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Q02252

- MMSA_HUMAN

UniProt

Q02252 - MMSA_HUMAN

Protein

Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial

Gene

ALDH6A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (24 Jan 2001)
      Previous versions | rss
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    Functioni

    Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.

    Catalytic activityi

    2-methyl-3-oxopropanoate + CoA + H2O + NAD+ = propanoyl-CoA + HCO3- + NADH.
    3-oxopropanoate + CoA + NAD(P)+ = acetyl-CoA + CO2 + NAD(P)H.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei317 – 3171NucleophilePROSITE-ProRule annotation
    Binding sitei417 – 4171NADSequence Analysis

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi209 – 2135NADSequence Analysis
    Nucleotide bindingi261 – 2666NADSequence Analysis

    GO - Molecular functioni

    1. fatty-acyl-CoA binding Source: UniProtKB
    2. malonate-semialdehyde dehydrogenase (acetylating) activity Source: UniProtKB
    3. methylmalonate-semialdehyde dehydrogenase (acylating) activity Source: UniProtKB
    4. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. branched-chain amino acid catabolic process Source: Reactome
    2. brown fat cell differentiation Source: Ensembl
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. small molecule metabolic process Source: Reactome
    5. thymine catabolic process Source: BHF-UCL
    6. thymine metabolic process Source: UniProtKB
    7. valine catabolic process Source: BHF-UCL
    8. valine metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    ReactomeiREACT_197. Branched-chain amino acid catabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial (EC:1.2.1.18, EC:1.2.1.27)
    Short name:
    MMSDH
    Short name:
    Malonate-semialdehyde dehydrogenase [acylating]
    Alternative name(s):
    Aldehyde dehydrogenase family 6 member A1
    Gene namesi
    Name:ALDH6A1
    Synonyms:MMSDH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:7179. ALDH6A1.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrial matrix Source: Reactome
    3. mitochondrion Source: UniProtKB
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Methylmalonate semialdehyde dehydrogenase deficiency (MMSDHD) [MIM:614105]: A metabolic disorder characterized by elevated beta-alanine, 3-hydroxypropionic acid, and both isomers of 3-amino and 3-hydroxyisobutyric acids in urine organic acids.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti446 – 4461G → R in MMSDHD. 1 Publication
    VAR_010244

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi614105. phenotype.
    Orphaneti289307. Developmental delay due to methylmalonate semialdehyde dehydrogenase deficiency.
    PharmGKBiPA24703.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 3333MitochondrionBy similarityAdd
    BLAST
    Chaini34 – 535502Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrialPRO_0000007189Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei47 – 471N6-acetyllysine; alternateBy similarity
    Modified residuei47 – 471N6-succinyllysine; alternateBy similarity
    Modified residuei52 – 521N6-acetyllysine; alternateBy similarity
    Modified residuei52 – 521N6-succinyllysine; alternateBy similarity
    Modified residuei55 – 551N6-acetyllysine; alternateBy similarity
    Modified residuei55 – 551N6-succinyllysine; alternateBy similarity
    Modified residuei76 – 761N6-acetyllysine; alternateBy similarity
    Modified residuei76 – 761N6-succinyllysine; alternateBy similarity
    Modified residuei87 – 871N6-acetyllysineBy similarity
    Modified residuei117 – 1171N6-acetyllysine; alternateBy similarity
    Modified residuei117 – 1171N6-succinyllysine; alternateBy similarity
    Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
    Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
    Modified residuei298 – 2981N6-acetyllysineBy similarity
    Modified residuei330 – 3301N6-acetyllysineBy similarity
    Modified residuei331 – 3311N6-acetyllysineBy similarity
    Modified residuei364 – 3641N6-acetyllysine; alternateBy similarity
    Modified residuei364 – 3641N6-succinyllysine; alternateBy similarity
    Modified residuei376 – 3761N6-acetyllysine; alternateBy similarity
    Modified residuei376 – 3761N6-succinyllysine; alternateBy similarity
    Modified residuei391 – 3911N6-succinyllysineBy similarity
    Modified residuei500 – 5001N6-acetyllysineBy similarity
    Modified residuei517 – 5171N6-succinyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ02252.
    PaxDbiQ02252.
    PeptideAtlasiQ02252.
    PRIDEiQ02252.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00024990.
    UCD-2DPAGEQ02252.

    PTM databases

    PhosphoSiteiQ02252.

    Expressioni

    Gene expression databases

    ArrayExpressiQ02252.
    BgeeiQ02252.
    CleanExiHS_ALDH6A1.
    GenevestigatoriQ02252.

