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Q5JTC6 (AMER1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
APC membrane recruitment protein 1

Short name=Amer1
Alternative name(s):
Protein FAM123B
Wilms tumor gene on the X chromosome protein
Gene names
Name:AMER1
Synonyms:FAM123B, WTX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1135 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4 Ref.8 Ref.9 Ref.11 Ref.12

Subunit structure

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. Ref.4 Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

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. Ref.4 Ref.8 Ref.9 Ref.11 Ref.12

Tissue specificity

Detected in fetal and adult kidney, brain and spleen. Ref.9

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Miscellaneous

Inactivated in approximately one-third of Wilms tumors.

Sequence similarities

Belongs to the Amer family.

Ontologies

Keywords
   Biological processWnt signaling pathway
   Cellular componentCell membrane
Cytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandLipid-binding
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processWnt signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

adipose tissue development

Inferred from electronic annotation. Source: Ensembl

bone development

Inferred from electronic annotation. Source: Ensembl

mesenchymal cell differentiation involved in kidney development

Inferred from electronic annotation. Source: Ensembl

negative regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype Ref.11. Source: UniProtKB

regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.8Ref.11Ref.12. Source: UniProtKB

   Molecular_functionbeta-catenin binding

Inferred from direct assay Ref.12. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from direct assay Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AMER3Q8N9444EBI-6169747,EBI-8869590

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5JTC6-1)

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.
Isoform 2 (identifier: Q5JTC6-2)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11351135APC membrane recruitment protein 1
PRO_0000281887

Regions

Compositional bias370 – 41142Glu-rich
Compositional bias755 – 7628Poly-Glu
Compositional bias930 – 93910Poly-Glu
Compositional bias952 – 1104153Pro-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.13
Modified residue2461Phosphoserine Ref.5

Natural variations

Alternative sequence786 – 80419MSCSS…LPELP → IRCPGTEDKRQVTQACGTW in isoform 2.
VSP_024091
Alternative sequence805 – 1135331Missing in isoform 2.
VSP_024092
Natural variant1591F → L.
Corresponds to variant rs34677493 [ dbSNP | Ensembl ].
VAR_053870
Natural variant2781A → S.
Corresponds to variant rs35718712 [ dbSNP | Ensembl ].
VAR_053871
Natural variant2921K → N. Ref.1
VAR_031304

Experimental info

Mutagenesis541K → 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. Ref.11
Mutagenesis581K → 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. Ref.11
Mutagenesis791K → 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. Ref.11
Mutagenesis831K → 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. Ref.11
Mutagenesis1661K → 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. Ref.11
Mutagenesis1811K → 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. Ref.11
Mutagenesis1831K → 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. Ref.11
Isoform 2:
Sequence conflict7861I → R in BAC04964. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Amer1-S1) [UniParc].

Last modified April 3, 2007. Version 2.
Checksum: 7C77EF692A0F60D3

FASTA1,135124,029
        10         20         30         40         50         60 
METQKDEAAQ AKGAAASGST REQTAEKGAK NKAAEATEGP TSEPSSSGPG RLKKTAMKLF 

        70         80         90        100        110        120 
GGKKGICTLP SFFGGGRSKG SGKGSSKKGL SKSKTHDGLS EAAHGPEDVV SEGTGFSLPL 

       130        140        150        160        170        180 
PELPCQFPSS QSAHGALETG SRCKTSVAGA TEKAVAEKFP SMPKPKKGLK GFFSSIRRHR 

       190        200        210        220        230        240 
KSKVTGAEQS EPGAKGPERV RARPHEHVSS APQVPCFEET FQAPRKENAN PQDAPGPKVS 

       250        260        270        280        290        300 
PTPEPSPPAT EKMACKDPEK PMEACASAHV QPKPAPEASS LEEPHSPETG EKVVAGEVNP 

       310        320        330        340        350        360 
PNGPVGDPLS LLFGDVTSLK SFDSLTGCGD IIAEQDMDSM TDSMASGGQR ANRDGTKRSS 

       370        380        390        400        410        420 
CLVTYQGGGE EMALPDDDDE EEEEEEEVEL EEEEEEVKEE EEDDDLEYLW ETAQMYPRPN 

       430        440        450        460        470        480 
MNLGYHPTTS PGHHGYMLLD PVRSYPGLAP GELLTPQSDQ QESAPNSDEG YYDSTTPGFE 

       490        500        510        520        530        540 
DDSGEALGLV RRDCLPRDSY SGDALYEFYE PDDSLENSPP GDDCLYDLHG RSSEMFDPFL 

       550        560        570        580        590        600 
NFEPFLSSRP PGAMETEEER LVTIQKQLLY WELRREQLEA QEARAREAHA REAHAREAYT 

       610        620        630        640        650        660 
REAYGREAYA REAHTWEAHG REARTREAQA REVRCRETQV RETQARQEKP VLEYQMRPLG 

       670        680        690        700        710        720 
PSVMGLAAGV SGTSQISHRG ITSAFPTTAS SEPDWRDFRP LEKRYEGTCS KKDQSTCLMQ 

       730        740        750        760        770        780 
LFQSDAMFEP DMQEANFGGS PRRAYPTYSP PEDPEEEEVE KEGNATVSFS QALVEFTSNG 

