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CBS_HUMAN
ID   CBS_HUMAN               Reviewed;         551 AA.
AC   P35520; B2R993; D3DSK4; Q99425; Q9BWC5;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 237.
DE   RecName: Full=Cystathionine beta-synthase {ECO:0000305};
DE            EC=4.2.1.22 {ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653, ECO:0000269|PubMed:23981774, ECO:0000269|PubMed:25044645};
DE   AltName: Full=Beta-thionase;
DE   AltName: Full=Serine sulfhydrase;
GN   Name=CBS;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=7903580; DOI=10.1093/hmg/2.10.1633;
RA   Kraus J.P., Le K., Swaroop M., Ohura T., Tahara T., Rosenberg L.E.,
RA   Roper M.D., Kozich V.;
RT   "Human cystathionine beta-synthase cDNA: sequence, alternative splicing and
RT   expression in cultured cells.";
RL   Hum. Mol. Genet. 2:1633-1638(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Liver;
RX   PubMed=7598711; DOI=10.1006/bbrc.1995.1886;
RA   Chasse J.-F., Paly E., Paris D., Paul V., Sinet P.-M., Kamoun P.,
RA   London J.;
RT   "Genomic organization of the human cystathionine beta-synthase gene:
RT   evidence for various cDNAs.";
RL   Biochem. Biophys. Res. Commun. 211:826-832(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=8022826; DOI=10.1073/pnas.91.14.6614;
RA   Kruger W.D., Cox D.R.;
RT   "A yeast system for expression of human cystathionine beta-synthase:
RT   structural and functional conservation of the human and yeast genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:6614-6618(1994).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9383285; DOI=10.1007/s003359900611;
RA   Chasse J.-F., Paul V., Escanez R., Kamoun P., London J.;
RT   "Human cystathionine beta-synthase: gene organization and expression of
RT   different 5' alternative splicing.";
RL   Mamm. Genome 8:917-921(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX   PubMed=9790750; DOI=10.1006/geno.1998.5437;
RA   Kraus J.P., Oliveriusova J., Sokolova J., Kraus E., Vlcek C.,
RA   de Franchis R., Maclean K.N., Bao L., Bukovska G., Patterson D., Paces V.,
RA   Ansorge W., Kozich V.;
RT   "The human cystathionine beta-synthase (CBS) gene: complete sequence,
RT   alternative splicing, and polymorphisms.";
RL   Genomics 52:312-324(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10830953; DOI=10.1038/35012518;
RA   Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA   Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA   Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA   Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA   Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA   Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA   Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA   Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA   Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA   Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA   Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT   "The DNA sequence of human chromosome 21.";
RL   Nature 405:311-319(2000).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [10]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-69.
RC   TISSUE=Brain, Eye, Lung, and Muscle;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [11]
RP   CHARACTERIZATION.
RX   PubMed=681363; DOI=10.1016/s0021-9258(19)46963-9;
RA   Kraus J.P., Packman S., Fowler B., Rosenberg L.E.;
RT   "Purification and properties of cystathionine beta-synthase from human
RT   liver. Evidence for identical subunits.";
RL   J. Biol. Chem. 253:6523-6528(1978).
RN   [12]
RP   SUMOYLATION AT LYS-211, AND SUBCELLULAR LOCATION.
RX   PubMed=17087506; DOI=10.1021/bi0615644;
RA   Kabil O., Zhou Y., Banerjee R.;
RT   "Human cystathionine beta-synthase is a target for sumoylation.";
RL   Biochemistry 45:13528-13536(2006).
RN   [13]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [14]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [17]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [18]
RP   CHARACTERIZATION OF VARIANTS CBSD LEU-49; ARG-65; ARG-78; ASN-102; VAL-114;
RP   GLN-125; LYS-144; ARG-148; TYR-165; LYS-176; ALA-180; MET-191; LYS-228;
RP   ARG-262; LYS-266; THR-278; LYS-302; ARG-305; SER-307; CYS-369; LEU-422;
RP   THR-435; GLN-439; ASN-444; LEU-466 AND SER-539, FUNCTION, CATALYTIC
RP   ACTIVITY, PATHWAY, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=20506325; DOI=10.1002/humu.21273;
RA   Kozich V., Sokolova J., Klatovska V., Krijt J., Janosik M., Jelinek K.,
RA   Kraus J.P.;
RT   "Cystathionine beta-synthase mutations: effect of mutation topology on
RT   folding and activity.";
RL   Hum. Mutat. 31:809-819(2010).
RN   [19]
RP   X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-413 IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE AND IRON, SUBUNIT, ACTIVITY REGULATION, AND REGION.
