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O43570

- CAH12_HUMAN

UniProt

O43570 - CAH12_HUMAN

Protein

Carbonic anhydrase 12

Gene

CA12

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 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Reversible hydration of carbon dioxide.

    Catalytic activityi

    H2CO3 = CO2 + H2O.

    Cofactori

    Zinc.

    Enzyme regulationi

    Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA), benzenesulfonamide and derivatives (4-carboxyethylbenzene-sulfonamide, 4-carboxyethylbenzene-sulfonamide ethyl ester, 4-(acetyl-2-aminoethyl)benzene-sulfonamide, 4-aminoethylbenzene-sulfonamide) and Foscarnet (phosphonoformate trisodium salt).6 Publications

    Kineticsi

    1. KM=12.0 mM for CO21 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei94 – 941Proton acceptorBy similarity
    Metal bindingi119 – 1191Zinc; catalytic
    Metal bindingi121 – 1211Zinc; catalytic
    Metal bindingi145 – 1451Zinc; catalytic
    Active sitei154 – 1541By similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. bicarbonate transport Source: Reactome
    2. one-carbon metabolic process Source: InterPro
    3. 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 12 (EC:4.2.1.1)
    Alternative name(s):
    Carbonate dehydratase XII
    Carbonic anhydrase XII
    Short name:
    CA-XII
    Tumor antigen HOM-RCC-3.1.3
    Gene namesi
    Name:CA12
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:1371. CA12.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: ProtInc
    2. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Hyperchlorhidrosis, isolated (HCHLH) [MIM:143860]: A disorder characterized by excessive sweating and increased sweat chloride levels. Affected individuals suffer from episodes of hyponatremic dehydration and report increased amounts of visible salt precipitates in sweat.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti143 – 1431E → K in HCHLH; mild reduction of activity; mutant enzyme is highly inhibited by acetazolamide and shows higher sensitivity to inhibition by anions compared to wild-type; the mutation affects the chloride-mediated negative feedback regulation of the enzyme leading to excessive chloride secretion in sweat. 1 Publication
    VAR_065292

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi143860. phenotype.
    PharmGKBiPA25987.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Chaini25 – 354330Carbonic anhydrase 12PRO_0000004248Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi28 – 281N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi50 ↔ 2301 Publication
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi162 – 1621N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiO43570.
    PaxDbiO43570.
    PRIDEiO43570.

    PTM databases

    PhosphoSiteiO43570.

    Expressioni

    Tissue specificityi

    Highly expressed in colon, kidney, prostate, intestine and activated lymphocytes. Expressed at much higher levels in the renal cell cancers than in surrounding normal kidney tissue. Moderately expressed in pancreas, ovary and testis.

    Gene expression databases

    ArrayExpressiO43570.
    BgeeiO43570.
    CleanExiHS_CA12.
    GenevestigatoriO43570.

    Organism-specific databases

    HPAiCAB025181.
    CAB062549.
    HPA008773.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi107225. 7 interactions.
    IntActiO43570. 10 interactions.
    MINTiMINT-1392387.
    STRINGi9606.ENSP00000178638.

    Structurei

    Secondary structure

    1
    354
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 363
    Helixi40 – 423
    Helixi43 – 464
    Helixi48 – 514
    Beta strandi52 – 543
    Helixi62 – 643
    Beta strandi65 – 673
    Beta strandi75 – 784
    Beta strandi85 – 917
    Beta strandi93 – 997
    Beta strandi105 – 1117
    Beta strandi113 – 12210
    Beta strandi132 – 1354
    Beta strandi141 – 15010
    Turni151 – 1533
    Helixi157 – 1604
    Beta strandi167 – 17812
    Helixi181 – 1877
    Helixi188 – 1925
    Beta strandi199 – 2035
    Helixi207 – 2104
    Beta strandi218 – 2236
    Beta strandi234 – 2418
    Beta strandi243 – 2464
    Helixi247 – 2559
    Beta strandi258 – 2603
    Beta strandi285 – 2895

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JCZX-ray1.55A/B30-291[»]
    1JD0X-ray1.50A/B30-291[»]
    4HT2X-ray1.45A/B/C/D30-291[»]
    4KP5X-ray1.45A/B/C/D30-291[»]
    4KP8X-ray1.80A/B/C/D30-291[»]
    ProteinModelPortaliO43570.
    SMRiO43570. Positions 31-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43570.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 301277ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini323 – 35432CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei302 – 32221HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni226 – 2272Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the alpha-carbonic anhydrase family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG3338.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiO43570.
    KOiK01672.
    OMAiPPCYPTV.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiO43570.
    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.
    IPR018430. Carbonic_anhydrase_CA12.
    [Graphical view]
    PANTHERiPTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF19. PTHR18952:SF19. 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 (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O43570-1) [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

