PIMT_HUMAN
ID PIMT_HUMAN Reviewed; 227 AA.
AC P22061; A8K109; J3KP72; Q14661; Q16556; Q5VYC1; Q5VYC2; Q93061; Q96II9;
AC Q99625; Q9BQV7; Q9BQV8; Q9NP03;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 4.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Protein-L-isoaspartate(D-aspartate) O-methyltransferase {ECO:0000305|PubMed:3167043};
DE Short=PIMT;
DE EC=2.1.1.77 {ECO:0000269|PubMed:3167043, ECO:0000269|PubMed:6469980};
DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase;
DE AltName: Full=Protein L-isoaspartyl/D-aspartyl methyltransferase;
DE AltName: Full=Protein-beta-aspartate methyltransferase;
GN Name=PCMT1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP PROTEIN SEQUENCE (ISOFORM 1), ACETYLATION AT ALA-2, AND CLEAVAGE OF
RP INITIATOR METHIONINE.
RC TISSUE=Erythrocyte;
RX PubMed=2684970; DOI=10.1016/s0021-9258(19)47228-1;
RA Ingrosso D., Fowler A.V., Bleibaum J., Clarke S.;
RT "Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from
RT human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small
RT molecule S-adenosylmethionine-dependent methyltransferases.";
RL J. Biol. Chem. 264:20131-20139(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND VARIANT ILE-120.
RC TISSUE=Brain cortex;
RX PubMed=1339271; DOI=10.1016/s0006-291x(05)80987-8;
RA Maclaren D.C., Kagan R.M., Clarke S.;
RT "Alternative splicing of the human isoaspartyl protein carboxyl
RT methyltransferase RNA leads to the generation of a C-terminal -RDEL
RT sequence in isozyme II.";
RL Biochem. Biophys. Res. Commun. 185:277-283(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=7592526; DOI=10.1093/oxfordjournals.jbchem.a124763;
RA Takeda R., Mizobuchi M., Murao K., Sato M., Takahara J.;
RT "Characterization of three cDNAs encoding two isozymes of an isoaspartyl
RT protein carboxyl methyltransferase from human erythroid leukemia cells.";
RL J. Biochem. 117:683-685(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Shirasawa T., Takahashi H., Endoh R., Sakamoto K., Hirokawa K., Mori H.;
RT "Gene expression of carboxyl methyltransferase is altered in Alzheimer's
RT disease and the product is localized to neurofibrillary tangles.";
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP ILE-120.
RC TISSUE=Muscle, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-18.
RC TISSUE=Foreskin;
RX PubMed=8914929; DOI=10.1006/abbi.1996.0513;
RA Devry C.G., Tsai W., Clarke S.;
RT "Structure of the human gene encoding the protein repair L-isoaspartyl (D-
RT aspartyl) O-methyltransferase.";
RL Arch. Biochem. Biophys. 335:321-332(1996).
RN [10]
RP PROTEIN SEQUENCE OF 5-19; 44-60; 106-170; 179-198 AND 205-220, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=3167043; DOI=10.1021/bi00414a042;
RA Gilbert J.M., Fowler A., Bleibaum J., Clarke S.;
RT "Purification of homologous protein carboxyl methyltransferase isozymes
RT from human and bovine erythrocytes.";
RL Biochemistry 27:5227-5233(1988).
RN [11]
RP PROTEIN SEQUENCE OF 5-18; 25-37; 82-98; 114-144 AND 179-221, VARIANT
RP ILE-120, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-53; 100-139 AND 169-224.
RX PubMed=8074695; DOI=10.1006/bbrc.1994.2209;
RA Tsai W., Clarke S.;
RT "Amino acid polymorphisms of the human L-isoaspartyl/D-aspartyl
RT methyltransferase involved in protein repair.";
RL Biochem. Biophys. Res. Commun. 203:491-497(1994).
RN [13]
RP PARTIAL PROTEIN SEQUENCE (ISOFORM 2), AND VARIANT ILE-120.
RC TISSUE=Erythrocyte;
RX PubMed=1998518; DOI=10.1016/s0006-291x(05)81242-2;
RA Ingrosso D., Kagan R.M., Clarke S.;
RT "Distinct C-terminal sequences of isozymes I and II of the human
RT erythrocyte L-isoaspartyl/D-aspartyl protein methyltransferase.";
RL Biochem. Biophys. Res. Commun. 175:351-358(1991).
RN [14]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=6469980; DOI=10.1016/s0021-9258(18)90571-5;
RA Murray E.D. Jr., Clarke S.;
RT "Synthetic peptide substrates for the erythrocyte protein carboxyl
RT methyltransferase. Detection of a new site of methylation at isomerized L-
RT aspartyl residues.";
RL J. Biol. Chem. 259:10722-10732(1984).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP VARIANT ILE-120.