RX   PubMed=11483494; DOI=10.1093/emboj/20.15.3910;
RA   Meier M., Janosik M., Kery V., Kraus J.P., Burkhard P.;
RT   "Structure of human cystathionine beta-synthase: a unique pyridoxal 5'-
RT   phosphate-dependent heme protein.";
RL   EMBO J. 20:3910-3916(2001).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 45-406 IN COMPLEX WITH PYRIDOXAL
RP   PHOSPHATE AND IRON, ALLOSTERIC ACTIVATOR ADOMET, MUTAGENESIS OF CYS-272 AND
RP   CYS-275, AND REGION.
RX   PubMed=12173932; DOI=10.1021/bi026052d;
RA   Taoka S., Lepore B.W., Kabil O., Ojha S., Ringe D., Banerjee R.;
RT   "Human cystathionine beta-synthase is a heme sensor protein. Evidence that
RT   the redox sensor is heme and not the vicinal cysteines in the CXXC motif
RT   seen in the crystal structure of the truncated enzyme.";
RL   Biochemistry 41:10454-10461(2002).
RN   [21]
RP   REVIEW ON CBSD VARIANTS.
RX   PubMed=10338090;
RX   DOI=10.1002/(sici)1098-1004(1999)13:5<362::aid-humu4>3.0.co;2-k;
RA   Kraus J.P., Janosik M., Kozich V., Mandell R., Shih V.E., Sperandeo M.P.,
RA   Sebastio G., de Franchis R., Andria G., Kluijtmans L.A.J., Blom H.J.,
RA   Boers G.H.J., Gordon R.B., Kamoun P., Tsai M.Y., Kruger W.D., Koch H.G.,
RA   Ohura T., Gaustadnes M.;
RT   "Cystathionine beta-synthase mutations in homocystinuria.";
RL   Hum. Mutat. 13:362-375(1999).
RN   [22]
RP   VARIANT CBSD THR-278.
RX   PubMed=1301198; DOI=10.1002/humu.1380010206;
RA   Kozich V., Kraus J.P.;
RT   "Screening for mutations by expressing patient cDNA segments in E. coli:
RT   homocystinuria due to cystathionine beta-synthase deficiency.";
RL   Hum. Mutat. 1:113-123(1992).
RN   [23]
RP   VARIANTS CBSD VAL-114 AND LEU-145.
RX   PubMed=8353501; DOI=10.1093/hmg/2.6.815;
RA   Kozich V., de Franchis R., Kraus J.P.;
RT   "Molecular defect in a patient with pyridoxine-responsive homocystinuria.";
RL   Hum. Mol. Genet. 2:815-816(1993).
RN   [24]
RP   VARIANTS CBSD THR-278 AND SER-307.
RX   PubMed=7506602; DOI=10.1093/hmg/2.11.1857;
RA   Hu F.L., Gu Z., Kozich V., Kraus J.P., Ramesh V., Shih V.E.;
RT   "Molecular basis of cystathionine beta-synthase deficiency in pyridoxine
RT   responsive and nonresponsive homocystinuria.";
RL   Hum. Mol. Genet. 2:1857-1860(1993).
RN   [25]
RP   VARIANTS CBSD ARG-78 AND ASN-102.
RX   PubMed=7981678; DOI=10.1093/hmg/3.7.1103;
RA   de Franchis R., Kozich V., McInnes R., Kraus J.P.;
RT   "Identical genotypes in siblings with different homocystinuric phenotypes:
RT   identification of three mutations in cystathionine beta-synthase using an
RT   improved bacterial expression system.";
RL   Hum. Mol. Genet. 3:1103-1108(1994).
RN   [26]
RP   VARIANTS CBSD GLN-125 AND ASP-131.
RX   PubMed=7849717; DOI=10.1093/hmg/3.10.1883;
RA   Marble M., Geraghty M.T., de Franchis R., Kraus J.P., Valle D.;
RT   "Characterization of a cystathionine beta-synthase allele with three
RT   mutations in cis in a patient with B6 nonresponsive homocystinuria.";
RL   Hum. Mol. Genet. 3:1883-1886(1994).
RN   [27]
RP   VARIANTS CBSD.
RX   PubMed=7967489; DOI=10.1007/bf00711354;
RA   Kraus J.P.;
RT   "Komrower Lecture. Molecular basis of phenotype expression in
RT   homocystinuria.";
RL   J. Inherit. Metab. Dis. 17:383-390(1994).
RN   [28]
RP   VARIANTS CBSD ARG-139; LYS-144 AND THR-278.
