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P30838

- AL3A1_HUMAN

UniProt

P30838 - AL3A1_HUMAN

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Protein

Aldehyde dehydrogenase, dimeric NADP-preferring

Gene

ALDH3A1

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

Functioni

ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation. This protein preferentially oxidizes aromatic aldehyde substrates. It may play a role in the oxidation of toxic aldehydes.

Catalytic activityi

An aldehyde + NAD(P)+ + H2O = a carboxylate + NAD(P)H.

Kineticsi

Has a high Km for acetaldehyde.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei210 – 21011 Publication
    Active sitei244 – 24411 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi188 – 1936NAD or NADPBy similarity

    GO - Molecular functioni

    1. 3-chloroallyl aldehyde dehydrogenase activity Source: Ensembl
    2. alcohol dehydrogenase (NADP+) activity Source: UniProtKB
    3. aldehyde dehydrogenase (NAD) activity Source: UniProtKB
    4. aldehyde dehydrogenase [NAD(P)+] activity Source: UniProtKB-EC

    GO - Biological processi

    1. aging Source: Ensembl
    2. cellular aldehyde metabolic process Source: UniProtKB
    3. oxidation-reduction process Source: UniProtKB
    4. positive regulation of cell proliferation Source: Ensembl
    5. response to cAMP Source: Ensembl
    6. response to drug Source: Ensembl
    7. response to glucocorticoid Source: Ensembl
    8. response to hypoxia Source: Ensembl
    9. response to nutrient Source: Ensembl
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD, NADP

    Enzyme and pathway databases

    SABIO-RKP30838.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde dehydrogenase, dimeric NADP-preferring (EC:1.2.1.5)
    Alternative name(s):
    ALDHIII
    Aldehyde dehydrogenase 3
    Aldehyde dehydrogenase family 3 member A1
    Gene namesi
    Name:ALDH3A1
    Synonyms:ALDH3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:405. ALDH3A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: UniProtKB
    3. endoplasmic reticulum Source: LIFEdb
    4. extracellular space Source: UniProt
    5. plasma membrane Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi244 – 2441C → S: Abolishes activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA24697.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 453452Aldehyde dehydrogenase, dimeric NADP-preferringPRO_0000056470Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei178 – 1781N6-acetyllysine1 Publication
    Modified residuei194 – 1941N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP30838.
    PaxDbiP30838.
    PRIDEiP30838.

    PTM databases

    PhosphoSiteiP30838.

    Expressioni

    Tissue specificityi

    High levels in stomach, esophagus and lung; low level in the liver and kidney.

    Gene expression databases

    BgeeiP30838.
    CleanExiHS_ALDH3A1.
    ExpressionAtlasiP30838. baseline and differential.
    GenevestigatoriP30838.

    Organism-specific databases

    HPAiCAB045957.
    HPA051150.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi106720. 7 interactions.
    IntActiP30838. 2 interactions.
    STRINGi9606.ENSP00000225740.

    Structurei

    Secondary structure

    1
    453
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi3 – 1614Combined sources
    Turni17 – 204Combined sources
    Helixi23 – 3917Combined sources
    Helixi41 – 5212Combined sources
    Helixi56 – 616Combined sources
    Helixi64 – 8219Combined sources
    Helixi91 – 933Combined sources
    Beta strandi96 – 1049Combined sources
    Beta strandi106 – 1116Combined sources
    Beta strandi114 – 1163Combined sources
    Helixi119 – 13012Combined sources
    Beta strandi134 – 1385Combined sources
    Beta strandi141 – 1433Combined sources
    Helixi144 – 15714Combined sources
    Turni160 – 1623Combined sources
    Helixi170 – 1767Combined sources
    Beta strandi182 – 1887Combined sources
    Helixi190 – 20112Combined sources
    Turni202 – 2043Combined sources
    Beta strandi207 – 2104Combined sources
    Beta strandi216 – 2194Combined sources
    Helixi225 – 23713Combined sources
    Helixi238 – 2414Combined sources
    Beta strandi249 – 2524Combined sources
    Helixi254 – 2563Combined sources
    Helixi257 – 27216Combined sources
    Helixi276 – 2783Combined sources
    Helixi288 – 29811Combined sources
    Beta strandi301 – 3055Combined sources
    Turni311 – 3144Combined sources
    Beta strandi319 – 3235Combined sources
    Helixi329 – 3313Combined sources
    Beta strandi337 – 3448Combined sources
    Helixi348 – 35710Combined sources
    Beta strandi362 – 3676Combined sources
    Helixi371 – 38010Combined sources
    Beta strandi384 – 3896Combined sources
    Helixi393 – 3953Combined sources
    Helixi406 – 4083Combined sources
    Helixi416 – 4216Combined sources
    Beta strandi423 – 4308Combined sources
    Helixi437 – 4426Combined sources
    Beta strandi443 – 4453Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3SZAX-ray1.48A/B1-453[»]
    3SZBX-ray1.51A/B1-453[»]
    4H80X-ray2.50A/B/C/D/E/F/G/H1-453[»]
    4L1OX-ray2.30A/B1-453[»]
    4L2OX-ray1.94A/B/E/G1-453[»]
    ProteinModelPortaliP30838.
    SMRiP30838. Positions 2-453.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30838.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1012.
    GeneTreeiENSGT00390000002825.
    HOGENOMiHOG000271515.
    HOVERGENiHBG050483.
    InParanoidiP30838.
    KOiK00129.
    OMAiAWIRKEP.
    PhylomeDBiP30838.
    TreeFamiTF314264.