RX PubMed=10496068; DOI=10.1007/s100380050161;
RA DeVry C.G., Clarke S.;
RT "Polymorphic forms of the protein L-isoaspartate (D-aspartate) O-
RT methyltransferase involved in the repair of age-damaged proteins.";
RL J. Hum. Genet. 44:275-288(1999).
RN [18] {ECO:0007744|PDB:1KR5}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 2-227 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE.
RX PubMed=11792715; DOI=10.1074/jbc.m200229200;
RA Ryttersgaard C., Griffith S.C., Sawaya M.R., MacLaren D.C., Clarke S.,
RA Yeates T.O.;
RT "Crystal structure of human L-isoaspartyl methyltransferase.";
RL J. Biol. Chem. 277:10642-10646(2002).
RN [19] {ECO:0007744|PDB:1I1N}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-227 IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE, AND SUBUNIT.
RX PubMed=11847284; DOI=10.1110/ps.37802;
RA Smith C.D., Carson M., Friedman A.M., Skinner M.M., Delucas L.,
RA Chantalat L., Weise L., Shirasawa T., Chattopadhyay D.;
RT "Crystal structure of human L-isoaspartyl-O-methyl-transferase with S-
RT adenosyl homocysteine at 1.6-A resolution and modeling of an isoaspartyl-
RT containing peptide at the active site.";
RL Protein Sci. 11:625-635(2002).
RN [20]
RP VARIANT [LARGE SCALE ANALYSIS] ILE-120, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Initiates the repair of damaged proteins by catalyzing methyl
CC esterification of L-isoaspartyl and D-aspartyl residues produced by
CC spontaneous isomerization and racemization of L-aspartyl and L-
CC asparaginyl residues in aging peptides and proteins (PubMed:3167043,
CC PubMed:6469980). Acts on EIF4EBP2, microtubule-associated protein 2,
CC calreticulin, clathrin light chains a and b, Ubiquitin C-terminal
CC hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1,
CC stathmin, beta-synuclein and alpha-synuclein (By similarity).
CC {ECO:0000250|UniProtKB:P23506, ECO:0000269|PubMed:3167043,
CC ECO:0000269|PubMed:6469980}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-L-isoaspartate + S-adenosyl-L-methionine =
CC [protein]-L-isoaspartate alpha-methyl ester + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:12705, Rhea:RHEA-COMP:12143, Rhea:RHEA-
CC COMP:12144, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90596,
CC ChEBI:CHEBI:90598; EC=2.1.1.77; Evidence={ECO:0000269|PubMed:3167043,
CC ECO:0000269|PubMed:6469980};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12706;
CC Evidence={ECO:0000305|PubMed:3167043};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11847284}.
CC -!- INTERACTION:
CC P22061; Q13155: AIMP2; NbExp=3; IntAct=EBI-353343, EBI-745226;
CC P22061; P49247: RPIA; NbExp=3; IntAct=EBI-353343, EBI-744831;
CC P22061; PRO_0000449623 [P0DTD1]: rep; Xeno; NbExp=2; IntAct=EBI-353343, EBI-25475864;
CC P22061-2; Q92870-2: APBB2; NbExp=3; IntAct=EBI-12386584, EBI-21535880;
CC P22061-2; P54253: ATXN1; NbExp=3; IntAct=EBI-12386584, EBI-930964;
CC P22061-2; Q92989: CLP1; NbExp=3; IntAct=EBI-12386584, EBI-2559831;
CC P22061-2; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-12386584, EBI-21553822;
CC P22061-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-12386584, EBI-10976677;
CC P22061-2; Q15051-2: IQCB1; NbExp=3; IntAct=EBI-12386584, EBI-11944935;
CC P22061-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-12386584, EBI-10975473;
CC P22061-2; O14901: KLF11; NbExp=3; IntAct=EBI-12386584, EBI-948266;
CC P22061-2; P28331-2: NDUFS1; NbExp=3; IntAct=EBI-12386584, EBI-6190702;
CC P22061-2; P60891: PRPS1; NbExp=3; IntAct=EBI-12386584, EBI-749195;
CC P22061-2; P49247: RPIA; NbExp=4; IntAct=EBI-12386584, EBI-744831;
CC P22061-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-12386584, EBI-5235340;
CC P22061-2; O76024: WFS1; NbExp=3; IntAct=EBI-12386584, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:3167043}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P22061-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P22061-2; Sequence=VSP_004716;
CC -!- POLYMORPHISM: The allele frequencies for the polymorphism at codon 120
CC differ between ethnic groups; in the Caucasian population Ile-120 is
CC present at a frequency of 0.45, while it is found at a frequency of
CC 0.88 and 0.81 in the Asian and the African populations respectively.
