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UniProtKB/Swiss-Prot entry P00918


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CAH2_HUMAN
Primary accession number P00918
Secondary accession numbers Q6FI12 Q96ET9
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    November 4, 2008 (Entry version 117)
Name and origin of the protein
Protein name Carbonic anhydrase 2
Synonyms EC 4.2.1.1
Carbonic anhydrase II
CA-II
Carbonate dehydratase II
Carbonic anhydrase C
CAC
Gene name
Name: CA2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/15.11.4687; PubMed=3108857 [NCBI, ExPASy, EBI, Israel, Japan]
Montgomery J.C., Venta P.J., Tashian R.E., Hewett-Emmett D.;
"Nucleotide sequence of human liver carbonic anhydrase II cDNA.";
Nucleic Acids Res. 15:4687-4687(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/0888-7543(87)90008-5; PubMed=3121496 [NCBI, ExPASy, EBI, Israel, Japan]
Murakami H., Marelich G.P., Grubb J.H., Kyle J.W., Sly W.S.;
"Cloning, expression, and sequence homologies of cDNA for human carbonic anhydrase II.";
Genomics 1:159-166(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-260.
PubMed=4207120 [NCBI, ExPASy, EBI, Israel, Japan]
Lin K.-T.D., Deutsch H.F.;
"Human carbonic anhydrases. XII. The complete primary structure of the C isozyme.";
J. Biol. Chem. 249:2329-2337(1974).
[6]
PROTEIN SEQUENCE OF 2-260.
PubMed=823150 [NCBI, ExPASy, EBI, Israel, Japan]
Henderson L.E., Henriksson D., Nyman P.O.;
"Primary structure of human carbonic anhydrase C.";
J. Biol. Chem. 251:5457-5463(1976).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
DOI=10.1016/0167-4781(85)90006-5; PubMed=3000449 [NCBI, ExPASy, EBI, Israel, Japan]
Venta P.J., Montgomery J.C., Hewett-Emmett D., Tashian R.E.;
"Comparison of the 5' regions of human and mouse carbonic anhydrase II genes and identification of possible regulatory elements.";
Biochim. Biophys. Acta 826:195-201(1985).
[8]
INTERACTION WITH SLC4A4.
DOI=10.1021/bi0353124; PubMed=14567693 [NCBI, ExPASy, EBI, Israel, Japan]
Alvarez B.V., Loiselle F.B., Supuran C.T., Schwartz G.J., Casey J.R.;
"Direct extracellular interaction between carbonic anhydrase IV and the human NBC1 sodium/bicarbonate co-transporter.";
Biochemistry 42:12321-12329(2003).
[9]
INTERACTION WITH SLC4A7.
DOI=10.1152/ajpcell.00382.2003; PubMed=14736710 [NCBI, ExPASy, EBI, Israel, Japan]
Loiselle F.B., Morgan P.E., Alvarez B.V., Casey J.R.;
"Regulation of the human NBC3 Na+/HCO3- cotransporter by carbonic anhydrase II and PKA.";
Am. J. Physiol. 286:C1423-C1433(2004).
[10]
INTERACTION WITH SLC4A4.
DOI=10.1113/jphysiol.2004.065110; PubMed=15218065 [NCBI, ExPASy, EBI, Israel, Japan]
Pushkin A., Abuladze N., Gross E., Newman D., Tatishchev S., Lee I., Fedotoff O., Bondar G., Azimov R., Ngyuen M., Kurtz I.;
"Molecular mechanism of kNBC1-carbonic anhydrase II interaction in proximal tubule cells.";
J. Physiol. (Lond.) 559:55-65(2004).
[11]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=4621826 [NCBI, ExPASy, EBI, Israel, Japan]
Liljas A., Kannan K.K., Bergsten P.-C., Waara I., Fridborg K., Strandberg B., Carlbom U., Jaerup L., Loevgren S., Petef M.;
"Crystal structure of human carbonic anhydrase C.";
Nature New Biol. 235:131-137(1972).
