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Protein

Cystathionine beta-synthase

Gene

CBS

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

Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (PubMed:23981774, PubMed:20506325, PubMed:23974653). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity).By similarity3 Publications

Caution

There is a duplication of the CBS gene on chromosome 21. CBS, which was originally identified as the gene encoding cystathionine beta-synthase, and CBSL (AC P12345) encode identical proteins.Curated

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

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

pyridoxal 5'-phosphate1 Publication

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

Allosterically activated by S-adenosyl-methionine/AdoMet. Activated by S-adenosylhomocysteine/AdoHcy (PubMed:20506325). Binds non-covalently to a heme group that may control the redox sensitivity of the enzyme (PubMed:11483494, PubMed:12173932, PubMed:22738154).5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-cysteine biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine.3 Publications
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Cystathionine beta-synthase-like protein (CBSL), Cystathionine beta-synthase (CBS)
  2. Cystathionine gamma-lyase (CTH)
This subpathway is part of the pathway L-cysteine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-cysteine from L-homocysteine and L-serine, the pathway L-cysteine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi52Iron (heme axial ligand)2 Publications1
Metal bindingi65Iron (heme axial ligand)2 Publications1
<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 sitei149Pyridoxal phosphate2 Publications1
Binding sitei349Pyridoxal phosphate2 Publications1

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

GO - Biological processi

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

Molecular functionAllosteric enzyme, Lyase
Biological processAmino-acid biosynthesis, Cysteine biosynthesis
LigandHeme, Iron, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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BioCyci
MetaCyc:HS08461-MONOMER

BRENDA Comprehensive Enzyme Information System

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BRENDAi
4.2.1.22 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-1614603 Cysteine formation from homocysteine
R-HSA-2408508 Metabolism of ingested SeMet, Sec, MeSec into H2Se

SABIO-RK: Biochemical Reaction Kinetics Database

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SABIO-RKi
P35520

SIGNOR Signaling Network Open Resource

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SIGNORi
P35520

UniPathway: a resource for the exploration and annotation of metabolic pathways

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UniPathwayi
UPA00136;UER00201

<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:
Cystathionine beta-synthaseCurated (EC:4.2.1.224 Publications)
Alternative name(s):
Beta-thionase
Serine sulfhydrase
<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:CBS
<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 21

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000160200.17

Human Gene Nomenclature Database

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HGNCi
HGNC:1550 CBS

Online Mendelian Inheritance in Man (OMIM)

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MIMi
613381 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P35520

