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P49189

- AL9A1_HUMAN

UniProt

P49189 - AL9A1_HUMAN

Protein

4-trimethylaminobutyraldehyde dehydrogenase

Gene

ALDH9A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (01 Feb 2005)
      Previous versions | rss
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    Functioni

    Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction.1 Publication

    Catalytic activityi

    4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH.
    An aldehyde + NAD+ + H2O = a carboxylate + NADH.
    4-aminobutanal + NAD+ + H2O = 4-aminobutanoate + NADH.

    Kineticsi

    1. KM=11 µM for 4-aminobutyraldehyde

    pH dependencei

    Optimum pH is about 9.4 with propionaldehyde as substrate, and 7.5 with 4-aminobutyraldehyde as substrate.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei157 – 1571Transition state stabilizerBy similarity
    Active sitei254 – 2541Proton acceptorPROSITE-ProRule annotation
    Active sitei288 – 2881NucleophilePROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi232 – 2376NADBy similarity

    GO - Molecular functioni

    1. 1-pyrroline dehydrogenase activity Source: UniProtKB-EC
    2. 3-chloroallyl aldehyde dehydrogenase activity Source: Reactome
    3. 4-trimethylammoniobutyraldehyde dehydrogenase activity Source: UniProtKB-EC
    4. aldehyde dehydrogenase (NAD) activity Source: UniProtKB
    5. amine binding Source: Ensembl
    6. aminobutyraldehyde dehydrogenase activity Source: UniProtKB
    7. NAD binding Source: Ensembl

    GO - Biological processi

    1. carnitine biosynthetic process Source: Reactome
    2. cellular aldehyde metabolic process Source: UniProtKB
    3. cellular nitrogen compound metabolic process Source: Reactome
    4. hormone metabolic process Source: UniProtKB
    5. kidney development Source: Ensembl
    6. liver development Source: Ensembl
    7. neurotransmitter biosynthetic process Source: UniProtKB
    8. oxidation-reduction process Source: UniProtKB
    9. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06992-MONOMER.
    ReactomeiREACT_2125. Carnitine synthesis.
    SABIO-RKP49189.
    UniPathwayiUPA00118.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-trimethylaminobutyraldehyde dehydrogenase (EC:1.2.1.47)
    Short name:
    TMABADH
    Alternative name(s):
    Aldehyde dehydrogenase E3 isozyme
    Aldehyde dehydrogenase family 9 member A1 (EC:1.2.1.3)
    Gamma-aminobutyraldehyde dehydrogenase (EC:1.2.1.19)
    R-aminobutyraldehyde dehydrogenase
    Gene namesi
    Name:ALDH9A1
    Synonyms:ALDH4, ALDH7, ALDH9
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:412. ALDH9A1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt
    4. mitochondrion Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24706.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 4944934-trimethylaminobutyraldehyde dehydrogenasePRO_0000056485Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine4 Publications
    Modified residuei30 – 301N6-acetyllysine; alternateBy similarity
    Modified residuei30 – 301N6-succinyllysine; alternateBy similarity
    Modified residuei59 – 591N6-succinyllysineBy similarity
    Modified residuei298 – 2981N6-acetyllysine1 Publication
    Modified residuei303 – 3031N6-acetyllysine; alternateBy similarity
    Modified residuei303 – 3031N6-succinyllysine; alternateBy similarity
    Modified residuei344 – 3441N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP49189.
    PaxDbiP49189.
    PRIDEiP49189.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00479877.

    PTM databases

    PhosphoSiteiP49189.

    Expressioni

    Tissue specificityi

    High expression in adult liver, skeletal muscle, and kidney. Low levels in heart, pancreas, lung and brain. Expressed in all regions of the brain. Expression levels are variable in the different brain areas, with the highest levels in the spinal cord and the lowest in the occipital pole.1 Publication

    Developmental stagei

    Strongly expressed in human embryonic brain (gestational age 12 weeks).