[12]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1002/prot.340040406; PubMed=3151019 [NCBI, ExPASy, EBI, Israel, Japan]
Eriksson A.E., Jones T.A., Liljas A.;
"Refined structure of human carbonic anhydrase II at 2.0-A resolution.";
Proteins 4:274-282(1988).
[13]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1002/prot.340040407; PubMed=3151020 [NCBI, ExPASy, EBI, Israel, Japan]
Eriksson A.E., Kylsten P.M., Jones T.A., Liljas A.;
"Crystallographic studies of inhibitor binding sites in human carbonic anhydrase II: a pentacoordinated binding of the SCN-ion to the zinc at high pH.";
Proteins 4:283-293(1988).
[14]
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
PubMed=9541386 [NCBI, ExPASy, EBI, Israel, Japan]
Stams T., Chen Y., Boriack-Sjodin P.A., Hurt J.D., Liao J., May J.A., Dean T., Laipis P., Silverman D.N., Christianson D.W.;
"Structures of murine carbonic anhydrase IV and human carbonic anhydrase II complexed with brinzolamide: molecular basis of isozyme-drug discrimination.";
Protein Sci. 7:556-563(1998).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1021/bi001649j; PubMed=11076507 [NCBI, ExPASy, EBI, Israel, Japan]
Cox J.D., Hunt J.A., Compher K.M., Fierke C.A., Christianson D.W.;
"Structural influence of hydrophobic core residues on metal binding and specificity in carbonic anhydrase II.";
Biochemistry 39:13687-13694(2000).
[16]
VARIANT JOGJAKARTA GLU-18.
DOI=10.1007/BF00484072; PubMed=6817747 [NCBI, ExPASy, EBI, Israel, Japan]
Jones G.L., Sofro A.S.M., Shaw D.C.;
"Chemical and enzymological characterization of an Indonesian variant of human erythrocyte carbonic anhydrase II, CAII Jogjakarta (17 Lys leads to Glu).";
Biochem. Genet. 20:979-1000(1982).
[17]
VARIANT MELBOURNE HIS-236.
DOI=10.1007/BF00274768; PubMed=6407977 [NCBI, ExPASy, EBI, Israel, Japan]
Jones G.L., Shaw D.C.;
"A chemical and enzymological comparison of the common major human erythrocyte carbonic anhydrase II, its minor component, and a new genetic variant, CA II Melbourne (237 Pro leads to His).";
Hum. Genet. 63:392-399(1983).
[18]
VARIANT OPTB3 TYR-107.
PubMed=1928091 [NCBI, ExPASy, EBI, Israel, Japan]
Venta P.J., Welty R.J., Johnson T.M., Sly W.S., Tashian R.E.;
"Carbonic anhydrase II deficiency syndrome in a Belgian family is caused by a point mutation at an invariant histidine residue (107 His-->Tyr): complete structure of the normal human CA II gene.";
Am. J. Hum. Genet. 49:1082-1090(1991).
[19]
VARIANT OPTB3 TYR-107.
PubMed=1542674 [NCBI, ExPASy, EBI, Israel, Japan]
Roth D.E., Venta P.J., Tashian R.E., Sly W.S.;
"Molecular basis of human carbonic anhydrase II deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 89:1804-1808(1992).
[20]
VARIANT OPTB3 TYR-107.
DOI=10.1007/s004390050068; PubMed=8834238 [NCBI, ExPASy, EBI, Israel, Japan]
Soda H., Yukizane S., Yoshida I., Koga Y., Aramaki S., Kato H.;
"A point mutation in exon 3 (His 107-->Tyr) in two unrelated Japanese patients with carbonic anhydrase II deficiency with central nervous system involvement.";
Hum. Genet. 97:435-437(1996).
[21]
VARIANT OPTB3 PRO-92.
DOI=10.1002/(SICI)1098-1004(1997)9:5<383::AID-HUMU1>3.3.CO;2-K; PubMed=9143915 [NCBI, ExPASy, EBI, Israel, Japan]
Hu P.Y., Lim E.J., Ciccolella J., Strisciuglio P., Sly W.S.;
"Seven novel mutations in carbonic anhydrase II deficiency syndrome identified by SSCP and direct sequencing analysis.";
Hum. Mutat. 9:383-387(1997).
[22]
VARIANTS OPTB3 PRO-92; TYR-94; TYR-107 AND ARG-144, AND CHARACTERIZATION OF VARIANTS TYR-94 AND ARG-144.
DOI=10.1002/humu.9266; PubMed=15300855 [NCBI, ExPASy, EBI, Israel, Japan]
Shah G.N., Bonapace G., Hu P.Y., Strisciuglio P., Sly W.S.;
"Carbonic anhydrase II deficiency syndrome (osteopetrosis with renal tubular acidosis and brain calcification): novel mutations in CA2 identified by direct sequencing expand the opportunity for genotype-phenotype correlation.";
Hum. Mutat. 24:272-272(2004).
Comments
  • FUNCTION: Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide.
  • CATALYTIC ACTIVITY: H2CO3 = CO2 + H2O.
  • COFACTOR: Zinc.
  • SUBUNIT: Interacts with SLC4A4. Interaction with SLC4A7 regulates SLC4A7 transporter activity.
  • SUBCELLULAR LOCATION: Cytoplasm.
  • DISEASE: Defects in CA2 are the cause of autosomal recessive osteopetrosis type 3 (OPTB3) [MIM:259730]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.
  • SIMILARITY: Belongs to the alpha-carbonic anhydrase family.
  • WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=CA2";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M77181; AAA51909.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77176; AAA51909.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77177; AAA51909.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77178; AAA51909.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77179; AAA51909.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M77180; AAA51909.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00339; CAA68426.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03251; CAA27012.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
J03037; AAA51908.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR536526; CAG38763.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR541875; CAG46673.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011949; AAH11949.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M36532; AAA51911.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A27175; CRHU2.
RefSeq NP_000058.1; -.
UniGene Hs.155097
3D structure databases
PDB
12CA; X-ray; 2.40 A; A=1-260.[ExPASy / RCSB / EBI]
1A42; X-ray; 2.25 A; A=1-260.[ExPASy / RCSB / EBI]
1AM6; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1AVN; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1BCD; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1BIC; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1BN1; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1BN3; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
1BN4; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1BNM; X-ray; 2.60 A; A=1-260.[ExPASy / RCSB / EBI]
1BNN; X-ray; 2.30 A; A=1-260.[ExPASy / RCSB / EBI]
1BNQ; X-ray; 2.40 A; A=1-260.[ExPASy / RCSB / EBI]
1BNT; X-ray; 2.15 A; A=1-260.[ExPASy / RCSB / EBI]
1BNU; X-ray; 2.15 A; A=1-260.[ExPASy / RCSB / EBI]
1BNV; X-ray; 2.40 A; A=1-260.[ExPASy / RCSB / EBI]
1BNW; X-ray; 2.25 A; A=1-260.[ExPASy / RCSB / EBI]
1BV3; X-ray; 1.85 A; A=1-260.[ExPASy / RCSB / EBI]
1CA2; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1CA3; X-ray; 2.30 A; A=1-260.[ExPASy / RCSB / EBI]
1CAH; X-ray; 1.88 A; A=1-260.[ExPASy / RCSB / EBI]
1CAI; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1CAJ; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1CAK; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1CAL; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
1CAM; X-ray; 1.70 A; A=1-260.[ExPASy / RCSB / EBI]
1CAN; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1CAO; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1CAY; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1CAZ; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1CCS; X-ray; 2.35 A; A=1-260.[ExPASy / RCSB / EBI]
1CCT; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
1CCU; X-ray; 2.25 A; A=1-260.[ExPASy / RCSB / EBI]
1CIL; X-ray; 1.60 A; A=1-260.[ExPASy / RCSB / EBI]
1CIM; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1CIN; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1CNB; X-ray; 2.35 A; A=1-260.[ExPASy / RCSB / EBI]
1CNC; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
1CNG; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1CNH; X-ray; 2.05 A; A=1-260.[ExPASy / RCSB / EBI]
1CNI; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1CNJ; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1CNK; X-ray; 2.15 A; A=1-260.[ExPASy / RCSB / EBI]
1CNW; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1CNX; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1CNY; X-ray; 2.30 A; A=1-260.[ExPASy / RCSB / EBI]
1CRA; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1CVA; X-ray; 2.25 A; A=1-260.[ExPASy / RCSB / EBI]
1CVB; X-ray; 2.40 A; A=1-260.[ExPASy / RCSB / EBI]
1CVC; X-ray; 2.30 A; A=1-260.[ExPASy / RCSB / EBI]
1CVD; X-ray; 2.20 A; A=5-259.[ExPASy / RCSB / EBI]
1CVE; X-ray; 2.25 A; A=1-260.[ExPASy / RCSB / EBI]
1CVF; X-ray; 2.25 A; A=1-260.[ExPASy / RCSB / EBI]
1CVH; X-ray; 2.30 A; A=5-259.[ExPASy / RCSB / EBI]
1DCA; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
1DCB; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1EOU; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1F2W; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1FQL; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1FQM; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1FQN; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1FQR; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1FR4; X-ray; 1.60 A; A=1-260.[ExPASy / RCSB / EBI]
1FR7; X-ray; 1.50 A; A/B=1-260.[ExPASy / RCSB / EBI]
1FSN; X-ray; 2.00 A; A/B=1-260.[ExPASy / RCSB / EBI]
1FSQ; X-ray; 2.00 A; A/B=1-260.[ExPASy / RCSB / EBI]
1FSR; X-ray; 2.00 A; A/B=1-260.[ExPASy / RCSB / EBI]
1G0E; X-ray; 1.60 A; A=1-260.[ExPASy / RCSB / EBI]
1G0F; X-ray; 1.60 A; A=1-260.[ExPASy / RCSB / EBI]
1G1D; X-ray; 2.04 A; A=1-260.[ExPASy / RCSB / EBI]