RX   PubMed=7611293;
RA   Shih V.E., Fringer J.M., Mandell R., Kraus J.P., Berry G.T.,
RA   Heidenreich R.A., Korson M.S., Levy H.L., Ramesh V.;
RT   "A missense mutation (I278T) in the cystathionine beta-synthase gene
RT   prevalent in pyridoxine-responsive homocystinuria and associated with mild
RT   clinical phenotype.";
RL   Am. J. Hum. Genet. 57:34-39(1995).
RN   [29]
RP   VARIANTS CBSD SER-88; GLN-125 AND MET-257.
RX   PubMed=7762555;
RA   Sebastio G., Sperandeo M.P., Panico M., de Franchis R., Kraus J.P.,
RA   Andria G.;
RT   "The molecular basis of homocystinuria due to cystathionine beta-synthase
RT   deficiency in Italian families, and report of four novel mutations.";
RL   Am. J. Hum. Genet. 56:1324-1333(1995).
RN   [30]
RP   VARIANTS CBSD TYR-165 AND MET-371.
RX   PubMed=7635485; DOI=10.1007/bf00207394;
RA   Kluijtmans L.A.J., Blom H.J., Boers G.H.J., van Oost B.A., Trijbels F.J.M.,
RA   van den Heuvel L.P.W.J.;
RT   "Two novel missense mutations in the cystathionine beta-synthase gene in
RT   homocystinuric patients.";
RL   Hum. Genet. 96:249-250(1995).
RN   [31]
RP   VARIANTS CBSD MET-168; HIS-224; THR-278; SER-307; VAL-331 AND GLU-454.
RX   PubMed=8528202; DOI=10.1093/hmg/4.7.1155;
RA   Kruger W.D., Cox D.R.;
RT   "A yeast assay for functional detection of mutations in the human
RT   cystathionine beta-synthase gene.";
RL   Hum. Mol. Genet. 4:1155-1161(1995).
RN   [32]
RP   VARIANT CBSD LEU-290.
RX   PubMed=7564249; DOI=10.1007/bf00711769;
RA   Sperandeo M.P., Panico M., Pepe A., Candito M., de Franchis R., Kraus J.P.,
RA   Andria G., Sebastio G.;
RT   "Molecular analysis of patients affected by homocystinuria due to
RT   cystathionine beta-synthase deficiency: report of a new mutation in exon 8
RT   and a deletion in intron 11.";
RL   J. Inherit. Metab. Dis. 18:211-214(1995).
RN   [33]
RP   VARIANT CBSD ASN-444, AND CHARACTERIZATION OF VARIANT CBSD ASN-444.
RX   PubMed=8755636; DOI=10.1172/jci118791;
RA   Kluijtmans L.A.J., Boers G.H.J., Stevens E.M.B., Renier W.O., Kraus J.P.,
RA   Trijbels F.J.M., van den Heuvel L.P.W.J., Blom H.J.;
RT   "Defective cystathionine beta-synthase regulation by S-adenosylmethionine
RT   in a partially pyridoxine responsive homocystinuria patient.";
RL   J. Clin. Invest. 98:285-289(1996).
RN   [34]
RP   VARIANTS CBSD ARG-116; THR-278 AND LEU-290.
RX   PubMed=8803779; DOI=10.1007/bf01799266;
RA   Sperandeo M.P., Candito M., Sebastio G., Rolland M.O., Turc-Carel C.,
RA   Giudicelli H., Dellamonica P., Andria G.;
RT   "Homocysteine response to methionine challenge in four obligate
RT   heterozygotes for homocystinuria and relationship with cystathionine beta-
RT   synthase mutations.";
RL   J. Inherit. Metab. Dis. 19:351-356(1996).
RN   [35]
RP   VARIANTS CBSD LYS-144; THR-278; GLU-331; MET-353 AND GLN-439.
RX   PubMed=9156316;
RA   Dawson P.A., Cox A.J., Emmerson B.T., Dudman N.P.B., Kraus J.P.,
RA   Gordon R.B.;
RT   "Characterisation of five missense mutations in the cystathionine beta-
RT   synthase gene from three patients with B6-nonresponsive homocystinuria.";
RL   Eur. J. Hum. Genet. 5:15-21(1997).
RN   [36]
RP   VARIANTS CBSD MET-262; LYS-266; THR-278; SER-307; ALA-320 AND CYS-369.
