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)

Q16790

- CAH9_HUMAN

UniProt

Q16790 - CAH9_HUMAN

Protein

Carbonic anhydrase 9

Gene

CA9

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 142 (01 Oct 2014)
      Sequence version 2 (06 Dec 2005)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Reversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia.1 Publication

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

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

    pH dependencei

    Optimum pH is 6.5.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei200 – 2001Proton acceptorBy similarity
    Metal bindingi226 – 2261Zinc; catalytic
    Metal bindingi228 – 2281Zinc; catalytic
    Metal bindingi251 – 2511Zinc; catalytic

    GO - Molecular functioni

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

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. cellular response to hypoxia Source: Reactome
    3. morphogenesis of an epithelium Source: Ensembl
    4. one-carbon metabolic process Source: InterPro
    5. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    6. response to drug Source: Ensembl
    7. response to testosterone Source: Ensembl
    8. secretion Source: Ensembl
    9. 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_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    REACT_121123. Reversible hydration of carbon dioxide.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carbonic anhydrase 9 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase IX
    Carbonic anhydrase IX
    Short name:
    CA-IX
    Short name:
    CAIX
    Membrane antigen MN
    P54/58N
    Renal cell carcinoma-associated antigen G250
    Short name:
    RCC-associated antigen G250
    pMW1
    Gene namesi
    Name:CA9
    Synonyms:G250, MN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:1383. CA9.

    Subcellular locationi

    Nucleus 1 Publication. Nucleusnucleolus 1 Publication. Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cell projectionmicrovillus membrane 1 Publication; Single-pass type I membrane protein 1 Publication
    Note: Found on the surface microvilli and in the nucleus, particularly in nucleolus.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. integral component of membrane Source: ProtInc
    3. microvillus membrane Source: UniProtKB-SubCell
    4. nucleolus Source: UniProtKB-SubCell
    5. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25998.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 37371 PublicationAdd
    BLAST
    Chaini38 – 459422Carbonic anhydrase 9PRO_0000004243Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi115 – 1151O-linked (GlcNAc...)1 Publication
    Disulfide bondi156 ↔ 336
    Disulfide bondi174 – 174InterchainCurated
    Glycosylationi346 – 3461N-linked (GlcNAc...)2 Publications
    Modified residuei449 – 4491Phosphotyrosine1 Publication

    Post-translational modificationi

    Asn-346 bears high-mannose type glycan structures.

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiQ16790.
    PaxDbiQ16790.
    PRIDEiQ16790.

    PTM databases

    PhosphoSiteiQ16790.

    Expressioni

    Tissue specificityi

    Expressed primarily in carcinoma cells lines. Expression is restricted to very few normal tissues and the most abundant expression is found in the epithelial cells of gastric mucosa.

    Inductioni

    By hypoxia.1 Publication

    Gene expression databases

    BgeeiQ16790.
    CleanExiHS_CA9.
    GenevestigatoriQ16790.

    Organism-specific databases

    HPAiCAB005100.
    CAB017107.

    Interactioni

    Subunit structurei

    Forms oligomers linked by disulfide bonds.3 Publications

    Protein-protein interaction databases

    BioGridi107223. 31 interactions.
    DIPiDIP-48973N.
    STRINGi9606.ENSP00000367608.

    Structurei

    Secondary structure

    1
    459
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni137 – 1393
    Beta strandi143 – 1475
    Helixi149 – 1524
    Helixi154 – 1574
    Helixi168 – 1703
    Beta strandi171 – 1733
    Beta strandi181 – 1844
    Beta strandi193 – 1975
    Beta strandi202 – 2054
    Beta strandi211 – 2155
    Beta strandi218 – 22912
    Beta strandi238 – 2414
    Beta strandi247 – 25610
    Helixi262 – 2654
    Beta strandi271 – 28111
    Helixi287 – 2937
    Helixi294 – 2996
    Beta strandi305 – 3084
    Helixi313 – 3164
    Beta strandi324 – 3307
    Beta strandi338 – 34710
    Beta strandi349 – 3513
    Helixi353 – 3619
    Beta strandi387 – 3893