1G3Z; X-ray; 1.86 A; A=1-260.[ExPASy / RCSB / EBI]
1G45; X-ray; 1.83 A; A=1-260.[ExPASy / RCSB / EBI]
1G46; X-ray; 1.84 A; A=1-260.[ExPASy / RCSB / EBI]
1G48; X-ray; 1.86 A; A=1-260.[ExPASy / RCSB / EBI]
1G4J; X-ray; 1.84 A; A=1-260.[ExPASy / RCSB / EBI]
1G4O; X-ray; 1.96 A; A=1-260.[ExPASy / RCSB / EBI]
1G52; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1G53; X-ray; 1.94 A; A=1-260.[ExPASy / RCSB / EBI]
1G54; X-ray; 1.86 A; A=1-260.[ExPASy / RCSB / EBI]
1H4N; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1H9N; X-ray; 1.85 A; A=1-260.[ExPASy / RCSB / EBI]
1H9Q; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
1HCA; X-ray; 2.30 A; A=1-260.[ExPASy / RCSB / EBI]
1HEA; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1HEB; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1HEC; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1HED; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1HVA; X-ray; 2.30 A; A=1-260.[ExPASy / RCSB / EBI]
1I8Z; X-ray; 1.93 A; A=1-260.[ExPASy / RCSB / EBI]
1I90; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1I91; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1I9L; X-ray; 1.93 A; A=1-260.[ExPASy / RCSB / EBI]
1I9M; X-ray; 1.84 A; A=1-260.[ExPASy / RCSB / EBI]
1I9N; X-ray; 1.86 A; A=1-260.[ExPASy / RCSB / EBI]
1I9O; X-ray; 1.86 A; A=1-260.[ExPASy / RCSB / EBI]
1I9P; X-ray; 1.92 A; A=1-260.[ExPASy / RCSB / EBI]
1I9Q; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1IF4; X-ray; 1.93 A; A=1-260.[ExPASy / RCSB / EBI]
1IF5; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1IF6; X-ray; 2.09 A; A=1-260.[ExPASy / RCSB / EBI]
1IF7; X-ray; 1.98 A; A=1-260.[ExPASy / RCSB / EBI]
1IF8; X-ray; 1.94 A; A=1-260.[ExPASy / RCSB / EBI]
1IF9; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1KWQ; X-ray; 2.60 A; A=1-260.[ExPASy / RCSB / EBI]
1KWR; X-ray; 2.25 A; A=1-260.[ExPASy / RCSB / EBI]
1LG5; X-ray; 1.75 A; A=1-260.[ExPASy / RCSB / EBI]
1LG6; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
1LGD; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1LUG; X-ray; 0.95 A; A=2-260.[ExPASy / RCSB / EBI]
1LZV; X-ray; 2.30 A; A=1-260.[ExPASy / RCSB / EBI]
1MOO; X-ray; 1.05 A; A=1-260.[ExPASy / RCSB / EBI]
1MUA; X-ray; 1.70 A; A=4-259.[ExPASy / RCSB / EBI]
1OKL; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1OKM; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
1OKN; X-ray; 2.40 A; A=1-260.[ExPASy / RCSB / EBI]
1OQ5; X-ray; 1.50 A; A=1-260.[ExPASy / RCSB / EBI]
1RAY; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1RAZ; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1RZA; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1RZB; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1RZC; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1RZD; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1RZE; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1T9N; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1TB0; X-ray; 2.00 A; X=1-260.[ExPASy / RCSB / EBI]
1TBT; X-ray; 2.00 A; X=1-260.[ExPASy / RCSB / EBI]
1TE3; X-ray; 2.00 A; X=1-260.[ExPASy / RCSB / EBI]