RX   PubMed=9361025; DOI=10.1093/hmg/6.13.2213;
RA   Kim C.E., Gallagher P.M., Guttormsen A.B., Refsum H., Ueland P.M., Ose L.,
RA   Foelling I., Whitehead A.S., Tsai M.Y., Kruger W.D.;
RT   "Functional modeling of vitamin responsiveness in yeast: a common
RT   pyridoxine-responsive cystathionine beta-synthase mutation in
RT   homocystinuria.";
RL   Hum. Mol. Genet. 6:2213-2221(1997).
RN   [37]
RP   VARIANTS CBSD GLU-384 AND SER-539.
RX   PubMed=8990018;
RX   DOI=10.1002/(sici)1098-1004(1997)9:1<81::aid-humu18>3.0.co;2-l;
RA   Aral B., Coude M., London J., Aupetit J., Chasse J.-F., Zabot M.-T.,
RA   Chadefaux-Vekemans B., Kamoun P.;
RT   "Two novel mutations (K384E and L539S) in the C-terminal moiety of the
RT   cystathionine beta-synthase protein in two French pyridoxine-responsive
RT   homocystinuria patients.";
RL   Hum. Mutat. 9:81-82(1997).
RN   [38]
RP   VARIANTS CBSD LYS-176; THR-278 AND SER-307.
RX   PubMed=9266356; DOI=10.1023/a:1005325911665;
RA   Kozich V., Janosik M., Sokolova J., Oliveriusova J., Orendac M.,
RA   Kraus J.P., Elleder D.;
RT   "Analysis of CBS alleles in Czech and Slovak patients with homocystinuria:
RT   report on three novel mutations E176K, W409X and 1223 + 37 del99.";
RL   J. Inherit. Metab. Dis. 20:363-366(1997).
RN   [39]
RP   VARIANTS CBSD TYR-370 AND GLN-439.
RX   PubMed=10462600; DOI=10.1054/modi00200129;
RA   Tsai M.Y., Wong P.W.K., Garg U., Hanson N.Q., Schwichtenberg K.;
RT   "Two novel mutations in the cystathionine beta-synthase gene of
RT   homocystinuric patients.";
RL   Mol. Diagn. 2:129-133(1997).
RN   [40]
RP   VARIANTS CBSD LYS-144 AND TYR-165.
RX   PubMed=10215408;
RX   DOI=10.1002/(sici)1098-1004(1998)11:4<332::aid-humu16>3.0.co;2-p;
RA   Gordon R.B., Cox A.J., Dawson P.A., Emmerson B.T., Kraus J.P., Dudman N.P.;
RT   "Mutational analysis of the cystathionine beta-synthase gene: a splicing
RT   mutation, two missense mutations and an insertion in patients with
RT   homocystinuria.";
RL   Hum. Mutat. 11:332-332(1998).
RN   [41]
RP   VARIANTS CBSD PRO-101; LYS-228; MET-262; THR-278; SER-307 AND PRO-355.
RX   PubMed=9889017; DOI=10.1006/mgme.1998.2771;
RA   Gallagher P.M., Naughten E., Hanson N.Q., Schwichtenberg K., Bignell M.,
RA   Yuan M., Ward P., Yap S., Whitehead A.S., Tsai M.Y.;
RT   "Characterization of mutations in the cystathionine beta-synthase gene in
RT   Irish patients with homocystinuria.";
RL   Mol. Genet. Metab. 65:298-302(1998).
RN   [42]
RP   VARIANTS CBSD TRP-58; VAL-126; LYS-302 AND CYS-336.
RX   PubMed=10408774;
RX   DOI=10.1002/(sici)1098-1004(1999)13:6<453::aid-humu4>3.0.co;2-k;
RA   de Franchis R., Kraus E., Kozich V., Sebastio G., Kraus J.P.;
RT   "Four novel mutations in the cystathionine beta-synthase gene: effect of a
RT   second linked mutation on the severity of the homocystinuric phenotype.";
RL   Hum. Mutat. 13:453-457(1999).
RN   [43]
RP   VARIANTS CBSD ARG-262 AND THR-278, AND VARIANT GLN-102.
RX   PubMed=11013450;
RX   DOI=10.1002/1098-1004(200010)16:4<372::aid-humu12>3.0.co;2-j;
RA   Gat-Yablonski G., Mandel H., Fowler B., Taleb O., Sela B.-A.;
RT   "Homocystinuria in the Arab population of Israel: identification of two
RT   novel mutations using DGGE analysis.";
RL   Hum. Mutat. 16:372-372(2000).
RN   [44]
RP   VARIANTS CBSD ARG-65; VAL-114; LYS-144; THR-155; TYR-165; LYS-176 AND
RP   THR-278, AND CHARACTERIZATION OF VARIANTS CBSD VAL-114; LYS-144; THR-155;
RP   TYR-165; LYS-176 AND THR-278.
RX   PubMed=11359213; DOI=10.1086/320597;
RA   Janosik M., Oliveriusova J., Janosikova B., Sokolova J., Kraus E.,
RA   Kraus J.P., Kozich V.;
RT   "Impaired heme binding and aggregation of mutant cystathionine beta-
RT   synthase subunits in homocystinuria.";
RL   Am. J. Hum. Genet. 68:1506-1513(2001).
RN   [45]
RP   VARIANTS CBSD PRO-125 AND THR-361.
RX   PubMed=11553052; DOI=10.1034/j.1399-0004.2001.600212.x;
RA   Castro R., Heil S.G., Rivera I., Jakobs C., de Almeida I.T., Blom H.J.;
RT   "Molecular genetic analysis of the cystathionine beta-synthase gene in
RT   Portuguese homocystinuria patients: three novel mutations.";
RL   Clin. Genet. 60:161-163(2001).
RN   [46]
RP   VARIANTS CBSD ARG-85; THR-278; LEU-422; THR-435; ASN-444 AND LEU-466, AND
RP   CHARACTERIZATION OF VARIANTS CBSD ARG-85; LEU-422; THR-435 AND LEU-466.
RX   PubMed=12007221; DOI=10.1002/humu.10089;
RA   Maclean K.N., Gaustadnes M., Oliveriusova J., Janosik M., Kraus E.,
RA   Kozich V., Kery V., Skovby F., Ruediger N., Ingerslev J., Stabler S.P.,
RA   Allen R.H., Kraus J.P.;
RT   "High homocysteine and thrombosis without connective tissue disorders are
RT   associated with a novel class of cystathionine beta-synthase (CBS)
RT   mutations.";
RL   Hum. Mutat. 19:641-655(2002).
RN   [47]
RP   VARIANTS CBSD LEU-49; PRO-101; ARG-109; GLN-125; LYS-144; TYR-165; LYS-228;
RP   THR-278; LYS-302; SER-307; GLU-331; CYS-336; SER-347; MET-353; CYS-369;
RP   MET-371 AND GLN-439, AND CHARACTERIZATION OF VARIANTS CBSD PRO-101;
RP   ARG-109; LYS-228 AND SER-347.
RX   PubMed=12124992; DOI=10.1002/humu.10104;
RA   Gaustadnes M., Wilcken B., Oliveriusova J., McGill J., Fletcher J.,
RA   Kraus J.P., Wilcken D.E.;
RT   "The molecular basis of cystathionine beta-synthase deficiency in
RT   Australian patients: genotype-phenotype correlations and response to
RT   treatment.";
RL   Hum. Mutat. 20:117-126(2002).
RN   [48]
RP   VARIANTS CBSD TRP-125; MET-191; TYR-275; CYS-336; PRO-338; ASN-349; GLN-379
RP   AND PRO-456.
RX   PubMed=12815602; DOI=10.1002/humu.9153;
RA   Urreizti R., Balcells S., Rodes M., Vilarinho L., Baldellou A., Couce M.L.,
RA   Munoz C., Campistol J., Pinto X., Vilaseca M.A., Grinberg D.;
RT   "Spectrum of CBS mutations in 16 homocystinuric patients from the iberian
RT   peninsula: high prevalence of T191M and absence of I278T or G307S.";
RL   Hum. Mutat. 22:103-103(2003).
RN   [49]
RP   VARIANTS CBSD PRO-101; THR-226; SER-228; PRO-231; THR-278; SER-307;
RP   ALA-320; MET-353; ASN-376 AND LYS-526, AND CHARACTERIZATION OF VARIANTS
RP   CBSD PRO-101; THR-226; SER-228; PRO-231; THR-278; SER-307; ALA-320;
RP   MET-353; ASN-376 AND LYS-526.
RX   PubMed=14635102; DOI=10.1002/humu.10290;
RA   Kruger W.D., Wang L., Jhee K.H., Singh R.H., Elsas L.J. II;
RT   "Cystathionine beta-synthase deficiency in Georgia (USA): correlation of
RT   clinical and biochemical phenotype with genotype.";
RL   Hum. Mutat. 22:434-441(2003).
RN   [50]
RP   VARIANTS CBSD MET-143; ARG-148; LYS-228 AND THR-278, AND CHARACTERIZATION
RP   OF VARIANTS CBSD MET-143 AND ARG-148.
