Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P35520 (CBS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 167. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystathionine beta-synthase

EC=4.2.1.22
Alternative name(s):
Beta-thionase
Serine sulfhydrase
Gene names
Name:CBS
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length551 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury By similarity.

Catalytic activity

L-serine + L-homocysteine = L-cystathionine + H2O.

Cofactor

Pyridoxal phosphate.

Enzyme regulation

Allosterically activated by adenosyl-methionine (AdoMet).

Pathway

Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2.

Subunit structure

Homotetramer. Ref.15

Subcellular location

Cytoplasm. Nucleus Ref.11.

Tissue specificity

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.

Involvement in disease

Cystathionine beta-synthase deficiency (CBSD) [MIM:236200]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.40 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47 Ref.48 Ref.49 Ref.50 Ref.51 Ref.52

Sequence similarities

Belongs to the cysteine synthase/cystathionine beta-synthase family.

Contains 1 CBS domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Cysteine biosynthesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainCBS domain
   LigandHeme
Iron
Metal-binding
Pyridoxal phosphate
   Molecular functionLyase
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-cysteine catabolic process

Inferred from direct assay PubMed 15520012. Source: UniProtKB

L-serine catabolic process

Inferred from direct assay PubMed 18776696. Source: UniProtKB

L-serine metabolic process

Inferred from direct assay PubMed 19010420. Source: UniProtKB

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

cartilage development involved in endochondral bone morphogenesis

Inferred from electronic annotation. Source: Ensembl

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cerebellum morphogenesis

Inferred from electronic annotation. Source: Ensembl

cysteine biosynthetic process from serine

Inferred from electronic annotation. Source: InterPro

cysteine biosynthetic process via cystathionine

Inferred from electronic annotation. Source: InterPro

endochondral ossification

Inferred from electronic annotation. Source: Ensembl

homocysteine catabolic process

Inferred from direct assay PubMed 18776696. Source: UniProtKB

homocysteine metabolic process

Inferred from direct assay PubMed 19010420PubMed 20031578. Source: UniProtKB

hydrogen sulfide biosynthetic process

Inferred from direct assay PubMed 15520012. Source: UniProtKB

maternal process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of JUN kinase activity

Inferred from electronic annotation. Source: Ensembl

regulation of blood vessel size

Inferred from electronic annotation. Source: Ensembl

regulation of cGMP metabolic process

Inferred from electronic annotation. Source: Ensembl

response to folic acid

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

sulfur amino acid metabolic process

Traceable author statement. Source: Reactome

superoxide metabolic process

Inferred from electronic annotation. Source: Ensembl

transsulfuration

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Inferred from direct assay PubMed 16780588. Source: UniProtKB

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionadenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

cystathionine beta-synthase activity

Inferred from direct assay PubMed 18776696PubMed 19010420PubMed 7929220. Source: UniProtKB

enzyme binding

Inferred from physical interaction Ref.11. Source: UniProtKB

heme binding

Inferred from direct assay PubMed 7929220. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 16189514PubMed 19447967PubMed 21900206. Source: IntAct

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

modified amino acid binding

Inferred from direct assay PubMed 20031578. Source: UniProtKB

protein homodimerization activity

Inferred from direct assay Ref.15. Source: UniProtKB

pyridoxal phosphate binding

Inferred from direct assay PubMed 18776696PubMed 7929220. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-740135,EBI-740135

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P35520-1)

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.
Isoform 2 (identifier: P35520-2)

Also known as: Minor;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 551550Cystathionine beta-synthase
PRO_0000167133

Regions

Domain418 – 47659CBS
Region256 – 2605Pyridoxal phosphate binding

Sites

Metal binding521Iron (heme axial ligand)
Metal binding651Iron (heme axial ligand)
Binding site1491Pyridoxal phosphate
Binding site3491Pyridoxal phosphate

Amino acid modifications

Modified residue271Phosphoserine Ref.14
Modified residue1191N6-(pyridoxal phosphate)lysine
Cross-link211Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.11