<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

Keywords - Cellular componenti

Cytoplasm, Nucleus

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

<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

Cystathionine beta-synthase deficiency (CBSD)40 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn enzymatic deficiency resulting in altered sulfur metabolism and homocystinuria. The clinical features of untreated homocystinuria due to CBS deficiency include myopia, ectopia lentis, mental retardation, skeletal anomalies resembling Marfan syndrome, and thromboembolic events. Light skin and hair can also be present. Biochemical features include increased urinary homocystine and methionine.
See also OMIM:236200
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_00804949P → L in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation. 3 PublicationsCorresponds to variant dbSNP:rs148865119EnsemblClinVar.1
Natural variantiVAR_00805058R → W in CBSD; linked with V-114; 18% of activity. 1 PublicationCorresponds to variant dbSNP:rs555959266Ensembl.1
Natural variantiVAR_02179065H → R in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation. 2 Publications1
Natural variantiVAR_00217178P → R in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation. 2 PublicationsCorresponds to variant dbSNP:rs786204608EnsemblClinVar.1
Natural variantiVAR_00805185G → R in CBSD; loss of cystathionine beta-synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs863223435EnsemblClinVar.1
Natural variantiVAR_07459087T → N in CBSD; decreased cystathionine beta-synthase activity; increased aggregation. 1 Publication1
Natural variantiVAR_00217288P → S in CBSD. 1 Publication1
Natural variantiVAR_021791101L → P in CBSD; common mutation in Irish population; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs786204757EnsemblClinVar.1
Natural variantiVAR_002173102K → N in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation. 2 PublicationsCorresponds to variant dbSNP:rs786204609EnsemblClinVar.1
Natural variantiVAR_021792109C → R in CBSD; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs778220779EnsemblClinVar.1
Natural variantiVAR_002174114A → V in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates. 3 PublicationsCorresponds to variant dbSNP:rs121964964EnsemblClinVar.1
Natural variantiVAR_008053116G → R in CBSD. 1 PublicationCorresponds to variant dbSNP:rs760214620EnsemblClinVar.1
Natural variantiVAR_008054121R → C in CBSD. Corresponds to variant dbSNP:rs775992753EnsemblClinVar.1
Natural variantiVAR_008055121R → H in CBSD. Corresponds to variant dbSNP:rs770095972EnsemblClinVar.1
Natural variantiVAR_008056121R → L in CBSD; mild form. Corresponds to variant dbSNP:rs770095972EnsemblClinVar.1
Natural variantiVAR_046923125R → P in CBSD. 1 Publication1
Natural variantiVAR_002175125R → Q in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation. 4 PublicationsCorresponds to variant dbSNP:rs781444670EnsemblClinVar.1
Natural variantiVAR_008057125R → W in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. 2 PublicationsCorresponds to variant dbSNP:rs886057100EnsemblClinVar.1
Natural variantiVAR_008058126M → V in CBSD; loss of activity. 1 Publication1
Natural variantiVAR_008059128E → D in CBSD. 1
Natural variantiVAR_002176131E → D in CBSD; linked with Q-125; loss of activity. 1 Publication1
Natural variantiVAR_008060139G → R in CBSD; mild form. 1 PublicationCorresponds to variant dbSNP:rs121964965EnsemblClinVar.1
Natural variantiVAR_021793143I → M in CBSD; 4% of activity; stable. 1 Publication1
Natural variantiVAR_002177144E → K in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation. 6 PublicationsCorresponds to variant dbSNP:rs121964966EnsemblClinVar.1
Natural variantiVAR_002178145P → L in CBSD. 1 PublicationCorresponds to variant dbSNP:rs121964963EnsemblClinVar.1
Natural variantiVAR_008061148G → R in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation. 3 PublicationsCorresponds to variant dbSNP:rs755952006EnsemblClinVar.1
Natural variantiVAR_008063151 – 159Missing in CBSD. 9
Natural variantiVAR_008062151G → R in CBSD. Corresponds to variant dbSNP:rs373782713Ensembl.1
Natural variantiVAR_008064152I → M in CBSD; severe form. 1
Natural variantiVAR_046924154L → Q in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. 1 Publication1
Natural variantiVAR_008065155A → T in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates. 1 Publication1
Natural variantiVAR_046925155A → V in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. 1 Publication1
Natural variantiVAR_002179165C → Y in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation. 5 Publications1
Natural variantiVAR_046926168V → A in CBSD. 1 Publication1
Natural variantiVAR_002180168V → M in CBSD. 1 PublicationCorresponds to variant dbSNP:rs121964970EnsemblClinVar.1
Natural variantiVAR_046927173M → V in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure. 1 Publication1
Natural variantiVAR_066098173Missing in CBSD; loss of activity. 1 Publication1
Natural variantiVAR_008066176E → K in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates. 3 Publications1
Natural variantiVAR_008067180V → A in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation. 1 Publication1
Natural variantiVAR_008068191T → M in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure. 4 PublicationsCorresponds to variant dbSNP:rs121964973EnsemblClinVar.1
Natural variantiVAR_008069198D → V in CBSD. 1
Natural variantiVAR_066099200P → L in CBSD. 1 PublicationCorresponds to variant dbSNP:rs758712880Ensembl.1
Natural variantiVAR_002181224R → H in CBSD. 1 PublicationCorresponds to variant dbSNP:rs761647392Ensembl.1
Natural variantiVAR_008070226A → T in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure. 2 PublicationsCorresponds to variant dbSNP:rs763835246EnsemblClinVar.1
Natural variantiVAR_021794228N → K in CBSD; loss of cystathionine beta-synthase activity; decreased homotetramer formation. 4 Publications1
Natural variantiVAR_046928228N → S in CBSD; has significantly decreased levels of enzyme activity. 1 Publication1
Natural variantiVAR_046929231A → P in CBSD; has significantly decreased levels of enzyme activity. 1 Publication1
Natural variantiVAR_008071234D → N in CBSD; decreased cystathionine beta-synthase activity; changed localization; decreased interaction with pyridoxal 5'-phosphate; no effect on homotetramer formation. 1 PublicationCorresponds to variant dbSNP:rs773734233EnsemblClinVar.1
Natural variantiVAR_046930234Missing in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. 1 Publication1
Natural variantiVAR_002182239E → K in CBSD. 1
Natural variantiVAR_046931247 – 256Missing in CBSD. 1 Publication10
Natural variantiVAR_002183257T → M in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs758236584EnsemblClinVar.1
Natural variantiVAR_008072262T → M in CBSD; moderate form. 2 PublicationsCorresponds to variant dbSNP:rs149119723EnsemblClinVar.1
Natural variantiVAR_021795262T → R in CBSD; severe form; loss of cystathionine beta-synthase activity; loss of homotetramer formation. 2 Publications1
Natural variantiVAR_008073266R → G in CBSD. 1
Natural variantiVAR_008074266R → K in CBSD; mild form; decreased cystathionine beta-synthase activity; decreased homotetramer formation; no effect on heme-binding; decreased stability. 3 PublicationsCorresponds to variant dbSNP:rs121964969EnsemblClinVar.1
Natural variantiVAR_074591269Missing in CBSD; loss of expression. 1 Publication1
Natural variantiVAR_008075270Missing in CBSD. 1
Natural variantiVAR_021796275C → Y in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. 2 Publications1
Natural variantiVAR_066100278I → S in CBSD; loss of activity. 1 Publication1
Natural variantiVAR_002184278I → T in CBSD; mild to severe form; common mutation; decreased expression; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; severely affects homotetramer formation by promoting formation of larger aggregates. 19 PublicationsCorresponds to variant dbSNP:rs5742905EnsemblClinVar.1
Natural variantiVAR_066101281D → N in CBSD; loss of activity. 1 Publication1
Natural variantiVAR_046932288A → P in CBSD. 1 Publication1
Natural variantiVAR_046933288A → T in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. 1 PublicationCorresponds to variant dbSNP:rs141502207EnsemblClinVar.1
Natural variantiVAR_002185290P → L in CBSD. 2 PublicationsCorresponds to variant dbSNP:rs760912339Ensembl.1
Natural variantiVAR_008076302E → K in CBSD; no effect on cystathionine beta-synthase activity; inhibited by AdoHcy and impaired activation by AdoMet; no effect on homotetramer formation. 3 PublicationsCorresponds to variant dbSNP:rs779270933EnsemblClinVar.1
Natural variantiVAR_008077305G → R in CBSD; loss of cystathionine beta-synthase activity; no effect on homotetramer formation. 1 Publication1
Natural variantiVAR_002186307G → S in CBSD; moderate to severe form; linked with D-534; common mutation; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; no effect on homotetramer formation. 8 PublicationsCorresponds to variant dbSNP:rs121964962EnsemblClinVar.1
Natural variantiVAR_008078320V → A in CBSD; has 36% of wild-type enzyme activity. 2 PublicationsCorresponds to variant dbSNP:rs781567152EnsemblClinVar.1
Natural variantiVAR_066102321D → V in CBSD; loss of activity. 1 Publication1
Natural variantiVAR_008079331A → E in CBSD. 2 PublicationsCorresponds to variant dbSNP:rs777919630EnsemblClinVar.1
Natural variantiVAR_002187331A → V in CBSD. 1 PublicationCorresponds to variant dbSNP:rs777919630EnsemblClinVar.1
Natural variantiVAR_002188336R → C in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure. 6 PublicationsCorresponds to variant dbSNP:rs398123151EnsemblClinVar.1
Natural variantiVAR_008080336R → H in CBSD; mild form; no effect on expression; exhibits an activity lower than 4% of the wild-type enzyme; altered stimulation by AdoMet; absent capacity to form multimeric quaternary structure. 2 PublicationsCorresponds to variant dbSNP:rs760417941EnsemblClinVar.1
Natural variantiVAR_021797338L → P in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. 2 Publications1
Natural variantiVAR_021798347G → S in CBSD; protein expression is comparable to wild-type; loss of activity. 2 PublicationsCorresponds to variant dbSNP:rs771298943EnsemblClinVar.1
Natural variantiVAR_021799349S → N in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. 2 Publications1
Natural variantiVAR_008081352S → N in CBSD. 1
Natural variantiVAR_008082353T → M in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. 4 PublicationsCorresponds to variant dbSNP:rs121964972EnsemblClinVar.1
Natural variantiVAR_008083354V → M in CBSD. Corresponds to variant dbSNP:rs267606146Ensembl.1
Natural variantiVAR_021800355A → P in CBSD. 1 Publication1
Natural variantiVAR_046934361A → T in CBSD. 1 PublicationCorresponds to variant dbSNP:rs745764562Ensembl.1
Natural variantiVAR_008084369R → C in CBSD; when linked with C-491 severe form; decreased cystathionine beta-synthase activity; decreased homotetramer formation. 3 PublicationsCorresponds to variant dbSNP:rs117687681EnsemblClinVar.1
Natural variantiVAR_002189369R → H in CBSD. Corresponds to variant dbSNP:rs11700812EnsemblClinVar.1
Natural variantiVAR_008085370C → Y in CBSD. 1 PublicationCorresponds to variant dbSNP:rs757920190EnsemblClinVar.1
Natural variantiVAR_002190371V → M in CBSD. 2 PublicationsCorresponds to variant dbSNP:rs372010465EnsemblClinVar.1
Natural variantiVAR_046935376D → N in CBSD; has significantly decreased levels of enzyme activity. 1 Publication1
Natural variantiVAR_021801379R → Q in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. 2 PublicationsCorresponds to variant dbSNP:rs763036586EnsemblClinVar.1
Natural variantiVAR_046936379R → W in CBSD. 1 PublicationCorresponds to variant dbSNP:rs769080151EnsemblClinVar.1
Natural variantiVAR_002191384K → E in CBSD; severe form. 1 PublicationCorresponds to variant dbSNP:rs121964967EnsemblClinVar.1
Natural variantiVAR_008086384K → N in CBSD; moderate form. 1
Natural variantiVAR_008087391M → I in CBSD. 1
Natural variantiVAR_021802422P → L in CBSD; changed cystathionine beta-synthase activity; impaired stimulation by AdoMet; does not affect homotetramer formation. 2 PublicationsCorresponds to variant dbSNP:rs28934892EnsemblClinVar.1
Natural variantiVAR_074592427P → L in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet. 2 PublicationsCorresponds to variant dbSNP:rs863223434EnsemblClinVar.1
Natural variantiVAR_008088434T → N in CBSD. 1
Natural variantiVAR_008089435I → T in CBSD; no effect on cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; does not affect homotetramer formation. 2 Publications1
Natural variantiVAR_008090439R → Q in CBSD; no effect on cystathionine beta-synthase activity; increased homotetramer formation. 4 PublicationsCorresponds to variant dbSNP:rs756467921EnsemblClinVar.1
Natural variantiVAR_002192444D → N in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet; increased homotetramer formation. 5 PublicationsCorresponds to variant dbSNP:rs28934891EnsemblClinVar.1
Natural variantiVAR_066103446A → S in CBSD. 1 Publication1
Natural variantiVAR_074593449V → G in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet. 1 Publication1
Natural variantiVAR_002193454V → E in CBSD. 1 Publication1
Natural variantiVAR_021803456L → P in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. 2 Publications1
Natural variantiVAR_008091466S → L in CBSD; increased cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation. 2 PublicationsCorresponds to variant dbSNP:rs121964971EnsemblClinVar.1
Natural variantiVAR_008092491R → C in CBSD; linked with C-369. 1
Natural variantiVAR_074594500S → L in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet. 2 PublicationsCorresponds to variant dbSNP:rs755106884Ensembl.1
Natural variantiVAR_046937526Q → K in CBSD; has significantly decreased levels of enzyme activity. 1 Publication1
Natural variantiVAR_008093534V → D in CBSD; linked with S-307. 1
Natural variantiVAR_002194539L → S in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation. 2 PublicationsCorresponds to variant dbSNP:rs121964968EnsemblClinVar.1
Natural variantiVAR_074595540L → Q in CBSD; no effect on cystathionine beta-synthase activity; altered stimulation by AdoMet. 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>Mutagenesisi272C → A: Reduced heme content and cystathionine beta-synthase activity. 1 Publication1
Mutagenesisi275C → S: Reduced heme content and cystathionine beta-synthase activity. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNET

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DisGeNETi
102724560
875

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

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GeneReviewsi
CBS

MalaCards human disease database

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MalaCardsi
CBS
MIMi236200 phenotype

Open Targets

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OpenTargetsi
ENSG00000160200
ENSG00000274276

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

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Orphaneti
394 Classic homocystinuria

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA26123

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3399911

Drug and drug target database

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DrugBanki
DB00151 L-Cysteine
DB00133 L-Serine
DB00114 Pyridoxal Phosphate
DB00118 S-Adenosylmethionine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1443

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
CBS

Domain mapping of disease mutations (DMDM)

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DMDMi
543959

<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_00001671331 – 551Cystathionine beta-synthaseAdd BLAST551

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei27PhosphoserineCombined sources1
Modified residuei119N6-(pyridoxal phosphate)lysine2 Publications1
Modified residuei199PhosphoserineCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P35520

MaxQB - The MaxQuant DataBase

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MaxQBi
P35520

PeptideAtlas

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PeptideAtlasi
P35520

PRoteomics IDEntifications database

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PRIDEi
P35520

ProteomicsDB human proteome resource

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ProteomicsDBi
55074
55075 [P35520-2]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P35520

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

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PhosphoSitePlusi
P35520

<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

In the adult strongly expressed in liver and pancreas, some expression in heart and brain, weak expression in lung and kidney. In the fetus, expressed in brain, liver and kidney.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000160200 Expressed in 89 organ(s), highest expression level in right lobe of liver

CleanEx database of gene expression profiles

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CleanExi
HS_CBS

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P35520 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P35520 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA001223

<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

Homotetramer.4 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
107321, 82 interactors
3195666, 1 interactor

Protein interaction database and analysis system

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IntActi
P35520, 22 interactors

Molecular INTeraction database

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MINTi
P35520

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
P35520

<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

1551
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
P35520

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

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SMRi
P35520

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
P35520

<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>Domaini418 – 476CBSPROSITE-ProRule annotationAdd BLAST59

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni256 – 260Pyridoxal phosphate binding2 Publications5

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1252 Eukaryota
COG0031 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00510000047027

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000217392

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG000918

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P35520

KEGG Orthology (KO)

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KOi
K01697

Identification of Orthologs from Complete Genome Data

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OMAi
IGYRMVQ

Database of Orthologous Groups

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OrthoDBi
EOG091G02TP

Database for complete collections of gene phylogenies

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PhylomeDBi
P35520

TreeFam database of animal gene trees

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TreeFami
TF300784

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR000644 CBS_dom
IPR005857 Cysta_beta_synth
IPR001216 P-phosphate_BS
IPR001926 PLP-dep
IPR036052 Trypto_synt_PLP_dependent

Pfam protein domain database

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Pfami
View protein in Pfam
PF00571 CBS, 1 hit
PF00291 PALP, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00116 CBS, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF53686 SSF53686, 1 hit

TIGRFAMs; a protein family database

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TIGRFAMsi
TIGR01137 cysta_beta, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51371 CBS, 1 hit
PS00901 CYS_SYNTHASE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>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: P35520-1) [UniParc]FASTAAdd to basket
Also known as: Major

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
MPSETPQAEV GPTGCPHRSG PHSAKGSLEK GSPEDKEAKE PLWIRPDAPS
60 70 80 90 100
RCTWQLGRPA SESPHHHTAP AKSPKILPDI LKKIGDTPMV RINKIGKKFG
110 120 130 140 150
LKCELLAKCE FFNAGGSVKD RISLRMIEDA ERDGTLKPGD TIIEPTSGNT
160 170 180 190 200
GIGLALAAAV RGYRCIIVMP EKMSSEKVDV LRALGAEIVR TPTNARFDSP
210 220 230 240 250
ESHVGVAWRL KNEIPNSHIL DQYRNASNPL AHYDTTADEI LQQCDGKLDM
260 270 280 290 300
LVASVGTGGT ITGIARKLKE KCPGCRIIGV DPEGSILAEP EELNQTEQTT
310 320 330 340 350
YEVEGIGYDF IPTVLDRTVV DKWFKSNDEE AFTFARMLIA QEGLLCGGSA
360 370 380 390 400
GSTVAVAVKA AQELQEGQRC VVILPDSVRN YMTKFLSDRW MLQKGFLKEE
410 420 430 440 450
DLTEKKPWWW HLRVQELGLS APLTVLPTIT CGHTIEILRE KGFDQAPVVD
460 470 480 490 500
EAGVILGMVT LGNMLSSLLA GKVQPSDQVG KVIYKQFKQI RLTDTLGRLS
510 520 530 540 550
HILEMDHFAL VVHEQIQYHS TGKSSQRQMV FGVVTAIDLL NFVAAQERDQ

K
Length:551
Mass (Da):60,587
Last modified:January 23, 2007 - 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:iF89E69C67BDE6701
GO
Isoform 2 (identifier: P35520-2) [UniParc]FASTAAdd to basket
Also known as: Minor

The sequence of this isoform differs from the canonical sequence as follows:
     518-518: Y → SQDQAWAGVVGGPAD

Show »
Length:565
Mass (Da):61,863
Checksum:i8BD062B080067092
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
C9JMA6C9JMA6_HUMAN
Cystathionine beta-synthase
CBS
177Annotation 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>
H7C2H4H7C2H4_HUMAN
Cystathionine beta-synthase
CBS
224Annotation 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>
H7C2W0H7C2W0_HUMAN
Cystathionine beta-synthase
CBS
159Annotation 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>
H7C1W6H7C1W6_HUMAN
Cystathionine beta-synthase
CBS
149Annotation 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 conflicti58R → P in CAA61252 (PubMed:9383285).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04692118R → C Functional polymorphism; associated with 1/3 to 2/3 the enzyme activity of the wild-type. 1 PublicationCorresponds to variant dbSNP:rs201827340EnsemblClinVar.1
Natural variantiVAR_00804949P → L in CBSD; decreased expression; no effect on cystathionine beta-synthase activity; increased homotetramer formation. 3 PublicationsCorresponds to variant dbSNP:rs148865119EnsemblClinVar.1
Natural variantiVAR_00805058R → W in CBSD; linked with V-114; 18% of activity. 1 PublicationCorresponds to variant dbSNP:rs555959266Ensembl.1
Natural variantiVAR_02179065H → R in CBSD; decreased cystathionine beta-synthase activity; inhibited by AdoMet and AdoHcy; decreased homotetramer formation. 2 Publications1
Natural variantiVAR_04692269A → P1 PublicationCorresponds to variant dbSNP:rs17849313Ensembl.1
Natural variantiVAR_00217178P → R in CBSD; severe form; associated in cis with N-102; decreased cystathionine beta-synthase activity; decreased homotetramer formation. 2 PublicationsCorresponds to variant dbSNP:rs786204608EnsemblClinVar.1
Natural variantiVAR_00805185G → R in CBSD; loss of cystathionine beta-synthase activity. 2 PublicationsCorresponds to variant dbSNP:rs863223435EnsemblClinVar.1
Natural variantiVAR_07459087T → N in CBSD; decreased cystathionine beta-synthase activity; increased aggregation. 1 Publication1
Natural variantiVAR_00217288P → S in CBSD. 1 Publication1
Natural variantiVAR_021791101L → P in CBSD; common mutation in Irish population; loss of activity. 3 PublicationsCorresponds to variant dbSNP:rs786204757EnsemblClinVar.1
Natural variantiVAR_002173102K → N in CBSD; associated in cis with R-78; decreased cystathionine beta-synthase activity; decreased homotetramer formation. 2 PublicationsCorresponds to variant dbSNP:rs786204609EnsemblClinVar.1
Natural variantiVAR_008052102K → Q1 PublicationCorresponds to variant dbSNP:rs34040148EnsemblClinVar.1
Natural variantiVAR_021792109C → R in CBSD; loss of activity. 1 PublicationCorresponds to variant dbSNP:rs778220779EnsemblClinVar.1
Natural variantiVAR_002174114A → V in CBSD; mild form; when linked with W-58 severe form; decreased cystathionine beta-synthase activity; decreases homotetramer formation by promoting formation of larger aggregates. 3 PublicationsCorresponds to variant dbSNP:rs121964964EnsemblClinVar.1
Natural variantiVAR_008053116G → R in CBSD. 1 PublicationCorresponds to variant dbSNP:rs760214620EnsemblClinVar.1
Natural variantiVAR_008054121R → C in CBSD. Corresponds to variant dbSNP:rs775992753EnsemblClinVar.1
Natural variantiVAR_008055121R → H in CBSD. Corresponds to variant dbSNP:rs770095972EnsemblClinVar.1
Natural variantiVAR_008056121R → L in CBSD; mild form. Corresponds to variant dbSNP:rs770095972EnsemblClinVar.1
Natural variantiVAR_046923125R → P in CBSD. 1 Publication1
Natural variantiVAR_002175125R → Q in CBSD; severe form; when linked with D-131 moderate form; loss of cystathionine beta-synthase activity; decreased homotetramer formation. 4 PublicationsCorresponds to variant dbSNP:rs781444670EnsemblClinVar.1
Natural variantiVAR_008057125R → W in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. 2 PublicationsCorresponds to variant dbSNP:rs886057100EnsemblClinVar.1
Natural variantiVAR_008058126M → V in CBSD; loss of activity. 1 Publication1
Natural variantiVAR_008059128E → D in CBSD. 1
Natural variantiVAR_002176131E → D in CBSD; linked with Q-125; loss of activity. 1 Publication1
Natural variantiVAR_008060139G → R in CBSD; mild form. 1 PublicationCorresponds to variant dbSNP:rs121964965EnsemblClinVar.1
Natural variantiVAR_021793143I → M in CBSD; 4% of activity; stable. 1 Publication1
Natural variantiVAR_002177144E → K in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; decreased homotetramer formation. 6 PublicationsCorresponds to variant dbSNP:rs121964966EnsemblClinVar.1
Natural variantiVAR_002178145P → L in CBSD. 1 PublicationCorresponds to variant dbSNP:rs121964963EnsemblClinVar.1
Natural variantiVAR_008061148G → R in CBSD; loss of cystathionine beta-synthase activity; impaired stimulation by AdoMet and AdoHcy; loss of homotetramer formation. 3 PublicationsCorresponds to variant dbSNP:rs755952006EnsemblClinVar.1
Natural variantiVAR_008063151 – 159Missing in CBSD. 9
Natural variantiVAR_008062151G → R in CBSD. Corresponds to variant dbSNP:rs373782713Ensembl.1
Natural variantiVAR_008064152I → M in CBSD; severe form. 1
Natural variantiVAR_046924154L → Q in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. 1 Publication1
Natural variantiVAR_008065155A → T in CBSD; complete loss of activity; severely affects homotetramer formation by promoting formation of larger aggregates. 1 Publication1
Natural variantiVAR_046925155A → V in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. 1 Publication1
Natural variantiVAR_002179165C → Y in CBSD; severe form; protein expression is comparable to wild-type; loss of cystathionine beta-synthase activity; no effect on homotetramer formation. 5 Publications1
Natural variantiVAR_046926168V → A in CBSD. 1 Publication1
Natural variantiVAR_002180168V → M in CBSD. 1 PublicationCorresponds to variant dbSNP:rs121964970EnsemblClinVar.1
Natural variantiVAR_046927173M → V in CBSD; presents 40% of the wild-type activity; highly reduced capacity to form multimeric quaternary structure. 1 Publication1
Natural variantiVAR_066098173Missing in CBSD; loss of activity. 1 Publication1
Natural variantiVAR_008066176E → K in CBSD; severe form; loss of cystathionine beta-synthase activity; inhibited by AdoMet; severely decreases homotetramer formation by promoting formation of larger aggregates. 3 Publications1
Natural variantiVAR_008067180V → A in CBSD; decreased cystathionine beta-synthase activity; decreases homotetramer formation. 1 Publication1
Natural variantiVAR_008068191T → M in CBSD; moderate and severe forms; loss of cystathionine beta-synthase activity; absent capacity to form multimeric quaternary structure. 4 PublicationsCorresponds to variant dbSNP:rs121964973EnsemblClinVar.1
Natural variantiVAR_008069198D → V in CBSD. 1
Natural variantiVAR_066099200P → L in CBSD. 1 PublicationCorresponds to variant dbSNP:rs758712880Ensembl.1
Natural variantiVAR_002181224R → H in CBSD. 1 PublicationCorresponds to variant dbSNP:rs761647392Ensembl.1
Natural variantiVAR_008070226A → T in CBSD; presents 20% of the wild-type activi