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Protein

H(+)/Cl(-) exchange transporter 5

Gene

CLCN5

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

Proton-coupled chloride transporter. Functions as antiport system and exchanges chloride ions against protons. Important for normal acidification of the endosome lumen. May play an important role in renal tubular function.

Miscellaneous

The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The absence of conserved gating glutamate residues is typical for family members that function as channels.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei168ChlorideBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei211Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transportBy similarity1
Sitei268Mediates proton transfer from the protein to the inner aqueous phaseBy similarity1
Binding sitei455Chloride; via amide nitrogenBy similarity1
Binding sitei558ChlorideBy similarity1
Binding sitei596ATP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi617 – 619ATPCombined sources1 Publication3
Nucleotide bindingi724 – 727ATPCombined sources1 Publication4

<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

  • antiporter activity Source: Reactome
  • ATP binding Source: UniProtKB-KW
  • chloride channel activity Source: ProtInc
  • chloride ion binding Source: GO_Central
  • identical protein binding Source: IntAct
  • solute:proton antiporter activity Source: GO_Central
  • voltage-gated chloride channel activity Source: GO_Central

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

Biological processAntiport, Ion transport, Transport
LigandATP-binding, Chloride, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-2672351 Stimuli-sensing channels

<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:
H(+)/Cl(-) exchange transporter 5
Alternative name(s):
Chloride channel protein 5
Short name:
ClC-5
Chloride transporter ClC-5
<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:CLCN5
Synonyms:CLCK2
<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 X

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000171365.15

Human Gene Nomenclature Database

More...
HGNCi
HGNC:2023 CLCN5

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
300008 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_P51795

<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 domaini1 – 54CytoplasmicBy similarityAdd BLAST54
<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>Transmembranei55 – 92HelicalBy similarityAdd BLAST38
Transmembranei138 – 161HelicalBy similarityAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei170 – 177HelicalBy similarity8
Transmembranei186 – 205HelicalBy similarityAdd BLAST20
Transmembranei211 – 230HelicalBy similarityAdd BLAST20
Intramembranei242 – 254HelicalBy similarityAdd BLAST13
Intramembranei258 – 266HelicalBy similarity9
Transmembranei278 – 296HelicalBy similarityAdd BLAST19
Transmembranei319 – 345HelicalBy similarityAdd BLAST27
Transmembranei352 – 372HelicalBy similarityAdd BLAST21
Transmembranei428 – 448HelicalBy similarityAdd BLAST21
Transmembranei453 – 472HelicalBy similarityAdd BLAST20
Intramembranei500 – 514HelicalBy similarityAdd BLAST15
Intramembranei515 – 517Note=Loop between two helicesBy similarity3
Intramembranei518 – 529HelicalBy similarityAdd BLAST12
Intramembranei530 – 534Note=Loop between two helicesBy similarity5
Transmembranei535 – 552HelicalBy similarityAdd BLAST18
Topological domaini553 – 746CytoplasmicBy similarityAdd BLAST194

