Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P23280

- CAH6_HUMAN

UniProt

P23280 - CAH6_HUMAN

Protein

Carbonic anhydrase 6

Gene

CA6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Reversible hydration of carbon dioxide. Its role in saliva is unknown.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.By similarity

    Enzyme regulationi

    Inhibited by coumarins, sulfonamide derivatives such as acetazolamide (AZA), saccharin and Foscarnet (phosphonoformate trisodium salt).4 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei85 – 851Proton acceptorBy similarity
    Metal bindingi111 – 1111Zinc; catalytic
    Metal bindingi113 – 1131Zinc; catalytic
    Metal bindingi138 – 1381Zinc; catalytic
    Active sitei146 – 1461By similarity

    GO - Molecular functioni

    1. carbonate dehydratase activity Source: Reactome
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. detection of chemical stimulus involved in sensory perception of bitter taste Source: UniProt
    3. one-carbon metabolic process Source: InterPro
    4. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi4.2.1.1. 2681.
    ReactomeiREACT_121123. Reversible hydration of carbon dioxide.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 6 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase VI
    Carbonic anhydrase VI
    Short name:
    CA-VI
    Salivary carbonic anhydrase
    Secreted carbonic anhydrase
    Gene namesi
    Name:CA6
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1380. CA6.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProt
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25995.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 308291Carbonic anhydrase 6PRO_0000004241Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi42 ↔ 224Sequence Analysis
    Glycosylationi67 – 671N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP23280.
    PRIDEiP23280.

    Expressioni

    Tissue specificityi

    Major constituent of saliva.

    Gene expression databases

    ArrayExpressiP23280.
    BgeeiP23280.
    CleanExiHS_CA6.
    GenevestigatoriP23280.

    Organism-specific databases

    HPAiHPA028550.
    HPA028692.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000366662.

    Structurei

    Secondary structure

    1
    308
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi35 – 384
    Helixi40 – 434
    Beta strandi44 – 463
    Helixi54 – 563
    Beta strandi68 – 703
    Beta strandi72 – 8211
    Beta strandi87 – 904
    Beta strandi96 – 983
    Beta strandi104 – 11411
    Beta strandi125 – 1284
    Beta strandi134 – 14310
    Beta strandi146 – 1483
    Helixi149 – 1524
    Beta strandi159 – 1679
    Helixi175 – 1773
    Helixi178 – 1836
    Helixi184 – 1874
    Beta strandi193 – 1997
    Helixi201 – 2044
    Beta strandi212 – 2176
    Beta strandi228 – 2358
    Helixi241 – 2499
    Beta strandi256 – 2583
    Beta strandi275 – 2773

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3FE4X-ray1.90A/B21-290[»]
    ProteinModelPortaliP23280.
    SMRiP23280. Positions 33-280.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP23280.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni220 – 2212Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3338.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    KOiK01672.
    OMAiPDGTEYI.
    PhylomeDBiP23280.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    IPR018428. Carbonic_anhydrase_CA6.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF17. PTHR18952:SF17. 1 hit.
    PfamiPF00194. Carb_anhydrase. 1 hit.
    [Graphical view]
    SMARTiSM01057. Carb_anhydrase. 1 hit.
    [Graphical view]
    SUPFAMiSSF51069. SSF51069. 1 hit.
    PROSITEiPS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P23280-1) [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

    MRALVLLLSL FLLGGQAQHV SDWTYSEGAL DEAHWPQHYP ACGGQRQSPI    50
    NLQRTKVRYN PSLKGLNMTG YETQAGEFPM VNNGHTVQIS LPSTMRMTVA 100
    DGTVYIAQQM HFHWGGASSE ISGSEHTVDG IRHVIEIHIV HYNSKYKSYD 150
    IAQDAPDGLA VLAAFVEVKN YPENTYYSNF ISHLANIKYP GQRTTLTGLD 200
    VQDMLPRNLQ HYYTYHGSLT TPPCTENVHW FVLADFVKLS RTQVWKLENS 250
    LLDHRNKTIH NDYRRTQPLN HRVVESNFPN QEYTLGSEFQ FYLHKIEEIL 300
    DYLRRALN 308
    Length:308
    Mass (Da):35,367
    Last modified:October 17, 2006 - v3
    Checksum:i6EBFF15085E7112D
    GO
    Isoform 2 (identifier: P23280-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         282-308: EYTLGSEFQFYLHKIEEILDYLRRALN → GKGHGGHRGRSQNPRVQPTSTRHPLALGSLEA

    Note: No experimental confirmation available.

