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Protein

Carbonic anhydrase 12

Gene

CA12

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Reversible hydration of carbon dioxide.

Catalytic activityi

H2CO3 = CO2 + H2O.

Cofactori

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

    • carbonate dehydratase activity Source: ProtInc
    • zinc ion binding Source: ProtInc

    GO - Biological processi

    • bicarbonate transport Source: Reactome
    • chloride ion homeostasis Source: UniProtKB
    • one-carbon metabolic process Source: InterPro
    • small molecule metabolic process Source: Reactome
    Complete GO annotation...

    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 Componenti: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:1371. CA12.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini25 – 301277ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei302 – 32221HelicalSequence AnalysisAdd
    BLAST
    Topological domaini323 – 35432CytoplasmicSequence AnalysisAdd
    BLAST

    GO - Cellular componenti

    • integral component of membrane Source: ProtInc
    • plasma membrane Source: Reactome
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Hyperchlorhidrosis, isolated (HCHLH)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionA 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.

    See also OMIM:143860
    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.

    Chemistry

    DrugBankiDB00562. Benzthiazide.
    DB00999. Hydrochlorothiazide.
    DB00774. Hydroflumethiazide.
    DB00909. Zonisamide.

    Polymorphism and mutation databases

    BioMutaiCA12.

    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

    BgeeiO43570.
    CleanExiHS_CA12.
    ExpressionAtlasiO43570. baseline and differential.
    GenevisibleiO43570. HS.

    Organism-specific databases

    HPAiCAB025181.
    CAB062549.
    CAB068179.
    HPA008773.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi107225. 8 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 – 363Combined sources
    Helixi40 – 423Combined sources
    Helixi43 – 464Combined sources
    Helixi48 – 514Combined sources
    Beta strandi52 – 543Combined sources
    Helixi62 – 643Combined sources
    Beta strandi65 – 673Combined sources
    Beta strandi75 – 784Combined sources
    Beta strandi85 – 917Combined sources
    Beta strandi93 – 997Combined sources
    Beta strandi105 – 1117Combined sources
    Beta strandi113 – 12210Combined sources
    Beta strandi132 – 1354Combined sources
    Beta strandi141 – 15010Combined sources
    Turni151 – 1533Combined sources
    Helixi157 – 1604Combined sources
    Beta strandi167 – 17812Combined sources
    Helixi181 – 1877Combined sources
    Helixi188 – 1925Combined sources
    Beta strandi199 – 2035Combined sources
    Helixi207 – 2104Combined sources
    Turni213 – 2164Combined sources
    Beta strandi218 – 2236Combined sources
    Beta strandi234 – 2418Combined sources
    Beta strandi243 – 2464Combined sources
    Helixi247 – 2559Combined sources
    Beta strandi258 – 2603Combined sources
    Beta strandi285 – 2895Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4Q0LX-ray2.00A/B/C/D30-291[»]
    4QJ0X-ray1.55A/B/C/D30-291[»]
    4QJOX-ray1.80A/B/C/D30-291[»]
    4QJWX-ray1.55A/B/C/D30-291[»]
    ProteinModelPortaliO43570.
    SMRiO43570. Positions 31-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43570.

    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.
    GeneTreeiENSGT00760000118915.
    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. AlignAdd to basket

    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

            10         20         30         40         50
    MPRRSLHAAA VLLLVILKEQ PSSPAPVNGS KWTYFGPDGE NSWSKKYPSC
    60 70 80 90 100
    GGLLQSPIDL HSDILQYDAS LTPLEFQGYN LSANKQFLLT NNGHSVKLNL
    110 120 130 140 150
    PSDMHIQGLQ SRYSATQLHL HWGNPNDPHG SEHTVSGQHF AAELHIVHYN
    160 170 180 190 200
    SDLYPDASTA SNKSEGLAVL AVLIEMGSFN PSYDKIFSHL QHVKYKGQEA
    210 220 230 240 250
    FVPGFNIEEL LPERTAEYYR YRGSLTTPPC NPTVLWTVFR NPVQISQEQL
    260 270 280 290 300
    LALETALYCT HMDDPSPREM INNFRQVQKF DERLVYTSFS QVQVCTAAGL
    310 320 330 340 350
    SLGIILSLAL AGILGICIVV VVSIWLFRRK SIKKGDNKGV IYKPATKMET

    EAHA
    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:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    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[»]
    4Q0LX-ray2.00A/B/C/D30-291[»]
    4QJ0X-ray1.55A/B/C/D30-291[»]
    4QJOX-ray1.80A/B/C/D30-291[»]
    4QJWX-ray1.55A/B/C/D30-291[»]
    ProteinModelPortaliO43570.
    SMRiO43570. Positions 31-291.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi107225. 8 interactions.
    IntActiO43570. 10 interactions.
    MINTiMINT-1392387.
    STRINGi9606.ENSP00000178638.

    Chemistry

    BindingDBiO43570.
    ChEMBLiCHEMBL3242.
    DrugBankiDB00562. Benzthiazide.
    DB00999. Hydrochlorothiazide.
    DB00774. Hydroflumethiazide.
    DB00909. Zonisamide.
    GuidetoPHARMACOLOGYi2747.

    PTM databases

    PhosphoSiteiO43570.

    Polymorphism and mutation databases

    BioMutaiCA12.

    Proteomic databases

    MaxQBiO43570.
    PaxDbiO43570.
    PRIDEiO43570.

    Protocols and materials databases

    DNASUi771.
    Structural Biology KnowledgebaseSearch...

    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]

    Organism-specific databases

    CTDi771.
    GeneCardsiGC15M063613.
    HGNCiHGNC:1371. CA12.
    HPAiCAB025181.
    CAB062549.
    CAB068179.
    HPA008773.
    MIMi143860. phenotype.
    603263. gene.
    neXtProtiNX_O43570.
    PharmGKBiPA25987.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG3338.
    GeneTreeiENSGT00760000118915.
    HOGENOMiHOG000112637.
    HOVERGENiHBG002837.
    InParanoidiO43570.
    KOiK01672.
    OMAiPPCYPTV.
    OrthoDBiEOG7WMCK7.
    PhylomeDBiO43570.
    TreeFamiTF316425.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSiCA12. human.
    EvolutionaryTraceiO43570.
    GeneWikiiCA12.
    GenomeRNAii771.
    NextBioi3114.
    PROiO43570.
    SOURCEiSearch...

    Gene expression databases

    BgeeiO43570.
    CleanExiHS_CA12.
    ExpressionAtlasiO43570. baseline and differential.
    GenevisibleiO43570. HS.

    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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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: June 24, 2015
    This is version 151 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.