Keywords - Cellular componenti

Cell membrane, Endosome, Golgi apparatus, Membrane

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Hypophosphatemic rickets, X-linked recessive (XLRHR)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. XLRH patients present with rickets or osteomalacia, hypophosphatemia due to decreased renal tubular phosphate reabsorption, hypercalciuria, and low molecular weight proteinuria. Patients develop nephrocalcinosis with progressive renal failure in adulthood. Female carriers may have asymptomatic hypercalciuria or hypophosphatemia only.
See also OMIM:300554
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_001618244S → L in XLRHR; trafficks normally to the cell surface and to early endosomes; displays complex glycosylation at the cell surface like wild-type protein; exhibits reduced current. 6 PublicationsCorresponds to variant dbSNP:rs151340626EnsemblClinVar.1
Nephrolithiasis 2 (NPHL2)14 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked recessive renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. Nephrolithiasis type 2 patients manifest hypercalciuria, hypophosphatemia, aminoaciduria, nephrocalcinosis and nephrolithiasis, renal insufficiency leading to renal failure in adulthood, rickets (33% of patients) and osteomalacia.
See also OMIM:300009
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00161530R → RH in NPHL2. 1 Publication1
Natural variantiVAR_00161657G → V in NPHL2; alters targeting to endosomes. 3 PublicationsCorresponds to variant dbSNP:rs151340629Ensembl.1
Natural variantiVAR_065591179G → D in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_001617200L → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 PublicationsCorresponds to variant dbSNP:rs151340622Ensembl.1
Natural variantiVAR_065592203S → L in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_065593212G → A in NPHL2; trafficks normally to the cell surface and to early endosomes; endergoes complex glycosylation at the cell surface like wild-type protein but exhibits significant reductions in outwardly rectifying ion currents. 1 Publication1
Natural variantiVAR_065594219C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications1
Natural variantiVAR_065595221C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications1
Natural variantiVAR_065596225L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 PublicationCorresponds to variant dbSNP:rs273585645EnsemblClinVar.1
Natural variantiVAR_065597260G → V in NPHL2; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows abolished current at the plasma membrane. 4 PublicationsCorresponds to variant dbSNP:rs151340630EnsemblClinVar.1
Natural variantiVAR_065598267E → A in NPHL2. 1 Publication1
Natural variantiVAR_065599267Missing in NPHL2. 1 Publication1
Natural variantiVAR_065600270S → G in NPHL2. 1 Publication1
Natural variantiVAR_065601270S → R in NPHL2; retained in the endoplasmic reticulum; alters protein stability; associated with an abolition of chloride current. 2 Publications1
Natural variantiVAR_065602272Y → C in NPHL2; trafficks normally to the cell surface and to early endosomes and displays complex glycosylation at the cell surface like wild-type protein; exhibits no current. 2 PublicationsCorresponds to variant dbSNP:rs273585644EnsemblClinVar.1
Natural variantiVAR_065603273F → L in NPHL2. 1 Publication1
Natural variantiVAR_065604278L → F in NPHL2; associated with a marked reduction to about 30% of wild-type chloride currents; no significant differences between the expression of the mutated and wild-type protein. 2 PublicationsCorresponds to variant dbSNP:rs273585648EnsemblClinVar.1
Natural variantiVAR_075519333G → R in NPHL2; unknown pathological significance. 1 Publication1
Natural variantiVAR_065605340N → K in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 PublicationsCorresponds to variant dbSNP:rs273585646EnsemblClinVar.1
Natural variantiVAR_065606462G → D in NPHL2. 1 Publication1
Natural variantiVAR_065607469L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_001621512G → R in NPHL2; abolishes the chloride currents. 1 Publication1
Natural variantiVAR_065608513G → E in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 1 Publication1
Natural variantiVAR_065609513G → R in NPHL2. 2 PublicationsCorresponds to variant dbSNP:rs273585647EnsemblClinVar.1
Natural variantiVAR_065610516R → W in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 2 PublicationsCorresponds to variant dbSNP:rs797044812EnsemblClinVar.1
Natural variantiVAR_001622520S → P in NPHL2. 1 PublicationCorresponds to variant dbSNP:rs151340623Ensembl.1
Natural variantiVAR_001623527E → D in NPHL2; abolishes the chloride currents; total loss of function. 2 Publications1
Natural variantiVAR_065612545S → N in NPHL2. 1 Publication1
Natural variantiVAR_065613546K → E in NPHL2; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows abolished current at the plasma membrane. 2 Publications1
Natural variantiVAR_065614547W → G in NPHL2; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows reduced current at the plasma membrane. 2 PublicationsCorresponds to variant dbSNP:rs273585650EnsemblClinVar.1
Natural variantiVAR_065615657T → S in NPHL2. 1 PublicationCorresponds to variant dbSNP:rs144207967Ensembl.1
Nephrolithiasis 1 (NPHL1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked recessive renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. Nephrolithiasis type 1 presents with hypercalciuria, nephrocalcinosis, renal stones and renal insufficiency. Patients lack urinary acidification defects, rickets, and osteomalacia.
See also OMIM:310468
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001620506G → E in NPHL1. 1 PublicationCorresponds to variant dbSNP:rs151340625Ensembl.1
Low molecular weight proteinuria with hypercalciuria and nephrocalcinosis (LMWPHN)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn X-linked renal disease belonging to the 'Dent disease complex', a group of disorders characterized by proximal renal tubular defect, hypercalciuria, nephrocalcinosis, and renal insufficiency. The spectrum of phenotypic features is remarkably similar in the various disorders, except for differences in the severity of bone deformities and renal impairment. LMWPHN is a slowly progressive disorder. Patients tend to have hypercalciuric nephrocalcinosis without rickets or renal failure.
See also OMIM:308990
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001619280R → P in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes. 2 PublicationsCorresponds to variant dbSNP:rs151340628Ensembl.1
Natural variantiVAR_065611524I → K in LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 2 Publications1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi211E → A: Abolishes proton transport, but not chloride transport. 1 Publication1
Mutagenesisi617Y → A: Strongly decreased affinity for ATP, but no effect on chloride transport. 1 Publication1
Mutagenesisi618S → A: No effect ATP binding or chloride transport. 1 Publication1
Mutagenesisi672Y → A: Abolishes interaction with NEDD4 and NEDD4L. 1 Publication1
Mutagenesisi727D → A: Strongly decreased affinity for ATP, but no effect on chloride transport. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

More...
DisGeNETi
1184

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
CLCN5

MalaCards human disease database

More...
MalaCardsi
CLCN5
MIMi300009 phenotype
300554 phenotype
308990 phenotype
310468 phenotype

Open Targets

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OpenTargetsi
ENSG00000171365

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
93622 Dent disease type 1

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26550

<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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000944461 – 746H(+)/Cl(-) exchange transporter 5Add BLAST746

<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

Ubiquitinated by NEDD4L in the presence of albumin; which promotes endocytosis and proteasomal degradation.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

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MaxQBi
P51795

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

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PaxDbi
P51795

PeptideAtlas

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PeptideAtlasi
P51795

PRoteomics IDEntifications database

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PRIDEi
P51795

ProteomicsDB human proteome resource

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ProteomicsDBi
56391
56392 [P51795-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P51795

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

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PhosphoSitePlusi
P51795

<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

Kidney. Moderately expressed in aortic vascular smooth muscle and endothelial cells, and at a slightly higher level in the coronary vascular smooth muscle.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000171365 Expressed in 164 organ(s), highest expression level in metanephros

CleanEx database of gene expression profiles

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CleanExi
HS_CLCN5

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P51795 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P51795 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA000401
HPA003213

<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

Interacts with NEDD4 and NEDD4L.1 Publication

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
107598, 9 interactors

Database of interacting proteins

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DIPi
DIP-29263N

Protein interaction database and analysis system

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IntActi
P51795, 2 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000365256

<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

1746
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
P51795

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

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SMRi
P51795

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

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EvolutionaryTracei
P51795

<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>Domaini586 – 650CBS 1PROSITE-ProRule annotationAdd BLAST65
Domaini682 – 742CBS 2PROSITE-ProRule annotationAdd BLAST61

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi167 – 171Selectivity filter part_1By similarity5
Motifi209 – 213Selectivity filter part_2By similarity5
Motifi453 – 457Selectivity filter part_3By similarity5

<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

Keywords - Domaini

CBS domain, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0475 Eukaryota
COG0038 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153763

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000164493

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG050984

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P51795

KEGG Orthology (KO)

More...
KOi
K05012

Identification of Orthologs from Complete Genome Data

More...
OMAi
TALINYP

Database of Orthologous Groups

More...
OrthoDBi
EOG091G01YH

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P51795

TreeFam database of animal gene trees

More...
TreeFami
TF313867

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.3080.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000644 CBS_dom
IPR014743 Cl-channel_core
IPR001807 Cl-channel_volt-gated
IPR002247 Cl_channel-5

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00571 CBS, 2 hits
PF00654 Voltage_CLC, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00762 CLCHANNEL
PR01116 CLCHANNEL5

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00116 CBS, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81340 SSF81340, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51371 CBS, 2 hits

<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>Sequences (2+)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.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P51795-1) [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
MDFLEEPIPG VGTYDDFNTI DWVREKSRDR DRHREITNKS KESTWALIHS
60 70 80 90 100
VSDAFSGWLL MLLIGLLSGS LAGLIDISAH WMTDLKEGIC TGGFWFNHEH
110 120 130 140 150
CCWNSEHVTF EERDKCPEWN SWSQLIISTD EGAFAYIVNY FMYVLWALLF
160 170 180 190 200
AFLAVSLVKV FAPYACGSGI PEIKTILSGF IIRGYLGKWT LVIKTITLVL
210 220 230 240 250
AVSSGLSLGK EGPLVHVACC CGNILCHCFN KYRKNEAKRR EVLSAAAAAG
260 270 280 290 300
VSVAFGAPIG GVLFSLEEVS YYFPLKTLWR SFFAALVAAF TLRSINPFGN
310 320 330 340 350
SRLVLFYVEF HTPWHLFELV PFILLGIFGG LWGALFIRTN IAWCRKRKTT
360 370 380 390 400
QLGKYPVIEV LVVTAITAIL AFPNEYTRMS TSELISELFN DCGLLDSSKL
410 420 430 440 450
CDYENRFNTS KGGELPDRPA GVGVYSAMWQ LALTLILKIV ITIFTFGMKI
460 470 480 490 500
PSGLFIPSMA VGAIAGRLLG VGMEQLAYYH QEWTVFNSWC SQGADCITPG
510 520 530 540 550
LYAMVGAAAC LGGVTRMTVS LVVIMFELTG GLEYIVPLMA AAMTSKWVAD
560 570 580 590 600
ALGREGIYDA HIRLNGYPFL EAKEEFAHKT LAMDVMKPRR NDPLLTVLTQ
610 620 630 640 650
DSMTVEDVET IISETTYSGF PVVVSRESQR LVGFVLRRDL IISIENARKK
660 670 680 690 700
QDGVVSTSII YFTEHSPPLP PYTPPTLKLR NILDLSPFTV TDLTPMEIVV
710 720 730 740
DIFRKLGLRQ CLVTHNGRLL GIITKKDVLK HIAQMANQDP DSILFN
Length:746
Mass (Da):83,147
Last modified:October 1, 1996 - v1
<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:iEF913C5BA40C85D8
GO
Isoform 2 (identifier: P51795-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAMWQGAMDNRGFQQGSFSSFQNSSSDEDLMDIPATAMDFSMRDDVPPLDREVGEDKSYNGGGIGSSNRIM

Show »
Length:816
Mass (Da):90,785
Checksum:iC9C63CC222959F35
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 are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A2R8YGW0A0A2R8YGW0_HUMAN
Chloride channel protein
CLCN5
590Annotation score:

Annotation score:2 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>
V9GYG7V9GYG7_HUMAN
H(+)/Cl(-) exchange transporter 5
CLCN5
64Annotation 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>
A0A2R8Y6C4A0A2R8Y6C4_HUMAN
H(+)/Cl(-) exchange transporter 5
CLCN5
265Annotation 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>
A0A2R8YF14A0A2R8YF14_HUMAN
H(+)/Cl(-) exchange transporter 5
CLCN5
63Annotation 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>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti732I → V in BAG51748 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00161530R → RH in NPHL2. 1 Publication1
Natural variantiVAR_00161657G → V in NPHL2; alters targeting to endosomes. 3 PublicationsCorresponds to variant dbSNP:rs151340629Ensembl.1
Natural variantiVAR_048694142M → I. Corresponds to variant dbSNP:rs34800648EnsemblClinVar.1
Natural variantiVAR_065591179G → D in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_001617200L → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 PublicationsCorresponds to variant dbSNP:rs151340622Ensembl.1
Natural variantiVAR_065592203S → L in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_065593212G → A in NPHL2; trafficks normally to the cell surface and to early endosomes; endergoes complex glycosylation at the cell surface like wild-type protein but exhibits significant reductions in outwardly rectifying ion currents. 1 Publication1
Natural variantiVAR_065594219C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications1
Natural variantiVAR_065595221C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications1
Natural variantiVAR_065596225L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 PublicationCorresponds to variant dbSNP:rs273585645EnsemblClinVar.1
Natural variantiVAR_001618244S → L in XLRHR; trafficks normally to the cell surface and to early endosomes; displays complex glycosylation at the cell surface like wild-type protein; exhibits reduced current. 6 PublicationsCorresponds to variant dbSNP:rs151340626EnsemblClinVar.1
Natural variantiVAR_065597260G → V in NPHL2; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows abolished current at the plasma membrane. 4 PublicationsCorresponds to variant dbSNP:rs151340630EnsemblClinVar.1
Natural variantiVAR_065598267E → A in NPHL2. 1 Publication1
Natural variantiVAR_065599267Missing in NPHL2. 1 Publication1
Natural variantiVAR_065600270S → G in NPHL2. 1 Publication1
Natural variantiVAR_065601270S → R in NPHL2; retained in the endoplasmic reticulum; alters protein stability; associated with an abolition of chloride current. 2 Publications1
Natural variantiVAR_065602272Y → C in NPHL2; trafficks normally to the cell surface and to early endosomes and displays complex glycosylation at the cell surface like wild-type protein; exhibits no current. 2 PublicationsCorresponds to variant dbSNP:rs273585644EnsemblClinVar.1
Natural variantiVAR_065603273F → L in NPHL2. 1 Publication1
Natural variantiVAR_065604278L → F in NPHL2; associated with a marked reduction to about 30% of wild-type chloride currents; no significant differences between the expression of the mutated and wild-type protein. 2 PublicationsCorresponds to variant dbSNP:rs273585648EnsemblClinVar.1
Natural variantiVAR_001619280R → P in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes. 2 PublicationsCorresponds to variant dbSNP:rs151340628Ensembl.1
Natural variantiVAR_075519333G → R in NPHL2; unknown pathological significance. 1 Publication1
Natural variantiVAR_065605340N → K in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 PublicationsCorresponds to variant dbSNP:rs273585646EnsemblClinVar.1
Natural variantiVAR_065606462G → D in NPHL2. 1 Publication1
Natural variantiVAR_065607469L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_001620506G → E in NPHL1. 1 PublicationCorresponds to variant dbSNP:rs151340625Ensembl.1
Natural variantiVAR_001621512G → R in NPHL2; abolishes the chloride currents. 1 Publication1
Natural variantiVAR_065608513G → E in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 1 Publication1
Natural variantiVAR_065609513G → R in NPHL2. 2 PublicationsCorresponds to variant dbSNP:rs273585647EnsemblClinVar.1
Natural variantiVAR_065610516R → W in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 2 PublicationsCorresponds to variant dbSNP:rs797044812EnsemblClinVar.1
Natural variantiVAR_001622520S → P in NPHL2. 1 PublicationCorresponds to variant dbSNP:rs151340623Ensembl.1
Natural variantiVAR_065611524I → K in LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 2 Publications1
Natural variantiVAR_001623527E → D in NPHL2; abolishes the chloride currents; total loss of function. 2 Publications1
Natural variantiVAR_065612545S → N in NPHL2. 1 Publication1
Natural variantiVAR_065613546K → E in NPHL2; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows abolished current at the plasma membrane. 2 Publications1
Natural variantiVAR_065614547W → G in NPHL2; delayed in processing of the protein and decrease in the stability of the mature complex glycosylated form causing lower cell surface expression; the early endosome distribution is normal; shows reduced current at the plasma membrane. 2 PublicationsCorresponds to variant dbSNP:rs273585650EnsemblClinVar.1
Natural variantiVAR_065615657T → S in NPHL2. 1 PublicationCorresponds to variant dbSNP:rs144207967Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0420461M → MAMWQGAMDNRGFQQGSFSS FQNSSSDEDLMDIPATAMDF SMRDDVPPLDREVGEDKSYN GGGIGSSNRIM in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X91906 mRNA Translation: CAA63000.1
AK056560 mRNA Translation: BAG51748.1
FO393402 Genomic DNA No translation available.
BC130429 mRNA Translation: AAI30430.1
BC130431 mRNA Translation: AAI30432.1
X81836 mRNA Translation: CAA57430.1
BK000969 mRNA Translation: DAA01544.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS14328.1 [P51795-1]
CCDS48115.1 [P51795-2]

Protein sequence database of the Protein Information Resource

More...
PIRi
I37277

NCBI Reference Sequences

More...
RefSeqi
NP_000075.1, NM_000084.4 [P51795-1]
NP_001121370.1, NM_001127898.3 [P51795-2]
NP_001121371.1, NM_001127899.3 [P51795-2]
NP_001269092.1, NM_001282163.1

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.166486
Hs.745501

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000307367; ENSP00000304257; ENSG00000171365 [P51795-1]
ENST00000376088; ENSP00000365256; ENSG00000171365 [P51795-2]
ENST00000376091; ENSP00000365259; ENSG00000171365 [P51795-2]
ENST00000376108; ENSP00000365276; ENSG00000171365 [P51795-1]
ENST00000642885; ENSP00000496632; ENSG00000171365 [P51795-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
1184

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:1184

UCSC genome browser

More...
UCSCi
uc004doq.2 human [P51795-1]