       790        800        810        820        830        840 
NLFSSMSCSS DSDSSFTQNL PELPPMVTFD IADVERDGEG KCEENPEFHN DEDLAASLEA 

       850        860        870        880        890        900 
FELGYYHKHA FNNYHSRFYQ GLPWGVSSLP RYLGLPGLHP RPPPAAMALN RRSRSLDTAE 

       910        920        930        940        950        960 
TLEMELSNSH LVQGYLESDE LQAQQEDSDE EDEEEEEGEW SRDSPLSLYT EPPGAYDWPA 

       970        980        990       1000       1010       1020 
WAPCPLPVGP GPAWISPNQL DRPSSQSPYR QATCCIPPMT MSISLSVPES RAPGESGPQL 

      1030       1040       1050       1060       1070       1080 
ARPSHLHLPM GPCYNLQPQA SQSMRARPRD VLLPVDEPSC SSSSGGFSPS PLPQAKPVGI 

      1090       1100       1110       1120       1130 
THGIPQLPRV RPEHPQPQPT HYGPSSLDLS KERAEQGASL ATSYSSTAMN GNLAK 

« Hide

Isoform 2 (Amer1-S2) (Short) [UniParc].

Checksum: 3DDEF91694003622
Show »

FASTA80487,823

References

« Hide 'large scale' references
[1]"An X chromosome gene, WTX, is commonly inactivated in Wilms tumor."
Rivera M.N., Kim W.J., Wells J., Driscoll D.R., Brannigan B.W., Han M., Kim J.C., Feinberg A.P., Gerald W.L., Vargas S.O., Chin L., Iafrate A.J., Bell D.W., Haber D.A.
Science 315:642-645(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Wilms tumor suppressor WTX negatively regulates WNT/beta-catenin signaling."
Major M.B., Camp N.D., Berndt J.D., Yi X., Goldenberg S.J., Hubbert C., Biechele T.L., Gingras A.-C., Zheng N., Maccoss M.J., Angers S., Moon R.T.
Science 316:1043-1046(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH CTNNB1; KEAP1; AXIN1; APC; FBXW11 AND BTRC.
[5]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Germline mutations in WTX cause a sclerosing skeletal dysplasia but do not predispose to tumorigenesis."
Jenkins Z.A., van Kogelenberg M., Morgan T., Jeffs A., Fukuzawa R., Pearl E., Thaller C., Hing A.V., Porteous M.E., Garcia-Minaur S., Bohring A., Lacombe D., Stewart F., Fiskerstrand T., Bindoff L., Berland S., Ades L.C., Tchan M. expand/collapse author list , David A., Wilson L.C., Hennekam R.C., Donnai D., Mansour S., Cormier-Daire V., Robertson S.P.
Nat. Genet. 41:95-100(2009) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EF186024 mRNA. Translation: ABM60755.1.
AK097146 mRNA. Translation: BAC04964.1.
AL355852 Genomic DNA. Translation: CAI40637.1.
AL355852 Genomic DNA. Translation: CAO03539.1.
CCDSCCDS14377.2. [Q5JTC6-1]
RefSeqNP_689637.3. NM_152424.3. [Q5JTC6-1]
UniGeneHs.314225.

3D structure databases

ProteinModelPortalQ5JTC6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid126556. 8 interactions.
IntActQ5JTC6. 6 interactions.
STRING9606.ENSP00000329117.

PTM databases

PhosphoSiteQ5JTC6.

Polymorphism databases

DMDM142984753.

Proteomic databases

MaxQBQ5JTC6.
PaxDbQ5JTC6.
PRIDEQ5JTC6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330258; ENSP00000329117; ENSG00000184675. [Q5JTC6-1]
ENST00000374869; ENSP00000364003; ENSG00000184675. [Q5JTC6-2]
ENST00000403336; ENSP00000384722; ENSG00000184675. [Q5JTC6-2]
GeneID139285.
KEGGhsa:139285.
UCSCuc004dvo.3. human. [Q5JTC6-1]

Organism-specific databases

CTD139285.
GeneCardsGC0XM063406.
HGNCHGNC:26837. AMER1.
MIM300373. phenotype.
300647. gene.
neXtProtNX_Q5JTC6.
Orphanet2780. Osteopathia striata - cranial sclerosis.
PharmGKBPA145148904.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG45581.
HOGENOMHOG000049188.
HOVERGENHBG107863.
InParanoidQ5JTC6.
OMADMDSMTD.
OrthoDBEOG7ZKS9T.
PhylomeDBQ5JTC6.
TreeFamTF333006.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeQ5JTC6.
CleanExHS_FAM123B.
GenevestigatorQ5JTC6.

Family and domain databases

InterProIPR019003. Uncharacterised_FAM123.
[Graphical view]
PfamPF09422. WTX. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi139285.
NextBio83932.
PROQ5JTC6.
SOURCESearch...

Entry information

Entry nameAMER1_HUMAN
AccessionPrimary (citable) accession number: Q5JTC6
Secondary accession number(s): A2IB86, Q8N885
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2007
Last sequence update: April 3, 2007
Last modified: July 9, 2014
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

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Human chromosome X

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