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O43570

- CAH12_HUMAN

UniProt

O43570 - CAH12_HUMAN

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Protein

Carbonic anhydrase 12

Gene

CA12

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  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
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: 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

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

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

BgeeiO43570.
CleanExiHS_CA12.
ExpressionAtlasiO43570. baseline and differential.
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 – 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
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[»]
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. 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

        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 .
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:
PDBei
RCSB PDBi
PDBji
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 CHEMBL3242.
DrugBanki DB00562. Benzthiazide.
DB00999. Hydrochlorothiazide.
DB00774. Hydroflumethiazide.
DB00909. Zonisamide.
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.
GeneTreei ENSGT00760000118915.
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

Bgeei O43570.
CleanExi HS_CA12.
ExpressionAtlasi O43570. baseline and differential.
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

« 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: November 26, 2014
This is version 145 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