[1]
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PROTEIN SEQUENCE (ISOFORM 1).
TISSUE=Erythrocyte;
PubMed=2684970 [NCBI, ExPASy, EBI, Israel, Japan]
Ingrosso D.,
Fowler A.V.,
Bleibaum J.,
Clarke S.;
"Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases.";
J. Biol. Chem. 264:20131-20139(1989).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT VAL-120.
TISSUE=Brain cortex;
DOI=10.1016/S0006-291X(05)80987-8; PubMed=1339271 [NCBI, ExPASy, EBI, Israel, Japan]
Maclaren D.C.,
Kagan R.M.,
Clarke S.;
"Alternative splicing of the human isoaspartyl protein carboxyl methyltransferase RNA leads to the generation of a C-terminal -RDEL sequence in isozyme II.";
Biochem. Biophys. Res. Commun. 185:277-283(1992).
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[3]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT VAL-120.
PubMed=7592526 [NCBI, ExPASy, EBI, Israel, Japan]
Takeda R.,
Mizobuchi M.,
Murao K.,
Sato M.,
Takahara J.;
"Characterization of three cDNAs encoding two isozymes of an isoaspartyl protein carboxyl methyltransferase from human erythroid leukemia cells.";
J. Biochem. 117:683-685(1995).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-120.
TISSUE=Brain;
Shirasawa T.,
Takahashi H.,
Endoh R.,
Sakamoto K.,
Hirokawa K.,
Mori H.;
"Gene expression of carboxyl methyltransferase is altered in Alzheimer's disease and the product is localized to neurofibrillary tangles.";
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-120.
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J.,
Palmer S.A.,
Sims S.K.,
Edwards C.A.,
Ashurst J.L.,
Wilming L.,
Jones M.C.,
Horton R.,
Hunt S.E.,
Scott C.E.,
Gilbert J.G.R.,
Clamp M.E.,
Bethel G.,
Milne S.,
Ainscough R.,
Almeida J.P.,
Ambrose K.D.,
Andrews T.D.,
Ashwell R.I.S., ![]()
Babbage A.K.,
Bagguley C.L.,
Bailey J.,
Banerjee R.,
Barker D.J.,
Barlow K.F.,
Bates K.,
Beare D.M.,
Beasley H.,
Beasley O.,
Bird C.P.,
Blakey S.E.,
Bray-Allen S.,
Brook J.,
Brown A.J.,
Brown J.Y.,
Burford D.C.,
Burrill W.,
Burton J.,
Carder C.,
Carter N.P.,
Chapman J.C.,
Clark S.Y.,
Clark G.,
Clee C.M.,
Clegg S.,
Cobley V.,
Collier R.E.,
Collins J.E.,
Colman L.K.,
Corby N.R.,
Coville G.J.,
Culley K.M.,
Dhami P.,
Davies J.,
Dunn M.,
Earthrowl M.E.,
Ellington A.E.,
Evans K.A.,
Faulkner L.,
Francis M.D.,
Frankish A.,
Frankland J.,
French L.,
Garner P.,
Garnett J.,
Ghori M.J.,
Gilby L.M.,
Gillson C.J.,
Glithero R.J.,
Grafham D.V.,
Grant M.,
Gribble S.,
Griffiths C.,
Griffiths M.N.D.,
Hall R.,
Halls K.S.,
Hammond S.,
Harley J.L.,
Hart E.A.,
Heath P.D.,
Heathcott R.,
Holmes S.J.,
Howden P.J.,
Howe K.L.,
Howell G.R.,
Huckle E.,
Humphray S.J.,
Humphries M.D.,
Hunt A.R.,
Johnson C.M.,
Joy A.A.,
Kay M.,
Keenan S.J.,
Kimberley A.M.,
King A.,
Laird G.K.,
Langford C.,
Lawlor S.,
Leongamornlert D.A.,
Leversha M.,
Lloyd C.R.,
Lloyd D.M.,
Loveland J.E.,
Lovell J.,
Martin S.,
Mashreghi-Mohammadi M.,
Maslen G.L.,
Matthews L.,
McCann O.T.,
McLaren S.J.,
McLay K.,
McMurray A.,
Moore M.J.F.,
Mullikin J.C.,
Niblett D.,
Nickerson T.,
Novik K.L.,
Oliver K.,
Overton-Larty E.K.,
Parker A.,
Patel R.,
Pearce A.V.,
Peck A.I.,
Phillimore B.J.C.T.,
Phillips S.,
Plumb R.W.,
Porter K.M.,
Ramsey Y.,
Ranby S.A.,
Rice C.M.,
Ross M.T.,
Searle S.M.,
Sehra H.K.,
Sheridan E.,
Skuce C.D.,
Smith S.,
Smith M.,
Spraggon L.,
Squares S.L.,
Steward C.A.,
Sycamore N.,
Tamlyn-Hall G.,
Tester J.,
Theaker A.J.,
Thomas D.W.,
Thorpe A.,
Tracey A.,
Tromans A.,
Tubby B.,
Wall M.,
Wallis J.M.,
West A.P.,
White S.S.,
Whitehead S.L.,
Whittaker H.,
Wild A.,
Willey D.J.,
Wilmer T.E.,
Wood J.M.,
Wray P.W.,
Wyatt J.C.,
Young L.,
Younger R.M.,
Bentley D.R.,
Coulson A.,
Durbin R.M.,
Hubbard T.,
Sulston J.E.,
Dunham I.,
Rogers J.,
Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
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[6]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT VAL-120.
