MMSA_HUMAN
ID MMSA_HUMAN Reviewed; 535 AA.
AC Q02252; B2R609; B4DFS8; J3KNU8; Q9UKM8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial;
DE Short=MMSDH;
DE Short=Malonate-semialdehyde dehydrogenase [acylating];
DE EC=1.2.1.18;
DE EC=1.2.1.27;
DE AltName: Full=Aldehyde dehydrogenase family 6 member A1;
DE Flags: Precursor;
GN Name=ALDH6A1; Synonyms=MMSDH;
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 NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT MMSDHD ARG-446.
RC TISSUE=Liver, and Lymphocyte;
RX PubMed=10947204; DOI=10.1023/a:1005616315087;
RA Chambliss K.L., Gray R.G.F., Rylance G., Pollitt R.J., Gibson K.M.;
RT "Molecular characterization of methylmalonate semialdehyde dehydrogenase
RT deficiency.";
RL J. Inherit. Metab. Dis. 23:497-504(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RA Ding J.H., Yang B.Z., Wilkinson J., Roe C.R.;
RT "Molecular basis of human MMSDH deficiency: gene organization and mutation
RT analysis.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Ding J.H., Yang B.Z., Wilkinson J.K., Roe C.R.;
RT "The structure and organization of the methylmalonic semialdehyde
RT dehydrogenase (MMSDH) gene.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Muscle;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-535 (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=1527093; DOI=10.1016/s0021-9258(18)41835-2;
RA Kedishvili N.Y., Popov K.M., Rougraff P.M., Zhao Y., Crabb D.W.,
RA Harris R.A.;
RT "CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member
RT of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary
RT relationships, and tissue distribution.";
RL J. Biol. Chem. 267:19724-19729(1992).
RN [9]
RP IDENTIFICATION BY MASS 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).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-262 AND SER-380, AND
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 [11]
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).
CC -!- FUNCTION: Plays a role in valine and pyrimidine metabolism. Binds fatty
CC acyl-CoA.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-methyl-3-oxopropanoate + CoA + H2O + NAD(+) = H(+) +
CC hydrogencarbonate + NADH + propanoyl-CoA; Xref=Rhea:RHEA:20804,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57392, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57700, ChEBI:CHEBI:57945; EC=1.2.1.27;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + NAD(+) = acetyl-CoA + CO2 + NADH;
CC Xref=Rhea:RHEA:22992, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.18;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-oxopropanoate + CoA + NADP(+) = acetyl-CoA + CO2 + NADPH;
CC Xref=Rhea:RHEA:22988, ChEBI:CHEBI:16526, ChEBI:CHEBI:33190,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349; EC=1.2.1.18;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Mitochondrion.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02252-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02252-2; Sequence=VSP_055067;
CC -!- DISEASE: Methylmalonate semialdehyde dehydrogenase deficiency (MMSDHD)
CC [MIM:614105]: A metabolic disorder characterized by elevated beta-
CC alanine, 3-hydroxypropionic acid, and both isomers of 3-amino and 3-
CC hydroxyisobutyric acids in urine organic acids.
CC {ECO:0000269|PubMed:10947204}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AJ249994; CAB76468.1; -; mRNA.
DR EMBL; AF159889; AAF80380.1; -; mRNA.
DR EMBL; AF148505; AAF04489.1; -; mRNA.
DR EMBL; AF148855; AAG29581.1; -; Genomic_DNA.
DR EMBL; AK312389; BAG35306.1; -; mRNA.
DR EMBL; AK294243; BAG57539.1; -; mRNA.
DR EMBL; AC005484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81159.1; -; Genomic_DNA.
DR EMBL; BC004909; AAH04909.1; -; mRNA.
DR EMBL; BC032371; AAH32371.1; -; mRNA.
DR EMBL; M93405; AAA36328.1; -; mRNA.
DR CCDS; CCDS61501.1; -. [Q02252-2]
DR CCDS; CCDS9826.1; -. [Q02252-1]
DR RefSeq; NP_001265522.1; NM_001278593.1. [Q02252-2]
DR RefSeq; NP_005580.1; NM_005589.3. [Q02252-1]
DR AlphaFoldDB; Q02252; -.
DR SMR; Q02252; -.
DR BioGRID; 110472; 36.
DR IntAct; Q02252; 9.
DR MINT; Q02252; -.
DR STRING; 9606.ENSP00000450436; -.
DR DrugBank; DB00157; NADH.
DR GlyGen; Q02252; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q02252; -.
DR MetOSite; Q02252; -.
DR PhosphoSitePlus; Q02252; -.
DR SwissPalm; Q02252; -.
DR BioMuta; ALDH6A1; -.
DR DMDM; 12643424; -.
DR REPRODUCTION-2DPAGE; IPI00024990; -.
DR UCD-2DPAGE; Q02252; -.
DR EPD; Q02252; -.
DR jPOST; Q02252; -.
DR MassIVE; Q02252; -.
DR MaxQB; Q02252; -.
DR PaxDb; Q02252; -.
DR PeptideAtlas; Q02252; -.
DR PRIDE; Q02252; -.
DR ProteomicsDB; 58069; -. [Q02252-1]
DR Antibodypedia; 25547; 513 antibodies from 31 providers.
DR DNASU; 4329; -.
DR Ensembl; ENST00000350259.8; ENSP00000342564.4; ENSG00000119711.13. [Q02252-2]
DR Ensembl; ENST00000553458.6; ENSP00000450436.1; ENSG00000119711.13. [Q02252-1]
DR GeneID; 4329; -.
DR KEGG; hsa:4329; -.