Natural variations

Alternative sequence5181Y → SQDQAWAGVVGGPAD in isoform 2.
VSP_001217
Natural variant181R → C Associated with 1/3 to 2/3 the enzyme activity of the wild-type. Ref.49
Corresponds to variant rs201827340 [ dbSNP | Ensembl ].
VAR_046921
Natural variant491P → L in CBSD. Ref.43
VAR_008049
Natural variant581R → W in CBSD; 18% of activity; linked with Val-113. Ref.38
VAR_008050
Natural variant651H → R in CBSD. Ref.40
VAR_021790
Natural variant691A → P. Ref.9
Corresponds to variant rs17849313 [ dbSNP | Ensembl ].
VAR_046922
Natural variant781P → R in CBSD; 50% of activity; severe form. Ref.21
VAR_002171
Natural variant851G → R in CBSD; loss of activity. Ref.42
VAR_008051
Natural variant881P → S in CBSD. Ref.25
VAR_002172
Natural variant1011L → P in CBSD; common mutation in Irish population; loss of activity. Ref.37 Ref.43 Ref.45
VAR_021791
Natural variant1021K → N in CBSD; 50% of activity. Ref.21
VAR_002173
Natural variant1021K → Q in CBSD; severe form; linked with Arg-77. Ref.39
Corresponds to variant rs34040148 [ dbSNP | Ensembl ].
VAR_008052
Natural variant1091C → R in CBSD; loss of activity. Ref.43
VAR_021792
Natural variant1141A → V in CBSD; mild form; when linked with W-58 severe form; partial loss of activity; affects tetramer formation by promoting formation of larger aggregates. Ref.19 Ref.40
VAR_002174
Natural variant1161G → R in CBSD. Ref.30
VAR_008053
Natural variant1211R → C in CBSD.
VAR_008054
Natural variant1211R → H in CBSD.
VAR_008055
Natural variant1211R → L in CBSD; mild form.
VAR_008056
Natural variant1251R → P in CBSD. Ref.41
VAR_046923
Natural variant1251R → Q in CBSD; severe form; loss of activity; when linked with D-132 moderate form. Ref.22 Ref.25 Ref.43
VAR_002175
Natural variant1251R → W in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. Ref.44 Ref.50
VAR_008057
Natural variant1261M → V in CBSD; loss of activity. Ref.38
VAR_008058
Natural variant1281E → D in CBSD.
VAR_008059
Natural variant1311E → D in CBSD; loss of activity; linked with Q-125. Ref.22
VAR_002176
Natural variant1391G → R in CBSD; mild form. Ref.24
VAR_008060
Natural variant1431I → M in CBSD; 4% of activity; stable. Ref.46
VAR_021793
Natural variant1441E → K in CBSD; loss of activity. Ref.24 Ref.31 Ref.36 Ref.40 Ref.43
VAR_002177
Natural variant1451P → L in CBSD; linked with Q-438. Ref.19
VAR_002178
Natural variant1481G → R in CBSD; loss of activity; absent capacity to form multimeric quaternary structure. Ref.46 Ref.50
VAR_008061
Natural variant151 – 1599Missing in CBSD.
VAR_008063
Natural variant1511G → R in CBSD.
VAR_008062
Natural variant1521I → M in CBSD; severe form.
VAR_008064
Natural variant1541L → Q in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. Ref.49
VAR_046924
Natural variant1551A → T in CBSD; complete loss of activity; severely affects tetramer formation by promoting formation of larger aggregates. Ref.40
VAR_008065
Natural variant1551A → V in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. Ref.49
VAR_046925
Natural variant1651C → Y in CBSD; severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity. Ref.26 Ref.36 Ref.40 Ref.43
VAR_002179
Natural variant1681V → A in CBSD. Ref.48
VAR_046926
Natural variant1681V → M in CBSD. Ref.27
VAR_002180
Natural variant1731M → V in CBSD; presents 40% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure. Ref.50
VAR_046927
Natural variant1731Missing in CBSD; loss of activity. Ref.51
VAR_066098
Natural variant1761E → K in CBSD; severe form; loss of activity; severely affects tetramer formation by promoting formation of larger aggregates. Ref.34 Ref.40
VAR_008066
Natural variant1801V → A in CBSD.
VAR_008067
Natural variant1911T → M in CBSD; moderate and severe forms; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. Ref.44 Ref.48 Ref.50
VAR_008068
Natural variant1981D → V in CBSD.
VAR_008069
Natural variant2001P → L in CBSD. Ref.51
VAR_066099
Natural variant2241R → H in CBSD. Ref.27
VAR_002181
Natural variant2261A → T in CBSD; presents 20% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure. Ref.45 Ref.50
VAR_008070
Natural variant2281N → K in CBSD; loss of activity. Ref.37 Ref.43 Ref.46
VAR_021794
Natural variant2281N → S in CBSD; has significantly decreased levels of enzyme activity. Ref.45
VAR_046928
Natural variant2311A → P in CBSD; has significantly decreased levels of enzyme activity. Ref.45
VAR_046929
Natural variant2341D → N in CBSD.
VAR_008071
Natural variant2341Missing in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. Ref.49
VAR_046930
Natural variant2391E → K in CBSD.
VAR_002182
Natural variant247 – 25610Missing in CBSD.
VAR_046931
Natural variant2571T → M in CBSD; moderate to severe form; protein expression is comparable to wild-type; significant decrease of enzyme activity. Ref.25 Ref.49
VAR_002183
Natural variant2621T → M in CBSD; moderate form. Ref.32 Ref.37
VAR_008072
Natural variant2621T → R in CBSD; severe form. Ref.39
VAR_021795
Natural variant2661R → G in CBSD.
VAR_008073
Natural variant2661R → K in CBSD; mild form. Ref.32