TISSUE=Muscle, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
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[7]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
TISSUE=Foreskin;
DOI=10.1006/abbi.1996.0513; PubMed=8914929 [NCBI, ExPASy, EBI, Israel, Japan]
Devry C.G.,
Tsai W.,
Clarke S.;
"Structure of the human gene encoding the protein repair L-isoaspartyl (D-aspartyl) O-methyltransferase.";
Arch. Biochem. Biophys. 335:321-332(1996).
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[8]
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PROTEIN SEQUENCE OF 5-19; 44-60; 106-170; 179-198 AND 205-220, AND VARIANT VAL-120.
DOI=10.1021/bi00414a042; PubMed=3167043 [NCBI, ExPASy, EBI, Israel, Japan]
Gilbert J.M.,
Fowler A.,
Bleibaum J.,
Clarke S.;
"Purification of homologous protein carboxyl methyltransferase isozymes from human and bovine erythrocytes.";
Biochemistry 27:5227-5233(1988).
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[9]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-53; 100-139 AND 169-224, AND VARIANT VAL-120.
DOI=10.1006/bbrc.1994.2209; PubMed=8074695 [NCBI, ExPASy, EBI, Israel, Japan]
Tsai W.,
Clarke S.;
"Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl methyltransferase involved in protein repair.";
Biochem. Biophys. Res. Commun. 203:491-497(1994).
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[10]
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PROTEIN SEQUENCE OF 82-98, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G.,
Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
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[11]
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PARTIAL PROTEIN SEQUENCE (ISOFORM 2).
TISSUE=Erythrocyte;
DOI=10.1016/S0006-291X(05)81242-2; PubMed=1998518 [NCBI, ExPASy, EBI, Israel, Japan]
Ingrosso D.,
Kagan R.M.,
Clarke S.;
"Distinct C-terminal sequences of isozymes I and II of the human erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase.";
Biochem. Biophys. Res. Commun. 175:351-358(1991).
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[12]
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VARIANT VAL-120.
DOI=10.1007/s100380050161; PubMed=10496068 [NCBI, ExPASy, EBI, Israel, Japan]
DeVry C.G.,
Clarke S.;
"Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins.";
J. Hum. Genet. 44:275-288(1999).
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[13]
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X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
DOI=10.1074/jbc.M200229200; PubMed=11792715 [NCBI, ExPASy, EBI, Israel, Japan]
Ryttersgaard C.,
Griffith S.C.,
Sawaya M.R.,
MacLaren D.C.,
Clarke S.,
Yeates T.O.;
"Crystal structure of human L-isoaspartyl methyltransferase.";
J. Biol. Chem. 277:10642-10646(2002).
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[14]
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X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
DOI=10.1110/ps.37802; PubMed=11847284 [NCBI, ExPASy, EBI, Israel, Japan]
Smith C.D.,
Carson M.,
Friedman A.M.,
Skinner M.M.,
Delucas L.,
Chantalat L.,
Weise L.,
Shirasawa T.,
Chattopadhyay D.;
"Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-adenosyl homocysteine at 1.6-A resolution and modeling of an isoaspartyl-containing peptide at the active site.";
Protein Sci. 11:625-635(2002).
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