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Protein

4-trimethylaminobutyraldehyde dehydrogenase

Gene

ALDH9A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

    Pathway:icarnitine biosynthesis

    This protein is involved in the pathway carnitine biosynthesis, which is part of Amine and polyamine biosynthesis.
    View all proteins of this organism that are known to be involved in the pathway carnitine biosynthesis and in Amine and polyamine biosynthesis.

    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

    GO - Biological processi

    • carnitine biosynthetic process Source: Reactome
    • cellular aldehyde metabolic process Source: UniProtKB
    • cellular nitrogen compound metabolic process Source: Reactome
    • hormone metabolic process Source: UniProtKB
    • neurotransmitter biosynthetic process Source: UniProtKB
    • oxidation-reduction process Source: UniProtKB
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06992-MONOMER.
    BRENDAi1.2.1.47. 2681.
    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 Componentsi: Chromosome 1, Unplaced

    Organism-specific databases

    HGNCiHGNC:412. ALDH9A1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • cytosol Source: Reactome
    • extracellular exosome Source: UniProtKB
    • mitochondrion Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24706.

    Polymorphism and mutation databases

    BioMutaiALDH9A1.
    DMDMi62511242.

    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

    BgeeiP49189.
    CleanExiHS_ALDH9A1.
    ExpressionAtlasiP49189. baseline.
    GenevisibleiP49189. HS.

    Organism-specific databases

    HPAiHPA006077.
    HPA010873.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi106725. 14 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. AlignAdd to basket

    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

            10         20         30         40         50
    MSTGTFVVSQ PLNYRGGARV EPADASGTEK AFEPATGRVI ATFTCSGEKE
    60 70 80 90 100
    VNLAVQNAKA AFKIWSQKSG MERCRILLEA ARIIREREDE IATMECINNG
    110 120 130 140 150
    KSIFEARLDI DISWQCLEYY AGLAASMAGE HIQLPGGSFG YTRREPLGVC
    160 170 180 190 200
    VGIGAWNYPF QIASWKSAPA LACGNAMVFK PSPFTPVSAL LLAEIYSEAG
    210 220 230 240 250
    VPPGLFNVVQ GGAATGQFLC QHPDVAKVSF TGSVPTGMKI MEMSAKGIKP
    260 270 280 290 300
    VTLELGGKSP LIIFSDCDMN NAVKGALMAN FLTQGQVCCN GTRVFVQKEI
    310 320 330 340 350
    LDKFTEEVVK QTQRIKIGDP LLEDTRMGPL INRPHLERVL GFVKVAKEQG
    360 370 380 390 400
    AKVLCGGDIY VPEDPKLKDG YYMRPCVLTN CRDDMTCVKE EIFGPVMSIL
    410 420 430 440 450
    SFDTEAEVLE RANDTTFGLA AGVFTRDIQR AHRVVAELQA GTCFINNYNV
    460 470 480 490
    SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESAF
    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.Curated

    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:
    EMBLi
    GenBanki
    DDBJi
    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.
    XP_011507596.1. XM_011509294.1. [P49189-2]
    UniGeneiHs.2533.

    Genome annotation databases

    EnsembliENST00000354775; ENSP00000346827; ENSG00000143149.
    ENST00000538148; ENSP00000440026; ENSG00000143149.
    GeneIDi223.
    KEGGihsa:223.
    UCSCiuc010pky.1. human. [P49189-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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.
    XP_011507596.1. XM_011509294.1. [P49189-2]
    UniGeneiHs.2533.

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi106725. 14 interactions.
    IntActiP49189. 5 interactions.
    MINTiMINT-5006004.
    STRINGi9606.ENSP00000346827.

    PTM databases

    PhosphoSiteiP49189.

    Polymorphism and mutation databases

    BioMutaiALDH9A1.
    DMDMi62511242.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00479877.

    Proteomic databases

    MaxQBiP49189.
    PaxDbiP49189.
    PRIDEiP49189.

    Protocols and materials databases

    DNASUi223.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000354775; ENSP00000346827; ENSG00000143149.
    ENST00000538148; ENSP00000440026; ENSG00000143149.
    GeneIDi223.
    KEGGihsa:223.
    UCSCiuc010pky.1. human. [P49189-1]

    Organism-specific databases

    CTDi223.
    GeneCardsiGC01M165632.
    H-InvDBHIX0199965.
    HGNCiHGNC:412. ALDH9A1.
    HPAiHPA006077.
    HPA010873.
    MIMi602733. gene.
    neXtProtiNX_P49189.
    PharmGKBiPA24706.
    GenAtlasiSearch...

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayiUPA00118.
    BioCyciMetaCyc:HS06992-MONOMER.
    BRENDAi1.2.1.47. 2681.
    ReactomeiREACT_2125. Carnitine synthesis.
    SABIO-RKP49189.

    Miscellaneous databases

    ChiTaRSiALDH9A1. human.
    GeneWikiiAldehyde_dehydrogenase_9_family,_member_A1.
    GenomeRNAii223.
    NextBioi35476095.
    PROiP49189.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP49189.
    CleanExiHS_ALDH9A1.
    ExpressionAtlasiP49189. baseline.
    GenevisibleiP49189. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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], CLEAVAGE OF INITIATOR METHIONINE [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], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    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: July 22, 2015
    This is version 144 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.