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Cystathionine beta-synthase (EC 4.2.1.22) (Beta-thionase) (Serine sulfhydrase)

 CBS_HUMAN               Reviewed;         551 AA.
P35520; B2R993; D3DSK4; Q99425; Q9BWC5;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 204.
RecName: Full=Cystathionine beta-synthase {ECO:0000305};
EC=4.2.1.22 {ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653, ECO:0000269|PubMed:23981774, ECO:0000269|PubMed:25044645};
AltName: Full=Beta-thionase;
AltName: Full=Serine sulfhydrase;
Name=CBS;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=7903580; DOI=10.1093/hmg/2.10.1633;
Kraus J.P., Le K., Swaroop M., Ohura T., Tahara T., Rosenberg L.E.,
Roper M.D., Kozich V.;
"Human cystathionine beta-synthase cDNA: sequence, alternative
splicing and expression in cultured cells.";
Hum. Mol. Genet. 2:1633-1638(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=7598711; DOI=10.1006/bbrc.1995.1886;
Chasse J.-F., Paly E., Paris D., Paul V., Sinet P.-M., Kamoun P.,
London J.;
"Genomic organization of the human cystathionine beta-synthase gene:
evidence for various cDNAs.";
Biochem. Biophys. Res. Commun. 211:826-832(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8022826; DOI=10.1073/pnas.91.14.6614;
Kruger W.D., Cox D.R.;
"A yeast system for expression of human cystathionine beta-synthase:
structural and functional conservation of the human and yeast genes.";
Proc. Natl. Acad. Sci. U.S.A. 91:6614-6618(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9383285; DOI=10.1007/s003359900611;
Chasse J.-F., Paul V., Escanez R., Kamoun P., London J.;
"Human cystathionine beta-synthase: gene organization and expression
of different 5' alternative splicing.";
Mamm. Genome 8:917-921(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=9790750; DOI=10.1006/geno.1998.5437;
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.;
"The human cystathionine beta-synthase (CBS) gene: complete sequence,
alternative splicing, and polymorphisms.";
Genomics 52:312-324(1998).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
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.,
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10830953; DOI=10.1038/35012518;
Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T.,
Park H.-S., Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y.,
Soeda E., Ohki M., Takagi T., Sakaki Y., Taudien S., Blechschmidt K.,
Polley A., Menzel U., Delabar J., Kumpf K., Lehmann R., Patterson D.,
Reichwald K., Rump A., Schillhabel M., Schudy A., Zimmermann W.,
Rosenthal A., Kudoh J., Shibuya K., Kawasaki K., Asakawa S.,
Shintani A., Sasaki T., Nagamine K., Mitsuyama S., Antonarakis S.E.,
Minoshima S., Shimizu N., Nordsiek G., Hornischer K., Brandt P.,
Scharfe M., Schoen O., Desario A., Reichelt J., Kauer G., Bloecker H.,
Ramser J., Beck A., Klages S., Hennig S., Riesselmann L., Dagand E.,
Wehrmeyer S., Borzym K., Gardiner K., Nizetic D., Francis F.,
Lehrach H., Reinhardt R., Yaspo M.-L.;
"The DNA sequence of human chromosome 21.";
Nature 405:311-319(2000).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
PRO-69.
TISSUE=Brain, Eye, Lung, and Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
CHARACTERIZATION.
PubMed=681363;
Kraus J.P., Packman S., Fowler B., Rosenberg L.E.;
"Purification and properties of cystathionine beta-synthase from human
liver. Evidence for identical subunits.";
J. Biol. Chem. 253:6523-6528(1978).
[12]
SUMOYLATION AT LYS-211, AND SUBCELLULAR LOCATION.
PubMed=17087506; DOI=10.1021/bi0615644;
Kabil O., Zhou Y., Banerjee R.;
"Human cystathionine beta-synthase is a target for sumoylation.";
Biochemistry 45:13528-13536(2006).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[18]
CHARACTERIZATION OF VARIANTS CBSD LEU-49; ARG-65; ARG-78; ASN-102;
VAL-114; GLN-125; LYS-144; ARG-148; TYR-165; LYS-176; ALA-180;
MET-191; LYS-228; ARG-262; LYS-266; THR-278; LYS-302; ARG-305;
SER-307; CYS-369; LEU-422; THR-435; GLN-439; ASN-444; LEU-466 AND
SER-539, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, ENZYME REGULATION, AND
SUBUNIT.
PubMed=20506325; DOI=10.1002/humu.21273;
Kozich V., Sokolova J., Klatovska V., Krijt J., Janosik M.,
Jelinek K., Kraus J.P.;
"Cystathionine beta-synthase mutations: effect of mutation topology on
folding and activity.";
Hum. Mutat. 31:809-819(2010).
[19]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-413 IN COMPLEX WITH
PYRIDOXAL PHOSPHATE AND IRON, SUBUNIT, ENZYME REGULATION, AND REGION.
PubMed=11483494; DOI=10.1093/emboj/20.15.3910;
Meier M., Janosik M., Kery V., Kraus J.P., Burkhard P.;
"Structure of human cystathionine beta-synthase: a unique pyridoxal
5'-phosphate-dependent heme protein.";
EMBO J. 20:3910-3916(2001).
[20]
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, AND REGION.
PubMed=12173932; DOI=10.1021/bi026052d;
Taoka S., Lepore B.W., Kabil O., Ojha S., Ringe D., Banerjee R.;
"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.";
Biochemistry 41:10454-10461(2002).
[21]
REVIEW ON CBSD VARIANTS.
PubMed=10338090;
DOI=10.1002/(SICI)1098-1004(1999)13:5<362::AID-HUMU4>3.0.CO;2-K;
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.;
"Cystathionine beta-synthase mutations in homocystinuria.";
Hum. Mutat. 13:362-375(1999).
[22]
VARIANT CBSD THR-278.
PubMed=1301198; DOI=10.1002/humu.1380010206;
Kozich V., Kraus J.P.;
"Screening for mutations by expressing patient cDNA segments in E.
coli: homocystinuria due to cystathionine beta-synthase deficiency.";
Hum. Mutat. 1:113-123(1992).
[23]
VARIANTS CBSD VAL-114 AND LEU-145.
PubMed=8353501; DOI=10.1093/hmg/2.6.815;
Kozich V., de Franchis R., Kraus J.P.;
"Molecular defect in a patient with pyridoxine-responsive
homocystinuria.";
Hum. Mol. Genet. 2:815-816(1993).
[24]
VARIANTS CBSD THR-278 AND SER-307.
PubMed=7506602; DOI=10.1093/hmg/2.11.1857;
Hu F.L., Gu Z., Kozich V., Kraus J.P., Ramesh V., Shih V.E.;
"Molecular basis of cystathionine beta-synthase deficiency in
pyridoxine responsive and nonresponsive homocystinuria.";
Hum. Mol. Genet. 2:1857-1860(1993).
[25]
VARIANTS CBSD ARG-78 AND ASN-102.
PubMed=7981678; DOI=10.1093/hmg/3.7.1103;
de Franchis R., Kozich V., McInnes R., Kraus J.P.;
"Identical genotypes in siblings with different homocystinuric
phenotypes: identification of three mutations in cystathionine beta-
synthase using an improved bacterial expression system.";
Hum. Mol. Genet. 3:1103-1108(1994).
[26]
VARIANTS CBSD GLN-125 AND ASP-131.
PubMed=7849717; DOI=10.1093/hmg/3.10.1883;
Marble M., Geraghty M.T., de Franchis R., Kraus J.P., Valle D.;
"Characterization of a cystathionine beta-synthase allele with three
mutations in cis in a patient with B6 nonresponsive homocystinuria.";
Hum. Mol. Genet. 3:1883-1886(1994).
[27]
VARIANTS CBSD.
PubMed=7967489; DOI=10.1007/BF00711354;
Kraus J.P.;
"Komrower Lecture. Molecular basis of phenotype expression in
homocystinuria.";
J. Inherit. Metab. Dis. 17:383-390(1994).
[28]
VARIANTS CBSD ARG-139; LYS-144 AND THR-278.
PubMed=7611293;
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.;
"A missense mutation (I278T) in the cystathionine beta-synthase gene
prevalent in pyridoxine-responsive homocystinuria and associated with
mild clinical phenotype.";
Am. J. Hum. Genet. 57:34-39(1995).
[29]
VARIANTS CBSD SER-88; GLN-125 AND MET-257.
PubMed=7762555;
Sebastio G., Sperandeo M.P., Panico M., de Franchis R., Kraus J.P.,
Andria G.;
"The molecular basis of homocystinuria due to cystathionine beta-
synthase deficiency in Italian families, and report of four novel
mutations.";
Am. J. Hum. Genet. 56:1324-1333(1995).
[30]
VARIANTS CBSD TYR-165 AND MET-371.
PubMed=7635485; DOI=10.1007/BF00207394;
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.;
"Two novel missense mutations in the cystathionine beta-synthase gene
in homocystinuric patients.";
Hum. Genet. 96:249-250(1995).
[31]
VARIANTS CBSD MET-168; HIS-224; THR-278; SER-307; VAL-331 AND GLU-454.
PubMed=8528202; DOI=10.1093/hmg/4.7.1155;
Kruger W.D., Cox D.R.;
"A yeast assay for functional detection of mutations in the human
cystathionine beta-synthase gene.";
Hum. Mol. Genet. 4:1155-1161(1995).
[32]
VARIANT CBSD LEU-290.
PubMed=7564249; DOI=10.1007/BF00711769;
Sperandeo M.P., Panico M., Pepe A., Candito M., de Franchis R.,
Kraus J.P., Andria G., Sebastio G.;
"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.";
J. Inherit. Metab. Dis. 18:211-214(1995).
[33]
VARIANT CBSD ASN-444, AND CHARACTERIZATION OF VARIANT CBSD ASN-444.
PubMed=8755636; DOI=10.1172/JCI118791;
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.;
"Defective cystathionine beta-synthase regulation by S-
adenosylmethionine in a partially pyridoxine responsive homocystinuria
patient.";
J. Clin. Invest. 98:285-289(1996).
[34]
VARIANTS CBSD ARG-116; THR-278 AND LEU-290.
PubMed=8803779; DOI=10.1007/BF01799266;
Sperandeo M.P., Candito M., Sebastio G., Rolland M.O., Turc-Carel C.,
Giudicelli H., Dellamonica P., Andria G.;
"Homocysteine response to methionine challenge in four obligate
heterozygotes for homocystinuria and relationship with cystathionine
beta-synthase mutations.";
J. Inherit. Metab. Dis. 19:351-356(1996).
[35]
VARIANTS CBSD LYS-144; THR-278; GLU-331; MET-353 AND GLN-439.
PubMed=9156316;
Dawson P.A., Cox A.J., Emmerson B.T., Dudman N.P.B., Kraus J.P.,
Gordon R.B.;
"Characterisation of five missense mutations in the cystathionine
beta-synthase gene from three patients with B6-nonresponsive
homocystinuria.";
Eur. J. Hum. Genet. 5:15-21(1997).
[36]
VARIANTS CBSD MET-262; LYS-266; THR-278; SER-307; ALA-320 AND CYS-369.
PubMed=9361025; DOI=10.1093/hmg/6.13.2213;
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.;
"Functional modeling of vitamin responsiveness in yeast: a common
pyridoxine-responsive cystathionine beta-synthase mutation in
homocystinuria.";
Hum. Mol. Genet. 6:2213-2221(1997).
[37]
VARIANTS CBSD GLU-384 AND SER-539.
PubMed=8990018;
DOI=10.1002/(SICI)1098-1004(1997)9:1<81::AID-HUMU18>3.3.CO;2-S;
Aral B., Coude M., London J., Aupetit J., Chasse J.-F., Zabot M.-T.,
Chadefaux-Vekemans B., Kamoun P.;
"Two novel mutations (K384E and L539S) in the C-terminal moiety of the
cystathionine beta-synthase protein in two French pyridoxine-
responsive homocystinuria patients.";
Hum. Mutat. 9:81-82(1997).
[38]
VARIANTS CBSD LYS-176; THR-278 AND SER-307.
PubMed=9266356; DOI=10.1023/A:1005325911665;
Kozich V., Janosik M., Sokolova J., Oliveriusova J., Orendac M.,
Kraus J.P., Elleder D.;
"Analysis of CBS alleles in Czech and Slovak patients with
homocystinuria: report on three novel mutations E176K, W409X and 1223
+ 37 del99.";
J. Inherit. Metab. Dis. 20:363-366(1997).
[39]
VARIANTS CBSD TYR-370 AND GLN-439.
PubMed=10462600; DOI=10.1054/MODI00200129;
Tsai M.Y., Wong P.W.K., Garg U., Hanson N.Q., Schwichtenberg K.;
"Two novel mutations in the cystathionine beta-synthase gene of
homocystinuric patients.";
Mol. Diagn. 2:129-133(1997).
[40]
VARIANTS CBSD LYS-144 AND TYR-165.
PubMed=10215408;
DOI=10.1002/(SICI)1098-1004(1998)11:4<332::AID-HUMU15>3.0.CO;2-S;
Gordon R.B., Cox A.J., Dawson P.A., Emmerson B.T., Kraus J.P.,
Dudman N.P.;
"Mutational analysis of the cystathionine beta-synthase gene: a
splicing mutation, two missense mutations and an insertion in patients
with homocystinuria.";
Hum. Mutat. 11:332-332(1998).
[41]
VARIANTS CBSD PRO-101; LYS-228; MET-262; THR-278; SER-307 AND PRO-355.
PubMed=9889017; DOI=10.1006/mgme.1998.2771;
Gallagher P.M., Naughten E., Hanson N.Q., Schwichtenberg K.,
Bignell M., Yuan M., Ward P., Yap S., Whitehead A.S., Tsai M.Y.;
"Characterization of mutations in the cystathionine beta-synthase gene
in Irish patients with homocystinuria.";
Mol. Genet. Metab. 65:298-302(1998).
[42]
VARIANTS CBSD TRP-58; VAL-126; LYS-302 AND CYS-336.
PubMed=10408774;
DOI=10.1002/(SICI)1098-1004(1999)13:6<453::AID-HUMU4>3.0.CO;2-K;
de Franchis R., Kraus E., Kozich V., Sebastio G., Kraus J.P.;
"Four novel mutations in the cystathionine beta-synthase gene: effect
of a second linked mutation on the severity of the homocystinuric
phenotype.";
Hum. Mutat. 13:453-457(1999).
[43]
VARIANTS CBSD GLN-102; ARG-262 AND THR-278.
PubMed=11013450;
DOI=10.1002/1098-1004(200010)16:4<372::AID-HUMU12>3.0.CO;2-J;
Gat-Yablonski G., Mandel H., Fowler B., Taleb O., Sela B.-A.;
"Homocystinuria in the Arab population of Israel: identification of
two novel mutations using DGGE analysis.";
Hum. Mutat. 16:372-372(2000).
[44]
VARIANTS CBSD ARG-65; VAL-114; LYS-144; THR-155; TYR-165; LYS-176 AND
THR-278, AND CHARACTERIZATION OF VARIANTS CBSD VAL-114; LYS-144;
THR-155; TYR-165; LYS-176 AND THR-278.
PubMed=11359213; DOI=10.1086/320597;
Janosik M., Oliveriusova J., Janosikova B., Sokolova J., Kraus E.,
Kraus J.P., Kozich V.;
"Impaired heme binding and aggregation of mutant cystathionine beta-
synthase subunits in homocystinuria.";
Am. J. Hum. Genet. 68:1506-1513(2001).
[45]
VARIANTS CBSD PRO-125 AND THR-361.
PubMed=11553052; DOI=10.1034/j.1399-0004.2001.600212.x;
Castro R., Heil S.G., Rivera I., Jakobs C., de Almeida I.T.,
Blom H.J.;
"Molecular genetic analysis of the cystathionine beta-synthase gene in
Portuguese homocystinuria patients: three novel mutations.";
Clin. Genet. 60:161-163(2001).
[46]
VARIANTS CBSD ARG-85; THR-278; LEU-422; THR-435; ASN-444 AND LEU-466,
AND CHARACTERIZATION OF VARIANTS CBSD ARG-85; LEU-422; THR-435 AND
LEU-466.
PubMed=12007221; DOI=10.1002/humu.10089;
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.;
"High homocysteine and thrombosis without connective tissue disorders
are associated with a novel class of cystathionine beta-synthase (CBS)
mutations.";
Hum. Mutat. 19:641-655(2002).
[47]
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, AND CHARACTERIZATION OF
VARIANTS CBSD PRO-101; ARG-109; LYS-228 AND SER-347.