Corresponds to variant rs28934275 [ dbSNP | Ensembl ].
VAR_008074
Natural variant2701Missing in CBSD.
VAR_008075
Natural variant2751C → Y in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. Ref.44 Ref.50
VAR_021796
Natural variant2781I → S in CBSD; loss of activity. Ref.51
VAR_066100
Natural variant2781I → T in CBSD; mild to severe form; common mutation; loss of activity; severely affects tetramer formation by promoting formation of larger aggregates. Ref.18 Ref.20 Ref.24 Ref.27 Ref.30 Ref.31 Ref.32 Ref.34 Ref.37 Ref.39 Ref.40 Ref.42 Ref.43 Ref.45 Ref.46 Ref.48 Ref.52
Corresponds to variant rs5742905 [ dbSNP | Ensembl ].
VAR_002184
Natural variant2811D → N in CBSD; loss of activity. Ref.51
VAR_066101
Natural variant2881A → P in CBSD. Ref.47
VAR_046932
Natural variant2881A → T in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. Ref.49
VAR_046933
Natural variant2901P → L in CBSD. Ref.28 Ref.30
VAR_002185
Natural variant3021E → K in CBSD; 5% of activity. Ref.38 Ref.43
VAR_008076
Natural variant3051G → R in CBSD.
VAR_008077
Natural variant3071G → S in CBSD; moderate to severe form; linked with D-534; has significantly decreased levels of enzyme activity; common mutation. Ref.20 Ref.27 Ref.32 Ref.34 Ref.37 Ref.43 Ref.45
VAR_002186
Natural variant3201V → A in CBSD; has 36% of wild-type enzyme activity. Ref.32 Ref.45
VAR_008078
Natural variant3211D → V in CBSD; loss of activity. Ref.51
VAR_066102
Natural variant3311A → E in CBSD. Ref.31 Ref.43
VAR_008079
Natural variant3311A → V in CBSD. Ref.27
VAR_002187
Natural variant3361R → C in CBSD; protein expression is comparable to wild-type; loss of activity; absent capacity to form multimeric quaternary structure. Ref.38 Ref.43 Ref.44 Ref.49 Ref.50 Ref.52
VAR_002188
Natural variant3361R → H in CBSD; mild form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. Ref.50
VAR_008080
Natural variant3381L → P in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. Ref.44 Ref.50
VAR_021797
Natural variant3471G → S in CBSD; protein expression is comparable to wild-type; loss of activity. Ref.43 Ref.49
VAR_021798
Natural variant3491S → N in CBSD; severe form; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. Ref.44 Ref.50
VAR_021799
Natural variant3521S → N in CBSD.
VAR_008081
Natural variant3531T → M in CBSD; protein expression is comparable to wild-type; significant decrease of enzyme activity. Ref.31 Ref.43 Ref.45 Ref.49
VAR_008082
Natural variant3541V → M in CBSD.
VAR_008083
Natural variant3551A → P in CBSD. Ref.37
VAR_021800
Natural variant3611A → T in CBSD. Ref.41
VAR_046934
Natural variant3691R → C in CBSD; when linked with C-491 severe form. Ref.32 Ref.43
Corresponds to variant rs117687681 [ dbSNP | Ensembl ].
VAR_008084
Natural variant3691R → H in CBSD.
Corresponds to variant rs11700812 [ dbSNP | Ensembl ].
VAR_002189
Natural variant3701C → Y in CBSD. Ref.35
VAR_008085
Natural variant3711V → M in CBSD. Ref.26 Ref.43
VAR_002190
Natural variant3761D → N in CBSD; has significantly decreased levels of enzyme activity. Ref.45
VAR_046935
Natural variant3791R → Q in CBSD; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. Ref.44 Ref.50
VAR_021801
Natural variant3791R → W in CBSD. Ref.47
VAR_046936
Natural variant3841K → E in CBSD; severe form. Ref.33
VAR_002191
Natural variant3841K → N in CBSD; moderate form.
VAR_008086
Natural variant3911M → I in CBSD.
VAR_008087
Natural variant4221P → L in CBSD; increased activity; does not affect tetramer formation; impaired stimulation by S-adenosylmethionine. Ref.42
Corresponds to variant rs28934892 [ dbSNP | Ensembl ].
VAR_021802
Natural variant4341T → N in CBSD.
VAR_008088
Natural variant4351I → T in CBSD; does not affect activity; does not affect tetramer formation; impaired stimulation by S-adenosylmethionine. Ref.42
VAR_008089
Natural variant4391R → Q in CBSD; linked with K-143. Ref.31 Ref.35 Ref.43
VAR_008090
Natural variant4441D → N in CBSD; impaired stimulation by S-adenosylmethionine. Ref.29 Ref.42
Corresponds to variant rs28934891 [ dbSNP | Ensembl ].
VAR_002192
Natural variant4461A → S in CBSD. Ref.51
VAR_066103
Natural variant4541V → E in CBSD. Ref.27
VAR_002193
Natural variant4561L → P in CBSD; severe; exhibits an activity lower than 4% of the wild-type enzyme; absent capacity to form multimeric quaternary structure. Ref.44 Ref.50
VAR_021803
Natural variant4661S → L in CBSD; increased activity; does not affect tetramer formation; impaired stimulation by S-adenosylmethionine. Ref.42
VAR_008091
Natural variant4911R → C in CBSD; linked with C-368.
VAR_008092
Natural variant5261Q → K in CBSD; has significantly decreased levels of enzyme activity. Ref.45
VAR_046937
Natural variant5341V → D in CBSD; linked with S-306.
VAR_008093
Natural variant5391L → S in CBSD. Ref.33
Corresponds to variant rs121964968 [ dbSNP | Ensembl ].
VAR_002194
Natural variant5481R → Q Presents 60% of the wild-type activity; dramatically reduced capacity to form multimeric quaternary structure. Ref.50
Corresponds to variant rs150828989 [ dbSNP | Ensembl ].
VAR_046938