RX   PubMed=15146473; DOI=10.1002/humu.9249;
RA   Orendac M., Pronicka E., Kubalska J., Janosik M., Sokolova J.,
RA   Linnebank M., Koch H.G., Kozich V.;
RT   "Identification and functional analysis of two novel mutations in the CBS
RT   gene in Polish patients with homocystinuria.";
RL   Hum. Mutat. 23:631-631(2004).
RN   [51]
RP   VARIANTS CBSD 247-LYS--GLY-256 DEL; PRO-288 AND TRP-379.
RX   PubMed=15365998; DOI=10.1002/humu.9280;
RA   Linnebank M., Janosik M., Kozich V., Pronicka E., Kubalska J., Sokolova J.,
RA   Linnebank A., Schmidt E., Leyendecker C., Klockgether T., Kraus J.P.,
RA   Koch H.G.;
RT   "The cystathionine beta-synthase (CBS) mutation c.1224-2A>C in Central
RT   Europe: vitamin B6 nonresponsiveness and a common ancestral haplotype.";
RL   Hum. Mutat. 24:352-353(2004).
RN   [52]
RP   VARIANTS CBSD ALA-168; MET-191 AND THR-278.
RX   PubMed=15993874; DOI=10.1016/j.cccn.2005.05.030;
RA   Porto M.P.R., Galdieri L.C., Pereira V.G., Vergani N., da Rocha J.C.C.,
RA   Micheletti C., Martins A.M., Perez A.B.A., Almeida V.D.;
RT   "Molecular analysis of homocystinuria in Brazilian patients.";
RL   Clin. Chim. Acta 362:71-78(2005).
RN   [53]
RP   VARIANTS CBSD GLN-154; VAL-155; ASP-234 DEL; MET-257; THR-288; CYS-336;
RP   SER-347 AND MET-353, VARIANT CYS-18, CHARACTERIZATION OF VARIANTS CBSD
RP   GLN-154; VAL-155; ASP-234 DEL; MET-257; THR-288; CYS-336; SER-347 AND
RP   MET-353, AND CHARACTERIZATION OF VARIANT CYS-18.
RX   PubMed=16205833; DOI=10.1007/s10038-005-0312-2;
RA   Lee S.-J., Lee D.H., Yoo H.-W., Koo S.K., Park E.-S., Park J.-W., Lim H.G.,
RA   Jung S.-C.;
RT   "Identification and functional analysis of cystathionine beta-synthase gene
RT   mutations in patients with homocystinuria.";
RL   J. Hum. Genet. 50:648-654(2005).
RN   [54]
RP   CHARACTERIZATION OF VARIANTS CBSD TRP-125; ARG-148; VAL-173; MET-191;
RP   THR-226; TYR-275; CYS-336; HIS-336; PRO-338; ASN-349; GLN-379 AND PRO-456,
RP   AND CHARACTERIZATION OF VARIANT GLN-548.
RX   PubMed=16429402; DOI=10.1002/humu.9395;
RA   Urreizti R., Asteggiano C., Cozar M., Frank N., Vilaseca M.A., Grinberg D.,
RA   Balcells S.;
RT   "Functional assays testing pathogenicity of 14 cystathionine-beta synthase
RT   mutations.";
RL   Hum. Mutat. 27:211-211(2006).
RN   [55]
RP   VARIANTS CBSD MET-173 DEL; LEU-200; SER-278; ASN-281; VAL-321 AND SER-446,
RP   AND CHARACTERIZATION OF VARIANTS CBSD MET-173 DEL; SER-278; ASN-281 AND
RP   VAL-321.
RX   PubMed=21520339; DOI=10.1002/humu.21514;
RA   Cozar M., Urreizti R., Vilarinho L., Grosso C., Dodelson de Kremer R.,
RA   Asteggiano C.G., Dalmau J., Garcia A.M., Vilaseca M.A., Grinberg D.,
RA   Balcells S.;
RT   "Identification and functional analyses of CBS alleles in Spanish and
RT   Argentinian homocystinuric patients.";
RL   Hum. Mutat. 32:835-842(2011).
RN   [56]
RP   VARIANTS CBSD THR-278 AND CYS-336.
RX   PubMed=21240075; DOI=10.1097/pat.0b013e3283419dbb;
RA   Kwok J.S., Fung S.L., Lui G.C., Law E.L., Chan M.H., Leung C.B., Tang N.L.;
RT   "CBS gene mutations found in a Chinese pyridoxine-responsive homocystinuria
RT   patient.";
RL   Pathology 43:81-83(2011).
RN   [57]
RP   VARIANT CBSD LYS-266, CHARACTERIZATION OF VARIANT CBSD LYS-266, AND
RP   ACTIVITY REGULATION.