PubMed=12124992; DOI=10.1002/humu.10104;
Gaustadnes M., Wilcken B., Oliveriusova J., McGill J., Fletcher J.,
Kraus J.P., Wilcken D.E.;
"The molecular basis of cystathionine beta-synthase deficiency in
Australian patients: genotype-phenotype correlations and response to
treatment.";
Hum. Mutat. 20:117-126(2002).
[48]
VARIANTS CBSD TRP-125; MET-191; TYR-275; CYS-336; PRO-338; ASN-349;
GLN-379 AND PRO-456.
PubMed=12815602; DOI=10.1002/humu.9153;
Urreizti R., Balcells S., Rodes M., Vilarinho L., Baldellou A.,
Couce M.L., Munoz C., Campistol J., Pinto X., Vilaseca M.A.,
Grinberg D.;
"Spectrum of CBS mutations in 16 homocystinuric patients from the
iberian peninsula: high prevalence of T191M and absence of I278T or
G307S.";
Hum. Mutat. 22:103-103(2003).
[49]
VARIANTS CBSD PRO-101; THR-226; SER-228; PRO-231; THR-278; SER-307;
ALA-320; MET-353; ASN-376 AND LYS-526, AND 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.
PubMed=14635102; DOI=10.1002/humu.10290;
Kruger W.D., Wang L., Jhee K.H., Singh R.H., Elsas L.J. II;
"Cystathionine beta-synthase deficiency in Georgia (USA): correlation
of clinical and biochemical phenotype with genotype.";
Hum. Mutat. 22:434-441(2003).
[50]
VARIANTS CBSD MET-143; ARG-148; LYS-228 AND THR-278, AND
CHARACTERIZATION OF VARIANTS CBSD MET-143 AND ARG-148.
PubMed=15146473; DOI=10.1002/humu.9249;
Orendac M., Pronicka E., Kubalska J., Janosik M., Sokolova J.,
Linnebank M., Koch H.G., Kozich V.;
"Identification and functional analysis of two novel mutations in the
CBS gene in Polish patients with homocystinuria.";
Hum. Mutat. 23:631-631(2004).
[51]
VARIANTS CBSD 247-LYS--GLY-256 DEL; PRO-288 AND TRP-379.
PubMed=15365998; DOI=10.1002/humu.9280;
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.;
"The cystathionine beta-synthase (CBS) mutation c.1224-2A>C in Central
Europe: vitamin B6 nonresponsiveness and a common ancestral
haplotype.";
Hum. Mutat. 24:352-353(2004).
[52]
VARIANTS CBSD ALA-168; MET-191 AND THR-278.
PubMed=15993874; DOI=10.1016/j.cccn.2005.05.030;
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.;
"Molecular analysis of homocystinuria in Brazilian patients.";
Clin. Chim. Acta 362:71-78(2005).
[53]
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, AND CHARACTERIZATION OF VARIANT CYS-18.
PubMed=16205833; DOI=10.1007/s10038-005-0312-2;
Lee S.-J., Lee D.H., Yoo H.-W., Koo S.K., Park E.-S., Park J.-W.,
Lim H.G., Jung S.-C.;
"Identification and functional analysis of cystathionine beta-synthase
gene mutations in patients with homocystinuria.";
J. Hum. Genet. 50:648-654(2005).
[54]
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, AND CHARACTERIZATION OF VARIANT GLN-548.
PubMed=16429402; DOI=10.1002/humu.9395;
Urreizti R., Asteggiano C., Cozar M., Frank N., Vilaseca M.A.,
Grinberg D., Balcells S.;
"Functional assays testing pathogenicity of 14 cystathionine-beta
synthase mutations.";
Hum. Mutat. 27:211-211(2006).
[55]
VARIANTS CBSD MET-173 DEL; LEU-200; SER-278; ASN-281; VAL-321 AND
SER-446, AND CHARACTERIZATION OF VARIANTS CBSD MET-173 DEL; SER-278;
ASN-281 AND VAL-321.
PubMed=21520339; DOI=10.1002/humu.21514;
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.;
"Identification and functional analyses of CBS alleles in Spanish and
Argentinian homocystinuric patients.";
Hum. Mutat. 32:835-842(2011).
[56]
VARIANTS CBSD THR-278 AND CYS-336.
PubMed=21240075; DOI=10.1097/PAT.0b013e3283419dbb;
Kwok J.S., Fung S.L., Lui G.C., Law E.L., Chan M.H., Leung C.B.,
Tang N.L.;
"CBS gene mutations found in a Chinese pyridoxine-responsive
homocystinuria patient.";
Pathology 43:81-83(2011).
[57]
VARIANT CBSD LYS-266, CHARACTERIZATION OF VARIANT CBSD LYS-266, AND
ENZYME REGULATION.
PubMed=22738154; DOI=10.1021/bi300421z;
Smith A.T., Su Y., Stevens D.J., Majtan T., Kraus J.P., Burstyn J.N.;
"Effect of the disease-causing R266K mutation on the heme and PLP
environments of human cystathionine beta-synthase.";
Biochemistry 51:6360-6370(2012).
[58]
VARIANTS CBSD ARG-85; ASN-87 AND ASN-234, CHARACTERIZATION OF VARIANTS
CBSD ASN-87 AND ASN-234, FUNCTION, CATALYTIC ACTIVITY, PATHWAY,
COFACTOR, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=23981774; DOI=10.1016/j.gene.2013.08.021;
Casique L., Kabil O., Banerjee R., Martinez J.C., De Lucca M.;
"Characterization of two pathogenic mutations in cystathionine beta-
synthase: different intracellular locations for wild-type and mutant
proteins.";
Gene 531:117-124(2013).
[59]
VARIANT CBSD GLY-449, CHARACTERIZATION OF VARIANTS CBSD LEU-427;
ASN-444; GLY-449; LEU-500 AND GLN-540, AND CATALYTIC ACTIVITY.
PubMed=25044645; DOI=10.1002/humu.22616;
Mendes M.I., Santos A.S., Smith D.E., Lino P.R., Colaco H.G.,
de Almeida I.T., Vicente J.B., Salomons G.S., Rivera I., Blom H.J.,
Leandro P.;
"Insights into the regulatory domain of cystathionine Beta-synthase:
characterization of six variant proteins.";
Hum. Mutat. 35:1195-1202(2014).
[60]
VARIANTS CBSD LEU-49; LYS-269 DEL; THR-278; HIS-336; LEU-427; ASN-444;
LEU-500 AND GLN-540, CHARACTERIZATION OF VARIANTS CBSD LEU-49; LYS-269
DEL; THR-278; HIS-336; LEU-427; ASN-444; LEU-500 AND GLN-540,
FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND ENZYME REGULATION.
PubMed=23974653; DOI=10.1007/s10545-013-9647-6;
Mendes M.I., Colaco H.G., Smith D.E., Ramos R.J., Pop A.,
van Dooren S.J., Tavares de Almeida I., Kluijtmans L.A., Janssen M.C.,
Rivera I., Salomons G.S., Leandro P., Blom H.J.;
"Reduced response of Cystathionine Beta-Synthase (CBS) to S-
Adenosylmethionine (SAM): Identification and functional analysis of
CBS gene mutations in Homocystinuria patients.";
J. Inherit. Metab. Dis. 37:245-254(2014).
-!- FUNCTION: 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). {ECO:0000250|UniProtKB:P32232,
ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:23981774}.
-!- CATALYTIC ACTIVITY: L-serine + L-homocysteine = L-cystathionine +
H(2)O. {ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:23981774, ECO:0000269|PubMed:25044645}.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
Evidence={ECO:0000269|PubMed:23981774};
-!- ENZYME REGULATION: 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). {ECO:0000269|PubMed:11483494,
ECO:0000269|PubMed:12173932, ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:22738154, ECO:0000269|PubMed:23974653}.
-!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-
cysteine from L-homocysteine and L-serine: step 1/2.
{ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:23981774}.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11483494,
ECO:0000269|PubMed:12173932, ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:23981774}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-740135, EBI-740135;
Q08426:EHHADH; NbExp=3; IntAct=EBI-740135, EBI-2339219;
Q13526:PIN1; NbExp=3; IntAct=EBI-740135, EBI-714158;
P54619:PRKAG1; NbExp=3; IntAct=EBI-740135, EBI-1181439;
P25786:PSMA1; NbExp=3; IntAct=EBI-740135, EBI-359352;
P57075:UBASH3A; NbExp=3; IntAct=EBI-740135, EBI-2105393;
Q7KZS0:UBE2I; NbExp=3; IntAct=EBI-740135, EBI-10180829;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17087506,
ECO:0000269|PubMed:23981774}. Nucleus
{ECO:0000269|PubMed:17087506}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Major;
IsoId=P35520-1; Sequence=Displayed;
Name=2; Synonyms=Minor;
IsoId=P35520-2; Sequence=VSP_001217;
-!- 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.