Experimental info

Mutagenesis2721C → A: Reduced heme content and cystathionine beta-synthase activity. Ref.16
Mutagenesis2751C → S: Reduced heme content and cystathionine beta-synthase activity. Ref.16
Sequence conflict581R → P in CAA61252. Ref.4

Secondary structure

.......................................................................................... 551
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Major) [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F89E69C67BDE6701

FASTA55160,587
        10         20         30         40         50         60 
MPSETPQAEV GPTGCPHRSG PHSAKGSLEK GSPEDKEAKE PLWIRPDAPS RCTWQLGRPA 

        70         80         90        100        110        120 
SESPHHHTAP AKSPKILPDI LKKIGDTPMV RINKIGKKFG LKCELLAKCE FFNAGGSVKD 

       130        140        150        160        170        180 
RISLRMIEDA ERDGTLKPGD TIIEPTSGNT GIGLALAAAV RGYRCIIVMP EKMSSEKVDV 

       190        200        210        220        230        240 
LRALGAEIVR TPTNARFDSP ESHVGVAWRL KNEIPNSHIL DQYRNASNPL AHYDTTADEI 

       250        260        270        280        290        300 
LQQCDGKLDM LVASVGTGGT ITGIARKLKE KCPGCRIIGV DPEGSILAEP EELNQTEQTT 

       310        320        330        340        350        360 
YEVEGIGYDF IPTVLDRTVV DKWFKSNDEE AFTFARMLIA QEGLLCGGSA GSTVAVAVKA 

       370        380        390        400        410        420 
AQELQEGQRC VVILPDSVRN YMTKFLSDRW MLQKGFLKEE DLTEKKPWWW HLRVQELGLS 

       430        440        450        460        470        480 
APLTVLPTIT CGHTIEILRE KGFDQAPVVD EAGVILGMVT LGNMLSSLLA GKVQPSDQVG 

       490        500        510        520        530        540 
KVIYKQFKQI RLTDTLGRLS HILEMDHFAL VVHEQIQYHS TGKSSQRQMV FGVVTAIDLL 

       550 
NFVAAQERDQ K 

« Hide

Isoform 2 (Minor) [UniParc].

Checksum: 8BD062B080067092
Show »