    Show »
    Length:313
    Mass (Da):35,365
    Checksum:i1CF67B5ED1BD9384
    GO
    Isoform 3 (identifier: P23280-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         27-86: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:248
    Mass (Da):28,687
    Checksum:i39A6223C958A3029
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti103 – 1031T → I in AAA51892. (PubMed:1899030)Curated
    Sequence conflicti103 – 1031T → I in BAD89434. (PubMed:16710414)Curated
    Sequence conflicti148 – 1481S → T in AAA51892. (PubMed:1899030)Curated
    Sequence conflicti148 – 1481S → T in AAF22565. 1 PublicationCurated
    Sequence conflicti148 – 1481S → T in BAD89434. (PubMed:16710414)Curated
    Sequence conflicti270 – 2701N → K in AAA51892. (PubMed:1899030)Curated
    Sequence conflicti270 – 2701N → K in AAF22565. 1 PublicationCurated
    Sequence conflicti270 – 2701N → K in BAD89434. (PubMed:16710414)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti37 – 371Q → L.
    Corresponds to variant rs34265054 [ dbSNP | Ensembl ].
    VAR_033712
    Natural varianti55 – 551T → M.
    Corresponds to variant rs2274327 [ dbSNP | Ensembl ].
    VAR_028268
    Natural varianti58 – 581R → W.
    Corresponds to variant rs58800854 [ dbSNP | Ensembl ].
    VAR_061093
    Natural varianti68 – 681M → L.
    Corresponds to variant rs2274328 [ dbSNP | Ensembl ].
    VAR_028269
    Natural varianti70 – 701G → A.
    Corresponds to variant rs2274329 [ dbSNP | Ensembl ].
    VAR_028270
    Natural varianti90 – 901S → G.3 Publications
    Corresponds to variant rs2274333 [ dbSNP | Ensembl ].
    VAR_028271

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei27 – 8660Missing in isoform 3. 1 PublicationVSP_046668Add
    BLAST
    Alternative sequencei282 – 30827EYTLG…RRALN → GKGHGGHRGRSQNPRVQPTS TRHPLALGSLEA in isoform 2. 1 PublicationVSP_045435Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57892 mRNA. Translation: AAA51892.1.
    AF128418
    , AF128411, AF128412, AF128413, AF128414, AF128415, AF128416, AF128417 Genomic DNA. Translation: AAF22565.1.
    AB102863 mRNA. Translation: BAD89397.1.
    AB103091 mRNA. Translation: BAD89434.1.
    AL139415 Genomic DNA. Translation: CAC42429.1.
    CCDSiCCDS30578.1. [P23280-1]
    CCDS57970.1. [P23280-2]
    CCDS57971.1. [P23280-3]
    PIRiA37917. CRHU6.
    RefSeqiNP_001206.2. NM_001215.3. [P23280-1]
    NP_001257429.1. NM_001270500.1. [P23280-2]
    NP_001257430.1. NM_001270501.1. [P23280-3]
    UniGeneiHs.100322.

    Genome annotation databases

    EnsembliENST00000377436; ENSP00000366654; ENSG00000131686. [P23280-2]
    ENST00000377442; ENSP00000366661; ENSG00000131686. [P23280-3]
    ENST00000377443; ENSP00000366662; ENSG00000131686. [P23280-1]
    GeneIDi765.
    KEGGihsa:765.
    UCSCiuc001apm.4. human. [P23280-1]
    uc031plc.1. human.

    Polymorphism databases

    DMDMi116241278.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M57892 mRNA. Translation: AAA51892.1 .
    AF128418
    , AF128411 , AF128412 , AF128413 , AF128414 , AF128415 , AF128416 , AF128417 Genomic DNA. Translation: AAF22565.1 .
    AB102863 mRNA. Translation: BAD89397.1 .
    AB103091 mRNA. Translation: BAD89434.1 .
    AL139415 Genomic DNA. Translation: CAC42429.1 .
    CCDSi CCDS30578.1. [P23280-1 ]
    CCDS57970.1. [P23280-2 ]
    CCDS57971.1. [P23280-3 ]
    PIRi A37917. CRHU6.
    RefSeqi NP_001206.2. NM_001215.3. [P23280-1 ]
    NP_001257429.1. NM_001270500.1. [P23280-2 ]
    NP_001257430.1. NM_001270501.1. [P23280-3 ]
    UniGenei Hs.100322.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3FE4 X-ray 1.90 A/B 21-290 [» ]
    ProteinModelPortali P23280.
    SMRi P23280. Positions 33-280.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000366662.