    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.
    IPR012394. Aldehyde_DH_NAD(P).
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    PIRSFiPIRSF036492. ALDH. 1 hit.
    SUPFAMiSSF53720. SSF53720. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P30838-1 [UniParc]FASTAAdd to Basket

    « Hide

            10         20         30         40         50
    MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA
    60 70 80 90 100
    DLHKNEWNAY YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI
    110 120 130 140 150
    HSEPLGVVLV IGTWNYPFNL TIQPMVGAIA AGNSVVLKPS ELSENMASLL
    160 170 180 190 200
    ATIIPQYLDK DLYPVINGGV PETTELLKER FDHILYTGST GVGKIIMTAA
    210 220 230 240 250
    AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS GQTCVAPDYI
    260 270 280 290 300
    LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG
    310 320 330 340 350
    QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVL PIVCVRSLEE
    360 370 380 390 400
    AIQFINQREK PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL
    410 420 430 440 450
    PFGGVGNSGM GSYHGKKSFE TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM

    TQH
    Length:453
    Mass (Da):50,395
    Last modified:November 2, 2010 - v3
    Checksum:iD35C488A022FAACA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121R → P in AAB46377. (PubMed:1737758)Curated
    Sequence conflicti12 – 121R → P in AAB26658. (PubMed:8493892)Curated
    Sequence conflicti27 – 271I → F in AAA51696. 1 PublicationCurated
    Sequence conflicti170 – 1701V → L AA sequence (PubMed:2037078)Curated
    Sequence conflicti436 – 4361D → E AA sequence (PubMed:2037078)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti134 – 1341S → A.5 Publications
    Corresponds to variant rs887241 [ dbSNP | Ensembl ].
    VAR_018981
    Natural varianti309 – 3091G → E.
    Corresponds to variant rs3744692 [ dbSNP | Ensembl ].
    VAR_018982
    Natural varianti329 – 3291P → A in allele ALDH3A1*2. 1 Publication
    Corresponds to variant rs2228100 [ dbSNP | Ensembl ].
    VAR_011303

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M74542 mRNA. Translation: AAA51696.1.
    M77477 mRNA. Translation: AAB46377.1.
    S61044 mRNA. Translation: AAB26658.1.
    BT007102 mRNA. Translation: AAP35766.1.
    AK292193 mRNA. Translation: BAF84882.1.
    AK314584 mRNA. Translation: BAG37160.1.
    AC005722 Genomic DNA. No translation available.
    CH471212 Genomic DNA. Translation: EAW50909.1.
    BC004370 mRNA. Translation: AAH04370.1.
    BC008892 mRNA. Translation: AAH08892.1.
    BC021194 mRNA. Translation: AAH21194.1.
    CCDSiCCDS11212.1.
    PIRiA42584.
    RefSeqiNP_000682.3. NM_000691.4.
    NP_001128639.1. NM_001135167.1.
    NP_001128640.1. NM_001135168.1.
    UniGeneiHs.531682.

    Genome annotation databases

    EnsembliENST00000225740; ENSP00000225740; ENSG00000108602.
    ENST00000444455; ENSP00000388469; ENSG00000108602.
    ENST00000457500; ENSP00000411821; ENSG00000108602.
    GeneIDi218.
    KEGGihsa:218.
    UCSCiuc002gwj.3. human.

    Polymorphism databases

    DMDMi311033473.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M74542 mRNA. Translation: AAA51696.1 .
    M77477 mRNA. Translation: AAB46377.1 .
    S61044 mRNA. Translation: AAB26658.1 .
    BT007102 mRNA. Translation: AAP35766.1 .
    AK292193 mRNA. Translation: BAF84882.1 .
    AK314584 mRNA. Translation: BAG37160.1 .
    AC005722 Genomic DNA. No translation available.
    CH471212 Genomic DNA. Translation: EAW50909.1 .
    BC004370 mRNA. Translation: AAH04370.1 .
    BC008892 mRNA. Translation: AAH08892.1 .
    BC021194 mRNA. Translation: AAH21194.1 .
    CCDSi CCDS11212.1.
    PIRi A42584.
    RefSeqi NP_000682.3. NM_000691.4.
    NP_001128639.1. NM_001135167.1.
    NP_001128640.1. NM_001135168.1.
    UniGenei Hs.531682.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3SZA X-ray 1.48 A/B 1-453 [» ]
    3SZB X-ray 1.51 A/B 1-453 [» ]
    4H80 X-ray 2.50 A/B/C/D/E/F/G/H 1-453 [» ]
    4L1O X-ray 2.30 A/B 1-453 [» ]
    4L2O X-ray 1.94 A/B/E/G 1-453 [» ]
    ProteinModelPortali P30838.
    SMRi P30838. Positions 2-453.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106720. 7 interactions.
    IntActi P30838. 2 interactions.
    STRINGi 9606.ENSP00000225740.

    Chemistry

    BindingDBi P30838.
    ChEMBLi CHEMBL3578.

    PTM databases

    PhosphoSitei P30838.

    Polymorphism databases

    DMDMi 311033473.

    Proteomic databases

    MaxQBi P30838.
    PaxDbi P30838.
    PRIDEi P30838.

    Protocols and materials databases

    DNASUi 218.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000225740 ; ENSP00000225740 ; ENSG00000108602 .
    ENST00000444455 ; ENSP00000388469 ; ENSG00000108602 .
    ENST00000457500 ; ENSP00000411821 ; ENSG00000108602 .
    GeneIDi 218.
    KEGGi hsa:218.
    UCSCi uc002gwj.3. human.

    Organism-specific databases

    CTDi 218.
    GeneCardsi GC17M019641.
    H-InvDB HIX0013622.
    HGNCi HGNC:405. ALDH3A1.
    HPAi CAB045957.
    HPA051150.
    MIMi 100660. gene.
    neXtProti NX_P30838.
    PharmGKBi PA24697.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1012.
    GeneTreei ENSGT00390000002825.
    HOGENOMi HOG000271515.
    HOVERGENi HBG050483.
    InParanoidi P30838.
    KOi K00129.
    OMAi AWIRKEP.
    PhylomeDBi P30838.
    TreeFami TF314264.

    Enzyme and pathway databases

    SABIO-RK P30838.

    Miscellaneous databases

    ChiTaRSi ALDH3A1. human.
    EvolutionaryTracei P30838.
    GeneWikii Aldehyde_dehydrogenase_3_family,_member_A1.
    GenomeRNAii 218.
    NextBioi 882.
    PROi P30838.
    SOURCEi Search...

    Gene expression databases

    Bgeei P30838.
    CleanExi HS_ALDH3A1.
    ExpressionAtlasi P30838. baseline and differential.
    Genevestigatori P30838.

    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.
    IPR012394. Aldehyde_DH_NAD(P).
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036492. ALDH. 1 hit.
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    1. "Cloning and complete nucleotide sequence of a cDNA encoding the full-length open reading frame of the human aldehyde dehydrogenase type III gene."
      Schuuring E.M.D., Verhoeven E., Eckey R., Vos H.L., Michalides R.J.A.
      Submitted (AUG-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-134.
      Tissue: Stomach.
    2. "Human stomach aldehyde dehydrogenase cDNA and genomic cloning, primary structure, and expression in Escherichia coli."
      Hsu L.C., Chang W.-C., Shibuya A., Yoshida A.
      J. Biol. Chem. 267:3030-3037(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Stomach.
    3. "Human stomach aldehyde dehydrogenase, ALDH3."
      Hsu L.C., Yoshida A.
      Adv. Exp. Med. Biol. 328:141-152(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Stomach.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-134.
    5. "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], VARIANT ALA-134.
      Tissue: Cervix and Tongue.
    6. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ALA-134.
    8. "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], VARIANT ALA-134.
      Tissue: Pancreas.
    9. "Structural features of stomach aldehyde dehydrogenase distinguish dimeric aldehyde dehydrogenase as a 'variable' enzyme. 'Variable' and 'constant' enzymes within the alcohol and aldehyde dehydrogenase families."
      Yin S.-J., Vagelopoulos N., Wang S.-L., Joernvall H.
      FEBS Lett. 283:85-88(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 62-453.
      Tissue: Stomach.
    10. "Biochemical, immunological, and molecular characterization of a 'high Km' aldehyde dehydrogenase."
      Eckey R., Timmann R., Hempel J., Agarwal D.P., Goedde H.W.
      Adv. Exp. Med. Biol. 284:43-52(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    11. "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-178 AND LYS-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [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. Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEX WITH INHIBITOR, MUTAGENESIS OF CYS-244, ACTIVE SITE.
    15. "Mutations associated with Sjogren-Larsson syndrome."
      Tsukamoto N., Chang C., Yoshida A.
      Ann. Hum. Genet. 61:235-242(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT ALA-329.

    Entry informationi

    Entry nameiAL3A1_HUMAN
    AccessioniPrimary (citable) accession number: P30838
    Secondary accession number(s): A8K828, Q9BT37
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: November 2, 2010
    Last modified: November 26, 2014
    This is version 145 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3