FASTA56561,863

References

« Hide 'large scale' references
[1]"Human cystathionine beta-synthase cDNA: sequence, alternative splicing and expression in cultured cells."
Kraus J.P., Le K., Swaroop M., Ohura T., Tahara T., Rosenberg L.E., Roper M.D., Kozich V.
Hum. Mol. Genet. 2:1633-1638(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Genomic organization of the human cystathionine beta-synthase gene: evidence for various cDNAs."
Chasse J.-F., Paly E., Paris D., Paul V., Sinet P.-M., Kamoun P., London J.
Biochem. Biophys. Res. Commun. 211:826-832(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[3]"A yeast system for expression of human cystathionine beta-synthase: structural and functional conservation of the human and yeast genes."
Kruger W.D., Cox D.R.
Proc. Natl. Acad. Sci. U.S.A. 91:6614-6618(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"Human cystathionine beta-synthase: gene organization and expression of different 5' alternative splicing."
Chasse J.-F., Paul V., Escanez R., Kamoun P., London J.
Mamm. Genome 8:917-921(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"The human cystathionine beta-synthase (CBS) gene: complete sequence, alternative splicing, and polymorphisms."
Kraus J.P., Oliveriusova J., Sokolova J., Kraus E., Vlcek C., de Franchis R., Maclean K.N., Bao L., Bukovska G., Patterson D., Paces V., Ansorge W., Kozich V.
Genomics 52:312-324(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT PRO-69.
Tissue: Brain, Eye, Lung and Muscle.
[10]"Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits."
Kraus J.P., Packman S., Fowler B., Rosenberg L.E.
J. Biol. Chem. 253:6523-6528(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[11]"Human cystathionine beta-synthase is a target for sumoylation."
Kabil O., Zhou Y., Banerjee R.
Biochemistry 45:13528-13536(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-211, SUBCELLULAR LOCATION.
[12]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-phosphate-dependent heme protein."
Meier M., Janosik M., Kery V., Kraus J.P., Burkhard P.
EMBO J. 20:3910-3916(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-413 IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND IRON, SUBUNIT.
[16]"Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme."
Taoka S., Lepore B.W., Kabil O., Ojha S., Ringe D., Banerjee R.
Biochemistry 41:10454-10461(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 45-406 IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND IRON, ALLOSTERIC ACTIVATOR ADOMET, MUTAGENESIS OF CYS-272 AND CYS-275.
[17]"Cystathionine beta-synthase mutations in homocystinuria."
Kraus J.P., Janosik M., Kozich V., Mandell R., Shih V.E., Sperandeo M.P., Sebastio G., de Franchis R., Andria G., Kluijtmans L.A.J., Blom H.J., Boers G.H.J., Gordon R.B., Kamoun P., Tsai M.Y., Kruger W.D., Koch H.G., Ohura T., Gaustadnes M.
Hum. Mutat. 13:362-375(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON CBSD VARIANTS.
[18]"Screening for mutations by expressing patient cDNA segments in E. coli: homocystinuria due to cystathionine beta-synthase deficiency."
Kozich V., Kraus J.P.
Hum. Mutat. 1:113-123(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CBSD THR-278.
[19]"Molecular defect in a patient with pyridoxine-responsive homocystinuria."
Kozich V., de Franchis R., Kraus J.P.
Hum. Mol. Genet. 2:815-816(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD VAL-114 AND LEU-145.
[20]"Molecular basis of cystathionine beta-synthase deficiency in pyridoxine responsive and nonresponsive homocystinuria."
Hu F.L., Gu Z., Kozich V., Kraus J.P., Ramesh V., Shih V.E.
Hum. Mol. Genet. 2:1857-1860(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD THR-278 AND SER-307.
[21]"Identical genotypes in siblings with different homocystinuric phenotypes: identification of three mutations in cystathionine beta-synthase using an improved bacterial expression system."
de Franchis R., Kozich V., McInnes R., Kraus J.P.
Hum. Mol. Genet. 3:1103-1108(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD ARG-78 AND ASN-102.
[22]"Characterization of a cystathionine beta-synthase allele with three mutations in cis in a patient with B6 nonresponsive homocystinuria."
Marble M., Geraghty M.T., de Franchis R., Kraus J.P., Valle D.
Hum. Mol. Genet. 3:1883-1886(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD GLN-125 AND ASP-131.
[23]"Komrower Lecture. Molecular basis of phenotype expression in homocystinuria."
Kraus J.P.
J. Inherit. Metab. Dis. 17:383-390(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD.
[24]"A missense mutation (I278T) in the cystathionine beta-synthase gene prevalent in pyridoxine-responsive homocystinuria and associated with mild clinical phenotype."
Shih V.E., Fringer J.M., Mandell R., Kraus J.P., Berry G.T., Heidenreich R.A., Korson M.S., Levy H.L., Ramesh V.
Am. J. Hum. Genet. 57:34-39(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD ARG-139; LYS-144 AND THR-278.
[25]"The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations."
Sebastio G., Sperandeo M.P., Panico M., de Franchis R., Kraus J.P., Andria G.
Am. J. Hum. Genet. 56:1324-1333(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD SER-88; GLN-125 AND MET-257.
[26]"Two novel missense mutations in the cystathionine beta-synthase gene in homocystinuric patients."
Kluijtmans L.A.J., Blom H.J., Boers G.H.J., van Oost B.A., Trijbels F.J.M., van den Heuvel L.P.W.J.
Hum. Genet. 96:249-250(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD TYR-165 AND MET-371.
[27]"A yeast assay for functional detection of mutations in the human cystathionine beta-synthase gene."
Kruger W.D., Cox D.R.