    Organism-specific databases

    HPAiHPA029072.
    HPA029073.
    HPA029074.
    HPA029075.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi110472. 2 interactions.
    IntActiQ02252. 2 interactions.
    STRINGi9606.ENSP00000342564.

    Structurei

    3D structure databases

    ProteinModelPortaliQ02252.
    SMRiQ02252. Positions 38-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271507.
    HOVERGENiHBG105023.
    InParanoidiQ02252.
    KOiK00140.
    OMAiQVVEHCC.
    OrthoDBiEOG7J70F8.
    PhylomeDBiQ02252.
    TreeFamiTF105651.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR010061. MeMal-semiAld_DH.
    [Graphical view]
    PANTHERiPTHR11699:SF27. PTHR11699:SF27. 1 hit.
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01722. MMSDH. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q02252-1) [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

    MAALLAAAAV RARILQVSSK VKSSPTWYSA SSFSSSVPTV KLFIGGKFVE    50
    SKSDKWIDIH NPATNEVIGR VPQATKAEMD AAIASCKRAF PAWADTSVLS 100
    RQQVLLRYQQ LIKENLKEIA KLITLEQGKT LADAEGDVFR GLQVVEHACS 150
    VTSLMMGETM PSITKDMDLY SYRLPLGVCA GIAPFNFPAM IPLWMFPMAM 200
    VCGNTFLMKP SERVPGATML LAKLLQDSGA PDGTLNIIHG QHEAVNFICD 250
    HPDIKAISFV GSNKAGEYIF ERGSRHGKRV QANMGAKNHG VVMPDANKEN 300
    TLNQLVGAAF GAAGQRCMAL STAVLVGEAK KWLPELVEHA KNLRVNAGDQ 350
    PGADLGPLIT PQAKERVCNL IDSGTKEGAS ILLDGRKIKV KGYENGNFVG 400
    PTIISNVKPN MTCYKEEIFG PVLVVLETET LDEAIQIVNN NPYGNGTAIF 450
    TTNGATARKY AHLVDVGQVG VNVPIPVPLP MFSFTGSRSS FRGDTNFYGK 500
    QGIQFYTQLK TITSQWKEED ATLSSPAVVM PTMGR 535
    Length:535
    Mass (Da):57,840
    Last modified:January 24, 2001 - v2
    Checksum:i0786AF63897E7962
    GO
    Isoform 2 (identifier: Q02252-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         104-116: Missing.

    Show »
    Length:522
    Mass (Da):56,228
    Checksum:iFBAB6B1DA77B3ADB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti101 – 1011R → C in BAG57539. (PubMed:14702039)Curated
    Sequence conflicti212 – 2121E → K in BAG57539. (PubMed:14702039)Curated
    Sequence conflicti460 – 4601Y → H in BAG57539. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti446 – 4461G → R in MMSDHD. 1 Publication
    VAR_010244

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei104 – 11613Missing in isoform 2. 1 PublicationVSP_055067Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ249994 mRNA. Translation: CAB76468.1.
    AF159889 mRNA. Translation: AAF80380.1.
    AF148505 mRNA. Translation: AAF04489.1.
    AF148855 Genomic DNA. Translation: AAG29581.1.
    AK312389 mRNA. Translation: BAG35306.1.
    AK294243 mRNA. Translation: BAG57539.1.
    AC005484 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81159.1.
    BC004909 mRNA. Translation: AAH04909.1.
    BC032371 mRNA. Translation: AAH32371.1.
    M93405 mRNA. Translation: AAA36328.1.
    CCDSiCCDS61501.1. [Q02252-2]
    CCDS9826.1. [Q02252-1]
    RefSeqiNP_001265522.1. NM_001278593.1.
    NP_005580.1. NM_005589.3.
    UniGeneiHs.293970.
    Hs.744472.

    Genome annotation databases

    EnsembliENST00000350259; ENSP00000342564; ENSG00000119711. [Q02252-2]
    ENST00000553458; ENSP00000450436; ENSG00000119711. [Q02252-1]
    GeneIDi4329.
    KEGGihsa:4329.
    UCSCiuc001xpo.3. human. [Q02252-1]

    Polymorphism databases

    DMDMi12643424.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ249994 mRNA. Translation: CAB76468.1 .
    AF159889 mRNA. Translation: AAF80380.1 .
    AF148505 mRNA. Translation: AAF04489.1 .
    AF148855 Genomic DNA. Translation: AAG29581.1 .
    AK312389 mRNA. Translation: BAG35306.1 .
    AK294243 mRNA. Translation: BAG57539.1 .
    AC005484 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW81159.1 .
    BC004909 mRNA. Translation: AAH04909.1 .
    BC032371 mRNA. Translation: AAH32371.1 .
    M93405 mRNA. Translation: AAA36328.1 .
    CCDSi CCDS61501.1. [Q02252-2 ]
    CCDS9826.1. [Q02252-1 ]
    RefSeqi NP_001265522.1. NM_001278593.1.
    NP_005580.1. NM_005589.3.
    UniGenei Hs.293970.
    Hs.744472.

    3D structure databases

    ProteinModelPortali Q02252.
    SMRi Q02252. Positions 38-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110472. 2 interactions.
    IntActi Q02252. 2 interactions.
    STRINGi 9606.ENSP00000342564.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei Q02252.

    Polymorphism databases

    DMDMi 12643424.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00024990.
    UCD-2DPAGE Q02252.

    Proteomic databases

    MaxQBi Q02252.
    PaxDbi Q02252.
    PeptideAtlasi Q02252.
    PRIDEi Q02252.

    Protocols and materials databases

    DNASUi 4329.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000350259 ; ENSP00000342564 ; ENSG00000119711 . [Q02252-2 ]
    ENST00000553458 ; ENSP00000450436 ; ENSG00000119711 . [Q02252-1 ]
    GeneIDi 4329.
    KEGGi hsa:4329.
    UCSCi uc001xpo.3. human. [Q02252-1 ]

    Organism-specific databases

    CTDi 4329.
    GeneCardsi GC14M074527.
    HGNCi HGNC:7179. ALDH6A1.
    HPAi HPA029072.
    HPA029073.
    HPA029074.
    HPA029075.
    MIMi 603178. gene.
    614105. phenotype.
    neXtProti NX_Q02252.
    Orphaneti 289307. Developmental delay due to methylmalonate semialdehyde dehydrogenase deficiency.
    PharmGKBi PA24703.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1012.
    HOGENOMi HOG000271507.
    HOVERGENi HBG105023.
    InParanoidi Q02252.
    KOi K00140.
    OMAi QVVEHCC.
    OrthoDBi EOG7J70F8.
    PhylomeDBi Q02252.
    TreeFami TF105651.

    Enzyme and pathway databases

    Reactomei REACT_197. Branched-chain amino acid catabolism.

    Miscellaneous databases

    GeneWikii Aldehyde_dehydrogenase_6_family,_member_A1.
    GenomeRNAii 4329.
    NextBioi 17035.
    PROi Q02252.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q02252.
    Bgeei Q02252.
    CleanExi HS_ALDH6A1.
    Genevestigatori Q02252.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR010061. MeMal-semiAld_DH.
    [Graphical view ]
    PANTHERi PTHR11699:SF27. PTHR11699:SF27. 1 hit.
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR01722. MMSDH. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of methylmalonate semialdehyde dehydrogenase deficiency."
      Chambliss K.L., Gray R.G.F., Rylance G., Pollitt R.J., Gibson K.M.
      J. Inherit. Metab. Dis. 23:497-504(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT MMSDHD ARG-446.
      Tissue: Liver and Lymphocyte.
    2. "Molecular basis of human MMSDH deficiency: gene organization and mutation analysis."
      Ding J.H., Yang B.Z., Wilkinson J., Roe C.R.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Skin.
    3. "The structure and organization of the methylmalonic semialdehyde dehydrogenase (MMSDH) gene."
      Ding J.H., Yang B.Z., Wilkinson J.K., Roe C.R.
      Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
    4. "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.
      , 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] (ISOFORMS 1 AND 2).
      Tissue: Amygdala.
    5. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Brain and Muscle.
    8. "CoA-dependent methylmalonate-semialdehyde dehydrogenase, a unique member of the aldehyde dehydrogenase superfamily. cDNA cloning, evolutionary relationships, and tissue distribution."
      Kedishvili N.Y., Popov K.M., Rougraff P.M., Zhao Y., Crabb D.W., Harris R.A.
      J. Biol. Chem. 267:19724-19729(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-535 (ISOFORM 1).
      Tissue: Liver.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiMMSA_HUMAN
    AccessioniPrimary (citable) accession number: Q02252
    Secondary accession number(s): B2R609
    , B4DFS8, J3KNU8, Q9UKM8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 24, 2001
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3