-!- 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. {ECO:0000269|PubMed:10215408,
ECO:0000269|PubMed:10408774, ECO:0000269|PubMed:10462600,
ECO:0000269|PubMed:11013450, ECO:0000269|PubMed:11359213,
ECO:0000269|PubMed:11553052, ECO:0000269|PubMed:12007221,
ECO:0000269|PubMed:12124992, ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:1301198, ECO:0000269|PubMed:14635102,
ECO:0000269|PubMed:15146473, ECO:0000269|PubMed:15365998,
ECO:0000269|PubMed:15993874, ECO:0000269|PubMed:16205833,
ECO:0000269|PubMed:16429402, ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:21240075, ECO:0000269|PubMed:21520339,
ECO:0000269|PubMed:22738154, ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:23981774, ECO:0000269|PubMed:25044645,
ECO:0000269|PubMed:7506602, ECO:0000269|PubMed:7564249,
ECO:0000269|PubMed:7611293, ECO:0000269|PubMed:7635485,
ECO:0000269|PubMed:7762555, ECO:0000269|PubMed:7849717,
ECO:0000269|PubMed:7967489, ECO:0000269|PubMed:7981678,
ECO:0000269|PubMed:8353501, ECO:0000269|PubMed:8528202,
ECO:0000269|PubMed:8755636, ECO:0000269|PubMed:8803779,
ECO:0000269|PubMed:8990018, ECO:0000269|PubMed:9156316,
ECO:0000269|PubMed:9266356, ECO:0000269|PubMed:9361025,
ECO:0000269|PubMed:9889017}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
synthase family. {ECO:0000305}.
-!- 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. {ECO:0000305}.
-!- WEB RESOURCE: Name=CBS mutation database;
URL="http://cbs.lf1.cuni.cz/index.php";
-----------------------------------------------------------------------
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EMBL; L19501; AAA19874.1; -; mRNA.
EMBL; X82166; CAA57656.1; -; mRNA.
EMBL; L14577; AAA98524.1; -; mRNA.
EMBL; X88562; CAA61252.1; -; Genomic_DNA.
EMBL; X91910; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98811; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98812; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98813; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98814; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98815; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98816; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98817; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98818; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98819; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98820; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98821; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98822; CAA61252.1; JOINED; Genomic_DNA.
EMBL; X98823; CAA61252.1; JOINED; Genomic_DNA.
EMBL; AF042836; AAC64684.1; -; Genomic_DNA.
EMBL; AF042836; AAC64683.1; -; Genomic_DNA.
EMBL; BT007154; AAP35818.1; -; mRNA.
EMBL; AK313691; BAG36440.1; -; mRNA.
EMBL; AP001630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471079; EAX09508.1; -; Genomic_DNA.
EMBL; CH471079; EAX09509.1; -; Genomic_DNA.
EMBL; CH471079; EAX09510.1; -; Genomic_DNA.
EMBL; CH471079; EAX09511.1; -; Genomic_DNA.
EMBL; CH471079; EAX09515.1; -; Genomic_DNA.
EMBL; BC000440; AAH00440.1; -; mRNA.
EMBL; BC007257; AAH07257.1; -; mRNA.
EMBL; BC010242; AAH10242.1; -; mRNA.
EMBL; BC011381; AAH11381.1; -; mRNA.
CCDS; CCDS13693.1; -. [P35520-1]
PIR; A55760; A55760.
RefSeq; NP_000062.1; NM_000071.2. [P35520-1]
RefSeq; NP_001171479.1; NM_001178008.2. [P35520-1]
RefSeq; NP_001171480.1; NM_001178009.2. [P35520-1]
RefSeq; NP_001307227.1; NM_001320298.1. [P35520-1]
RefSeq; NP_001308002.1; NM_001321073.1. [P35520-1]
RefSeq; XP_011528079.1; XM_011529777.1. [P35520-2]
RefSeq; XP_011528083.1; XM_011529781.1. [P35520-2]
RefSeq; XP_011528084.1; XM_011529782.1. [P35520-2]
RefSeq; XP_011544396.1; XM_011546094.1. [P35520-2]
RefSeq; XP_011544397.1; XM_011546095.2. [P35520-2]
RefSeq; XP_011544399.1; XM_011546097.2. [P35520-2]
RefSeq; XP_011544400.1; XM_011546098.1. [P35520-2]
RefSeq; XP_011544401.1; XM_011546099.1. [P35520-1]
RefSeq; XP_016883700.1; XM_017028211.1. [P35520-2]
RefSeq; XP_016883701.1; XM_017028212.1. [P35520-2]
RefSeq; XP_016883702.1; XM_017028213.1. [P35520-2]
RefSeq; XP_016883703.1; XM_017028214.1. [P35520-1]
RefSeq; XP_016883704.1; XM_017028215.1. [P35520-1]
RefSeq; XP_016883705.1; XM_017028216.1. [P35520-1]
RefSeq; XP_016883706.1; XM_017028217.1. [P35520-1]
RefSeq; XP_016883707.1; XM_017028218.1. [P35520-1]
RefSeq; XP_016883978.1; XM_017028489.1. [P35520-2]
RefSeq; XP_016883979.1; XM_017028490.1. [P35520-1]
RefSeq; XP_016883980.1; XM_017028491.1. [P35520-1]
RefSeq; XP_016883981.1; XM_017028492.1. [P35520-1]
UniGene; Hs.533013; -.
PDB; 1JBQ; X-ray; 2.60 A; A/B/C/D/E/F=2-413.
PDB; 1M54; X-ray; 2.90 A; A/B/C/D/E/F=44-406.
PDB; 4COO; X-ray; 2.00 A; A/B=1-551.
PDB; 4L0D; X-ray; 2.97 A; A/B=1-551.
PDB; 4L27; X-ray; 3.39 A; A/B/C/D=2-551.
PDB; 4L28; X-ray; 2.63 A; A/B/C/D=2-551.
PDB; 4L3V; X-ray; 3.63 A; A/B/C=2-551.
PDB; 4PCU; X-ray; 3.58 A; A/B=1-551.
PDB; 4UUU; X-ray; 1.71 A; A/B=406-547.
PDB; 5MMS; X-ray; 2.80 A; A/B/C/D/E/F=1-408.
PDBsum; 1JBQ; -.
PDBsum; 1M54; -.
PDBsum; 4COO; -.
PDBsum; 4L0D; -.
PDBsum; 4L27; -.
PDBsum; 4L28; -.
PDBsum; 4L3V; -.
PDBsum; 4PCU; -.
PDBsum; 4UUU; -.
PDBsum; 5MMS; -.
ProteinModelPortal; P35520; -.
SMR; P35520; -.
BioGrid; 107321; 71.
IntAct; P35520; 22.
MINT; MINT-133409; -.
BindingDB; P35520; -.
ChEMBL; CHEMBL3399911; -.
DrugBank; DB00151; L-Cysteine.
DrugBank; DB00133; L-Serine.
DrugBank; DB00114; Pyridoxal Phosphate.
DrugBank; DB00118; S-Adenosylmethionine.
GuidetoPHARMACOLOGY; 1443; -.
iPTMnet; P35520; -.
PhosphoSitePlus; P35520; -.
BioMuta; CBS; -.
DMDM; 543959; -.
EPD; P35520; -.
MaxQB; P35520; -.
PaxDb; P35520; -.
PeptideAtlas; P35520; -.
PRIDE; P35520; -.
DNASU; 875; -.
Ensembl; ENST00000352178; ENSP00000344460; ENSG00000160200. [P35520-1]
Ensembl; ENST00000359624; ENSP00000352643; ENSG00000160200. [P35520-1]
Ensembl; ENST00000398158; ENSP00000381225; ENSG00000160200. [P35520-1]
Ensembl; ENST00000398165; ENSP00000381231; ENSG00000160200. [P35520-1]
GeneID; 102724560; -.
GeneID; 875; -.
KEGG; hsa:102724560; -.
KEGG; hsa:875; -.
UCSC; uc002zct.3; human. [P35520-1]
CTD; 102724560; -.