Hum. Mol. Genet. 4:1155-1161(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD MET-168; HIS-224; THR-278; SER-307; VAL-331 AND GLU-454.
[28]"Molecular analysis of patients affected by homocystinuria due to cystathionine beta-synthase deficiency: report of a new mutation in exon 8 and a deletion in intron 11."
Sperandeo M.P., Panico M., Pepe A., Candito M., de Franchis R., Kraus J.P., Andria G., Sebastio G.
J. Inherit. Metab. Dis. 18:211-214(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CBSD LEU-290.
[29]"Defective cystathionine beta-synthase regulation by S-adenosylmethionine in a partially pyridoxine responsive homocystinuria patient."
Kluijtmans L.A.J., Boers G.H.J., Stevens E.M.B., Renier W.O., Kraus J.P., Trijbels F.J.M., van den Heuvel L.P.W.J., Blom H.J.
J. Clin. Invest. 98:285-289(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CBSD ASN-444, CHARACTERIZATION OF VARIANT CBSD ASN-444.
[30]"Homocysteine response to methionine challenge in four obligate heterozygotes for homocystinuria and relationship with cystathionine beta-synthase mutations."
Sperandeo M.P., Candito M., Sebastio G., Rolland M.O., Turc-Carel C., Giudicelli H., Dellamonica P., Andria G.
J. Inherit. Metab. Dis. 19:351-356(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD ARG-116; THR-278 AND LEU-290.
[31]"Characterisation of five missense mutations in the cystathionine beta-synthase gene from three patients with B6-nonresponsive homocystinuria."
Dawson P.A., Cox A.J., Emmerson B.T., Dudman N.P.B., Kraus J.P., Gordon R.B.
Eur. J. Hum. Genet. 5:15-21(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD LYS-144; THR-278; GLU-331; MET-353 AND GLN-439.
[32]"Functional modeling of vitamin responsiveness in yeast: a common pyridoxine-responsive cystathionine beta-synthase mutation in homocystinuria."
Kim C.E., Gallagher P.M., Guttormsen A.B., Refsum H., Ueland P.M., Ose L., Foelling I., Whitehead A.S., Tsai M.Y., Kruger W.D.
Hum. Mol. Genet. 6:2213-2221(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD MET-262; LYS-266; THR-278; SER-307; ALA-320 AND CYS-369.
[33]"Two novel mutations (K384E and L539S) in the C-terminal moiety of the cystathionine beta-synthase protein in two French pyridoxine-responsive homocystinuria patients."
Aral B., Coude M., London J., Aupetit J., Chasse J.-F., Zabot M.-T., Chadefaux-Vekemans B., Kamoun P.
Hum. Mutat. 9:81-82(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD GLU-384 AND SER-539.
[34]"Analysis of CBS alleles in Czech and Slovak patients with homocystinuria: report on three novel mutations E176K, W409X and 1223 + 37 del99."
Kozich V., Janosik M., Sokolova J., Oliveriusova J., Orendac M., Kraus J.P., Elleder D.
J. Inherit. Metab. Dis. 20:363-366(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD LYS-176; THR-278 AND SER-307.
[35]"Two novel mutations in the cystathionine beta-synthase gene of homocystinuric patients."
Tsai M.Y., Wong P.W.K., Garg U., Hanson N.Q., Schwichtenberg K.
Mol. Diagn. 2:129-133(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD TYR-370 AND GLN-439.
[36]"Mutational analysis of the cystathionine beta-synthase gene: a splicing mutation, two missense mutations and an insertion in patients with homocystinuria."
Gordon R.B., Cox A.J., Dawson P.A., Emmerson B.T., Kraus J.P., Dudman N.P.
Hum. Mutat. 11:332-332(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD LYS-144 AND TYR-165.
[37]"Characterization of mutations in the cystathionine beta-synthase gene in Irish patients with homocystinuria."
Gallagher P.M., Naughten E., Hanson N.Q., Schwichtenberg K., Bignell M., Yuan M., Ward P., Yap S., Whitehead A.S., Tsai M.Y.
Mol. Genet. Metab. 65:298-302(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD PRO-101; LYS-228; MET-262; THR-278; SER-307 AND PRO-355.
[38]"Four novel mutations in the cystathionine beta-synthase gene: effect of a second linked mutation on the severity of the homocystinuric phenotype."
de Franchis R., Kraus E., Kozich V., Sebastio G., Kraus J.P.
Hum. Mutat. 13:453-457(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD TRP-58; VAL-126; LYS-302 AND CYS-336.
[39]"Homocystinuria in the Arab population of Israel: identification of two novel mutations using DGGE analysis."
Gat-Yablonski G., Mandel H., Fowler B., Taleb O., Sela B.-A.
Hum. Mutat. 16:372-372(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD GLN-102; ARG-262 AND THR-278.
[40]"Impaired heme binding and aggregation of mutant cystathionine beta-synthase subunits in homocystinuria."
Janosik M., Oliveriusova J., Janosikova B., Sokolova J., Kraus E., Kraus J.P., Kozich V.
Am. J. Hum. Genet. 68:1506-1513(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD ARG-65; VAL-114; LYS-144; THR-155; TYR-165; LYS-176 AND THR-278, CHARACTERIZATION OF VARIANTS CBSD VAL-114; LYS-144; THR-155; TYR-165; LYS-176 AND THR-278.
[41]"Molecular genetic analysis of the cystathionine beta-synthase gene in Portuguese homocystinuria patients: three novel mutations."
Castro R., Heil S.G., Rivera I., Jakobs C., de Almeida I.T., Blom H.J.
Clin. Genet. 60:161-163(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD PRO-125 AND THR-361.
[42]"High homocysteine and thrombosis without connective tissue disorders are associated with a novel class of cystathionine beta-synthase (CBS) mutations."
Maclean K.N., Gaustadnes M., Oliveriusova J., Janosik M., Kraus E., Kozich V., Kery V., Skovby F., Ruediger N., Ingerslev J., Stabler S.P., Allen R.H., Kraus J.P.
Hum. Mutat. 19:641-655(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD ARG-85; THR-278; LEU-422; THR-435; ASN-444 AND LEU-466, CHARACTERIZATION OF VARIANTS CBSD ARG-85; LEU-422; THR-435 AND LEU-466.
[43]"The molecular basis of cystathionine beta-synthase deficiency in Australian patients: genotype-phenotype correlations and response to treatment."