    MPRRSLHAAA VLLLVILKEQ PSSPAPVNGS KWTYFGPDGE NSWSKKYPSC    50
    GGLLQSPIDL HSDILQYDAS LTPLEFQGYN LSANKQFLLT NNGHSVKLNL 100
    PSDMHIQGLQ SRYSATQLHL HWGNPNDPHG SEHTVSGQHF AAELHIVHYN 150
    SDLYPDASTA SNKSEGLAVL AVLIEMGSFN PSYDKIFSHL QHVKYKGQEA 200
    FVPGFNIEEL LPERTAEYYR YRGSLTTPPC NPTVLWTVFR NPVQISQEQL 250
    LALETALYCT HMDDPSPREM INNFRQVQKF DERLVYTSFS QVQVCTAAGL 300
    SLGIILSLAL AGILGICIVV VVSIWLFRRK SIKKGDNKGV IYKPATKMET 350
    EAHA 354
    Length:354
    Mass (Da):39,451
    Last modified:June 1, 1998 - v1
    Checksum:i9016216BF2CA6C0C
    GO
    Isoform 2 (identifier: O43570-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         292-302: Missing.

    Show »
    Length:343
    Mass (Da):38,408
    Checksum:i87FD35255B137D18
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti305 – 3051I → T in BAG38121. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti143 – 1431E → K in HCHLH; mild reduction of activity; mutant enzyme is highly inhibited by acetazolamide and shows higher sensitivity to inhibition by anions compared to wild-type; the mutation affects the chloride-mediated negative feedback regulation of the enzyme leading to excessive chloride secretion in sweat. 1 Publication
    VAR_065292

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei292 – 30211Missing in isoform 2. 2 PublicationsVSP_000772Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051882 mRNA. Translation: AAC39789.1.
    AF037335 mRNA. Translation: AAC63952.1.
    BT006656 mRNA. Translation: AAP35302.1.
    AK315769 mRNA. Translation: BAG38121.1.
    BC000278 mRNA. Translation: AAH00278.1.
    BC011691 mRNA. Translation: AAH11691.1.
    BC023981 mRNA. Translation: AAH23981.1.
    CCDSiCCDS10185.1. [O43570-1]
    CCDS10186.1. [O43570-2]
    RefSeqiNP_001209.1. NM_001218.4. [O43570-1]
    NP_996808.1. NM_206925.2. [O43570-2]
    UniGeneiHs.210995.

    Genome annotation databases

    EnsembliENST00000178638; ENSP00000178638; ENSG00000074410. [O43570-1]
    ENST00000344366; ENSP00000343088; ENSG00000074410. [O43570-2]
    GeneIDi771.
    KEGGihsa:771.
    UCSCiuc002amc.3. human. [O43570-1]
    uc002amd.3. human. [O43570-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF051882 mRNA. Translation: AAC39789.1 .
    AF037335 mRNA. Translation: AAC63952.1 .
    BT006656 mRNA. Translation: AAP35302.1 .
    AK315769 mRNA. Translation: BAG38121.1 .
    BC000278 mRNA. Translation: AAH00278.1 .
    BC011691 mRNA. Translation: AAH11691.1 .
    BC023981 mRNA. Translation: AAH23981.1 .
    CCDSi CCDS10185.1. [O43570-1 ]
    CCDS10186.1. [O43570-2 ]
    RefSeqi NP_001209.1. NM_001218.4. [O43570-1 ]
    NP_996808.1. NM_206925.2. [O43570-2 ]
    UniGenei Hs.210995.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JCZ X-ray 1.55 A/B 30-291 [» ]
    1JD0 X-ray 1.50 A/B 30-291 [» ]
    4HT2 X-ray 1.45 A/B/C/D 30-291 [» ]
    4KP5 X-ray 1.45 A/B/C/D 30-291 [» ]
    4KP8 X-ray 1.80 A/B/C/D 30-291 [» ]
    ProteinModelPortali O43570.
    SMRi O43570. Positions 31-291.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107225. 7 interactions.
    IntActi O43570. 10 interactions.
    MINTi MINT-1392387.
    STRINGi 9606.ENSP00000178638.