CTD; 875; -.
DisGeNET; 102724560; -.
DisGeNET; 875; -.
EuPathDB; HostDB:ENSG00000160200.17; -.
GeneCards; CBS; -.
GeneReviews; CBS; -.
HGNC; HGNC:1550; CBS.
HPA; HPA001223; -.
MalaCards; CBS; -.
MIM; 236200; phenotype.
MIM; 613381; gene.
neXtProt; NX_P35520; -.
OpenTargets; ENSG00000160200; -.
OpenTargets; ENSG00000274276; -.
Orphanet; 394; Classical homocystinuria.
PharmGKB; PA26123; -.
eggNOG; KOG1252; Eukaryota.
eggNOG; COG0031; LUCA.
GeneTree; ENSGT00510000047027; -.
HOGENOM; HOG000217392; -.
HOVERGEN; HBG000918; -.
InParanoid; P35520; -.
KO; K01697; -.
OMA; SYLSKFA; -.
OrthoDB; EOG091G02TP; -.
PhylomeDB; P35520; -.
TreeFam; TF300784; -.
BioCyc; MetaCyc:HS08461-MONOMER; -.
BRENDA; 4.2.1.22; 2681.
Reactome; R-HSA-1614603; Cysteine formation from homocysteine.
Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
SABIO-RK; P35520; -.
UniPathway; UPA00136; UER00201.
ChiTaRS; CBS; human.
EvolutionaryTrace; P35520; -.
GeneWiki; Cystathionine_beta_synthase; -.
PRO; PR:P35520; -.
Proteomes; UP000005640; Chromosome 21.
Bgee; ENSG00000160200; -.
CleanEx; HS_CBS; -.
ExpressionAtlas; P35520; baseline and differential.
Genevisible; P35520; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0070025; F:carbon monoxide binding; IDA:BHF-UCL.
GO; GO:0004122; F:cystathionine beta-synthase activity; IDA:UniProtKB.
GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
GO; GO:0070026; F:nitric oxide binding; IDA:BHF-UCL.
GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IDA:BHF-UCL.
GO; GO:0019825; F:oxygen binding; IDA:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:BHF-UCL.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0019344; P:cysteine biosynthetic process; IDA:BHF-UCL.
GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
GO; GO:0042262; P:DNA protection; IMP:BHF-UCL.
GO; GO:0043418; P:homocysteine catabolic process; IDA:UniProtKB.
GO; GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IDA:UniProtKB.
GO; GO:0019448; P:L-cysteine catabolic process; IDA:UniProtKB.
GO; GO:0006565; P:L-serine catabolic process; IDA:UniProtKB.
GO; GO:0006563; P:L-serine metabolic process; IDA:UniProtKB.
GO; GO:0019346; P:transsulfuration; TAS:Reactome.
InterPro; IPR000644; CBS_dom.
InterPro; IPR005857; Cysta_beta_synth.
InterPro; IPR001216; P-phosphate_BS.
InterPro; IPR001926; PLP-dep.
InterPro; IPR036052; Trypto_synt_PLP_dependent.
Pfam; PF00571; CBS; 1.
Pfam; PF00291; PALP; 1.
SMART; SM00116; CBS; 1.
SUPFAM; SSF53686; SSF53686; 1.
TIGRFAMs; TIGR01137; cysta_beta; 1.
PROSITE; PS51371; CBS; 1.
PROSITE; PS00901; CYS_SYNTHASE; 1.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; Alternative splicing;
Amino-acid biosynthesis; CBS domain; Complete proteome;
Cysteine biosynthesis; Cytoplasm; Disease mutation; Heme; Iron;
Isopeptide bond; Lyase; Metal-binding; Nucleus; Phosphoprotein;
Polymorphism; Pyridoxal phosphate; Reference proteome;
Ubl conjugation.
CHAIN 1 551 Cystathionine beta-synthase.
/FTId=PRO_0000167133.
DOMAIN 418 476 CBS. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
REGION 256 260 Pyridoxal phosphate binding.
{ECO:0000269|PubMed:11483494,
ECO:0000269|PubMed:12173932}.
METAL 52 52 Iron (heme axial ligand).
{ECO:0000269|PubMed:11483494,
ECO:0000269|PubMed:12173932}.
METAL 65 65 Iron (heme axial ligand).
{ECO:0000269|PubMed:11483494,
ECO:0000269|PubMed:12173932}.
BINDING 149 149 Pyridoxal phosphate.
{ECO:0000269|PubMed:11483494,
ECO:0000269|PubMed:12173932}.
BINDING 349 349 Pyridoxal phosphate.
{ECO:0000269|PubMed:11483494,
ECO:0000269|PubMed:12173932}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 119 119 N6-(pyridoxal phosphate)lysine.
{ECO:0000269|PubMed:11483494,
ECO:0000269|PubMed:12173932}.
MOD_RES 199 199 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 211 211 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000269|PubMed:17087506}.
VAR_SEQ 518 518 Y -> SQDQAWAGVVGGPAD (in isoform 2).
{ECO:0000305}.
/FTId=VSP_001217.
VARIANT 18 18 R -> C (functional polymorphism;
associated with 1/3 to 2/3 the enzyme
activity of the wild-type;
dbSNP:rs201827340).
{ECO:0000269|PubMed:16205833}.
/FTId=VAR_046921.
VARIANT 49 49 P -> L (in CBSD; decreased expression; no
effect on cystathionine beta-synthase
activity; increased homotetramer
formation; dbSNP:rs148865119).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:23974653}.
/FTId=VAR_008049.
VARIANT 58 58 R -> W (in CBSD; linked with V-114; 18%
of activity; dbSNP:rs555959266).
{ECO:0000269|PubMed:10408774}.
/FTId=VAR_008050.
VARIANT 65 65 H -> R (in CBSD; decreased cystathionine
beta-synthase activity; inhibited by
AdoMet and AdoHcy; decreased homotetramer
formation). {ECO:0000269|PubMed:11359213,
ECO:0000269|PubMed:20506325}.
/FTId=VAR_021790.
VARIANT 69 69 A -> P (in dbSNP:rs17849313).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_046922.
VARIANT 78 78 P -> R (in CBSD; severe form; linked with
Q-102; decreased cystathionine beta-
synthase activity; decreased homotetramer
formation; dbSNP:rs786204608).
{ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:7981678}.
/FTId=VAR_002171.
VARIANT 85 85 G -> R (in CBSD; loss of cystathionine
beta-synthase activity;
dbSNP:rs863223435).
{ECO:0000269|PubMed:12007221,
ECO:0000269|PubMed:23981774}.
/FTId=VAR_008051.
VARIANT 87 87 T -> N (in CBSD; decreased cystathionine
beta-synthase activity; increased
aggregation).
{ECO:0000269|PubMed:23981774}.
/FTId=VAR_074590.
VARIANT 88 88 P -> S (in CBSD).
{ECO:0000269|PubMed:7762555}.
/FTId=VAR_002172.
VARIANT 101 101 L -> P (in CBSD; common mutation in Irish
population; loss of activity;
dbSNP:rs786204757).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:14635102,
ECO:0000269|PubMed:9889017}.
/FTId=VAR_021791.
VARIANT 102 102 K -> N (in CBSD; decreased cystathionine
beta-synthase activity; decreased
homotetramer formation;
dbSNP:rs786204609).
{ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:7981678}.
/FTId=VAR_002173.
VARIANT 102 102 K -> Q (in CBSD; severe form; linked with
R-78; dbSNP:rs34040148).
{ECO:0000269|PubMed:11013450}.
/FTId=VAR_008052.
VARIANT 109 109 C -> R (in CBSD; loss of activity;
dbSNP:rs778220779).
{ECO:0000269|PubMed:12124992}.
/FTId=VAR_021792.
VARIANT 114 114 A -> 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;
dbSNP:rs121964964).
{ECO:0000269|PubMed:11359213,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:8353501}.
/FTId=VAR_002174.
VARIANT 116 116 G -> R (in CBSD; dbSNP:rs760214620).
{ECO:0000269|PubMed:8803779}.
/FTId=VAR_008053.
VARIANT 121 121 R -> C (in CBSD; dbSNP:rs775992753).
/FTId=VAR_008054.
VARIANT 121 121 R -> H (in CBSD; dbSNP:rs770095972).
/FTId=VAR_008055.
VARIANT 121 121 R -> L (in CBSD; mild form;
dbSNP:rs770095972).