    Gene expression databases

    ArrayExpressiP49189.
    BgeeiP49189.
    CleanExiHS_ALDH9A1.
    GenevestigatoriP49189.

    Organism-specific databases

    HPAiHPA006077.
    HPA010873.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi106725. 15 interactions.
    IntActiP49189. 5 interactions.
    MINTiMINT-5006004.
    STRINGi9606.ENSP00000346827.

    Structurei

    3D structure databases

    ProteinModelPortaliP49189.
    SMRiP49189. Positions 2-494.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1012.
    HOVERGENiHBG000097.
    InParanoidiP49189.
    KOiK00149.
    OrthoDBiEOG7327P4.
    PhylomeDBiP49189.
    TreeFamiTF314257.

    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.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 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: P49189-1) [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

    MSTGTFVVSQ PLNYRGGARV EPADASGTEK AFEPATGRVI ATFTCSGEKE    50
    VNLAVQNAKA AFKIWSQKSG MERCRILLEA ARIIREREDE IATMECINNG 100
    KSIFEARLDI DISWQCLEYY AGLAASMAGE HIQLPGGSFG YTRREPLGVC 150
    VGIGAWNYPF QIASWKSAPA LACGNAMVFK PSPFTPVSAL LLAEIYSEAG 200
    VPPGLFNVVQ GGAATGQFLC QHPDVAKVSF TGSVPTGMKI MEMSAKGIKP 250
    VTLELGGKSP LIIFSDCDMN NAVKGALMAN FLTQGQVCCN GTRVFVQKEI 300
    LDKFTEEVVK QTQRIKIGDP LLEDTRMGPL INRPHLERVL GFVKVAKEQG 350
    AKVLCGGDIY VPEDPKLKDG YYMRPCVLTN CRDDMTCVKE EIFGPVMSIL 400
    SFDTEAEVLE RANDTTFGLA AGVFTRDIQR AHRVVAELQA GTCFINNYNV 450
    SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESAF 494
    Length:494
    Mass (Da):53,802
    Last modified:February 1, 2005 - v3
    Checksum:i1E1CDF910D763BA1
    GO
    Isoform 2 (identifier: P49189-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-70: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:424
    Mass (Da):46,455
    Checksum:i211F5F4B06E9B453
    GO

    Sequence cautioni

    The sequence CAH74061.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti19 – 257RVEPADA → AGAGGR in AAB18827. (PubMed:8786138)Curated
    Sequence conflicti150 – 1501C → Q AA sequence (PubMed:8269919)Curated
    Sequence conflicti159 – 1591P → W AA sequence (PubMed:8269919)Curated
    Sequence conflicti172 – 1721A → R AA sequence (PubMed:8269919)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti116 – 1161C → S in allele ALDH9A1*2. 2 Publications
    VAR_011304

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7070Missing in isoform 2. 1 PublicationVSP_056305Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34252 mRNA. Translation: AAB18827.1.
    AF172093 mRNA. Translation: AAF43600.1.
    AK302183 mRNA. Translation: BAG63549.1.
    AK302191 mRNA. Translation: BAG63554.1.
    AK312751 mRNA. Translation: BAG35618.1.
    AL451074 Genomic DNA. Translation: CAH74061.1. Different initiation.
    U50203 mRNA. Translation: AAB06721.1.
    X75425 mRNA. Translation: CAA53176.1.
    PIRiG02054. S39532.
    RefSeqiNP_000687.3. NM_000696.3.
    UniGeneiHs.2533.

    Genome annotation databases

    EnsembliENST00000354775; ENSP00000346827; ENSG00000143149.
    ENST00000538148; ENSP00000440026; ENSG00000143149.
    GeneIDi223.
    KEGGihsa:223.
    UCSCiuc010pky.1. human.