DR MANE-Select; ENST00000553458.6; ENSP00000450436.1; NM_005589.4; NP_005580.1.
DR UCSC; uc001xpo.5; human. [Q02252-1]
DR CTD; 4329; -.
DR DisGeNET; 4329; -.
DR GeneCards; ALDH6A1; -.
DR HGNC; HGNC:7179; ALDH6A1.
DR HPA; ENSG00000119711; Group enriched (kidney, liver).
DR MalaCards; ALDH6A1; -.
DR MIM; 603178; gene.
DR MIM; 614105; phenotype.
DR neXtProt; NX_Q02252; -.
DR OpenTargets; ENSG00000119711; -.
DR Orphanet; 289307; Developmental delay due to methylmalonate semialdehyde dehydrogenase deficiency.
DR PharmGKB; PA24703; -.
DR VEuPathDB; HostDB:ENSG00000119711; -.
DR eggNOG; KOG2449; Eukaryota.
DR GeneTree; ENSGT00940000156110; -.
DR InParanoid; Q02252; -.
DR OMA; HGKRAQC; -.
DR PhylomeDB; Q02252; -.
DR TreeFam; TF105651; -.
DR BRENDA; 1.2.1.18; 2681.
DR BRENDA; 1.2.1.27; 2681.
DR PathwayCommons; Q02252; -.
DR Reactome; R-HSA-70895; Branched-chain amino acid catabolism.
DR SignaLink; Q02252; -.
DR BioGRID-ORCS; 4329; 7 hits in 1080 CRISPR screens.
DR ChiTaRS; ALDH6A1; human.
DR GeneWiki; Aldehyde_dehydrogenase_6_family,_member_A1; -.
DR GenomeRNAi; 4329; -.
DR Pharos; Q02252; Tbio.
DR PRO; PR:Q02252; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q02252; protein.
DR Bgee; ENSG00000119711; Expressed in adult organism and 212 other tissues.
DR ExpressionAtlas; Q02252; baseline and differential.
DR Genevisible; Q02252; HS.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000062; F:fatty-acyl-CoA binding; ISS:UniProtKB.
DR GO; GO:0018478; F:malonate-semialdehyde dehydrogenase (acetylating) activity; ISS:UniProtKB.
DR GO; GO:0102662; F:malonate-semialdehyde dehydrogenase (acetylating, NAD+) activity; IEA:RHEA.
DR GO; GO:0004491; F:methylmalonate-semialdehyde dehydrogenase (acylating) activity; IMP:BHF-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0009083; P:branched-chain amino acid catabolic process; TAS:Reactome.
DR GO; GO:0050873; P:brown fat cell differentiation; IEA:Ensembl.
DR GO; GO:0006210; P:thymine catabolic process; IMP:BHF-UCL.
DR GO; GO:0019859; P:thymine metabolic process; ISS:UniProtKB.
DR GO; GO:0006574; P:valine catabolic process; IMP:BHF-UCL.
DR GO; GO:0006573; P:valine metabolic process; ISS:UniProtKB.
DR CDD; cd07085; ALDH_F6_MMSDH; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR010061; MeMal-semiAld_DH.
DR PANTHER; PTHR43866; PTHR43866; 1.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01722; MMSDH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant; Mitochondrion; NAD;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Transit peptide.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 34..535
FT /note="Methylmalonate-semialdehyde dehydrogenase
FT [acylating], mitochondrial"
FT /id="PRO_0000007189"
FT ACT_SITE 317
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 209..213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 261..266
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 417
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT MOD_RES 47
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 47
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 52
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 52
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 55
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 55
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 76
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 76
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 87
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 117
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 117
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 129
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 129
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 298
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 330
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 331
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 364
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 364
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 376
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 376
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 380
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 391
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 500
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT MOD_RES 517
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQ20"
FT VAR_SEQ 104..116
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055067"
FT VARIANT 446
FT /note="G -> R (in MMSDHD; dbSNP:rs72552258)"
FT /evidence="ECO:0000269|PubMed:10947204"
FT /id="VAR_010244"
FT CONFLICT 101
FT /note="R -> C (in Ref. 4; BAG57539)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="E -> K (in Ref. 4; BAG57539)"
FT /evidence="ECO:0000305"
FT CONFLICT 460
FT /note="Y -> H (in Ref. 4; BAG57539)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 535 AA; 57840 MW; 0786AF63897E7962 CRC64;
MAALLAAAAV RARILQVSSK VKSSPTWYSA SSFSSSVPTV KLFIGGKFVE SKSDKWIDIH
NPATNEVIGR VPQATKAEMD AAIASCKRAF PAWADTSVLS RQQVLLRYQQ LIKENLKEIA
KLITLEQGKT LADAEGDVFR GLQVVEHACS VTSLMMGETM PSITKDMDLY SYRLPLGVCA
GIAPFNFPAM IPLWMFPMAM VCGNTFLMKP SERVPGATML LAKLLQDSGA PDGTLNIIHG
QHEAVNFICD HPDIKAISFV GSNKAGEYIF ERGSRHGKRV QANMGAKNHG VVMPDANKEN
TLNQLVGAAF GAAGQRCMAL STAVLVGEAK KWLPELVEHA KNLRVNAGDQ PGADLGPLIT
PQAKERVCNL IDSGTKEGAS ILLDGRKIKV KGYENGNFVG PTIISNVKPN MTCYKEEIFG
PVLVVLETET LDEAIQIVNN NPYGNGTAIF TTNGATARKY AHLVDVGQVG VNVPIPVPLP
MFSFTGSRSS FRGDTNFYGK QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR
