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P30838

- AL3A1_HUMAN

UniProt

P30838 - AL3A1_HUMAN

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
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 3 (02 Nov 2010)
      Previous versions | rss
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    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

      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

      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

      ArrayExpressiP30838.
      BgeeiP30838.
      CleanExiHS_ALDH3A1.
      GenevestigatoriP30838.

      Organism-specific databases

      HPAiCAB045957.
      HPA051150.

      Interactioni

      Subunit structurei

      Homodimer.1 Publication

      Protein-protein interaction databases

      BioGridi106720. 4 interactions.
      IntActiP30838. 2 interactions.
      STRINGi9606.ENSP00000225740.

      Structurei

      Secondary structure

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

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      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.
      HOGENOMiHOG000271515.
      HOVERGENiHBG050483.
      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

      MSKISEAVKR ARAAFSSGRT RPLQFRIQQL EALQRLIQEQ EQELVGALAA    50
      DLHKNEWNAY YEEVVYVLEE IEYMIQKLPE WAADEPVEKT PQTQQDELYI 100
      HSEPLGVVLV IGTWNYPFNL TIQPMVGAIA AGNSVVLKPS ELSENMASLL 150
      ATIIPQYLDK DLYPVINGGV PETTELLKER FDHILYTGST GVGKIIMTAA 200
      AKHLTPVTLE LGGKSPCYVD KNCDLDVACR RIAWGKFMNS GQTCVAPDYI 250
      LCDPSIQNQI VEKLKKSLKE FYGEDAKKSR DYGRIISARH FQRVMGLIEG 300
      QKVAYGGTGD AATRYIAPTI LTDVDPQSPV MQEEIFGPVL PIVCVRSLEE 350
      AIQFINQREK PLALYMFSSN DKVIKKMIAE TSSGGVAAND VIVHITLHSL 400
      PFGGVGNSGM GSYHGKKSFE TFSHRRSCLV RPLMNDEGLK VRYPPSPAKM 450
      TQH 453
      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:
      EMBL
      GenBank
      DDBJ
      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:
      EMBL
      GenBank
      DDBJ
      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:
      PDBe
      RCSB PDB
      PDBj
      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. 4 interactions.
      IntActi P30838. 2 interactions.
      STRINGi 9606.ENSP00000225740.

      Chemistry

      ChEMBLi CHEMBL3578.
      DrugBanki DB00157. NADH.

      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.
      HOGENOMi HOG000271515.
      HOVERGENi HBG050483.
      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

      ArrayExpressi P30838.
      Bgeei P30838.
      CleanExi HS_ALDH3A1.
      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

      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: October 1, 2014
      This is version 143 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