1TEQ; X-ray; 2.00 A; X=1-260.[ExPASy / RCSB / EBI]
1TEU; X-ray; 2.00 A; X=1-260.[ExPASy / RCSB / EBI]
1TG3; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1TG9; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1TH9; X-ray; 1.63 A; A=1-260.[ExPASy / RCSB / EBI]
1THK; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1TTM; X-ray; 1.95 A; A=1-260.[ExPASy / RCSB / EBI]
1UGA; X-ray; 2.00 A; A=3-260.[ExPASy / RCSB / EBI]
1UGB; X-ray; 2.00 A; A=3-260.[ExPASy / RCSB / EBI]
1UGC; X-ray; 2.00 A; A=3-260.[ExPASy / RCSB / EBI]
1UGD; X-ray; 2.00 A; A=3-260.[ExPASy / RCSB / EBI]
1UGE; X-ray; 1.90 A; A=3-260.[ExPASy / RCSB / EBI]
1UGF; X-ray; 2.00 A; A=3-260.[ExPASy / RCSB / EBI]
1UGG; X-ray; 2.20 A; A=3-260.[ExPASy / RCSB / EBI]
1XEG; X-ray; 1.81 A; A=1-260.[ExPASy / RCSB / EBI]
1XEV; X-ray; 2.20 A; A/B/C/D=1-260.[ExPASy / RCSB / EBI]
1XPZ; X-ray; 2.02 A; A=3-260.[ExPASy / RCSB / EBI]
1XQ0; X-ray; 1.76 A; A=1-260.[ExPASy / RCSB / EBI]
1YDA; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1YDB; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
1YDC; X-ray; 1.95 A; A=1-260.[ExPASy / RCSB / EBI]
1YDD; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
1YO0; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1YO1; X-ray; 1.70 A; A=1-260.[ExPASy / RCSB / EBI]
1YO2; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
1Z9Y; X-ray; 1.66 A; A=1-260.[ExPASy / RCSB / EBI]
1ZE8; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1ZFK; X-ray; 1.56 A; A=1-260.[ExPASy / RCSB / EBI]
1ZFQ; X-ray; 1.55 A; A=1-260.[ExPASy / RCSB / EBI]
1ZGE; X-ray; 1.65 A; A=1-260.[ExPASy / RCSB / EBI]
1ZGF; X-ray; 1.75 A; A=1-260.[ExPASy / RCSB / EBI]
1ZH9; X-ray; 1.70 A; A=1-260.[ExPASy / RCSB / EBI]
1ZSA; X-ray; 2.50 A; A=1-260.[ExPASy / RCSB / EBI]
1ZSB; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
1ZSC; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
2ABE; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
2AW1; X-ray; 1.46 A; A=2-260.[ExPASy / RCSB / EBI]
2AX2; X-ray; 1.50 A; A=1-260.[ExPASy / RCSB / EBI]
2CA2; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
2CBA; X-ray; 1.54 A; A=1-260.[ExPASy / RCSB / EBI]
2CBB; X-ray; 1.67 A; A=1-260.[ExPASy / RCSB / EBI]
2CBC; X-ray; 1.88 A; A=1-260.[ExPASy / RCSB / EBI]
2CBD; X-ray; 1.67 A; A=1-260.[ExPASy / RCSB / EBI]
2CBE; X-ray; 1.82 A; A=1-260.[ExPASy / RCSB / EBI]
2EU2; X-ray; 1.15 A; A=1-260.[ExPASy / RCSB / EBI]
2EU3; X-ray; 1.60 A; A=1-260.[ExPASy / RCSB / EBI]
2EZ7; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
2F14; X-ray; 1.71 A; A=1-260.[ExPASy / RCSB / EBI]
2FMG; X-ray; 1.60 A; A=1-260.[ExPASy / RCSB / EBI]
2FMZ; X-ray; 1.60 A; A=1-260.[ExPASy / RCSB / EBI]
2FNK; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
2FNM; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
2FNN; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
2FOQ; X-ray; 1.25 A; A=1-260.[ExPASy / RCSB / EBI]
2FOS; X-ray; 1.10 A; A=1-260.[ExPASy / RCSB / EBI]
2FOU; X-ray; 0.99 A; A=1-260.[ExPASy / RCSB / EBI]
2FOV; X-ray; 1.15 A; A=1-260.[ExPASy / RCSB / EBI]
2GD8; X-ray; 1.46 A; A=2-260.[ExPASy / RCSB / EBI]