/FTId=VAR_008056.
VARIANT 125 125 R -> P (in CBSD).
{ECO:0000269|PubMed:11553052}.
/FTId=VAR_046923.
VARIANT 125 125 R -> Q (in CBSD; severe form; when linked
with D-131 moderate form; loss of
cystathionine beta-synthase activity;
decreased homotetramer formation;
dbSNP:rs781444670).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:7762555,
ECO:0000269|PubMed:7849717}.
/FTId=VAR_002175.
VARIANT 125 125 R -> W (in CBSD; exhibits an activity
lower than 4% of the wild-type enzyme;
absent capacity to form multimeric
quaternary structure).
{ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:16429402}.
/FTId=VAR_008057.
VARIANT 126 126 M -> V (in CBSD; loss of activity).
{ECO:0000269|PubMed:10408774}.
/FTId=VAR_008058.
VARIANT 128 128 E -> D (in CBSD).
/FTId=VAR_008059.
VARIANT 131 131 E -> D (in CBSD; linked with Q-125; loss
of activity).
{ECO:0000269|PubMed:7849717}.
/FTId=VAR_002176.
VARIANT 139 139 G -> R (in CBSD; mild form;
dbSNP:rs121964965).
{ECO:0000269|PubMed:7611293}.
/FTId=VAR_008060.
VARIANT 143 143 I -> M (in CBSD; 4% of activity; stable).
{ECO:0000269|PubMed:15146473}.
/FTId=VAR_021793.
VARIANT 144 144 E -> K (in CBSD; loss of cystathionine
beta-synthase activity; impaired
stimulation by AdoMet and AdoHcy;
decreased homotetramer formation;
dbSNP:rs121964966).
{ECO:0000269|PubMed:10215408,
ECO:0000269|PubMed:11359213,
ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:7611293,
ECO:0000269|PubMed:9156316}.
/FTId=VAR_002177.
VARIANT 145 145 P -> L (in CBSD; dbSNP:rs121964963).
{ECO:0000269|PubMed:8353501}.
/FTId=VAR_002178.
VARIANT 148 148 G -> R (in CBSD; loss of cystathionine
beta-synthase activity; impaired
stimulation by AdoMet and AdoHcy; loss of
homotetramer formation;
dbSNP:rs755952006).
{ECO:0000269|PubMed:15146473,
ECO:0000269|PubMed:16429402,
ECO:0000269|PubMed:20506325}.
/FTId=VAR_008061.
VARIANT 151 159 Missing (in CBSD).
/FTId=VAR_008063.
VARIANT 151 151 G -> R (in CBSD; dbSNP:rs373782713).
/FTId=VAR_008062.
VARIANT 152 152 I -> M (in CBSD; severe form).
/FTId=VAR_008064.
VARIANT 154 154 L -> Q (in CBSD; protein expression is
comparable to wild-type; significant
decrease of enzyme activity).
{ECO:0000269|PubMed:16205833}.
/FTId=VAR_046924.
VARIANT 155 155 A -> T (in CBSD; complete loss of
activity; severely affects homotetramer
formation by promoting formation of
larger aggregates).
{ECO:0000269|PubMed:11359213}.
/FTId=VAR_008065.
VARIANT 155 155 A -> V (in CBSD; protein expression is
comparable to wild-type; significant
decrease of enzyme activity).
{ECO:0000269|PubMed:16205833}.
/FTId=VAR_046925.
VARIANT 165 165 C -> Y (in CBSD; severe form; protein
expression is comparable to wild-type;
loss of cystathionine beta-synthase
activity; no effect on homotetramer
formation). {ECO:0000269|PubMed:10215408,
ECO:0000269|PubMed:11359213,
ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:7635485}.
/FTId=VAR_002179.
VARIANT 168 168 V -> A (in CBSD).
{ECO:0000269|PubMed:15993874}.
/FTId=VAR_046926.
VARIANT 168 168 V -> M (in CBSD; dbSNP:rs121964970).
{ECO:0000269|PubMed:8528202}.
/FTId=VAR_002180.
VARIANT 173 173 M -> V (in CBSD; presents 40% of the
wild-type activity; highly reduced
capacity to form multimeric quaternary
structure).
{ECO:0000269|PubMed:16429402}.
/FTId=VAR_046927.
VARIANT 173 173 Missing (in CBSD; loss of activity).
{ECO:0000269|PubMed:21520339}.
/FTId=VAR_066098.
VARIANT 176 176 E -> K (in CBSD; severe form; loss of
cystathionine beta-synthase activity;
inhibited by AdoMet; severely decreases
homotetramer formation by promoting
formation of larger aggregates).
{ECO:0000269|PubMed:11359213,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:9266356}.
/FTId=VAR_008066.
VARIANT 180 180 V -> A (in CBSD; decreased cystathionine
beta-synthase activity; decreases
homotetramer formation).
{ECO:0000269|PubMed:20506325}.
/FTId=VAR_008067.
VARIANT 191 191 T -> M (in CBSD; moderate and severe
forms; loss of cystathionine beta-
synthase activity; absent capacity to
form multimeric quaternary structure;
dbSNP:rs121964973).
{ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:15993874,
ECO:0000269|PubMed:16429402,
ECO:0000269|PubMed:20506325}.
/FTId=VAR_008068.
VARIANT 198 198 D -> V (in CBSD).
/FTId=VAR_008069.
VARIANT 200 200 P -> L (in CBSD; dbSNP:rs758712880).
{ECO:0000269|PubMed:21520339}.
/FTId=VAR_066099.
VARIANT 224 224 R -> H (in CBSD; dbSNP:rs761647392).
{ECO:0000269|PubMed:8528202}.
/FTId=VAR_002181.
VARIANT 226 226 A -> T (in CBSD; presents 20% of the
wild-type activity; dramatically reduced
capacity to form multimeric quaternary
structure). {ECO:0000269|PubMed:14635102,
ECO:0000269|PubMed:16429402}.
/FTId=VAR_008070.
VARIANT 228 228 N -> K (in CBSD; loss of cystathionine
beta-synthase activity; decreased
homotetramer formation).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:15146473,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:9889017}.
/FTId=VAR_021794.
VARIANT 228 228 N -> S (in CBSD; has significantly
decreased levels of enzyme activity).
{ECO:0000269|PubMed:14635102}.
/FTId=VAR_046928.
VARIANT 231 231 A -> P (in CBSD; has significantly
decreased levels of enzyme activity).
{ECO:0000269|PubMed:14635102}.
/FTId=VAR_046929.
VARIANT 234 234 D -> N (in CBSD; decreased cystathionine
beta-synthase activity; changed
localization; decreased interaction with
pyridoxal 5'-phosphate; no effect on
homotetramer formation;
dbSNP:rs773734233).
{ECO:0000269|PubMed:23981774}.
/FTId=VAR_008071.
VARIANT 234 234 Missing (in CBSD; protein expression is
comparable to wild-type; significant
decrease of enzyme activity).
{ECO:0000269|PubMed:16205833}.
/FTId=VAR_046930.
VARIANT 239 239 E -> K (in CBSD).
/FTId=VAR_002182.
VARIANT 247 256 Missing (in CBSD).
{ECO:0000269|PubMed:15365998}.
/FTId=VAR_046931.
VARIANT 257 257 T -> M (in CBSD; moderate to severe form;
protein expression is comparable to wild-
type; significant decrease of enzyme
activity; dbSNP:rs758236584).
{ECO:0000269|PubMed:16205833,
ECO:0000269|PubMed:7762555}.
/FTId=VAR_002183.
VARIANT 262 262 T -> M (in CBSD; moderate form;
dbSNP:rs149119723).
{ECO:0000269|PubMed:9361025,
ECO:0000269|PubMed:9889017}.
/FTId=VAR_008072.
VARIANT 262 262 T -> R (in CBSD; severe form; loss of
cystathionine beta-synthase activity;
loss of homotetramer formation).
{ECO:0000269|PubMed:11013450,
ECO:0000269|PubMed:20506325}.
/FTId=VAR_021795.
VARIANT 266 266 R -> G (in CBSD).
/FTId=VAR_008073.
VARIANT 266 266 R -> K (in CBSD; mild form; decreased
cystathionine beta-synthase activity;
decreased homotetramer formation; no
effect on heme-binding; decreased
stability; dbSNP:rs28934275).
{ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:22738154,
ECO:0000269|PubMed:9361025}.
/FTId=VAR_008074.