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HKFX-ray2.01P83-91[»]
    3IAIX-ray2.20A/B/C/D137-391[»]
    ProteinModelPortaliQ16790.
    SMRiQ16790. Positions 139-391.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ16790.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini38 – 414377ExtracellularAdd
    BLAST
    Topological domaini436 – 45924CytoplasmicAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei415 – 43521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni38 – 11275Proteoglycan-like (PG)Add
    BLAST
    Regioni113 – 414302CatalyticAdd
    BLAST
    Regioni332 – 3332Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3338.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiQ16790.
    KOiK01672.
    OMAiSRYFRYE.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiQ16790.
    TreeFamiTF316425.

    Family and domain databases

    Gene3Di3.10.200.10. 1 hit.
    InterProiIPR018429. CA9.
    IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF18. PTHR18952:SF18. 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q16790-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPVHPQRL PRMQEDSPLG    50
    GGSSGEDDPL GEEDLPSEED SPREEDPPGE EDLPGEEDLP GEEDLPEVKP 100
    KSEEEGSLKL EDLPTVEAPG DPQEPQNNAH RDKEGDDQSH WRYGGDPPWP 150
    RVSPACAGRF QSPVDIRPQL AAFCPALRPL ELLGFQLPPL PELRLRNNGH 200
    SVQLTLPPGL EMALGPGREY RALQLHLHWG AAGRPGSEHT VEGHRFPAEI 250
    HVVHLSTAFA RVDEALGRPG GLAVLAAFLE EGPEENSAYE QLLSRLEEIA 300
    EEGSETQVPG LDISALLPSD FSRYFQYEGS LTTPPCAQGV IWTVFNQTVM 350
    LSAKQLHTLS DTLWGPGDSR LQLNFRATQP LNGRVIEASF PAGVDSSPRA 400
    AEPVQLNSCL AAGDILALVF GLLFAVTSVA FLVQMRRQHR RGTKGGVSYR 450
    PAEVAETGA 459
    Length:459
    Mass (Da):49,698
    Last modified:December 6, 2005 - v2
    Checksum:iBA67195483F0F5CE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti33 – 331V → M.2 Publications
    Corresponds to variant rs2071676 [ dbSNP | Ensembl ].
    VAR_010787
    Natural varianti326 – 3261Q → R.
    Corresponds to variant rs3829078 [ dbSNP | Ensembl ].
    VAR_020049

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66839 mRNA. Translation: CAA47315.1.
    AJ010588 mRNA. Translation: CAB82444.1.
    AL133410, AL357874 Genomic DNA. Translation: CAI10985.1.
    AL357874, AL133410 Genomic DNA. Translation: CAI13455.1.
    CH471071 Genomic DNA. Translation: EAW58359.1.
    BC014950 mRNA. Translation: AAH14950.1.
    CCDSiCCDS6585.1.
    PIRiI38013.
    RefSeqiNP_001207.2. NM_001216.2.
    UniGeneiHs.63287.

    Genome annotation databases

    EnsembliENST00000378357; ENSP00000367608; ENSG00000107159.
    GeneIDi768.
    KEGGihsa:768.
    UCSCiuc003zxo.4. human.

    Polymorphism databases

    DMDMi83300925.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X66839 mRNA. Translation: CAA47315.1 .
    AJ010588 mRNA. Translation: CAB82444.1 .
    AL133410 , AL357874 Genomic DNA. Translation: CAI10985.1 .
    AL357874 , AL133410 Genomic DNA. Translation: CAI13455.1 .
    CH471071 Genomic DNA. Translation: EAW58359.1 .
    BC014950 mRNA. Translation: AAH14950.1 .
    CCDSi CCDS6585.1.
    PIRi I38013.
    RefSeqi NP_001207.2. NM_001216.2.
    UniGenei Hs.63287.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HKF X-ray 2.01 P 83-91 [» ]
    3IAI X-ray 2.20 A/B/C/D 137-391 [» ]
    ProteinModelPortali Q16790.
    SMRi Q16790. Positions 139-391.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107223. 31 interactions.
    DIPi DIP-48973N.
    STRINGi 9606.ENSP00000367608.

