Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Carbonic anhydrase 9  

UniProtKB / Swiss-Prot ID :  CAH9_HUMAN

Gene Name (Synonyms) : 
CA9, G250, MN  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Nucleus. Nucleus, nucleolus. Cell membrane; Single-pass type I membrane protein. Cell projection, microvillus membrane; Single-pass type I membrane protein. Note=Found on the surface microvilli and in the nucleus, particularly in nucleolus. 

Protein Function :  Reversible hydration of carbon dioxide. Participates in pH regulation. May be involved in the control of cell proliferation and transformation. Appears to be a novel specific biomarker for a cervical neoplasia. 

Transmembrane Topology (topPTM) : CAH9_HUMAN 

Protein Sequence MAPLCPSPWLPLLIPAPAPGLTVQLLLSLLLLVPVHPQRLPRMQEDSPLGGGSSGEDDPLGEEDLPSEED...
Predicted Secondary Structure CCCCCCCCCCCCCCCCCCCCHHHHHHHHHHHHCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCCC...
Protein Variant
LocationDescription
33V -> M (in dbSNP:rs2071676). VAR_010787
326Q -> R (in dbSNP:rs3829078). VAR_020049
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
115O-linked (GlcNAc)EDLPTVEAP
HHHCCCCCC
37.97Phosphositeplus
Link-
115O-linked (GlcNAc...).EDLPTVEAP
HHHCCCCCC
37.97UniProtKB
Link-
346N-linked (GlcNAc...).WTVFNQTVM
EEEECCCCE
32.07UniProtKB
Link-
443PhosphothreonineHRRGTKGGV
HHCCCCCCE
25.38Phosphositeplus
Link-
448PhosphoserineKGGVSYRPA
CCCEEECCH
20.78HPRD
Link-
448PhosphoserineKGGVSYRPA
CCCEEECCH
20.78PhosphoELM
Link-
448PhosphoserineKGGVSYRPA
CCCEEECCH
20.78Phosphositeplus
Link-
449PhosphotyrosineGGVSYRPAE
CCEEECCHH
20.43Phosphositeplus
Link-
449Phosphotyrosine.GGVSYRPAE
CCEEECCHH
20.43UniProtKB
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
CTNA1_HUMANin vitro
in vivo
HPRD:04417HPRD14567991
CTNB1_HUMANin vitro
in vivo
HPRD:04417HPRD14567991
CADH1_HUMANin vitro
in vivo
HPRD:04417HPRD14567991
- top -

Disease Reference
Kegg disease
H00021 Renal cell carcinoma
There are no disease associations of PTM sites.
Drug Reference
Kegg drug
D00218 Acetazolamide (JP16/USP/INN); Diamox (TN)
D00219 Acetohexamide (JP16/USP/INN); Dymelor (TN)
D00518 Diclofenamide (JP16/INN); Dichlorphenamide (USP); Daranide (TN)
D00652 Brinzolamide (JAN/USP/INN); Azopt (TN)
D00653 Dorzolamide hydrochloride (JP16/USP); Trusopt (TN)
D00655 Methazolamide (JAN/USP/INN); Neptazane (TN)
D01196 Acetazolamide sodium (JAN); Diamox (TN)
D01822 Clofenamide (JAN/INN)
D02441 Ethoxzolamide; Cardrase (TN)
D03845 Sezolamide hydrochloride (USAN)
D07871 Dorzolamide (INN); Trusopt (TN)
D09593 Girentuximab (USAN/INN)
D09632 Iodine (124I) girentuximab (USAN/INN)
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Biochemical characterization of CA IX, one of the most activecarbonic anhydrase isozymes.";
Hilvo M., Baranauskiene L., Salzano A.M., Scaloni A., Matulis D.,Innocenti A., Scozzafava A., Monti S.M., Di Fiore A., De Simone G.,Lindfors M., Janis J., Valjakka J., Pastorekova S., Pastorek J.,Kulomaa M.S., Nordlund H.R., Supuran C.T., Parkkila S.;
J. Biol. Chem. 283:27799-27809(2008).
Cited for: FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346,AND DISULFIDE BONDS.
"Crystal structure of the catalytic domain of the tumor-associatedhuman carbonic anhydrase IX.";
Alterio V., Hilvo M., Di Fiore A., Supuran C.T., Pan P., Parkkila S.,Scaloni A., Pastorek J., Pastorekova S., Pedone C., Scozzafava A.,Monti S.M., De Simone G.;
Proc. Natl. Acad. Sci. U.S.A. 106:16233-16238(2009).
Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 137-391 IN COMPLEX WITH ZINCION AND THE INHIBITOR ACETAZOLAMIDE, GLYCOSYLATION AT ASN-346,DISULFIDE BOND, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
O-linked Glycosylation
ReferencePubMed
"Biochemical characterization of CA IX, one of the most activecarbonic anhydrase isozymes.";
Hilvo M., Baranauskiene L., Salzano A.M., Scaloni A., Matulis D.,Innocenti A., Scozzafava A., Monti S.M., Di Fiore A., De Simone G.,Lindfors M., Janis J., Valjakka J., Pastorekova S., Pastorek J.,Kulomaa M.S., Nordlund H.R., Supuran C.T., Parkkila S.;
J. Biol. Chem. 283:27799-27809(2008).
Cited for: FUNCTION, SUBUNIT, INDUCTION, GLYCOSYLATION AT THR-115 AND ASN-346,AND DISULFIDE BONDS.
Phosphorylation
ReferencePubMed
"The role of carbonic anhydrase IX overexpression in kidney cancer.";
Dorai T., Sawczuk I.S., Pastorek J., Wiernik P.H., Dutcher J.P.;
Eur. J. Cancer 41:2935-2947(2005).
Cited for: PHOSPHORYLATION AT TYR-449.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures