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Protein

Aldehyde dehydrogenase, dimeric NADP-preferring

Gene

ALDH3A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

      • 3-chloroallyl aldehyde dehydrogenase activity Source: GO_Central
      • alcohol dehydrogenase (NADP+) activity Source: UniProtKB
      • aldehyde dehydrogenase (NAD) activity Source: UniProtKB
      • aldehyde dehydrogenase [NAD(P)+] activity Source: UniProtKB-EC
      • benzaldehyde dehydrogenase (NAD+) activity Source: CACAO

      GO - Biological processi

      Complete GO annotation...

      Keywords - Molecular functioni

      Oxidoreductase

      Keywords - Ligandi

      NAD, NADP

      Enzyme and pathway databases

      BRENDAi1.2.1.5. 2681.
      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 Componenti: Chromosome 17

      Organism-specific databases

      HGNCiHGNC:405. ALDH3A1.

      Subcellular locationi

      GO - Cellular componenti

      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.

      Polymorphism and mutation databases

      BioMutaiALDH3A1.
      DMDMi311033473.

      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.
      GenevisibleiP30838. HS.

      Organism-specific databases

      HPAiCAB045957.
      HPA051150.
      HPA063783.

      Interactioni

      Subunit structurei

      Homodimer.1 Publication

      Protein-protein interaction databases

      BioGridi106720. 11 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.
      OMAiELYIHSE.
      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 (Ref. 1) Curated
      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.

      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.
      CCDSiCCDS11212.1.
      PIRiA42584.
      RefSeqiNP_000682.3. NM_000691.4.
      NP_001128639.1. NM_001135167.1.
      NP_001128640.1. NM_001135168.1.
      UniGeneiHs.531682.

      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...

      Protein-protein interaction databases

      BioGridi106720. 11 interactions.
      IntActiP30838. 2 interactions.
      STRINGi9606.ENSP00000225740.

      Chemistry

      BindingDBiP30838.
      ChEMBLiCHEMBL3578.

      PTM databases

      PhosphoSiteiP30838.

      Polymorphism and mutation databases

      BioMutaiALDH3A1.
      DMDMi311033473.

      Proteomic databases

      MaxQBiP30838.
      PaxDbiP30838.
      PRIDEiP30838.

      Protocols and materials databases

      DNASUi218.
      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

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

      Organism-specific databases

      CTDi218.
      GeneCardsiGC17M019641.
      H-InvDBHIX0013622.
      HGNCiHGNC:405. ALDH3A1.
      HPAiCAB045957.
      HPA051150.
      HPA063783.
      MIMi100660. gene.
      neXtProtiNX_P30838.
      PharmGKBiPA24697.
      GenAtlasiSearch...

      Phylogenomic databases

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

      Enzyme and pathway databases

      BRENDAi1.2.1.5. 2681.
      SABIO-RKP30838.

      Miscellaneous databases

      ChiTaRSiALDH3A1. human.
      EvolutionaryTraceiP30838.
      GeneWikiiAldehyde_dehydrogenase_3_family,_member_A1.
      GenomeRNAii218.
      NextBioi882.
      PROiP30838.
      SOURCEiSearch...

      Gene expression databases

      BgeeiP30838.
      CleanExiHS_ALDH3A1.
      ExpressionAtlasiP30838. baseline and differential.
      GenevisibleiP30838. 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.
      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]
      ProtoNetiSearch...

      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: July 22, 2015
      This is version 152 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

      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.