    Chemistry

    BindingDBi Q16790.
    ChEMBLi CHEMBL3594.

    PTM databases

    PhosphoSitei Q16790.

    Polymorphism databases

    DMDMi 83300925.

    Proteomic databases

    MaxQBi Q16790.
    PaxDbi Q16790.
    PRIDEi Q16790.

    Protocols and materials databases

    DNASUi 768.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378357 ; ENSP00000367608 ; ENSG00000107159 .
    GeneIDi 768.
    KEGGi hsa:768.
    UCSCi uc003zxo.4. human.

    Organism-specific databases

    CTDi 768.
    GeneCardsi GC09P035673.
    H-InvDB HIX0008019.
    HGNCi HGNC:1383. CA9.
    HPAi CAB005100.
    CAB017107.
    MIMi 603179. gene.
    neXtProti NX_Q16790.
    PharmGKBi PA25998.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi Q16790.
    KOi K01672.
    OMAi SRYFRYE.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi Q16790.
    TreeFami TF316425.

    Enzyme and pathway databases

    BRENDAi 4.2.1.1. 2681.
    Reactomei REACT_121092. Regulation of gene expression by Hypoxia-inducible Factor.
    REACT_121123. Reversible hydration of carbon dioxide.

    Miscellaneous databases

    EvolutionaryTracei Q16790.
    GeneWikii Carbonic_anhydrase_9.
    GenomeRNAii 768.
    NextBioi 3106.
    PROi Q16790.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16790.
    CleanExi HS_CA9.
    Genevestigatori Q16790.

    Family and domain databases

    Gene3Di 3.10.200.10. 1 hit.
    InterProi IPR018429. CA9.
    IPR001148. Carbonic_anhydrase_a.
    IPR023561. Carbonic_anhydrase_a-class.
    IPR018338. Carbonic_anhydrase_a-class_CS.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF18. PTHR18952:SF18. 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. "Cloning and characterization of MN, a human tumor-associated protein with a domain homologous to carbonic anhydrase and a putative helix-loop-helix DNA binding segment."
      Pastorek J., Pastorekova S., Callebaut I., Mornon J.-P., Zelnik V., Opavsky R., Zat'Ovicova M., Liao S., Portetelle D., Stanbridge E.J., Zavada J., Burny A., Kettmann R.
      Oncogene 9:2877-2888(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, VARIANT MET-33.
      Tissue: Carcinoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Renal cell carcinoma.
    3. "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].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 MET-33.
      Tissue: Colon.
    6. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 38-52.
    7. "A novel quasi-viral agent, MaTu, is a two-component system."
      Pastorekova S., Zavadova Z., Kostal M., Babusikova O., Zavada J.
      Virology 187:620-626(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    8. "Expression of MaTu-MN protein in human tumor cultures and in clinical specimens."
      Zavada J., Zavadova Z., Pastorekova S., Ciampor F., Pastorek J., Zelnik V.
      Int. J. Cancer 54:268-274(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    9. "The role of carbonic anhydrase IX overexpression in kidney cancer."
      Dorai T., Sawczuk I.S., Pastorek J., Wiernik P.H., Dutcher J.P.
      Eur. J. Cancer 41:2935-2947(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-449.
    10. "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.
    11. "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.
    12. Cited for: FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346, DISULFIDE BONDS.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "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.
    15. "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.
    16. "Stabilization of antibody structure upon association to a human carbonic anhydrase IX epitope studied by X-ray crystallography, microcalorimetry, and molecular dynamics simulations."
      Kral V., Mader P., Collard R., Fabry M., Horejsi M., Rezacova P., Kozisek M., Zavada J., Sedlacek J., Rulisek L., Brynda J.
      Proteins 71:1275-1287(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 83-91 IN COMPLEX WITH SPECIFIC ANTIBODIES.
    17. Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-391 IN COMPLEX WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, GLYCOSYLATION AT ASN-346, DISULFIDE BOND, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiCAH9_HUMAN
    AccessioniPrimary (citable) accession number: Q16790
    Secondary accession number(s): Q5T4R1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: December 6, 2005
    Last modified: October 1, 2014
    This is version 142 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

    3D-structure, 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3