RX   PubMed=22738154; DOI=10.1021/bi300421z;
RA   Smith A.T., Su Y., Stevens D.J., Majtan T., Kraus J.P., Burstyn J.N.;
RT   "Effect of the disease-causing R266K mutation on the heme and PLP
RT   environments of human cystathionine beta-synthase.";
RL   Biochemistry 51:6360-6370(2012).
RN   [58]
RP   VARIANTS CBSD ARG-85; ASN-87 AND ASN-234, CHARACTERIZATION OF VARIANTS CBSD
RP   ASN-87 AND ASN-234, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, COFACTOR,
RP   SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=23981774; DOI=10.1016/j.gene.2013.08.021;
RA   Casique L., Kabil O., Banerjee R., Martinez J.C., De Lucca M.;
RT   "Characterization of two pathogenic mutations in cystathionine beta-
RT   synthase: different intracellular locations for wild-type and mutant
RT   proteins.";
RL   Gene 531:117-124(2013).
RN   [59]
RP   VARIANT CBSD GLY-449, CHARACTERIZATION OF VARIANTS CBSD LEU-427; ASN-444;
RP   GLY-449; LEU-500 AND GLN-540, AND CATALYTIC ACTIVITY.
RX   PubMed=25044645; DOI=10.1002/humu.22616;
RA   Mendes M.I., Santos A.S., Smith D.E., Lino P.R., Colaco H.G.,
RA   de Almeida I.T., Vicente J.B., Salomons G.S., Rivera I., Blom H.J.,
RA   Leandro P.;
RT   "Insights into the regulatory domain of cystathionine Beta-synthase:
RT   characterization of six variant proteins.";
RL   Hum. Mutat. 35:1195-1202(2014).
RN   [60]
RP   VARIANTS CBSD LEU-49; LYS-269 DEL; THR-278; HIS-336; LEU-427; ASN-444;
RP   LEU-500 AND GLN-540, CHARACTERIZATION OF VARIANTS CBSD LEU-49; LYS-269 DEL;
RP   THR-278; HIS-336; LEU-427; ASN-444; LEU-500 AND GLN-540, FUNCTION,
RP   CATALYTIC ACTIVITY, PATHWAY, AND ACTIVITY REGULATION.
RX   PubMed=23974653; DOI=10.1007/s10545-013-9647-6;
RA   Mendes M.I., Colaco H.G., Smith D.E., Ramos R.J., Pop A., van Dooren S.J.,
RA   Tavares de Almeida I., Kluijtmans L.A., Janssen M.C., Rivera I.,
RA   Salomons G.S., Leandro P., Blom H.J.;
RT   "Reduced response of Cystathionine Beta-Synthase (CBS) to S-
RT   Adenosylmethionine (SAM): Identification and functional analysis of CBS
RT   gene mutations in Homocystinuria patients.";
RL   J. Inherit. Metab. Dis. 37:245-254(2014).
CC   -!- FUNCTION: Hydro-lyase catalyzing the first step of the transsulfuration
CC       pathway, where the hydroxyl group of L-serine is displaced by L-
CC       homocysteine in a beta-replacement reaction to form L-cystathionine,
CC       the precursor of L-cysteine. This catabolic route allows the
CC       elimination of L-methionine and the toxic metabolite L-homocysteine
CC       (PubMed:23981774, PubMed:20506325, PubMed:23974653). Also involved in
CC       the production of hydrogen sulfide, a gasotransmitter with signaling
CC       and cytoprotective effects on neurons (By similarity).
CC       {ECO:0000250|UniProtKB:P32232, ECO:0000269|PubMed:20506325,
CC       ECO:0000269|PubMed:23974653, ECO:0000269|PubMed:23981774}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-homocysteine + L-serine = H2O + L,L-cystathionine;
CC         Xref=Rhea:RHEA:10112, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:58161, ChEBI:CHEBI:58199; EC=4.2.1.22;
CC         Evidence={ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653,
CC         ECO:0000269|PubMed:23981774, ECO:0000269|PubMed:25044645};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:23981774};
CC   -!- ACTIVITY REGULATION: Allosterically activated by S-adenosyl-
CC       methionine/AdoMet. Activated by S-adenosylhomocysteine/AdoHcy
CC       (PubMed:20506325). Binds non-covalently to a heme group that may
CC       control the redox sensitivity of the enzyme (PubMed:11483494,
CC       PubMed:12173932, PubMed:22738154). {ECO:0000269|PubMed:11483494,
CC       ECO:0000269|PubMed:12173932, ECO:0000269|PubMed:20506325,
CC       ECO:0000269|PubMed:22738154, ECO:0000269|PubMed:23974653}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-homocysteine and L-serine: step 1/2.