    Chemistry

    BindingDBi O43570.
    ChEMBLi CHEMBL2095180.
    DrugBanki DB00819. Acetazolamide.
    GuidetoPHARMACOLOGYi 2747.

    PTM databases

    PhosphoSitei O43570.

    Proteomic databases

    MaxQBi O43570.
    PaxDbi O43570.
    PRIDEi O43570.

    Protocols and materials databases

    DNASUi 771.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000178638 ; ENSP00000178638 ; ENSG00000074410 . [O43570-1 ]
    ENST00000344366 ; ENSP00000343088 ; ENSG00000074410 . [O43570-2 ]
    GeneIDi 771.
    KEGGi hsa:771.
    UCSCi uc002amc.3. human. [O43570-1 ]
    uc002amd.3. human. [O43570-2 ]

    Organism-specific databases

    CTDi 771.
    GeneCardsi GC15M063613.
    HGNCi HGNC:1371. CA12.
    HPAi CAB025181.
    CAB062549.
    HPA008773.
    MIMi 143860. phenotype.
    603263. gene.
    neXtProti NX_O43570.
    PharmGKBi PA25987.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG3338.
    HOGENOMi HOG000112637.
    HOVERGENi HBG002837.
    InParanoidi O43570.
    KOi K01672.
    OMAi PPCYPTV.
    OrthoDBi EOG7WMCK7.
    PhylomeDBi O43570.
    TreeFami TF316425.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi CA12. human.
    EvolutionaryTracei O43570.
    GeneWikii CA12.
    GenomeRNAii 771.
    NextBioi 3114.
    PROi O43570.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43570.
    Bgeei O43570.
    CleanExi HS_CA12.
    Genevestigatori O43570.

    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.
    IPR018430. Carbonic_anhydrase_CA12.
    [Graphical view ]
    PANTHERi PTHR18952. PTHR18952. 1 hit.
    PTHR18952:SF19. PTHR18952:SF19. 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 carbonic anhydrase XII: cDNA cloning, expression, and chromosomal localization of a carbonic anhydrase gene that is overexpressed in some renal cell cancers."
      Tuereci O., Sahin U., Vollmar E., Siemer S., Goettert E., Seitz G., Parkkila A.-K., Shah G.N., Grubb J.H., Pfreundschuh M., Sly W.S.
      Proc. Natl. Acad. Sci. U.S.A. 95:7608-7613(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
      Tissue: Renal cell carcinoma.
    2. "Down-regulation of transmembrane carbonic anhydrases in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgenes."
      Ivanov S.V., Kuzmin I., Wei M.-H., Pack S., Geil L., Johnson B.E., Stanbridge E.J., Lerman M.I.
      Proc. Natl. Acad. Sci. U.S.A. 95:12596-12601(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    3. "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] (ISOFORM 2).
    4. "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] (ISOFORM 1).
      Tissue: Trachea.
    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] (ISOFORMS 1 AND 2).
      Tissue: Eye and Kidney.
    6. "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.
    7. "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.
    8. "Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II."
      Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S., Kooren J., Mallik S., Christianson D.W.
      J. Am. Chem. Soc. 129:5528-5537(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION.
    9. "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.
    10. "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.
    11. "Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide."
      Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.
      Proteins 74:164-175(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    12. "Crystal structure of the dimeric extracellular domain of human carbonic anhydrase XII, a bitopic membrane protein overexpressed in certain cancer tumor cells."
      Whittington D.A., Waheed A., Ulmasov B., Shah G.N., Grubb J.H., Sly W.S., Christianson D.W.
      Proc. Natl. Acad. Sci. U.S.A. 98:9545-9550(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 30-291 IN COMPLEX WITH ZINC ION AND THE INHIBITOR ACETAZOLAMIDE, DISULFIDE BOND, SUBUNIT.
    13. "Hyperchlorhidrosis caused by homozygous mutation in CA12, encoding carbonic anhydrase XII."
      Feldshtein M., Elkrinawi S., Yerushalmi B., Marcus B., Vullo D., Romi H., Ofir R., Landau D., Sivan S., Supuran C.T., Birk O.S.
      Am. J. Hum. Genet. 87:713-720(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT HCHLH LYS-143.

    Entry informationi

    Entry nameiCAH12_HUMAN
    AccessioniPrimary (citable) accession number: O43570
    Secondary accession number(s): B2RE24, Q53YE5, Q9BWG2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 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 15
      Human chromosome 15: 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