2GEH; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
2H15; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
2H4N; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
2HD6; X-ray; 1.80 A; A=2-260.[ExPASy / RCSB / EBI]
2HKK; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
2HL4; X-ray; 1.55 A; A=2-260.[ExPASy / RCSB / EBI]
2HNC; X-ray; 1.55 A; A=2-260.[ExPASy / RCSB / EBI]
2HOC; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
2ILI; X-ray; 1.05 A; A=2-260.[ExPASy / RCSB / EBI]
2NNG; X-ray; 1.20 A; A=1-260.[ExPASy / RCSB / EBI]
2NNO; X-ray; 1.01 A; A=1-260.[ExPASy / RCSB / EBI]
2NNS; X-ray; 1.03 A; A=1-260.[ExPASy / RCSB / EBI]
2NNV; X-ray; 1.10 A; A=1-260.[ExPASy / RCSB / EBI]
2NWO; X-ray; 1.70 A; A=1-260.[ExPASy / RCSB / EBI]
2NWP; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
2NWY; X-ray; 1.65 A; A=1-260.[ExPASy / RCSB / EBI]
2NWZ; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
2NXR; X-ray; 1.70 A; A=1-260.[ExPASy / RCSB / EBI]
2NXS; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
2NXT; X-ray; 1.15 A; A=1-260.[ExPASy / RCSB / EBI]
2O4Z; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
2OSF; X-ray; 1.60 A; A=2-260.[ExPASy / RCSB / EBI]
2OSM; X-ray; 1.60 A; A=2-260.[ExPASy / RCSB / EBI]
2POU; X-ray; 1.60 A; A=1-260.[ExPASy / RCSB / EBI]
2POV; X-ray; 1.60 A; A=1-259.[ExPASy / RCSB / EBI]
2POW; X-ray; 1.75 A; A=1-260.[ExPASy / RCSB / EBI]
2Q1B; X-ray; 1.70 A; A=1-260.[ExPASy / RCSB / EBI]
2Q38; X-ray; 1.95 A; A=1-260.[ExPASy / RCSB / EBI]
2QO8; X-ray; 1.40 A; A=2-260.[ExPASy / RCSB / EBI]
2QOA; X-ray; 1.60 A; A=2-260.[ExPASy / RCSB / EBI]
2QP6; X-ray; 1.45 A; A=2-260.[ExPASy / RCSB / EBI]
3B4F; X-ray; 1.89 A; A=1-260.[ExPASy / RCSB / EBI]
3BL0; X-ray; 1.90 A; A=1-260.[ExPASy / RCSB / EBI]
3BL1; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
3CA2; X-ray; 2.00 A; A=1-260.[ExPASy / RCSB / EBI]
3CAJ; X-ray; 1.80 A; A=1-260.[ExPASy / RCSB / EBI]
3CYU; X-ray; 1.70 A; A=1-260.[ExPASy / RCSB / EBI]
4CA2; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
4CAC; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
5CA2; X-ray; 2.10 A; A=1-260.[ExPASy / RCSB / EBI]
5CAC; X-ray; 2.20 A; A=1-260.[ExPASy / RCSB / EBI]
6CA2; X-ray; 2.50 A; A=1-260.[ExPASy / RCSB / EBI]
7CA2; X-ray; 2.40 A; A=1-260.[ExPASy / RCSB / EBI]
8CA2; X-ray; 2.40 A; A=1-260.[ExPASy / RCSB / EBI]
9CA2; X-ray; 2.80 A; A=1-260.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 12CA; -.
1A42; -.
1AM6; -.
1AVN; -.
1BCD; -.
1BIC; -.
1BN1; -.
1BN3; -.
1BN4; -.
1BNM; -.
1BNN; -.
1BNQ; -.
1BNT; -.
1BNU; -.
1BNV; -.
1BNW; -.
1BV3; -.
1CA2; -.
1CA3; -.
1CAH; -.
1CAI; -.
1CAJ; -.
1CAK; -.
1CAL; -.
1CAM; -.
1CAN; -.
1CAO; -.
1CAY; -.
1CAZ; -.
1CCS; -.
1CCT; -.
1CCU; -.
1CIL; -.
1CIM; -.
1CIN; -.
1CNB; -.
1CNC; -.
1CNG; -.
1CNH; -.
1CNI; -.
1CNJ; -.
1CNK; -.
1CNW; -.
1CNX; -.
1CNY; -.
1CRA; -.
1CVA; -.
1CVB; -.
1CVC; -.
1CVD; -.
1CVE; -.
1CVF; -.
1CVH; -.
1DCA; -.
1DCB; -.
1EOU; -.
1F2W; -.
1FQL; -.
1FQM; -.
1FQN; -.
1FQR; -.
1FR4; -.
1FR7; -.
1FSN; -.
1FSQ; -.
1FSR; -.
1G0E; -.
1G0F; -.
1G1D; -.
1G3Z; -.
1G45; -.
1G46; -.
1G48; -.
1G4J; -.
1G4O; -.
1G52; -.
1G53; -.