CC Val-120 is found at a frequency of 0.55 in the Caucasians, 0.12 and
CC 0.19 in the Asian and African populations respectively. The Ile-120
CC variant has higher specific activity and thermostability than the Val-
CC 120 variant. The Val-120 variant has a higher affinity for protein
CC substrates.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L-
CC isoaspartyl/D-aspartyl protein methyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW47786.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; M93008; AAA90934.1; -; mRNA.
DR EMBL; M93009; AAA90933.1; -; mRNA.
DR EMBL; D25545; BAA05028.1; -; mRNA.
DR EMBL; D25546; BAA05029.1; -; mRNA.
DR EMBL; D25547; BAA05030.1; -; mRNA.
DR EMBL; D13892; BAA02991.1; -; mRNA.
DR EMBL; AK289724; BAF82413.1; -; mRNA.
DR EMBL; AL355312; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW47786.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC007501; AAH07501.1; -; mRNA.
DR EMBL; BC008748; AAH08748.1; -; mRNA.
DR EMBL; U49740; AAB38386.1; -; Genomic_DNA.
DR EMBL; S73902; AAC60639.2; -; Genomic_DNA.
DR EMBL; S73903; AAC60640.1; -; Genomic_DNA.
DR EMBL; S73905; AAC60641.2; -; Genomic_DNA.
DR CCDS; CCDS59041.1; -. [P22061-2]
DR PIR; A34489; A34489.
DR PIR; JH0624; JH0624.
DR RefSeq; NP_001238978.1; NM_001252049.1.
DR RefSeq; NP_001238982.1; NM_001252053.1.
DR RefSeq; NP_005380.2; NM_005389.2.
DR PDB; 1I1N; X-ray; 1.50 A; A=2-227.
DR PDB; 1KR5; X-ray; 2.10 A; A=2-227.
DR PDBsum; 1I1N; -.
DR PDBsum; 1KR5; -.
DR AlphaFoldDB; P22061; -.
DR SMR; P22061; -.
DR BioGRID; 111141; 199.
DR IntAct; P22061; 92.
DR MINT; P22061; -.
DR STRING; 9606.ENSP00000356354; -.
DR BindingDB; P22061; -.
DR ChEMBL; CHEMBL4240; -.
DR DrugBank; DB01752; S-adenosyl-L-homocysteine.
DR DrugCentral; P22061; -.
DR GlyGen; P22061; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; P22061; -.
DR MetOSite; P22061; -.
DR PhosphoSitePlus; P22061; -.
DR SwissPalm; P22061; -.
DR BioMuta; PCMT1; -.
DR DMDM; 317373537; -.
DR OGP; P22061; -.
DR REPRODUCTION-2DPAGE; IPI00411680; -.
DR UCD-2DPAGE; P22061; -.
DR EPD; P22061; -.
DR jPOST; P22061; -.
DR MassIVE; P22061; -.
DR MaxQB; P22061; -.
DR PaxDb; P22061; -.
DR PeptideAtlas; P22061; -.
DR PRIDE; P22061; -.
DR ProteomicsDB; 53955; -. [P22061-1]
DR ProteomicsDB; 53956; -. [P22061-2]
DR Antibodypedia; 759; 283 antibodies from 31 providers.
DR DNASU; 5110; -.
DR Ensembl; ENST00000367378.6; ENSP00000356348.2; ENSG00000120265.19. [P22061-1]
DR Ensembl; ENST00000367384.7; ENSP00000356354.3; ENSG00000120265.19. [P22061-2]
DR Ensembl; ENST00000464889.7; ENSP00000420813.2; ENSG00000120265.19. [P22061-1]
DR GeneID; 5110; -.
DR KEGG; hsa:5110; -.
DR MANE-Select; ENST00000464889.7; ENSP00000420813.2; NM_001360452.2; NP_001347381.1.
DR UCSC; uc011eeg.3; human. [P22061-1]
DR CTD; 5110; -.
DR DisGeNET; 5110; -.
DR GeneCards; PCMT1; -.
DR HGNC; HGNC:8728; PCMT1.
DR HPA; ENSG00000120265; Low tissue specificity.
DR MIM; 176851; gene.
DR neXtProt; NX_P22061; -.
DR OpenTargets; ENSG00000120265; -.
DR VEuPathDB; HostDB:ENSG00000120265; -.
DR eggNOG; KOG1661; Eukaryota.
DR GeneTree; ENSGT00950000183032; -.
DR InParanoid; P22061; -.
DR OMA; TISAIHM; -.
DR OrthoDB; 1138104at2759; -.
