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Protein

Carbonic anhydrase 9

Gene

CA9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by coumarins, saccharin, sulfonamide derivatives such as acetazolamide (AZA) and Foscarnet (phosphonoformate trisodium salt).4 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 6.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei200Proton acceptorBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi226Zinc; catalytic1 Publication1
Metal bindingi228Zinc; catalytic1 Publication1
Metal bindingi251Zinc; catalytic1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.2.1.1 2681

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-HSA-1475029 Reversible hydration of carbon dioxide

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q16790

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Carbonic anhydrase 9 (EC:4.2.1.1)
Alternative name(s):
Carbonate dehydratase IX
Carbonic anhydrase IX
Short name:
CA-IX
Short name:
CAIX
Membrane antigen MN
P54/58N
Renal cell carcinoma-associated antigen G250
Short name:
RCC-associated antigen G250
pMW1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CA9
Synonyms:G250, MN
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 9

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000107159.12

Human Gene Nomenclature Database

More...
HGNCi
HGNC:1383 CA9

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
603179 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q16790

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini38 – 414ExtracellularAdd BLAST377
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei415 – 435HelicalSequence analysisAdd BLAST21
Topological domaini436 – 459CytoplasmicAdd BLAST24

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...
DisGeNETi
768

Open Targets

More...
OpenTargetsi
ENSG00000107159

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA25998

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3594

Drug and drug target database

More...
DrugBanki
DB00562 Benzthiazide
DB08846 Ellagic Acid
DB00999 Hydrochlorothiazide
DB00774 Hydroflumethiazide
DB09460 Sodium carbonate
DB05304 WX-G250
DB00909 Zonisamide

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CA9

Domain mapping of disease mutations (DMDM)

More...
DMDMi
83300925

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 371 PublicationAdd BLAST37
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000424338 – 459Carbonic anhydrase 9Add BLAST422

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi115O-linked (GlcNAc...) threonine1 Publication1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi156 ↔ 3361 Publication
Disulfide bondi174Interchain1 Publication
Glycosylationi346N-linked (GlcNAc...) asparagine2 Publications1
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei449Phosphotyrosine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Asn-346 bears high-mannose type glycan structures.

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q16790

MaxQB - The MaxQuant DataBase

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MaxQBi
Q16790

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q16790

PeptideAtlas

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PeptideAtlasi
Q16790

PRoteomics IDEntifications database

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PRIDEi
Q16790

ProteomicsDB human proteome resource

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ProteomicsDBi
61071

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q16790

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q16790

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed primarily in carcinoma cells lines. Expression is restricted to very few normal tissues and the most abundant expression is found in the epithelial cells of gastric mucosa.

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By hypoxia.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000107159 Expressed in 107 organ(s), highest expression level in body of stomach

CleanEx database of gene expression profiles

More...
CleanExi
HS_CA9

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q16790 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q16790 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB005100
CAB017107
HPA055207

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms oligomers linked by disulfide bonds.3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
GLRX3O760036EBI-12259996,EBI-374781

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107223, 32 interactors

Database of interacting proteins

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DIPi
DIP-48973N

Protein interaction database and analysis system

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IntActi
Q16790, 2 interactors

STRING: functional protein association networks

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STRINGi
9606.ENSP00000367608

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q16790

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q16790

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q16790

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q16790

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini139 – 390Alpha-carbonic anhydrasePROSITE-ProRule annotationAdd BLAST252

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni38 – 112Proteoglycan-like (PG)Add BLAST75
Regioni113 – 414CatalyticAdd BLAST302
Regioni332 – 333Substrate bindingBy similarity2

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the alpha-carbonic anhydrase family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0382 Eukaryota
COG3338 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161646

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000112637

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG002837

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q16790

KEGG Orthology (KO)

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KOi
K01672

Identification of Orthologs from Complete Genome Data

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OMAi
SRYFRYE

Database of Orthologous Groups

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OrthoDBi
EOG091G0XFM

Database for complete collections of gene phylogenies

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PhylomeDBi
Q16790

TreeFam database of animal gene trees

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TreeFami
TF316425

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.10.200.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR018429 CA9
IPR001148 CA_dom
IPR036398 CA_dom_sf
IPR023561 Carbonic_anhydrase_a-class
IPR018338 Carbonic_anhydrase_a-class_CS

The PANTHER Classification System

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PANTHERi
PTHR18952 PTHR18952, 1 hit
PTHR18952:SF18 PTHR18952:SF18, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF00194 Carb_anhydrase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM01057 Carb_anhydrase, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF51069 SSF51069, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00162 ALPHA_CA_1, 1 hit
PS51144 ALPHA_CA_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

Q16790-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPLCPSPWL PLLIPAPAPG LTVQLLLSLL LLVPVHPQRL PRMQEDSPLG
60 70 80 90 100
GGSSGEDDPL GEEDLPSEED SPREEDPPGE EDLPGEEDLP GEEDLPEVKP
110 120 130 140 150
KSEEEGSLKL EDLPTVEAPG DPQEPQNNAH RDKEGDDQSH WRYGGDPPWP
160 170 180 190 200
RVSPACAGRF QSPVDIRPQL AAFCPALRPL ELLGFQLPPL PELRLRNNGH
210 220 230 240 250
SVQLTLPPGL EMALGPGREY RALQLHLHWG AAGRPGSEHT VEGHRFPAEI
260 270 280 290 300
HVVHLSTAFA RVDEALGRPG GLAVLAAFLE EGPEENSAYE QLLSRLEEIA
310 320 330 340 350
EEGSETQVPG LDISALLPSD FSRYFQYEGS LTTPPCAQGV IWTVFNQTVM
360 370 380 390 400
LSAKQLHTLS DTLWGPGDSR LQLNFRATQP LNGRVIEASF PAGVDSSPRA
410 420 430 440 450
AEPVQLNSCL AAGDILALVF GLLFAVTSVA FLVQMRRQHR RGTKGGVSYR