    Chemistry

    BindingDBi P23280.
    ChEMBLi CHEMBL3025.

    Polymorphism databases

    DMDMi 116241278.

    Proteomic databases

    PaxDbi P23280.
    PRIDEi P23280.

    Protocols and materials databases

    DNASUi 765.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000377436 ; ENSP00000366654 ; ENSG00000131686 . [P23280-2 ]
    ENST00000377442 ; ENSP00000366661 ; ENSG00000131686 . [P23280-3 ]
    ENST00000377443 ; ENSP00000366662 ; ENSG00000131686 . [P23280-1 ]
    GeneIDi 765.
    KEGGi hsa:765.
    UCSCi uc001apm.4. human. [P23280-1 ]
    uc031plc.1. human.

    Organism-specific databases

    CTDi 765.
    GeneCardsi GC01P009005.
    H-InvDB HIX0028508.
    HIX0116265.
    HGNCi HGNC:1380. CA6.
    HPAi HPA028550.
    HPA028692.
    MIMi 114780. gene.
    neXtProti NX_P23280.
    PharmGKBi PA25995.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    KOi K01672.
    OMAi PDGTEYI.
    PhylomeDBi P23280.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 2681.
    Reactomei REACT_121123. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    EvolutionaryTracei P23280.
    GeneWikii Carbonic_anhydrase_VI.
    GenomeRNAii 765.
    NextBioi 3092.
    PROi P23280.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P23280.
    Bgeei P23280.
    CleanExi HS_CA6.
    Genevestigatori P23280.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    IPR018428. Carbonic_anhydrase_CA6.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF17. PTHR18952:SF17. 1 hit.
    Pfami PF00194. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SMARTi SM01057. Carb_anhydrase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51069. SSF51069. 1 hit.
    PROSITEi PS00162. ALPHA_CA_1. 1 hit.
    PS51144. ALPHA_CA_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human secreted carbonic anhydrase: cDNA cloning, nucleotide sequence, and hybridization histochemistry."
      Aldred P., Fu P., Barrett G., Penschow J.D., Wright R., Coghlan J.P., Fernley R.T.
      Biochemistry 30:569-575(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT GLY-90.
    2. Grubb D.J.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-90.
    3. "CA6 mRNA, nirs splice variant 1."
      Tabata Y., Hayashi A., Sameshima E., Iida K., Mitsuyama M., Kanai S., Furuya T., Saito T.
      Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), VARIANT GLY-90.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Saccharin inhibits carbonic anhydrases: possible explanation for its unpleasant metallic aftertaste."
      Koehler K., Hillebrecht A., Schulze Wischeler J., Innocenti A., Heine A., Supuran C.T., Klebe G.
      Angew. Chem. Int. Ed. Engl. 46:7697-7699(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    6. "Phosph(on)ate as a zinc-binding group in metalloenzyme inhibitors: X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I."
      Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.
      Bioorg. Med. Chem. Lett. 17:2210-2215(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    7. "A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases."
      Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.
      Bioorg. Med. Chem. Lett. 19:1371-1375(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    8. "Non-zinc mediated inhibition of carbonic anhydrases: coumarins are a new class of suicide inhibitors."
      Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.
      J. Am. Chem. Soc. 131:3057-3062(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    9. "Crystal structure of human erythrocyte carbonic anhydrase C. VI. The three-dimensional structure at high resolution in relation to other mammalian carbonic anhydrases."
      Kannan K.K., Liljas A., Waara I., Bergsten P.C., Loevgren S., Strandberg B., Bengtsson U., Carlbom U., Fridborg K., Jaerup L., Petef M.
      Cold Spring Harb. Symp. Quant. Biol. 36:221-231(1972) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 21-290 IN COMPLEX WITH MAGNESIUM ION.

    Entry informationi

    Entry nameiCAH6_HUMAN
    AccessioniPrimary (citable) accession number: P23280
    Secondary accession number(s): E7EMQ1
    , Q5FBW3, Q5FC00, Q96QX8, Q9UF03
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 140 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, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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