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P00352

- AL1A1_HUMAN

UniProt

P00352 - AL1A1_HUMAN

Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid By similarity.By similarity

    Catalytic activityi

    Retinal + NAD+ + H2O = retinoate + NADH.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei170 – 1701Transition state stabilizerBy similarity
    Active sitei269 – 2691Proton acceptor1 PublicationPROSITE-ProRule annotation
    Active sitei303 – 3031Nucleophile1 PublicationPROSITE-ProRule annotation
    Binding sitei456 – 4561NAD

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi246 – 2516NADBy similarity

    GO - Molecular functioni

    1. aldehyde dehydrogenase (NAD) activity Source: Reactome
    2. androgen binding Source: ProtInc
    3. Ras GTPase activator activity Source: UniProtKB
    4. retinal dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular aldehyde metabolic process Source: ProtInc
    2. ethanol oxidation Source: Reactome
    3. positive regulation of Ras GTPase activity Source: GOC
    4. retinol metabolic process Source: UniProtKB-UniPathway
    5. small molecule metabolic process Source: Reactome
    6. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS09183-MONOMER.
    ReactomeiREACT_34. Ethanol oxidation.
    SABIO-RKP00352.
    UniPathwayiUPA00912.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinal dehydrogenase 1 (EC:1.2.1.36)
    Short name:
    RALDH 1
    Short name:
    RalDH1
    Alternative name(s):
    ALDH-E1
    ALHDII
    Aldehyde dehydrogenase family 1 member A1
    Aldehyde dehydrogenase, cytosolic
    Gene namesi
    Name:ALDH1A1
    Synonyms:ALDC, ALDH1, PUMB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:402. ALDH1A1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: ProtInc
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24692.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 501500Retinal dehydrogenase 1PRO_0000056415Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Modified residuei91 – 911N6-acetyllysine1 Publication
    Modified residuei128 – 1281N6-acetyllysine1 Publication
    Modified residuei252 – 2521N6-acetyllysine1 Publication
    Modified residuei353 – 3531N6-acetyllysine1 Publication
    Modified residuei367 – 3671N6-acetyllysine1 Publication
    Modified residuei410 – 4101N6-acetyllysine1 Publication
    Modified residuei419 – 4191N6-acetyllysine1 Publication
    Modified residuei435 – 4351N6-acetyllysine1 Publication
    Modified residuei495 – 4951N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP00352.
    PaxDbiP00352.
    PeptideAtlasiP00352.
    PRIDEiP00352.

    2D gel databases

    DOSAC-COBS-2DPAGEP00352.
    REPRODUCTION-2DPAGEIPI00218914.
    P00352.
    SWISS-2DPAGEP00352.
    UCD-2DPAGEP00352.

    PTM databases

    PhosphoSiteiP00352.

    Expressioni

    Gene expression databases

    ArrayExpressiP00352.
    BgeeiP00352.
    CleanExiHS_ALDH1A1.
    GenevestigatoriP00352.

    Organism-specific databases

    HPAiCAB020690.
    HPA002123.

    Interactioni

    Subunit structurei

    Homotetramer.

    Protein-protein interaction databases

    BioGridi106718. 8 interactions.
    IntActiP00352. 6 interactions.
    MINTiMINT-4999613.
    STRINGi9606.ENSP00000297785.

    Structurei

    3D structure databases

    ProteinModelPortaliP00352.
    SMRiP00352. Positions 8-501.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271505.
    HOVERGENiHBG000097.
    InParanoidiP00352.
    KOiK07249.
    OMAiEWHDSAS.
    OrthoDBiEOG7PS1F7.
    PhylomeDBiP00352.
    TreeFamiTF300455.

    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]

    Sequencei

    Sequence statusi: Complete.

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

    P00352-1 [UniParc]FASTAAdd to Basket

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    MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC    50
    QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR 100
    LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN 150
    FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI GPALSCGNTV VVKPAEQTPL 200
    TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV 250
    GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG 300
    QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ 350
    YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE 400
    IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG 450
    TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN 500
    S 501
    Length:501
    Mass (Da):54,862
    Last modified:January 23, 2007 - v2
    Checksum:iB26464DC7168348E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti162 – 1621V → I in AAA35518. (PubMed:4015823)Curated
    Sequence conflicti162 – 1621V → I in AAA51695. (PubMed:2987944)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti121 – 1211N → S.1 Publication
    Corresponds to variant rs1049981 [ dbSNP | Ensembl ].
    VAR_048901
    Natural varianti125 – 1251G → R.
    Corresponds to variant rs11554423 [ dbSNP | Ensembl ].
    VAR_048902
    Natural varianti177 – 1771I → F.1 Publication
    Corresponds to variant rs8187929 [ dbSNP | Ensembl ].
    VAR_017778

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31994
    , M31982, M31983, M31984, M31985, M31986, M31987, M31988, M31989, M31990, M31991, M31992 Genomic DNA. Translation: AAA51692.1.
    AF003341 mRNA. Translation: AAC51652.1.
    AY390731 mRNA. Translation: AAR92229.1.
    BT006921 mRNA. Translation: AAP35567.1.
    AY338497 Genomic DNA. Translation: AAP88039.1.
    AL591031 Genomic DNA. Translation: CAI12257.1.
    CH471089 Genomic DNA. Translation: EAW62543.1.
    BC001505 mRNA. Translation: AAH01505.1.
    S61235 Genomic DNA. Translation: AAD13925.1.
    M26761 mRNA. Translation: AAA35518.1.
    K03000 mRNA. Translation: AAA51695.1.
    CCDSiCCDS6644.1.
    PIRiA33371. DEHUE1.
    RefSeqiNP_000680.2. NM_000689.4.
    UniGeneiHs.76392.

    Genome annotation databases

    EnsembliENST00000297785; ENSP00000297785; ENSG00000165092.
    GeneIDi216.
    KEGGihsa:216.
    UCSCiuc004ajd.3. human.

    Polymorphism databases

    DMDMi118495.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31994
    , M31982 , M31983 , M31984 , M31985 , M31986 , M31987 , M31988 , M31989 , M31990 , M31991 , M31992 Genomic DNA. Translation: AAA51692.1 .
    AF003341 mRNA. Translation: AAC51652.1 .
    AY390731 mRNA. Translation: AAR92229.1 .
    BT006921 mRNA. Translation: AAP35567.1 .
    AY338497 Genomic DNA. Translation: AAP88039.1 .
    AL591031 Genomic DNA. Translation: CAI12257.1 .
    CH471089 Genomic DNA. Translation: EAW62543.1 .
    BC001505 mRNA. Translation: AAH01505.1 .
    S61235 Genomic DNA. Translation: AAD13925.1 .
    M26761 mRNA. Translation: AAA35518.1 .
    K03000 mRNA. Translation: AAA51695.1 .
    CCDSi CCDS6644.1.
    PIRi A33371. DEHUE1.
    RefSeqi NP_000680.2. NM_000689.4.
    UniGenei Hs.76392.

    3D structure databases

    ProteinModelPortali P00352.
    SMRi P00352. Positions 8-501.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106718. 8 interactions.
    IntActi P00352. 6 interactions.
    MINTi MINT-4999613.
    STRINGi 9606.ENSP00000297785.

    Chemistry

    BindingDBi P00352.
    ChEMBLi CHEMBL3577.
    DrugBanki DB00157. NADH.
    DB00755. Tretinoin.
    DB00162. Vitamin A.

    PTM databases

    PhosphoSitei P00352.

    Polymorphism databases

    DMDMi 118495.

    2D gel databases

    DOSAC-COBS-2DPAGE P00352.
    REPRODUCTION-2DPAGE IPI00218914.
    P00352.
    SWISS-2DPAGE P00352.
    UCD-2DPAGE P00352.

    Proteomic databases

    MaxQBi P00352.
    PaxDbi P00352.
    PeptideAtlasi P00352.
    PRIDEi P00352.

    Protocols and materials databases

    DNASUi 216.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297785 ; ENSP00000297785 ; ENSG00000165092 .
    GeneIDi 216.
    KEGGi hsa:216.
    UCSCi uc004ajd.3. human.

    Organism-specific databases

    CTDi 216.
    GeneCardsi GC09M075515.
    HGNCi HGNC:402. ALDH1A1.
    HPAi CAB020690.
    HPA002123.
    MIMi 100640. gene.
    neXtProti NX_P00352.
    PharmGKBi PA24692.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1012.
    HOGENOMi HOG000271505.
    HOVERGENi HBG000097.
    InParanoidi P00352.
    KOi K07249.
    OMAi EWHDSAS.
    OrthoDBi EOG7PS1F7.
    PhylomeDBi P00352.
    TreeFami TF300455.

    Enzyme and pathway databases

    UniPathwayi UPA00912 .
    BioCyci MetaCyc:HS09183-MONOMER.
    Reactomei REACT_34. Ethanol oxidation.
    SABIO-RK P00352.

    Miscellaneous databases

    ChiTaRSi ALDH1A1. human.
    GeneWikii ALDH1A1.
    GenomeRNAii 216.
    NextBioi 874.
    PROi P00352.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P00352.
    Bgeei P00352.
    CleanExi HS_ALDH1A1.
    Genevestigatori P00352.

    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.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic structure of the human cytosolic aldehyde dehydrogenase gene."
      Hsu L.C., Chang W.-C., Yoshida A.
      Genomics 5:857-865(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning and expression of the full-length cDNAs encoding human liver class 1 and class 2 aldehyde dehydrogenase."
      Zheng C.F., Wang T.T., Weiner H.
      Alcohol. Clin. Exp. Res. 17:828-831(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-121.
      Tissue: Liver.
    3. "Cloning and expression of aldehyde dehydrogenase 1 (ALDH1A1) from human lens cDNA library."
      Ramana K.V., Xiao T., Ansari N.H.
      Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lens.
    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].
    5. NIEHS SNPs program
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-177.
    6. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Colon.
    9. "Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal response, retinal oxidation and implication in testicular feminization."
      Yoshida A., Hsu L.C., Yanagawa Y.
      Adv. Exp. Med. Biol. 328:37-44(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
    10. "Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme."
      Hempel J., von Bahr-Lindstroem H., Joernvall H.
      Eur. J. Biochem. 141:21-35(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-501, ACETYLATION AT SER-2.
      Tissue: Liver.
    11. "Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases."
      Yoshida A., Ikawa M., Hsu L.C., Tani K.
      Alcohol 2:103-106(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
    12. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
      Tissue: Liver.
    13. Cited for: PROTEIN SEQUENCE OF 266-273, ACTIVE SITES GLU-269 AND CYS-303, NAD-BINDING SITE CYS-456.
    14. "Aldehyde dehydrogenase from human erythrocytes: structural relationship to the liver cytosolic isozyme."
      Agarwal D.P., Cohn P., Goedde H.W., Hempel J.
      Enzyme 42:47-52(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE.
      Tissue: Erythrocyte.
    15. "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-91; LYS-128; LYS-252; LYS-353; LYS-367; LYS-410; LYS-419; LYS-435 AND LYS-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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].

    Entry informationi

    Entry nameiAL1A1_HUMAN
    AccessioniPrimary (citable) accession number: P00352
    Secondary accession number(s): O00768, Q5SYR1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 159 of the entry and version 2 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 9
      Human chromosome 9: 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