Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 192 (07 Oct 2020)
Sequence version 2 (12 Aug 2020)
Previous versions | rss
Help videoAdd a publicationFeedback
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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei238ChlorideBy 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>Sitei281Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transportBy similarity1
Sitei338Mediates proton transfer from the protein to the inner aqueous phaseBy similarity1
Binding sitei525Chloride; via amide nitrogenBy similarity1
Binding sitei628ChlorideBy similarity1
Binding sitei666ATP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi687 – 689ATPCombined sources1 Publication3
Nucleotide bindingi794 – 797ATPCombined 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

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

Pathway Commons web resource for biological pathway data

More...
PathwayCommonsi
P51795

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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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 & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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 – 124CytoplasmicBy similarityAdd BLAST124
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Transmembranei125 – 162HelicalBy similarityAdd BLAST38
Transmembranei208 – 231HelicalBy similarityAdd BLAST24
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'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>Intramembranei240 – 247HelicalBy similarity8
Transmembranei256 – 275HelicalBy similarityAdd BLAST20
Transmembranei281 – 300HelicalBy similarityAdd BLAST20
Intramembranei312 – 324HelicalBy similarityAdd BLAST13
Intramembranei328 – 336HelicalBy similarity9
Transmembranei348 – 366HelicalBy similarityAdd BLAST19
Transmembranei389 – 415HelicalBy similarityAdd BLAST27
Transmembranei422 – 442HelicalBy similarityAdd BLAST21
Transmembranei498 – 518HelicalBy similarityAdd BLAST21
Transmembranei523 – 542HelicalBy similarityAdd BLAST20
Intramembranei570 – 584HelicalBy similarityAdd BLAST15
Intramembranei585 – 587Note=Loop between two helicesBy similarity3
Intramembranei588 – 599HelicalBy similarityAdd BLAST12
Intramembranei600 – 604Note=Loop between two helicesBy similarity5
Transmembranei605 – 622HelicalBy similarityAdd BLAST18
Topological domaini623 – 816CytoplasmicBy 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.
Related information in OMIM
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_001618314S → 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001615100R → RH in NPHL2. 1 Publication1
Natural variantiVAR_001616127G → V in NPHL2; alters targeting to endosomes. 3 PublicationsCorresponds to variant dbSNP:rs151340629EnsemblClinVar.1
Natural variantiVAR_065591249G → D in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_001617270L → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 PublicationsCorresponds to variant dbSNP:rs151340622EnsemblClinVar.1
Natural variantiVAR_065592273S → L in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_065593282G → 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_065594289C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications1
Natural variantiVAR_065595291C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications1
Natural variantiVAR_065596295L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 PublicationCorresponds to variant dbSNP:rs273585645EnsemblClinVar.1
Natural variantiVAR_065597330G → 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_065598337E → A in NPHL2. 1 Publication1
Natural variantiVAR_065599337Missing in NPHL2. 1 Publication1
Natural variantiVAR_065600340S → G in NPHL2. 1 Publication1
Natural variantiVAR_065601340S → R in NPHL2; retained in the endoplasmic reticulum; alters protein stability; associated with an abolition of chloride current. 2 Publications1
Natural variantiVAR_065602342Y → 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_065603343F → L in NPHL2. 1 Publication1
Natural variantiVAR_065604348L → 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_075519403G → R in NPHL2; unknown pathological significance. 1 Publication1
Natural variantiVAR_065605410N → K in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 PublicationsCorresponds to variant dbSNP:rs273585646EnsemblClinVar.1
Natural variantiVAR_065606532G → D in NPHL2. 1 Publication1
Natural variantiVAR_065607539L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_001621582G → R in NPHL2; abolishes the chloride currents. 1 Publication1
Natural variantiVAR_065608583G → E in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 1 Publication1
Natural variantiVAR_065609583G → R in NPHL2. 2 PublicationsCorresponds to variant dbSNP:rs273585647EnsemblClinVar.1
Natural variantiVAR_065610586R → 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_001622590S → P in NPHL2. 1 PublicationCorresponds to variant dbSNP:rs151340623EnsemblClinVar.1
Natural variantiVAR_001623597E → D in NPHL2; abolishes the chloride currents; total loss of function. 2 Publications1
Natural variantiVAR_065612615S → N in NPHL2. 1 Publication1
Natural variantiVAR_065613616K → 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_065614617W → 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_065615727T → S in NPHL2. 1 PublicationCorresponds to variant dbSNP:rs144207967EnsemblClinVar.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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001620576G → E in NPHL1. 1 PublicationCorresponds to variant dbSNP:rs151340625EnsemblClinVar.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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001619350R → P in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes. 2 PublicationsCorresponds to variant dbSNP:rs151340628EnsemblClinVar.1
Natural variantiVAR_065611594I → 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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi281E → A: Abolishes proton transport, but not chloride transport. 1 Publication1
Mutagenesisi687Y → A: Strongly decreased affinity for ATP, but no effect on chloride transport. 1 Publication1
Mutagenesisi688S → A: No effect ATP binding or chloride transport. 1 Publication1
Mutagenesisi742Y → A: Abolishes interaction with NEDD4 and NEDD4L. 1 Publication1
Mutagenesisi797D → 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.

More...
GeneReviewsi
CLCN5

MalaCards human disease database

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

Open Targets

More...
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

More...
PharmGKBi
PA26550

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
P51795, Tbio

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
CLCN5

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000944461 – 816H(+)/Cl(-) exchange transporter 5Add BLAST816

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Encyclopedia of Proteome Dynamics

More...
EPDi
P51795

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P51795

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...
MassIVEi
P51795

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P51795

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

More...
PaxDbi
P51795

PeptideAtlas

More...
PeptideAtlasi
P51795

PRoteomics IDEntifications database

More...
PRIDEi
P51795

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
56391 [P51795-1]
56392 [P51795-2]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
P51795, 2 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P51795

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

More...
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

More...
Bgeei
ENSG00000171365, Expressed in metanephros and 180 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P51795, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P51795, HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
ENSG00000171365, Tissue enhanced (kidney)

<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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
107598, 10 interactors

Database of interacting proteins

More...
DIPi
DIP-29263N

Protein interaction database and analysis system

More...
IntActi
P51795, 4 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000365256

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P51795, protein

<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

1816
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P51795

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
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%5Fand%5Fdomains%5Fsection">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>Domaini656 – 720CBS 1PROSITE-ProRule annotationAdd BLAST65
Domaini752 – 812CBS 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>Motifi237 – 241Selectivity filter part_1By similarity5
Motifi279 – 283Selectivity filter part_2By similarity5
Motifi523 – 527Selectivity 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

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153763

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_003181_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P51795

KEGG Orthology (KO)

More...
KOi
K05012

Identification of Orthologs from Complete Genome Data

More...
OMAi
ACCCANL

Database of Orthologous Groups

More...
OrthoDBi
271925at2759

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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<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: P51795-2) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
MAMWQGAMDN RGFQQGSFSS FQNSSSDEDL MDIPATAMDF SMRDDVPPLD
60 70 80 90 100
REVGEDKSYN GGGIGSSNRI MDFLEEPIPG VGTYDDFNTI DWVREKSRDR
110 120 130 140 150
DRHREITNKS KESTWALIHS VSDAFSGWLL MLLIGLLSGS LAGLIDISAH
160 170 180 190 200
WMTDLKEGIC TGGFWFNHEH CCWNSEHVTF EERDKCPEWN SWSQLIISTD
210 220 230 240 250
EGAFAYIVNY FMYVLWALLF AFLAVSLVKV FAPYACGSGI PEIKTILSGF
260 270 280 290 300
IIRGYLGKWT LVIKTITLVL AVSSGLSLGK EGPLVHVACC CGNILCHCFN
310 320 330 340 350
KYRKNEAKRR EVLSAAAAAG VSVAFGAPIG GVLFSLEEVS YYFPLKTLWR
360 370 380 390 400
SFFAALVAAF TLRSINPFGN SRLVLFYVEF HTPWHLFELV PFILLGIFGG
410 420 430 440 450
LWGALFIRTN IAWCRKRKTT QLGKYPVIEV LVVTAITAIL AFPNEYTRMS
460 470 480 490 500
TSELISELFN DCGLLDSSKL CDYENRFNTS KGGELPDRPA GVGVYSAMWQ
510 520 530 540 550
LALTLILKIV ITIFTFGMKI PSGLFIPSMA VGAIAGRLLG VGMEQLAYYH
560 570 580 590 600
QEWTVFNSWC SQGADCITPG LYAMVGAAAC LGGVTRMTVS LVVIMFELTG
610 620 630 640 650
GLEYIVPLMA AAMTSKWVAD ALGREGIYDA HIRLNGYPFL EAKEEFAHKT
660 670 680 690 700
LAMDVMKPRR NDPLLTVLTQ DSMTVEDVET IISETTYSGF PVVVSRESQR
710 720 730 740 750
LVGFVLRRDL IISIENARKK QDGVVSTSII YFTEHSPPLP PYTPPTLKLR
760 770 780 790 800
NILDLSPFTV TDLTPMEIVV DIFRKLGLRQ CLVTHNGRLL GIITKKDVLK
810
HIAQMANQDP DSILFN
Length:816
Mass (Da):90,785
Last modified:August 12, 2020 - 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:iC9C63CC222959F35
GO
Isoform 2 (identifier: P51795-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.

Show »
Length:746
Mass (Da):83,147
Checksum:iEF913C5BA40C85D8
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: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>
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 conflicti802I → V in BAG51748 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_001615100R → RH in NPHL2. 1 Publication1
Natural variantiVAR_001616127G → V in NPHL2; alters targeting to endosomes. 3 PublicationsCorresponds to variant dbSNP:rs151340629EnsemblClinVar.1
Natural variantiVAR_048694212M → I. Corresponds to variant dbSNP:rs34800648EnsemblClinVar.1
Natural variantiVAR_065591249G → D in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_001617270L → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 PublicationsCorresponds to variant dbSNP:rs151340622EnsemblClinVar.1
Natural variantiVAR_065592273S → L in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_065593282G → 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_065594289C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications1
Natural variantiVAR_065595291C → R in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 Publications1
Natural variantiVAR_065596295L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 PublicationCorresponds to variant dbSNP:rs273585645EnsemblClinVar.1
Natural variantiVAR_001618314S → 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_065597330G → 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_065598337E → A in NPHL2. 1 Publication1
Natural variantiVAR_065599337Missing in NPHL2. 1 Publication1
Natural variantiVAR_065600340S → G in NPHL2. 1 Publication1
Natural variantiVAR_065601340S → R in NPHL2; retained in the endoplasmic reticulum; alters protein stability; associated with an abolition of chloride current. 2 Publications1
Natural variantiVAR_065602342Y → 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_065603343F → L in NPHL2. 1 Publication1
Natural variantiVAR_065604348L → 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_001619350R → P in LMWPHN; 70% reduction in chloride transport activity and alters targeting to endosomes. 2 PublicationsCorresponds to variant dbSNP:rs151340628EnsemblClinVar.1
Natural variantiVAR_075519403G → R in NPHL2; unknown pathological significance. 1 Publication1
Natural variantiVAR_065605410N → K in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 2 PublicationsCorresponds to variant dbSNP:rs273585646EnsemblClinVar.1
Natural variantiVAR_065606532G → D in NPHL2. 1 Publication1
Natural variantiVAR_065607539L → P in NPHL2; retained in the endoplasmic reticulum; improperly N-glycosylated and non-functional. 1 Publication1
Natural variantiVAR_001620576G → E in NPHL1. 1 PublicationCorresponds to variant dbSNP:rs151340625EnsemblClinVar.1
Natural variantiVAR_001621582G → R in NPHL2; abolishes the chloride currents. 1 Publication1
Natural variantiVAR_065608583G → E in NPHL2; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 1 Publication1
Natural variantiVAR_065609583G → R in NPHL2. 2 PublicationsCorresponds to variant dbSNP:rs273585647EnsemblClinVar.1
Natural variantiVAR_065610586R → 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_001622590S → P in NPHL2. 1 PublicationCorresponds to variant dbSNP:rs151340623EnsemblClinVar.1
Natural variantiVAR_065611594I → K in LMWPHN; causes retention in the endoplasmic reticulum and alters protein stability; total loss of function. 2 Publications1
Natural variantiVAR_001623597E → D in NPHL2; abolishes the chloride currents; total loss of function. 2 Publications1
Natural variantiVAR_065612615S → N in NPHL2. 1 Publication1
Natural variantiVAR_065613616K → 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_065614617W → 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_065615727T → S in NPHL2. 1 PublicationCorresponds to variant dbSNP:rs144207967EnsemblClinVar.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0606541 – 70Missing in isoform 2. CuratedAdd BLAST70

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

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 [P51795-2]

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

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/F641-816[»]
2JA3X-ray3.05A/B/C/D/E/F641-816[»]
SMRiP51795
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi107598, 10 interactors
DIPiDIP-29263N
IntActiP51795, 4 interactors
STRINGi9606.ENSP00000365256

PTM databases

GlyGeniP51795, 2 sites
iPTMnetiP51795
PhosphoSitePlusiP51795

Polymorphism and mutation databases

BioMutaiCLCN5

Proteomic databases

EPDiP51795
jPOSTiP51795
MassIVEiP51795
MaxQBiP51795
PaxDbiP51795
PeptideAtlasiP51795
PRIDEiP51795
ProteomicsDBi56391 [P51795-1]
56392 [P51795-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
396, 190 antibodies

The DNASU plasmid repository

More...
DNASUi
1184

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 [P51795-2]

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
HPAiENSG00000171365, Tissue enhanced (kidney)
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
GeneTreeiENSGT00940000153763
HOGENOMiCLU_003181_2_1_1
InParanoidiP51795
KOiK05012
OMAiACCCANL
OrthoDBi271925at2759
PhylomeDBiP51795
TreeFamiTF313867

Enzyme and pathway databases

PathwayCommonsiP51795
ReactomeiR-HSA-2672351, Stimuli-sensing channels

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
1184, 2 hits in 500 CRISPR screens

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
PharosiP51795, Tbio

Protein Ontology

More...
PROi
PR:P51795
RNActiP51795, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000171365, Expressed in metanephros and 180 other tissues
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...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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%5Fand%5Fisoforms">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: August 12, 2020
Last modified: October 7, 2020
This is version 192 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, Reference proteome

Documents

  1. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  6. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again