DR PhylomeDB; P22061; -.
DR TreeFam; TF314431; -.
DR BioCyc; MetaCyc:HS04385-MON; -.
DR BRENDA; 2.1.1.77; 2681.
DR PathwayCommons; P22061; -.
DR Reactome; R-HSA-5676934; Protein repair.
DR SABIO-RK; P22061; -.
DR SignaLink; P22061; -.
DR BioGRID-ORCS; 5110; 21 hits in 1081 CRISPR screens.
DR ChiTaRS; PCMT1; human.
DR EvolutionaryTrace; P22061; -.
DR GeneWiki; PCMT1; -.
DR GenomeRNAi; 5110; -.
DR Pharos; P22061; Tbio.
DR PRO; PR:P22061; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P22061; protein.
DR Bgee; ENSG00000120265; Expressed in endothelial cell and 211 other tissues.
DR ExpressionAtlas; P22061; baseline and differential.
DR Genevisible; P22061; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0006479; P:protein methylation; IDA:UniProtKB.
DR GO; GO:0030091; P:protein repair; TAS:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR000682; PCMT.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR11579; PTHR11579; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00080; pimt; 1.
DR PROSITE; PS01279; PCMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2684970"
FT CHAIN 2..227
FT /note="Protein-L-isoaspartate(D-aspartate) O-
FT methyltransferase"
FT /id="PRO_0000111875"
FT ACT_SITE 60
FT /evidence="ECO:0000250|UniProtKB:Q27869"
FT BINDING 57..60
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:11792715,
FT ECO:0000269|PubMed:11847284, ECO:0007744|PDB:1I1N,
FT ECO:0007744|PDB:1KR5"
FT BINDING 65
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:11792715,
FT ECO:0000269|PubMed:11847284, ECO:0007744|PDB:1I1N,
FT ECO:0007744|PDB:1KR5"
FT BINDING 89
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:11792715,
FT ECO:0000269|PubMed:11847284, ECO:0007744|PDB:1I1N,
FT ECO:0007744|PDB:1KR5"
FT BINDING 110..111
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:11792715,
FT ECO:0000269|PubMed:11847284, ECO:0007744|PDB:1I1N,
FT ECO:0007744|PDB:1KR5"
FT BINDING 142..143
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:11792715,
FT ECO:0000269|PubMed:11847284, ECO:0007744|PDB:1I1N,
FT ECO:0007744|PDB:1KR5"
FT BINDING 217
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:11792715,
FT ECO:0000269|PubMed:11847284, ECO:0007744|PDB:1I1N,
FT ECO:0007744|PDB:1KR5"
FT BINDING 222
FT /ligand="S-adenosyl-L-homocysteine"
FT /ligand_id="ChEBI:CHEBI:57856"
FT /evidence="ECO:0000269|PubMed:11792715,
FT ECO:0000269|PubMed:11847284, ECO:0007744|PDB:1I1N,
FT ECO:0007744|PDB:1KR5"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:2684970"
FT VAR_SEQ 226..227
FT /note="WK -> DEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:1339271,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7592526,
FT ECO:0000303|Ref.4"
FT /id="VSP_004716"
FT VARIANT 120
FT /note="V -> I (in dbSNP:rs4816)"
FT /evidence="ECO:0000269|PubMed:10496068,
FT ECO:0000269|PubMed:1339271, ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:1998518, ECO:0000269|Ref.11,
FT ECO:0007744|PubMed:21269460"
FT /id="VAR_006173"
FT CONFLICT 19
FT /note="K -> G (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="I -> L (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 60
FT /note="S -> A (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="C -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="A -> P (in Ref. 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="K -> R (in Ref. 2; AAA90933)"
FT /evidence="ECO:0000305"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 62..71
FT /evidence="ECO:0007829|PDB:1I1N"
FT TURN 72..75
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 91..100
FT /evidence="ECO:0007829|PDB:1I1N"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:1KR5"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 113..126
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 153..158
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 160..164
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 173..184
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1I1N"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:1I1N"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1I1N"
SQ SEQUENCE 227 AA; 24636 MW; 4EB1122379C8040A CRC64;
MAWKSGGASH SELIHNLRKN GIIKTDKVFE VMLATDRSHY AKCNPYMDSP QSIGFQATIS
APHMHAYALE LLFDQLHEGA KALDVGSGSG ILTACFARMV GCTGKVIGID HIKELVDDSV
NNVRKDDPTL LSSGRVQLVV GDGRMGYAEE APYDAIHVGA AAPVVPQALI DQLKPGGRLI
LPVGPAGGNQ MLEQYDKLQD GSIKMKPLMG VIYVPLTDKE KQWSRWK
