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HUMAN:CAH1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) CA1
Protein Name(s) Carbonic anhydrase 1

Carbonate dehydratase I Carbonic anhydrase B CAB Carbonic anhydrase I CA-I

External Links
UniProt P00915
EMBL X05014
M33987
BC027890
CCDS CCDS6237.1
PIR JQ0786
RefSeq NP_001122301.1
NP_001122302.1
NP_001122303.1
NP_001158302.1
NP_001729.1
UniGene Hs.23118
PDB 1AZM
1BZM
1CRM
1CZM
1HCB
1HUG
1HUH
1J9W
1JV0
2CAB
2FOY
2FW4
2IT4
2NMX
2NN1
2NN7
3LXE
3W6H
3W6I
PDBsum 1AZM
1BZM
1CRM
1CZM
1HCB
1HUG
1HUH
1J9W
1JV0
2CAB
2FOY
2FW4
2IT4
2NMX
2NN1
2NN7
3LXE
3W6H
3W6I
ProteinModelPortal P00915
SMR P00915
BioGrid 107214
IntAct P00915
STRING 9606.ENSP00000256119
BindingDB P00915
ChEMBL CHEMBL2095180
DrugBank DB00819
DB00381
DB00436
DB00562
DB01194
DB00880
DB00606
DB01119
DB01144
DB00869
DB01031
DB00999
DB00774
DB00703
DB00423
DB00232
DB01325
DB01021
DB00909
GuidetoPHARMACOLOGY 2597
PhosphoSite P00915
DMDM 115449
DOSAC-COBS-2DPAGE P00915
REPRODUCTION-2DPAGE IPI00215983
P00915
UCD-2DPAGE P00915
PaxDb P00915
PeptideAtlas P00915
PRIDE P00915
DNASU 759
Ensembl ENST00000431316
ENST00000523022
ENST00000523953
ENST00000542576
GeneID 759
KEGG hsa:759
UCSC uc003ydh.3
CTD 759
GeneCards GC08M086315
HGNC HGNC:1368
HPA CAB025790
HPA006558
MIM 114800
neXtProt NX_P00915
PharmGKB PA25984
eggNOG COG3338
HOGENOM HOG000112637
HOVERGEN HBG002837
InParanoid P00915
KO K01672
OMA VTWIICK
OrthoDB EOG7WMCK7
PhylomeDB P00915
TreeFam TF316425
BRENDA 4.2.1.1
Reactome REACT_121123
REACT_121329
REACT_121380
SABIO-RK P00915
EvolutionaryTrace P00915
GeneWiki CA1_(gene)
GenomeRNAi 759
NextBio 3070
PRO PR:P00915
Proteomes UP000005640
Bgee P00915
CleanEx HS_CA1
ExpressionAtlas P00915
Genevestigator P00915
GO GO:0005829
GO:0070062
GO:0004089
GO:0008270
GO:0015701
GO:0006730
GO:0044281
Gene3D 3.10.200.10
InterPro IPR001148
IPR023561
IPR018338
IPR018442
PANTHER PTHR18952
PTHR18952:SF82
Pfam PF00194
SMART SM01057
SUPFAM SSF51069
PROSITE PS00162
PS51144

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0016836

hydro-lyase activity

PMID:2114290[1]

ECO:0000314

F

Figure 1

complete
CACAO 5420

GO:0004089

carbonate dehydratase activity

PMID:7758465[2]

ECO:0000315

F

Table 1

complete
CACAO 5434

GO:0004064

hydrolase activity

PMID:7758465[2]

ECO:0000315

F

Table 4

complete
CACAO 5436

GO:0004089

carbonate dehydratase activity

PMID:7758465[2]

ECO:0000315

F

Table 2

complete
CACAO 5523

GO:0004089

carbonate dehydratase activity

PMID:4994926[3]

ECO:0000314

F

Figure 5

complete
CACAO 5793

GO:0004064

arylesterase activity

PMID:7758465[2]

ECO:0000315

F

Table 4

complete
CACAO 6167

enables

GO:0004089

carbonate dehydratase activity

PMID:7758465[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004064

arylesterase activity

PMID:7758465[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0016836

hydro-lyase activity

PMID:2114290[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0070062

extracellular exosome

PMID:23533145[4]

ECO:0007005

high throughput direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0004089

carbonate dehydratase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018338
InterPro:IPR018442
InterPro:IPR023561

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018442

C

Seeded From UniProt

complete

involved_in

GO:0006730

one-carbon metabolic process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018442

P

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR018338
InterPro:IPR018442
InterPro:IPR023561

F

Seeded From UniProt

complete

enables

GO:0004089

carbonate dehydratase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.1.1

F

Seeded From UniProt

complete

enables

GO:0004089

carbonate dehydratase activity

PMID:2121614[5]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0035722

interleukin-12-mediated signaling pathway

Reactome:R-HSA-9020591

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0015701

bicarbonate transport

Reactome:R-HSA-1475029
Reactome:R-HSA-1247673
Reactome:R-HSA-1237044

ECO:0000304

author statement supported by traceable reference used in manual assertion



P

Seeded From UniProt

complete

part_of

GO:0005829

cytosol

Reactome:R-HSA-8950623
Reactome:R-HSA-1475436
Reactome:R-HSA-1475435
Reactome:R-HSA-1475026
Reactome:R-HSA-1475022

ECO:0000304

author statement supported by traceable reference used in manual assertion





C

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0963
UniProtKB-SubCell:SL-0086

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Behravan, G et al. (1990) Fine tuning of the catalytic properties of carbonic anhydrase. Studies of a Thr200----His variant of human isoenzyme II. Eur. J. Biochem. 190 351-7 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 Engstrand, C et al. (1995) Catalytic and inhibitor-binding properties of some active-site mutants of human carbonic anhydrase I. Eur. J. Biochem. 229 696-702 PubMed GONUTS page
  3. Khalifah, RG (1971) The carbon dioxide hydration activity of carbonic anhydrase. I. Stop-flow kinetic studies on the native human isoenzymes B and C. J. Biol. Chem. 246 2561-73 PubMed GONUTS page
  4. Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
  5. Lowe, N et al. (1990) Structure and methylation patterns of the gene encoding human carbonic anhydrase I. Gene 93 277-83 PubMed GONUTS page