VARIANT 269 269 Missing (in CBSD; loss of expression).
{ECO:0000269|PubMed:23974653}.
/FTId=VAR_074591.
VARIANT 270 270 Missing (in CBSD).
/FTId=VAR_008075.
VARIANT 275 275 C -> Y (in CBSD; severe form; exhibits an
activity lower than 4% of the wild-type
enzyme; absent capacity to form
multimeric quaternary structure).
{ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:16429402}.
/FTId=VAR_021796.
VARIANT 278 278 I -> S (in CBSD; loss of activity).
{ECO:0000269|PubMed:21520339}.
/FTId=VAR_066100.
VARIANT 278 278 I -> 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; dbSNP:rs5742905).
{ECO:0000269|PubMed:11013450,
ECO:0000269|PubMed:11359213,
ECO:0000269|PubMed:12007221,
ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:1301198,
ECO:0000269|PubMed:14635102,
ECO:0000269|PubMed:15146473,
ECO:0000269|PubMed:15993874,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:21240075,
ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:7506602,
ECO:0000269|PubMed:7611293,
ECO:0000269|PubMed:8528202,
ECO:0000269|PubMed:8803779,
ECO:0000269|PubMed:9156316,
ECO:0000269|PubMed:9266356,
ECO:0000269|PubMed:9361025,
ECO:0000269|PubMed:9889017}.
/FTId=VAR_002184.
VARIANT 281 281 D -> N (in CBSD; loss of activity).
{ECO:0000269|PubMed:21520339}.
/FTId=VAR_066101.
VARIANT 288 288 A -> P (in CBSD).
{ECO:0000269|PubMed:15365998}.
/FTId=VAR_046932.
VARIANT 288 288 A -> T (in CBSD; protein expression is
comparable to wild-type; significant
decrease of enzyme activity;
dbSNP:rs141502207).
{ECO:0000269|PubMed:16205833}.
/FTId=VAR_046933.
VARIANT 290 290 P -> L (in CBSD; dbSNP:rs760912339).
{ECO:0000269|PubMed:7564249,
ECO:0000269|PubMed:8803779}.
/FTId=VAR_002185.
VARIANT 302 302 E -> K (in CBSD; no effect on
cystathionine beta-synthase activity;
inhibited by AdoHcy and impaired
activation by AdoMet; no effect on
homotetramer formation;
dbSNP:rs779270933).
{ECO:0000269|PubMed:10408774,
ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:20506325}.
/FTId=VAR_008076.
VARIANT 305 305 G -> R (in CBSD; loss of cystathionine
beta-synthase activity; no effect on
homotetramer formation).
{ECO:0000269|PubMed:20506325}.
/FTId=VAR_008077.
VARIANT 307 307 G -> 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; dbSNP:rs121964962).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:14635102,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:7506602,
ECO:0000269|PubMed:8528202,
ECO:0000269|PubMed:9266356,
ECO:0000269|PubMed:9361025,
ECO:0000269|PubMed:9889017}.
/FTId=VAR_002186.
VARIANT 320 320 V -> A (in CBSD; has 36% of wild-type
enzyme activity; dbSNP:rs781567152).
{ECO:0000269|PubMed:14635102,
ECO:0000269|PubMed:9361025}.
/FTId=VAR_008078.
VARIANT 321 321 D -> V (in CBSD; loss of activity).
{ECO:0000269|PubMed:21520339}.
/FTId=VAR_066102.
VARIANT 331 331 A -> E (in CBSD; dbSNP:rs777919630).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:9156316}.
/FTId=VAR_008079.
VARIANT 331 331 A -> V (in CBSD).
{ECO:0000269|PubMed:8528202}.
/FTId=VAR_002187.
VARIANT 336 336 R -> C (in CBSD; protein expression is
comparable to wild-type; loss of
activity; absent capacity to form
multimeric quaternary structure;
dbSNP:rs398123151).
{ECO:0000269|PubMed:10408774,
ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:16205833,
ECO:0000269|PubMed:16429402,
ECO:0000269|PubMed:21240075}.
/FTId=VAR_002188.
VARIANT 336 336 R -> 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;
dbSNP:rs760417941).
{ECO:0000269|PubMed:16429402,
ECO:0000269|PubMed:23974653}.
/FTId=VAR_008080.
VARIANT 338 338 L -> P (in CBSD; severe form; exhibits an
activity lower than 4% of the wild-type
enzyme; absent capacity to form
multimeric quaternary structure).
{ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:16429402}.
/FTId=VAR_021797.
VARIANT 347 347 G -> S (in CBSD; protein expression is
comparable to wild-type; loss of
activity; dbSNP:rs771298943).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:16205833}.
/FTId=VAR_021798.
VARIANT 349 349 S -> N (in CBSD; severe form; exhibits an
activity lower than 4% of the wild-type
enzyme; absent capacity to form
multimeric quaternary structure).
{ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:16429402}.
/FTId=VAR_021799.
VARIANT 352 352 S -> N (in CBSD).
/FTId=VAR_008081.
VARIANT 353 353 T -> M (in CBSD; protein expression is
comparable to wild-type; significant
decrease of enzyme activity;
dbSNP:rs121964972).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:14635102,
ECO:0000269|PubMed:16205833,
ECO:0000269|PubMed:9156316}.
/FTId=VAR_008082.
VARIANT 354 354 V -> M (in CBSD; dbSNP:rs267606146).
/FTId=VAR_008083.
VARIANT 355 355 A -> P (in CBSD).
{ECO:0000269|PubMed:9889017}.
/FTId=VAR_021800.
VARIANT 361 361 A -> T (in CBSD; dbSNP:rs745764562).
{ECO:0000269|PubMed:11553052}.
/FTId=VAR_046934.
VARIANT 369 369 R -> C (in CBSD; when linked with C-491
severe form; decreased cystathionine
beta-synthase activity; decreased
homotetramer formation;
dbSNP:rs117687681).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:9361025}.
/FTId=VAR_008084.
VARIANT 369 369 R -> H (in CBSD; dbSNP:rs11700812).
/FTId=VAR_002189.
VARIANT 370 370 C -> Y (in CBSD; dbSNP:rs757920190).
{ECO:0000269|PubMed:10462600}.
/FTId=VAR_008085.
VARIANT 371 371 V -> M (in CBSD; dbSNP:rs372010465).
{ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:7635485}.
/FTId=VAR_002190.
VARIANT 376 376 D -> N (in CBSD; has significantly
decreased levels of enzyme activity).
{ECO:0000269|PubMed:14635102}.
/FTId=VAR_046935.
VARIANT 379 379 R -> Q (in CBSD; exhibits an activity
lower than 4% of the wild-type enzyme;
absent capacity to form multimeric
quaternary structure; dbSNP:rs763036586).
{ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:16429402}.
/FTId=VAR_021801.
VARIANT 379 379 R -> W (in CBSD; dbSNP:rs769080151).
{ECO:0000269|PubMed:15365998}.
/FTId=VAR_046936.
VARIANT 384 384 K -> E (in CBSD; severe form;
dbSNP:rs121964967).
{ECO:0000269|PubMed:8990018}.
/FTId=VAR_002191.
VARIANT 384 384 K -> N (in CBSD; moderate form).
/FTId=VAR_008086.
VARIANT 391 391 M -> I (in CBSD).
/FTId=VAR_008087.
VARIANT 422 422 P -> L (in CBSD; changed cystathionine
beta-synthase activity; impaired
stimulation by AdoMet; does not affect
homotetramer formation;
dbSNP:rs28934892).
{ECO:0000269|PubMed:12007221,
ECO:0000269|PubMed:20506325}.
/FTId=VAR_021802.
VARIANT 427 427 P -> L (in CBSD; no effect on
cystathionine beta-synthase activity;
altered stimulation by AdoMet;
dbSNP:rs863223434).
{ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:25044645}.
/FTId=VAR_074592.
VARIANT 434 434 T -> N (in CBSD).
/FTId=VAR_008088.
VARIANT 435 435 I -> T (in CBSD; no effect on
cystathionine beta-synthase activity;
impaired stimulation by AdoMet and
AdoHcy; does not affect homotetramer
formation). {ECO:0000269|PubMed:12007221,
ECO:0000269|PubMed:20506325}.
/FTId=VAR_008089.
VARIANT 439 439 R -> Q (in CBSD; no effect on
cystathionine beta-synthase activity;
increased homotetramer formation;
dbSNP:rs756467921).
{ECO:0000269|PubMed:10462600,
ECO:0000269|PubMed:12124992,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:9156316}.
