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Protein

APC membrane recruitment protein 2

Gene

Amer2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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 (By similarity).By similarity

GO - Molecular functioni

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1919375. Amer2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 672672APC membrane recruitment protein 2PRO_0000281886Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541PhosphoserineCombined sources
Modified residuei223 – 2231PhosphoserineCombined sources
Modified residuei227 – 2271PhosphoserineCombined sources
Modified residuei244 – 2441PhosphoserineCombined sources
Modified residuei284 – 2841PhosphoserineCombined sources
Modified residuei356 – 3561PhosphoserineCombined sources
Modified residuei359 – 3591PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ8CCJ4.
PaxDbiQ8CCJ4.
PRIDEiQ8CCJ4.

PTM databases

iPTMnetiQ8CCJ4.
PhosphoSiteiQ8CCJ4.

Expressioni

Gene expression databases

BgeeiQ8CCJ4.

Interactioni

Subunit structurei

Interacts with APC.By similarity

Protein-protein interaction databases

IntActiQ8CCJ4. 2 interactions.
MINTiMINT-218421.
STRINGi10090.ENSMUSP00000022561.

Structurei

3D structure databases

ProteinModelPortaliQ8CCJ4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi204 – 2074Poly-Glu

Sequence similaritiesi

Belongs to the Amer family.Curated

Phylogenomic databases

eggNOGiENOG410IM10. Eukaryota.
ENOG410ZHFV. LUCA.
HOGENOMiHOG000168235.
HOVERGENiHBG107862.
InParanoidiQ8CCJ4.
OrthoDBiEOG77T14C.
PhylomeDBiQ8CCJ4.
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: Q8CCJ4-1) [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
METGRSRGGG AAVSERGGGA RAGVCGRQEQ AGALAADMDS HCECAAETPA
60 70 80 90 100
AEPPSGKINK AAFKLFKKRK SGGTMPSIFG VKNKGDGKSS GPTGMVRSRT
110 120 130 140 150
HDGLAEVLVL EGSKKEEPPG GSDHSGARPI PGPPKPSGPG LGSLASSSVA
160 170 180 190 200
KSHSFFSLLK KNGRSETGKG DHAEASKAGG KQKRGLKGIF SSMRWHRRDK
210 220 230 240 250
RGKEEEEKAV RAAGPGNLVL PGSLTASLEC VKEEPPRAAR RPDSPGQDAS
260 270 280 290 300
RHAAGEPAGG EQAPASAESA PERICLEAGS PTGSGDQSSR GEDAEGHRRE
310 320 330 340 350
EKPGAALESG AGEVQAAEDA SKTGDVPIKT VPLVDSEGGS GRASAVPDPS
360 370 380 390 400
SVDPPSDPSA DRICLMFSDV TSLKSFDSLT GCGDIIADPE EEAGPSCDKH
410 420 430 440 450
VPGPGKPVLS KKNASVVAYQ GGGEEMASPD QVDDTYLPEF WDMLSQTEDQ
460 470 480 490 500
GQGTQEGAAK AATASDIKLA PETSSDTRCG EAAKDMSSVK RRRLHRIPIE
510 520 530 540 550
SQQKEEPKHP EKEHQEGVPN SDEGYWDSTT PGPEEESISN SSSSKKVVIP
560 570 580 590 600
RDSDSGDALC DLYVEPEASP ATLPATEDPP CLSRLKPVSP GTITCPLRTP
610 620 630 640 650
GSLLKDSKIP ISIKHLSNLP SSHPVVHQQP ARSEVPRTKI PVSKVLVRRV
660 670
SNRGLAGTTI RAAACHDSAK KL
Length:672
Mass (Da):69,933
Last modified:April 3, 2007 - v2
Checksum:i5CE3FFDF4FFE1348
GO
Isoform 2 (identifier: Q8CCJ4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     255-380: Missing.

Show »
Length:546
Mass (Da):57,354
Checksum:iFA5F5882B0409627
GO

Sequence cautioni

The sequence AAH30356.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH56350.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB27452.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAC27972.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAE23912.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei255 – 380126Missing in isoform 2. 2 PublicationsVSP_024090Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC103355 Genomic DNA. No translation available.
AK032651 mRNA. Translation: BAC27972.1. Different initiation.
AK011185 mRNA. Translation: BAB27452.1. Different initiation.
AK139177 mRNA. Translation: BAE23912.1. Different initiation.
BC030356 mRNA. Translation: AAH30356.1. Different initiation.
BC056350 mRNA. Translation: AAH56350.1. Different initiation.
RefSeqiNP_001158177.1. NM_001164705.1.
NP_082389.1. NM_028113.3.
XP_006519653.1. XM_006519590.2. [Q8CCJ4-1]
UniGeneiMm.275499.

Genome annotation databases

GeneIDi72125.
KEGGimmu:72125.
UCSCiuc007ufb.2. mouse. [Q8CCJ4-2]
uc011zmz.1. mouse. [Q8CCJ4-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC103355 Genomic DNA. No translation available.
AK032651 mRNA. Translation: BAC27972.1. Different initiation.
AK011185 mRNA. Translation: BAB27452.1. Different initiation.
AK139177 mRNA. Translation: BAE23912.1. Different initiation.
BC030356 mRNA. Translation: AAH30356.1. Different initiation.
BC056350 mRNA. Translation: AAH56350.1. Different initiation.
RefSeqiNP_001158177.1. NM_001164705.1.
NP_082389.1. NM_028113.3.
XP_006519653.1. XM_006519590.2. [Q8CCJ4-1]
UniGeneiMm.275499.

3D structure databases

ProteinModelPortaliQ8CCJ4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8CCJ4. 2 interactions.
MINTiMINT-218421.
STRINGi10090.ENSMUSP00000022561.

PTM databases

iPTMnetiQ8CCJ4.
PhosphoSiteiQ8CCJ4.

Proteomic databases

MaxQBiQ8CCJ4.
PaxDbiQ8CCJ4.
PRIDEiQ8CCJ4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi72125.
KEGGimmu:72125.
UCSCiuc007ufb.2. mouse. [Q8CCJ4-2]
uc011zmz.1. mouse. [Q8CCJ4-1]

Organism-specific databases

CTDi219287.
MGIiMGI:1919375. Amer2.

Phylogenomic databases

eggNOGiENOG410IM10. Eukaryota.
ENOG410ZHFV. LUCA.
HOGENOMiHOG000168235.
HOVERGENiHBG107862.
InParanoidiQ8CCJ4.
OrthoDBiEOG77T14C.
PhylomeDBiQ8CCJ4.
TreeFamiTF333006.

Miscellaneous databases

NextBioi335506.
PROiQ8CCJ4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8CCJ4.

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 32-672 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-672 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  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 26-672 (ISOFORM 2).
    Strain: C57BL/6J.
    Tissue: Brain and Eye.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 599-608, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356 AND SER-359, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic brain.
  6. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-223; SER-227 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiAMER2_MOUSE
AccessioniPrimary (citable) accession number: Q8CCJ4
Secondary accession number(s): Q7TNC5, Q8K0U9, Q9D0Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: January 20, 2016
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.