    Polymorphism databases

    DMDMi62511242.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U34252 mRNA. Translation: AAB18827.1 .
    AF172093 mRNA. Translation: AAF43600.1 .
    AK302183 mRNA. Translation: BAG63549.1 .
    AK302191 mRNA. Translation: BAG63554.1 .
    AK312751 mRNA. Translation: BAG35618.1 .
    AL451074 Genomic DNA. Translation: CAH74061.1 . Different initiation.
    U50203 mRNA. Translation: AAB06721.1 .
    X75425 mRNA. Translation: CAA53176.1 .
    PIRi G02054. S39532.
    RefSeqi NP_000687.3. NM_000696.3.
    UniGenei Hs.2533.

    3D structure databases

    ProteinModelPortali P49189.
    SMRi P49189. Positions 2-494.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106725. 15 interactions.
    IntActi P49189. 5 interactions.
    MINTi MINT-5006004.
    STRINGi 9606.ENSP00000346827.

    Chemistry

    DrugBanki DB00157. NADH.

    PTM databases

    PhosphoSitei P49189.

    Polymorphism databases

    DMDMi 62511242.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00479877.

    Proteomic databases

    MaxQBi P49189.
    PaxDbi P49189.
    PRIDEi P49189.

    Protocols and materials databases

    DNASUi 223.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000354775 ; ENSP00000346827 ; ENSG00000143149 .
    ENST00000538148 ; ENSP00000440026 ; ENSG00000143149 .
    GeneIDi 223.
    KEGGi hsa:223.
    UCSCi uc010pky.1. human.

    Organism-specific databases

    CTDi 223.
    GeneCardsi GC01M165632.
    H-InvDB HIX0199965.
    HGNCi HGNC:412. ALDH9A1.
    HPAi HPA006077.
    HPA010873.
    MIMi 602733. gene.
    neXtProti NX_P49189.
    PharmGKBi PA24706.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1012.
    HOVERGENi HBG000097.
    InParanoidi P49189.
    KOi K00149.
    OrthoDBi EOG7327P4.
    PhylomeDBi P49189.
    TreeFami TF314257.

    Enzyme and pathway databases

    UniPathwayi UPA00118 .
    BioCyci MetaCyc:HS06992-MONOMER.
    Reactomei REACT_2125. Carnitine synthesis.
    SABIO-RK P49189.

    Miscellaneous databases

    ChiTaRSi ALDH9A1. human.
    GeneWikii Aldehyde_dehydrogenase_9_family,_member_A1.
    GenomeRNAii 223.
    NextBioi 906.
    PROi P49189.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49189.
    Bgeei P49189.
    CleanExi HS_ALDH9A1.
    Genevestigatori P49189.

    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.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression."
      Lin S.W., Chen J.C., Hsu L.C., Hsieh C.-L., Yoshida A.
      Genomics 34:376-380(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-116.
      Tissue: Liver.
    2. "Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis."
      Vaz F.M., Fouchier S.W., Ofman R., Sommer M., Wanders R.J.A.
      J. Biol. Chem. 275:7390-7394(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Tissue: Liver.
    3. "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: Spleen and Testis.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15; 247-258; 299-310; 315-326 AND 472-481, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    6. "Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution."
      Kikonyogo A., Pietruszko R.
      Biochem. J. 316:317-324(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 259-274; 353-366; 412-426 AND 434-453, NUCLEOTIDE SEQUENCE [MRNA] OF 29-494, CHARACTERIZATION, TISSUE SPECIFICITY, VARIANT SER-116.
      Tissue: Brain.
    7. "Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde."
      Kurys G., Shah P.C., Kikonyogo A., Reed D., Ambroziak W., Pietruszko R.
      Eur. J. Biochem. 218:311-320(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-494 (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    8. "Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde."
      Kurys G., Ambroziak W., Pietruszko R.
      J. Biol. Chem. 264:4715-4721(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
      Tissue: Liver.
    9. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-298, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAL9A1_HUMAN
    AccessioniPrimary (citable) accession number: P49189
    Secondary accession number(s): B2R6X1
    , B4DXY7, Q5VV90, Q6LCL1, Q9NZT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 2005
    Last modified: October 1, 2014
    This is version 135 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3