Gaustadnes M., Wilcken B., Oliveriusova J., McGill J., Fletcher J., Kraus J.P., Wilcken D.E.
Hum. Mutat. 20:117-126(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD LEU-49; PRO-101; ARG-109; GLN-125; LYS-144; TYR-165; LYS-228; THR-278; LYS-302; SER-307; GLU-331; CYS-336; SER-347; MET-353; CYS-369; MET-371 AND GLN-439, CHARACTERIZATION OF VARIANTS CBSD PRO-101; ARG-109; LYS-228 AND SER-347.
[44]"Spectrum of CBS mutations in 16 homocystinuric patients from the iberian peninsula: high prevalence of T191M and absence of I278T or G307S."
Urreizti R., Balcells S., Rodes M., Vilarinho L., Baldellou A., Couce M.L., Munoz C., Campistol J., Pinto X., Vilaseca M.A., Grinberg D.
Hum. Mutat. 22:103-103(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD TRP-125; MET-191; TYR-275; CYS-336; PRO-338; ASN-349; GLN-379 AND PRO-456.
[45]"Cystathionine beta-synthase deficiency in Georgia (USA): correlation of clinical and biochemical phenotype with genotype."
Kruger W.D., Wang L., Jhee K.H., Singh R.H., Elsas L.J. II
Hum. Mutat. 22:434-441(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD PRO-101; THR-226; SER-228; PRO-231; THR-278; SER-307; ALA-320; MET-353; ASN-376 AND LYS-526, CHARACTERIZATION OF VARIANTS CBSD PRO-101; THR-226; SER-228; PRO-231; THR-278; SER-307; ALA-320; MET-353; ASN-376 AND LYS-526.
[46]"Identification and functional analysis of two novel mutations in the CBS gene in Polish patients with homocystinuria."
Orendac M., Pronicka E., Kubalska J., Janosik M., Sokolova J., Linnebank M., Koch H.G., Kozich V.
Hum. Mutat. 23:631-631(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD MET-143; ARG-148; LYS-228 AND THR-278, CHARACTERIZATION OF VARIANTS CBSD MET-143 AND ARG-148.
[47]"The cystathionine beta-synthase (CBS) mutation c.1224-2A>C in Central Europe: vitamin B6 nonresponsiveness and a common ancestral haplotype."
Linnebank M., Janosik M., Kozich V., Pronicka E., Kubalska J., Sokolova J., Linnebank A., Schmidt E., Leyendecker C., Klockgether T., Kraus J.P., Koch H.G.
Hum. Mutat. 24:352-353(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD 247-LYS--GLY-256 DEL; PRO-288 AND TRP-379.
[48]"Molecular analysis of homocystinuria in Brazilian patients."
Porto M.P.R., Galdieri L.C., Pereira V.G., Vergani N., da Rocha J.C.C., Micheletti C., Martins A.M., Perez A.B.A., Almeida V.D.
Clin. Chim. Acta 362:71-78(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD ALA-168; MET-191 AND THR-278.
[49]"Identification and functional analysis of cystathionine beta-synthase gene mutations in patients with homocystinuria."
Lee S.-J., Lee D.H., Yoo H.-W., Koo S.K., Park E.-S., Park J.-W., Lim H.G., Jung S.-C.
J. Hum. Genet. 50:648-654(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD GLN-154; VAL-155; ASP-234 DEL; MET-257; THR-288; CYS-336; SER-347 AND MET-353, VARIANT CYS-18, CHARACTERIZATION OF VARIANTS CBSD GLN-154; VAL-155; ASP-234 DEL; MET-257; THR-288; CYS-336; SER-347 AND MET-353, CHARACTERIZATION OF VARIANT CYS-18.
[50]"Functional assays testing pathogenicity of 14 cystathionine-beta synthase mutations."
Urreizti R., Asteggiano C., Cozar M., Frank N., Vilaseca M.A., Grinberg D., Balcells S.
Hum. Mutat. 27:211-211(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANTS CBSD TRP-125; ARG-148; VAL-173; MET-191; THR-226; TYR-275; CYS-336; HIS-336; PRO-338; ASN-349; GLN-379 AND PRO-456, CHARACTERIZATION OF VARIANT GLN-548.
[51]"Identification and functional analyses of CBS alleles in Spanish and Argentinian homocystinuric patients."
Cozar M., Urreizti R., Vilarinho L., Grosso C., Dodelson de Kremer R., Asteggiano C.G., Dalmau J., Garcia A.M., Vilaseca M.A., Grinberg D., Balcells S.
Hum. Mutat. 32:835-842(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD MET-173 DEL; LEU-200; SER-278; ASN-281; VAL-321 AND SER-446, CHARACTERIZATION OF VARIANTS CBSD MET-173 DEL; SER-278; ASN-281 AND VAL-321.
[52]"CBS gene mutations found in a Chinese pyridoxine-responsive homocystinuria patient."
Kwok J.S., Fung S.L., Lui G.C., Law E.L., Chan M.H., Leung C.B., Tang N.L.
Pathology 43:81-83(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CBSD THR-278 AND CYS-336.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19501 mRNA. Translation: AAA19874.1.
X82166 mRNA. Translation: CAA57656.1.
L14577 mRNA. Translation: AAA98524.1.
X88562 expand/collapse EMBL AC list , X91910, X98811, X98812, X98813, X98814, X98815, X98816, X98817, X98818, X98819, X98820, X98821, X98822, X98823 Genomic DNA. Translation: CAA61252.1.
AF042836 Genomic DNA. Translation: AAC64684.1.
AF042836 Genomic DNA. Translation: AAC64683.1.
BT007154 mRNA. Translation: AAP35818.1.
AK313691 mRNA. Translation: BAG36440.1.
CH471079 Genomic DNA. Translation: EAX09508.1.
CH471079 Genomic DNA. Translation: EAX09509.1.
CH471079 Genomic DNA. Translation: EAX09510.1.
CH471079 Genomic DNA. Translation: EAX09511.1.
CH471079 Genomic DNA. Translation: EAX09515.1.
BC000440 mRNA. Translation: AAH00440.1.
BC007257 mRNA. Translation: AAH07257.1.
BC010242 mRNA. Translation: AAH10242.1.
BC011381 mRNA. Translation: AAH11381.1.
PIRA55760.
RefSeqNP_000062.1. NM_000071.2.
NP_001171479.1. NM_001178008.1.
NP_001171480.1. NM_001178009.1.
UniGeneHs.533013.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JBQX-ray2.60A/B/C/D/E/F2-413[»]
1M54X-ray2.90A/B/C/D/E/F45-406[»]
4COOX-ray2.00A/B1-551[»]
4L0DX-ray2.97A/B1-551[»]
4L27X-ray3.39A/B/C/D2-551[»]
4L28X-ray2.63A/B/C/D2-551[»]
4L3VX-ray3.63A/B/C2-551[»]
ProteinModelPortalP35520.
SMRP35520. Positions 41-550.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107321. 33 interactions.
IntActP35520. 9 interactions.
MINTMINT-133409.
STRING9606.ENSP00000344460.