/FTId=VAR_008090.
VARIANT 444 444 D -> N (in CBSD; decreased expression; no
effect on cystathionine beta-synthase
activity; altered stimulation by AdoMet;
increased homotetramer formation;
dbSNP:rs28934891).
{ECO:0000269|PubMed:12007221,
ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:25044645,
ECO:0000269|PubMed:8755636}.
/FTId=VAR_002192.
VARIANT 446 446 A -> S (in CBSD).
{ECO:0000269|PubMed:21520339}.
/FTId=VAR_066103.
VARIANT 449 449 V -> G (in CBSD; no effect on
cystathionine beta-synthase activity;
altered stimulation by AdoMet).
{ECO:0000269|PubMed:25044645}.
/FTId=VAR_074593.
VARIANT 454 454 V -> E (in CBSD).
{ECO:0000269|PubMed:8528202}.
/FTId=VAR_002193.
VARIANT 456 456 L -> P (in CBSD; severe; exhibits an
activity lower than 4% of the wild-type
enzyme; absent capacity to form
multimeric quaternary structure).
{ECO:0000269|PubMed:12815602,
ECO:0000269|PubMed:16429402}.
/FTId=VAR_021803.
VARIANT 466 466 S -> L (in CBSD; increased cystathionine
beta-synthase activity; impaired
stimulation by AdoMet and AdoHcy;
decreased homotetramer formation;
dbSNP:rs121964971).
{ECO:0000269|PubMed:12007221,
ECO:0000269|PubMed:20506325}.
/FTId=VAR_008091.
VARIANT 491 491 R -> C (in CBSD; linked with C-369).
/FTId=VAR_008092.
VARIANT 500 500 S -> L (in CBSD; no effect on
cystathionine beta-synthase activity;
altered stimulation by AdoMet;
dbSNP:rs755106884).
{ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:25044645}.
/FTId=VAR_074594.
VARIANT 526 526 Q -> K (in CBSD; has significantly
decreased levels of enzyme activity).
{ECO:0000269|PubMed:14635102}.
/FTId=VAR_046937.
VARIANT 534 534 V -> D (in CBSD; linked with S-307).
/FTId=VAR_008093.
VARIANT 539 539 L -> S (in CBSD; loss of cystathionine
beta-synthase activity; impaired
stimulation by AdoMet and AdoHcy; loss of
homotetramer formation;
dbSNP:rs121964968).
{ECO:0000269|PubMed:20506325,
ECO:0000269|PubMed:8990018}.
/FTId=VAR_002194.
VARIANT 540 540 L -> Q (in CBSD; no effect on
cystathionine beta-synthase activity;
altered stimulation by AdoMet).
{ECO:0000269|PubMed:23974653,
ECO:0000269|PubMed:25044645}.
/FTId=VAR_074595.
VARIANT 548 548 R -> Q (presents 60% of the wild-type
activity; highly reduced capacity to form
multimeric quaternary structure;
dbSNP:rs150828989).
{ECO:0000269|PubMed:16429402}.
/FTId=VAR_046938.
MUTAGEN 272 272 C->A: Reduced heme content and
cystathionine beta-synthase activity.
{ECO:0000269|PubMed:12173932}.
MUTAGEN 275 275 C->S: Reduced heme content and
cystathionine beta-synthase activity.
{ECO:0000269|PubMed:12173932}.
CONFLICT 58 58 R -> P (in Ref. 4; CAA61252).
{ECO:0000305}.
HELIX 60 62 {ECO:0000244|PDB:4COO}.
STRAND 75 79 {ECO:0000244|PDB:4COO}.
HELIX 80 82 {ECO:0000244|PDB:4COO}.
STRAND 83 85 {ECO:0000244|PDB:4COO}.
STRAND 89 91 {ECO:0000244|PDB:4COO}.
HELIX 95 98 {ECO:0000244|PDB:4COO}.
STRAND 103 109 {ECO:0000244|PDB:4COO}.
HELIX 110 112 {ECO:0000244|PDB:4COO}.
STRAND 113 117 {ECO:0000244|PDB:4L0D}.
HELIX 119 132 {ECO:0000244|PDB:4COO}.
STRAND 141 145 {ECO:0000244|PDB:4COO}.
HELIX 149 161 {ECO:0000244|PDB:4COO}.
STRAND 164 170 {ECO:0000244|PDB:4COO}.
HELIX 175 183 {ECO:0000244|PDB:4COO}.
STRAND 187 191 {ECO:0000244|PDB:4COO}.
STRAND 197 199 {ECO:0000244|PDB:4L27}.
HELIX 203 213 {ECO:0000244|PDB:4COO}.
STRAND 217 219 {ECO:0000244|PDB:4L28}.
TURN 222 224 {ECO:0000244|PDB:4COO}.
HELIX 227 234 {ECO:0000244|PDB:4COO}.
HELIX 236 243 {ECO:0000244|PDB:4COO}.
TURN 244 246 {ECO:0000244|PDB:4COO}.
STRAND 249 254 {ECO:0000244|PDB:4COO}.
STRAND 256 258 {ECO:0000244|PDB:4COO}.
HELIX 259 271 {ECO:0000244|PDB:4COO}.
STRAND 272 274 {ECO:0000244|PDB:1M54}.
STRAND 276 282 {ECO:0000244|PDB:4COO}.
STRAND 288 290 {ECO:0000244|PDB:4COO}.
HELIX 291 294 {ECO:0000244|PDB:4COO}.
HELIX 317 319 {ECO:0000244|PDB:4COO}.
STRAND 322 326 {ECO:0000244|PDB:4COO}.
HELIX 328 342 {ECO:0000244|PDB:4COO}.
HELIX 348 360 {ECO:0000244|PDB:4COO}.
HELIX 361 363 {ECO:0000244|PDB:4COO}.
STRAND 369 374 {ECO:0000244|PDB:4COO}.
HELIX 378 381 {ECO:0000244|PDB:4COO}.
TURN 382 386 {ECO:0000244|PDB:4COO}.
HELIX 388 393 {ECO:0000244|PDB:4COO}.
HELIX 399 404 {ECO:0000244|PDB:4COO}.
TURN 408 411 {ECO:0000244|PDB:4UUU}.
HELIX 414 417 {ECO:0000244|PDB:4UUU}.
HELIX 431 441 {ECO:0000244|PDB:4UUU}.
STRAND 444 449 {ECO:0000244|PDB:4UUU}.
STRAND 455 460 {ECO:0000244|PDB:4UUU}.
HELIX 461 469 {ECO:0000244|PDB:4UUU}.
HELIX 479 482 {ECO:0000244|PDB:4UUU}.
STRAND 489 491 {ECO:0000244|PDB:4UUU}.
HELIX 496 505 {ECO:0000244|PDB:4UUU}.
STRAND 509 515 {ECO:0000244|PDB:4UUU}.
STRAND 526 534 {ECO:0000244|PDB:4UUU}.
HELIX 536 544 {ECO:0000244|PDB:4UUU}.
SEQUENCE 551 AA; 60587 MW; F89E69C67BDE6701 CRC64;
MPSETPQAEV GPTGCPHRSG PHSAKGSLEK GSPEDKEAKE PLWIRPDAPS RCTWQLGRPA
SESPHHHTAP AKSPKILPDI LKKIGDTPMV RINKIGKKFG LKCELLAKCE FFNAGGSVKD
RISLRMIEDA ERDGTLKPGD TIIEPTSGNT GIGLALAAAV RGYRCIIVMP EKMSSEKVDV
LRALGAEIVR TPTNARFDSP ESHVGVAWRL KNEIPNSHIL DQYRNASNPL AHYDTTADEI
LQQCDGKLDM LVASVGTGGT ITGIARKLKE KCPGCRIIGV DPEGSILAEP EELNQTEQTT
YEVEGIGYDF IPTVLDRTVV DKWFKSNDEE AFTFARMLIA QEGLLCGGSA GSTVAVAVKA
AQELQEGQRC VVILPDSVRN YMTKFLSDRW MLQKGFLKEE DLTEKKPWWW HLRVQELGLS
APLTVLPTIT CGHTIEILRE KGFDQAPVVD EAGVILGMVT LGNMLSSLLA GKVQPSDQVG
KVIYKQFKQI RLTDTLGRLS HILEMDHFAL VVHEQIQYHS TGKSSQRQMV FGVVTAIDLL
NFVAAQERDQ K


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