.1.
AK098343 mRNA. Translation: BAC05288.1. Different initiation.
AL359757 Genomic DNA. Translation: CAH70807.1.
BC032653 mRNA. Translation: AAH32653.2. Different initiation.
BC041392 mRNA. Translation: AAH41392.1. Frameshift.
CCDSiCCDS53859.1. [Q8N7J2-1]
CCDS9312.1. [Q8N7J2-2]
RefSeqiNP_689917.2. NM_152704.3. [Q8N7J2-1]
NP_954589.1. NM_199138.2. [Q8N7J2-2]
XP_005266336.1. XM_005266279.2. [Q8N7J2-1]
XP_005266337.1. XM_005266280.2. [Q8N7J2-1]
XP_006719833.1. XM_006719770.2. [Q8N7J2-2]
UniGeneiHs.528335.
Hs.731897.

3D structure databases

ProteinModelPortaliQ8N7J2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8N7J2. 1 interaction.
STRINGi9606.ENSP00000426528.

PTM databases

iPTMnetiQ8N7J2.
PhosphoSiteiQ8N7J2.

Polymorphism and mutation databases

BioMutaiAMER2.
DMDMi338817901.

Proteomic databases

PaxDbiQ8N7J2.
PeptideAtlasiQ8N7J2.
PRIDEiQ8N7J2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000357816; ENSP00000350469; ENSG00000165566. [Q8N7J2-2]
ENST00000515384; ENSP00000426528; ENSG00000165566. [Q8N7J2-1]
GeneIDi219287.
KEGGihsa:219287.
UCSCiuc001uqb.5. human. [Q8N7J2-1]

Organism-specific databases

CTDi219287.
GeneCardsiAMER2.
H-InvDBHIX0011182.
HGNCiHGNC:26360. AMER2.
HPAiHPA039458.
MIMi614659. gene.
neXtProtiNX_Q8N7J2.
PharmGKBiPA145148898.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IM10. Eukaryota.
ENOG410ZHFV. LUCA.
GeneTreeiENSGT00530000063529.
HOGENOMiHOG000168235.
HOVERGENiHBG107862.
InParanoidiQ8N7J2.
OMAiLECVKEE.
OrthoDBiEOG77T14C.
PhylomeDBiQ8N7J2.
TreeFamiTF333006.

Miscellaneous databases

GenomeRNAii219287.
PROiQ8N7J2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N7J2.
CleanExiHS_FAM123A.
GenevisibleiQ8N7J2. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 47-671 (ISOFORM 1).
    Tissue: Brain and Cerebellum.
  2. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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] (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 24-671 (ISOFORM 2).
    Tissue: Brain and Eye.
  4. Cited for: VARIANT [LARGE SCALE ANALYSIS] THR-457.
  5. "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: INTERACTION WITH APC.
  6. "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.
  7. "Amer2 protein is a novel negative regulator of Wnt/beta-Catenin signaling involved in neuroectodermal patterning."
    Pfister A.S., Tanneberger K., Schambony A., Behrens J.
    J. Biol. Chem. 287:1734-1741(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PTDINS(4,5)P2-BINDING, INTERACTION WITH APC.

Entry informationi

Entry nameiAMER2_HUMAN
AccessioniPrimary (citable) accession number: Q8N7J2
Secondary accession number(s): Q5RL80
, Q5VX56, Q8N593, Q96NN5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: June 28, 2011
Last modified: July 6, 2016
This is version 93 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: 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

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.