Keywords - Coding sequence diversityi

Alternative splicing, 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
X91906 mRNA Translation: CAA63000.1
AK056560 mRNA Translation: BAG51748.1
FO393402 Genomic DNA No translation available.
BC130429 mRNA Translation: AAI30430.1
BC130431 mRNA Translation: AAI30432.1
X81836 mRNA Translation: CAA57430.1
BK000969 mRNA Translation: DAA01544.1
CCDSiCCDS14328.1 [P51795-1]
CCDS48115.1 [P51795-2]
PIRiI37277
RefSeqiNP_000075.1, NM_000084.4 [P51795-1]
NP_001121370.1, NM_001127898.3 [P51795-2]
NP_001121371.1, NM_001127899.3 [P51795-2]
NP_001269092.1, NM_001282163.1
UniGeneiHs.166486
Hs.745501

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2J9LX-ray2.30A/B/C/D/E/F571-746[»]
2JA3X-ray3.05A/B/C/D/E/F571-746[»]
ProteinModelPortaliP51795
SMRiP51795
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107598, 9 interactors
DIPiDIP-29263N
IntActiP51795, 2 interactors
STRINGi9606.ENSP00000365256

PTM databases

iPTMnetiP51795
PhosphoSitePlusiP51795

Proteomic databases

MaxQBiP51795
PaxDbiP51795
PeptideAtlasiP51795
PRIDEiP51795
ProteomicsDBi56391
56392 [P51795-2]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
1184
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000307367; ENSP00000304257; ENSG00000171365 [P51795-1]
ENST00000376088; ENSP00000365256; ENSG00000171365 [P51795-2]
ENST00000376091; ENSP00000365259; ENSG00000171365 [P51795-2]
ENST00000376108; ENSP00000365276; ENSG00000171365 [P51795-1]
ENST00000642885; ENSP00000496632; ENSG00000171365 [P51795-1]
GeneIDi1184
KEGGihsa:1184
UCSCiuc004doq.2 human [P51795-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
1184
DisGeNETi1184
EuPathDBiHostDB:ENSG00000171365.15

GeneCards: human genes, protein and diseases

More...
GeneCardsi
CLCN5
GeneReviewsiCLCN5
HGNCiHGNC:2023 CLCN5
HPAiHPA000401
HPA003213
MalaCardsiCLCN5
MIMi300008 gene
300009 phenotype
300554 phenotype
308990 phenotype
310468 phenotype
neXtProtiNX_P51795
OpenTargetsiENSG00000171365
Orphaneti93622 Dent disease type 1
PharmGKBiPA26550

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0475 Eukaryota
COG0038 LUCA
GeneTreeiENSGT00940000153763
HOGENOMiHOG000164493
HOVERGENiHBG050984
InParanoidiP51795
KOiK05012
OMAiTALINYP
OrthoDBiEOG091G01YH
PhylomeDBiP51795
TreeFamiTF313867

Enzyme and pathway databases

ReactomeiR-HSA-2672351 Stimuli-sensing channels

Miscellaneous databases

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

More...
ChiTaRSi
CLCN5 human
EvolutionaryTraceiP51795

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
CLCN5

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

More...
GenomeRNAii
1184

Protein Ontology

More...
PROi
PR:P51795

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000171365 Expressed in 164 organ(s), highest expression level in metanephros
CleanExiHS_CLCN5
ExpressionAtlasiP51795 baseline and differential
GenevisibleiP51795 HS

Family and domain databases

Gene3Di1.10.3080.10, 1 hit
InterProiView protein in InterPro
IPR000644 CBS_dom
IPR014743 Cl-channel_core
IPR001807 Cl-channel_volt-gated
IPR002247 Cl_channel-5
PfamiView protein in Pfam
PF00571 CBS, 2 hits
PF00654 Voltage_CLC, 1 hit
PRINTSiPR00762 CLCHANNEL
PR01116 CLCHANNEL5
SMARTiView protein in SMART
SM00116 CBS, 2 hits
SUPFAMiSSF81340 SSF81340, 1 hit
PROSITEiView protein in PROSITE
PS51371 CBS, 2 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
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 nameiCLCN5_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: P51795
Secondary accession number(s): A1L475
, B3KPN6, Q5JQD5, Q7RTN8
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 179 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: 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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