Chemistry

DrugBankDB00151. L-Cysteine.
DB00133. L-Serine.
DB00114. Pyridoxal Phosphate.
DB00165. Pyridoxine.
DB00118. S-Adenosylmethionine.
GuidetoPHARMACOLOGY1443.

PTM databases

PhosphoSiteP35520.

Polymorphism databases

DMDM543959.

Proteomic databases

PaxDbP35520.
PRIDEP35520.

Protocols and materials databases

DNASU875.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000352178; ENSP00000344460; ENSG00000160200. [P35520-1]
ENST00000359624; ENSP00000352643; ENSG00000160200. [P35520-1]
ENST00000398158; ENSP00000381225; ENSG00000160200. [P35520-1]
ENST00000398165; ENSP00000381231; ENSG00000160200. [P35520-1]
ENST00000398168; ENSP00000381234; ENSG00000160200. [P35520-2]
GeneID875.
KEGGhsa:875.
UCSCuc002zcs.1. human. [P35520-1]

Organism-specific databases

CTD875.
GeneCardsGC21M044473.
HGNCHGNC:1550. CBS.
HPAHPA001223.
MIM236200. phenotype.
613381. gene.
neXtProtNX_P35520.
Orphanet394. Classical homocystinuria.
PharmGKBPA26123.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0031.
HOGENOMHOG000217392.
HOVERGENHBG000918.
KOK01697.
OMADADSFEM.
OrthoDBEOG7J70F1.
PhylomeDBP35520.
TreeFamTF300784.

Enzyme and pathway databases

BioCycMetaCyc:HS08461-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP35520.
UniPathwayUPA00136; UER00201.

Gene expression databases

ArrayExpressP35520.
BgeeP35520.
CleanExHS_CBS.
GenevestigatorP35520.

Family and domain databases

InterProIPR000644. CBS_dom.
IPR001216. Cys_synth_BS.
IPR005857. Cysta_beta_synth.
IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
[Graphical view]
PfamPF00571. CBS. 1 hit.
PF00291. PALP. 1 hit.
[Graphical view]
SMARTSM00116. CBS. 1 hit.
[Graphical view]
SUPFAMSSF53686. SSF53686. 1 hit.
TIGRFAMsTIGR01137. cysta_beta. 1 hit.
PROSITEPS51371. CBS. 1 hit.
PS00901. CYS_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP35520.
GeneWikiCystathionine_beta_synthase.
GenomeRNAi875.
NextBio3642.
PROP35520.
SOURCESearch...

Entry information

Entry nameCBS_HUMAN
AccessionPrimary (citable) accession number: P35520
Secondary accession number(s): B2R993 expand/collapse secondary AC list , D3DSK4, Q99425, Q9BWC5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 167 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 21

Human chromosome 21: entries, gene names and cross-references to MIM