PAEVAETGA
Length:459
Mass (Da):49,698
Last modified:December 6, 2005 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBA67195483F0F5CE
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A087WYS4A0A087WYS4_HUMAN
Carbonic anhydrase 9
CA9
356Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_01078733V → M2 PublicationsCorresponds to variant dbSNP:rs2071676Ensembl.1
Natural variantiVAR_020049326Q → R. Corresponds to variant dbSNP:rs3829078Ensembl.1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X66839 mRNA Translation: CAA47315.1
AJ010588 mRNA Translation: CAB82444.1
AL133410 Genomic DNA No translation available.
AL357874 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58359.1
BC014950 mRNA Translation: AAH14950.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS6585.1

Protein sequence database of the Protein Information Resource

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PIRi
I38013

NCBI Reference Sequences

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RefSeqi
NP_001207.2, NM_001216.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.63287

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000378357; ENSP00000367608; ENSG00000107159

Database of genes from NCBI RefSeq genomes

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GeneIDi
768

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:768

UCSC genome browser

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UCSCi
uc003zxo.5 human

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X66839 mRNA Translation: CAA47315.1
AJ010588 mRNA Translation: CAB82444.1
AL133410 Genomic DNA No translation available.
AL357874 Genomic DNA No translation available.
CH471071 Genomic DNA Translation: EAW58359.1
BC014950 mRNA Translation: AAH14950.1
CCDSiCCDS6585.1
PIRiI38013
RefSeqiNP_001207.2, NM_001216.2
UniGeneiHs.63287

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2HKFX-ray2.01P83-91[»]
3IAIX-ray2.20A/B/C/D137-391[»]
5DVXX-ray1.60A/B140-399[»]
5FL4X-ray1.82A/B/C/D137-391[»]
5FL5X-ray2.05A/B/C/D137-391[»]
5FL6X-ray1.95A/B/C/D137-391[»]
6FE0X-ray1.91A/B/C/D137-391[»]
6FE1X-ray1.95A/B/C/D137-391[»]
6FE2X-ray1.87A/B/C/D137-391[»]
6G98X-ray2.47A/B/C/D135-391[»]
6G9UX-ray1.75A/B/C/D137-391[»]
ProteinModelPortaliQ16790
SMRiQ16790
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107223, 32 interactors
DIPiDIP-48973N
IntActiQ16790, 2 interactors
STRINGi9606.ENSP00000367608

Chemistry databases

BindingDBiQ16790
ChEMBLiCHEMBL3594
DrugBankiDB00562 Benzthiazide
DB08846 Ellagic Acid
DB00999 Hydrochlorothiazide
DB00774 Hydroflumethiazide
DB09460 Sodium carbonate
DB05304 WX-G250
DB00909 Zonisamide

PTM databases

iPTMnetiQ16790
PhosphoSitePlusiQ16790

Polymorphism and mutation databases

BioMutaiCA9
DMDMi83300925

Proteomic databases

EPDiQ16790
MaxQBiQ16790
PaxDbiQ16790
PeptideAtlasiQ16790
PRIDEiQ16790
ProteomicsDBi61071

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
768
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378357; ENSP00000367608; ENSG00000107159
GeneIDi768
KEGGihsa:768
UCSCiuc003zxo.5 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
768
DisGeNETi768
EuPathDBiHostDB:ENSG00000107159.12

GeneCards: human genes, protein and diseases

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GeneCardsi
CA9

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0008019
HGNCiHGNC:1383 CA9
HPAiCAB005100
CAB017107
HPA055207
MIMi603179 gene
neXtProtiNX_Q16790
OpenTargetsiENSG00000107159
PharmGKBiPA25998

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0382 Eukaryota
COG3338 LUCA
GeneTreeiENSGT00940000161646
HOGENOMiHOG000112637
HOVERGENiHBG002837
InParanoidiQ16790
KOiK01672
OMAiSRYFRYE
OrthoDBiEOG091G0XFM
PhylomeDBiQ16790
TreeFamiTF316425

Enzyme and pathway databases

BRENDAi4.2.1.1 2681
ReactomeiR-HSA-1234158 Regulation of gene expression by Hypoxia-inducible Factor
R-HSA-1475029 Reversible hydration of carbon dioxide
SIGNORiQ16790

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
CA9 human
EvolutionaryTraceiQ16790

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Carbonic_anhydrase_9

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
768

Protein Ontology

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PROi
PR:Q16790

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000107159 Expressed in 107 organ(s), highest expression level in body of stomach
CleanExiHS_CA9
ExpressionAtlasiQ16790 baseline and differential
GenevisibleiQ16790 HS

Family and domain databases

Gene3Di3.10.200.10, 1 hit
InterProiView protein in InterPro
IPR018429 CA9
IPR001148 CA_dom
IPR036398 CA_dom_sf
IPR023561 Carbonic_anhydrase_a-class
IPR018338 Carbonic_anhydrase_a-class_CS
PANTHERiPTHR18952 PTHR18952, 1 hit
PTHR18952:SF18 PTHR18952:SF18, 1 hit
PfamiView protein in Pfam
PF00194 Carb_anhydrase, 1 hit
SMARTiView protein in SMART
SM01057 Carb_anhydrase, 1 hit
SUPFAMiSSF51069 SSF51069, 1 hit
PROSITEiView protein in PROSITE
PS00162 ALPHA_CA_1, 1 hit
PS51144 ALPHA_CA_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCAH9_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q16790
Secondary accession number(s): Q5T4R1
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 6, 2005
Last modified: December 5, 2018
This is version 177 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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