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P08319

- ADH4_HUMAN

UniProt

P08319 - ADH4_HUMAN

Protein

Alcohol dehydrogenase 4

Gene

ADH4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 157 (01 Oct 2014)
      Sequence version 5 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Catalytic activityi

    An alcohol + NAD+ = an aldehyde or ketone + NADH.

    Cofactori

    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi47 – 471Zinc 1; catalytic
    Metal bindingi69 – 691Zinc 1; catalytic
    Metal bindingi99 – 991Zinc 2
    Metal bindingi102 – 1021Zinc 2
    Metal bindingi105 – 1051Zinc 2
    Metal bindingi113 – 1131Zinc 2
    Metal bindingi180 – 1801Zinc 1; catalytic
    Binding sitei229 – 2291NAD1 Publication
    Binding sitei234 – 2341NAD1 Publication
    Binding sitei375 – 3751NAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi48 – 492NAD1 Publication
    Nucleotide bindingi205 – 2106NAD1 Publication
    Nucleotide bindingi298 – 3003NAD1 Publication
    Nucleotide bindingi323 – 3253NAD1 Publication

    GO - Molecular functioni

    1. alcohol dehydrogenase (NAD) activity Source: UniProtKB
    2. alcohol dehydrogenase activity, zinc-dependent Source: UniProtKB
    3. alditol:NADP+ 1-oxidoreductase activity Source: Ensembl
    4. all-trans retinal binding Source: UniProtKB
    5. benzaldehyde dehydrogenase activity Source: UniProtKB
    6. ethanol binding Source: InterPro
    7. NAD binding Source: UniProtKB
    8. NADPH:quinone reductase activity Source: UniProtKB
    9. oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: UniProtKB
    10. retinol binding Source: UniProtKB
    11. retinol dehydrogenase activity Source: UniProtKB
    12. zinc ion binding Source: UniProtKB

    GO - Biological processi

    1. alcohol catabolic process Source: UniProtKB
    2. alcohol metabolic process Source: UniProtKB
    3. cellular aldehyde metabolic process Source: UniProtKB
    4. ethanol oxidation Source: UniProtKB
    5. quinone metabolic process Source: UniProtKB
    6. retinoid metabolic process Source: UniProtKB
    7. retinol metabolic process Source: UniProtKB
    8. small molecule metabolic process Source: Reactome
    9. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06569-MONOMER.
    ReactomeiREACT_34. Ethanol oxidation.
    SABIO-RKP08319.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alcohol dehydrogenase 4 (EC:1.1.1.1)
    Alternative name(s):
    Alcohol dehydrogenase class II pi chain
    Gene namesi
    Name:ADH4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:252. ADH4.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24573.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 380380Alcohol dehydrogenase 4PRO_0000160681Add
    BLAST

    Proteomic databases

    MaxQBiP08319.
    PaxDbiP08319.
    PRIDEiP08319.

    PTM databases

    PhosphoSiteiP08319.

    Expressioni

    Gene expression databases

    ArrayExpressiP08319.
    BgeeiP08319.
    CleanExiHS_ADH4.
    GenevestigatoriP08319.

    Organism-specific databases

    HPAiHPA020525.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi106639. 4 interactions.
    IntActiP08319. 1 interaction.
    STRINGi9606.ENSP00000265512.

    Structurei

    Secondary structure

    1
    380
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi8 – 158
    Beta strandi23 – 297
    Beta strandi36 – 4510
    Helixi48 – 525
    Beta strandi63 – 653
    Beta strandi70 – 789
    Beta strandi90 – 934
    Beta strandi100 – 1023
    Turni103 – 1064
    Helixi122 – 1243
    Beta strandi135 – 1384
    Beta strandi141 – 1444
    Turni147 – 1493
    Beta strandi152 – 1598
    Beta strandi162 – 1654
    Helixi172 – 1754
    Helixi176 – 1794
    Helixi181 – 19010
    Turni191 – 1933
    Beta strandi200 – 2045
    Helixi208 – 21912
    Beta strandi223 – 2286
    Helixi232 – 2343
    Helixi235 – 2406
    Beta strandi244 – 2474
    Helixi249 – 2513
    Helixi256 – 2638
    Beta strandi268 – 2736
    Helixi278 – 2869
    Turni290 – 2923
    Beta strandi293 – 2975
    Beta strandi307 – 3093
    Helixi311 – 3155
    Beta strandi318 – 3225
    Helixi325 – 3273
    Helixi330 – 34213
    Helixi349 – 3513
    Beta strandi352 – 3576
    Helixi358 – 3603
    Helixi361 – 3699
    Beta strandi374 – 3796

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3COSX-ray2.10A/B/C/D1-380[»]
    ProteinModelPortaliP08319.
    SMRiP08319. Positions 1-380.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08319.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1062.
    HOGENOMiHOG000294674.
    HOVERGENiHBG000195.
    InParanoidiP08319.
    KOiK13980.
    OMAiPLTNLCG.
    OrthoDBiEOG72NRQ6.
    PhylomeDBiP08319.
    TreeFamiTF300429.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR028632. Zinc_ADH_II.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PTHR11695:SF308. PTHR11695:SF308. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 2 hits.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P08319-1) [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

    MGTKGKVIKC KAAIAWEAGK PLCIEEVEVA PPKAHEVRIQ IIATSLCHTD    50
    ATVIDSKFEG LAFPVIVGHE AAGIVESIGP GVTNVKPGDK VIPLYAPLCR 100
    KCKFCLSPLT NLCGKISNLK SPASDQQLME DKTSRFTCKG KPVYHFFGTS 150
    TFSQYTVVSD INLAKIDDDA NLERVCLLGC GFSTGYGAAI NNAKVTPGST 200
    CAVFGLGGVG LSAVMGCKAA GASRIIGIDI NSEKFVKAKA LGATDCLNPR 250
    DLHKPIQEVI IELTKGGVDF ALDCAGGSET MKAALDCTTA GWGSCTFIGV 300
    AAGSKGLTIF PEELIIGRTI NGTFFGGWKS VDSIPKLVTD YKNKKFNLDA 350
    LVTHTLPFDK ISEAFDLMNQ GKSVRTILIF 380
    Length:380
    Mass (Da):40,222
    Last modified:October 5, 2010 - v5
    Checksum:i45721A08197629F1
    GO
    Isoform 2 (identifier: P08319-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MGTKGK → MLVRGPHFELQRCKTHLFSSNYLTQ

    Show »
    Length:399
    Mass (Da):42,607
    Checksum:iC4ABEC85C04B6C2D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti52 – 521T → S in AAA51595. (PubMed:3036213)Curated
    Sequence conflicti52 – 521T → S in CAA39813. (PubMed:1889753)Curated
    Sequence conflicti380 – 3801F → FGRCQEQFRILSD in AAA51595. (PubMed:3036213)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti309 – 3091I → V.2 Publications
    Corresponds to variant rs1126671 [ dbSNP | Ensembl ].
    VAR_023461
    Natural varianti318 – 3181R → H.1 Publication
    Corresponds to variant rs29001219 [ dbSNP | Ensembl ].
    VAR_023462
    Natural varianti374 – 3741V → I.2 Publications
    Corresponds to variant rs1126673 [ dbSNP | Ensembl ].
    VAR_023463

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 66MGTKGK → MLVRGPHFELQRCKTHLFSS NYLTQ in isoform 2. 1 PublicationVSP_036788

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15943 mRNA. Translation: AAA51595.1.
    X56411
    , X56412, X56413, X56414, X56415, X56416, X56417, X56418, X56419 Genomic DNA. Translation: CAA39813.1.
    AK290835 mRNA. Translation: BAF83524.1.
    AK295556 mRNA. Translation: BAG58459.1.
    AY974245 Genomic DNA. Translation: AAX59034.1.
    AC019131 Genomic DNA. No translation available.
    AP002026 Genomic DNA. No translation available.
    BC022319 mRNA. Translation: AAH22319.1.
    CCDSiCCDS34032.1. [P08319-1]
    PIRiA27109. DEHUAP.
    RefSeqiNP_000661.2. NM_000670.3. [P08319-1]
    UniGeneiHs.1219.

    Genome annotation databases

    EnsembliENST00000265512; ENSP00000265512; ENSG00000198099. [P08319-1]
    ENST00000505590; ENSP00000425416; ENSG00000198099. [P08319-2]
    ENST00000508393; ENSP00000424630; ENSG00000198099. [P08319-2]
    GeneIDi127.
    KEGGihsa:127.
    UCSCiuc003hun.3. human. [P08319-1]
    uc011ced.2. human. [P08319-2]

    Polymorphism databases

    DMDMi308153684.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15943 mRNA. Translation: AAA51595.1 .
    X56411
    , X56412 , X56413 , X56414 , X56415 , X56416 , X56417 , X56418 , X56419 Genomic DNA. Translation: CAA39813.1 .
    AK290835 mRNA. Translation: BAF83524.1 .
    AK295556 mRNA. Translation: BAG58459.1 .
    AY974245 Genomic DNA. Translation: AAX59034.1 .
    AC019131 Genomic DNA. No translation available.
    AP002026 Genomic DNA. No translation available.
    BC022319 mRNA. Translation: AAH22319.1 .
    CCDSi CCDS34032.1. [P08319-1 ]
    PIRi A27109. DEHUAP.
    RefSeqi NP_000661.2. NM_000670.3. [P08319-1 ]
    UniGenei Hs.1219.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3COS X-ray 2.10 A/B/C/D 1-380 [» ]
    ProteinModelPortali P08319.
    SMRi P08319. Positions 1-380.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106639. 4 interactions.
    IntActi P08319. 1 interaction.
    STRINGi 9606.ENSP00000265512.

    Chemistry

    BindingDBi P08319.
    ChEMBLi CHEMBL2096668.

    PTM databases

    PhosphoSitei P08319.

    Polymorphism databases

    DMDMi 308153684.

    Proteomic databases

    MaxQBi P08319.
    PaxDbi P08319.
    PRIDEi P08319.

    Protocols and materials databases

    DNASUi 127.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265512 ; ENSP00000265512 ; ENSG00000198099 . [P08319-1 ]
    ENST00000505590 ; ENSP00000425416 ; ENSG00000198099 . [P08319-2 ]
    ENST00000508393 ; ENSP00000424630 ; ENSG00000198099 . [P08319-2 ]
    GeneIDi 127.
    KEGGi hsa:127.
    UCSCi uc003hun.3. human. [P08319-1 ]
    uc011ced.2. human. [P08319-2 ]

    Organism-specific databases

    CTDi 127.
    GeneCardsi GC04M100044.
    H-InvDB HIX0200651.
    HGNCi HGNC:252. ADH4.
    HPAi HPA020525.
    MIMi 103740. gene.
    neXtProti NX_P08319.
    PharmGKBi PA24573.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1062.
    HOGENOMi HOG000294674.
    HOVERGENi HBG000195.
    InParanoidi P08319.
    KOi K13980.
    OMAi PLTNLCG.
    OrthoDBi EOG72NRQ6.
    PhylomeDBi P08319.
    TreeFami TF300429.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06569-MONOMER.
    Reactomei REACT_34. Ethanol oxidation.
    SABIO-RK P08319.

    Miscellaneous databases

    EvolutionaryTracei P08319.
    GeneWikii ADH4.
    GenomeRNAii 127.
    NextBioi 507.
    PROi P08319.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P08319.
    Bgeei P08319.
    CleanExi HS_ADH4.
    Genevestigatori P08319.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProi IPR013149. ADH_C.
    IPR013154. ADH_GroES-like.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR028632. Zinc_ADH_II.
    [Graphical view ]
    PANTHERi PTHR11695. PTHR11695. 1 hit.
    PTHR11695:SF308. PTHR11695:SF308. 1 hit.
    Pfami PF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50129. SSF50129. 2 hits.
    PROSITEi PS00059. ADH_ZINC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the class II enzyme of human liver alcohol dehydrogenase: combined cDNA and protein sequence determination of the pi subunit."
      Hoeoeg J.-O., von Bahr-Lindstroem H., Heden L.-O., Holmquist B., Larsson K., Hempel J., Vallee B.L., Joernvall H.
      Biochemistry 26:1926-1932(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
    2. "Cloning and characterization of the human ADH4 gene."
      von Bahr-Lindstroem H., Joernvall H., Hoeoeg J.-O.
      Gene 103:269-274(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
      Tissue: Fetal 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), VARIANTS VAL-309 AND ILE-374.
      Tissue: Hippocampus and Liver.
    4. NIEHS SNPs program
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-318.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1), VARIANTS VAL-309 AND ILE-374.
      Tissue: Liver.
    7. "Crystal structure of human class II alcohol dehydrogenase (ADH4) in complex with NAD and Zn."
      Structural genomics consortium (SGC)
      Submitted (APR-2008) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH NAD AND ZINC IONS.

    Entry informationi

    Entry nameiADH4_HUMAN
    AccessioniPrimary (citable) accession number: P08319
    Secondary accession number(s): A8K470
    , B4DIE7, C9J4A9, Q8TCD7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 157 of the entry and version 5 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

    Miscellaneous

    There are 7 different ADH's isozymes in human: three belongs to class-I: alpha, beta, and gamma, one to class-II: pi, one to class-III: chi, one to class-IV: ADH7 and one to class-V: ADH6.

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 4
      Human chromosome 4: 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