1G54; -.
1H4N; -.
1H9N; -.
1H9Q; -.
1HCA; -.
1HEA; -.
1HEB; -.
1HEC; -.
1HED; -.
1HVA; -.
1I8Z; -.
1I90; -.
1I91; -.
1I9L; -.
1I9M; -.
1I9N; -.
1I9O; -.
1I9P; -.
1I9Q; -.
1IF4; -.
1IF5; -.
1IF6; -.
1IF7; -.
1IF8; -.
1IF9; -.
1KWQ; -.
1KWR; -.
1LG5; -.
1LG6; -.
1LGD; -.
1LUG; -.
1LZV; -.
1MOO; -.
1MUA; -.
1OKL; -.
1OKM; -.
1OKN; -.
1OQ5; -.
1RAY; -.
1RAZ; -.
1RZA; -.
1RZB; -.
1RZC; -.
1RZD; -.
1RZE; -.
1T9N; -.
1TB0; -.
1TBT; -.
1TE3; -.
1TEQ; -.
1TEU; -.
1TG3; -.
1TG9; -.
1TH9; -.
1THK; -.
1TTM; -.
1UGA; -.
1UGB; -.
1UGC; -.
1UGD; -.
1UGE; -.
1UGF; -.
1UGG; -.
1XEG; -.
1XEV; -.
1XPZ; -.
1XQ0; -.
1YDA; -.
1YDB; -.
1YDC; -.
1YDD; -.
1YO0; -.
1YO1; -.
1YO2; -.
1Z9Y; -.
1ZE8; -.
1ZFK; -.
1ZFQ; -.
1ZGE; -.
1ZGF; -.
1ZH9; -.
1ZSA; -.
1ZSB; -.
1ZSC; -.
2ABE; -.
2AW1; -.
2AX2; -.
2CA2; -.
2CBA; -.
2CBB; -.
2CBC; -.
2CBD; -.
2CBE; -.
2EU2; -.
2EU3; -.
2EZ7; -.
2F14; -.
2FMG; -.
2FMZ; -.
2FNK; -.
2FNM; -.
2FNN; -.
2FOQ; -.
2FOS; -.
2FOU; -.
2FOV; -.
2GD8; -.
2GEH; -.
2H15; -.
2H4N; -.
2HD6; -.
2HKK; -.
2HL4; -.
2HNC; -.
2HOC; -.
2ILI; -.
2NNG; -.
2NNO; -.
2NNS; -.
2NNV; -.
2NWO; -.
2NWP; -.
2NWY; -.
2NWZ; -.
2NXR; -.
2NXS; -.
2NXT; -.
2O4Z; -.
2OSF; -.
2OSM; -.
2POU; -.
2POV; -.
2POW; -.
2Q1B; -.
2Q38; -.
2QO8; -.
2QOA; -.
2QP6; -.
3B4F; -.
3BL0; -.
3BL1; -.
3CA2; -.
3CAJ; -.
3CYU; -.
4CA2; -.
4CAC; -.
5CA2; -.
5CAC; -.
6CA2; -.
7CA2; -.
8CA2; -.
9CA2; -.
ModBase P00918.
Protein-protein interaction databases
IntAct P00918; -.
PTM databases
PhosphoSite P00918; -.
2D gel databases
HSC-2DPAGE P00918; -.
OGP P00918; -.
REPRODUCTION-2DPAGE IPI00218414; -.
P00918; -.
Organism-specific databases
H-InvDB HIX0007628; -.
HGNC HGNC:1373; CA2.
GenAtlas CA2.
HPA CAB010102; -.
HPA001550; -.
MIM 259730; phenotype. [NCBI / EBI]
611492; gene. [NCBI / EBI]
Orphanet 2785; Osteopetrosis, intermediate form.
PharmGKB PA24377; -.
GeneCards P00918.
Gene expression databases
ArrayExpress P00918; -.
CleanEx HS_CA2; -.