CC       {ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653,
CC       ECO:0000269|PubMed:23981774}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11483494,
CC       ECO:0000269|PubMed:12173932, ECO:0000269|PubMed:20506325,
CC       ECO:0000269|PubMed:23981774}.
CC   -!- INTERACTION:
CC       P35520; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-740135, EBI-1383687;
CC       P35520; P35520: CBS; NbExp=6; IntAct=EBI-740135, EBI-740135;
CC       P35520; P35222: CTNNB1; NbExp=3; IntAct=EBI-740135, EBI-491549;
CC       P35520; Q15438: CYTH1; NbExp=3; IntAct=EBI-740135, EBI-997830;
CC       P35520; Q08426: EHHADH; NbExp=4; IntAct=EBI-740135, EBI-2339219;
CC       P35520; O75344: FKBP6; NbExp=3; IntAct=EBI-740135, EBI-744771;
CC       P35520; P51116: FXR2; NbExp=3; IntAct=EBI-740135, EBI-740459;
CC       P35520; P06241: FYN; NbExp=3; IntAct=EBI-740135, EBI-515315;
CC       P35520; P22466: GAL; NbExp=3; IntAct=EBI-740135, EBI-6624768;
CC       P35520; P42858: HTT; NbExp=12; IntAct=EBI-740135, EBI-466029;
CC       P35520; Q92993-2: KAT5; NbExp=3; IntAct=EBI-740135, EBI-20795332;
CC       P35520; O75928-2: PIAS2; NbExp=3; IntAct=EBI-740135, EBI-348567;
CC       P35520; Q13526: PIN1; NbExp=4; IntAct=EBI-740135, EBI-714158;
CC       P35520; P17612: PRKACA; NbExp=3; IntAct=EBI-740135, EBI-476586;
CC       P35520; P54619: PRKAG1; NbExp=3; IntAct=EBI-740135, EBI-1181439;
CC       P35520; P25786: PSMA1; NbExp=4; IntAct=EBI-740135, EBI-359352;
CC       P35520; P57075: UBASH3A; NbExp=4; IntAct=EBI-740135, EBI-2105393;
CC       P35520; Q7KZS0: UBE2I; NbExp=6; IntAct=EBI-740135, EBI-10180829;
CC       P35520; Q9UJ78-2: ZMYM5; NbExp=3; IntAct=EBI-740135, EBI-17634549;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17087506,
CC       ECO:0000269|PubMed:23981774}. Nucleus {ECO:0000269|PubMed:17087506}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Major;
CC         IsoId=P35520-1; Sequence=Displayed;
CC       Name=2; Synonyms=Minor;
CC         IsoId=P35520-2; Sequence=VSP_001217;
CC   -!- TISSUE SPECIFICITY: In the adult strongly expressed in liver and
CC       pancreas, some expression in heart and brain, weak expression in lung
CC       and kidney. In the fetus, expressed in brain, liver and kidney.
CC   -!- DISEASE: Cystathionine beta-synthase deficiency (CBSD) [MIM:236200]: An
CC       enzymatic deficiency resulting in altered sulfur metabolism and
CC       homocystinuria. The clinical features of untreated homocystinuria due
CC       to CBS deficiency include myopia, ectopia lentis, intellectual
CC       disability, skeletal anomalies resembling Marfan syndrome, and
CC       thromboembolic events. Light skin and hair can also be present.
CC       Biochemical features include increased urinary homocystine and
CC       methionine. {ECO:0000269|PubMed:10215408, ECO:0000269|PubMed:10408774,
CC       ECO:0000269|PubMed:10462600, ECO:0000269|PubMed:11013450,
CC       ECO:0000269|PubMed:11359213, ECO:0000269|PubMed:11553052,
CC       ECO:0000269|PubMed:12007221, ECO:0000269|PubMed:12124992,
CC       ECO:0000269|PubMed:12815602, ECO:0000269|PubMed:1301198,
CC       ECO:0000269|PubMed:14635102, ECO:0000269|PubMed:15146473,
CC       ECO:0000269|PubMed:15365998, ECO:0000269|PubMed:15993874,
CC       ECO:0000269|PubMed:16205833, ECO:0000269|PubMed:16429402,
CC       ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:21240075,
CC       ECO:0000269|PubMed:21520339, ECO:0000269|PubMed:22738154,
CC       ECO:0000269|PubMed:23974653, ECO:0000269|PubMed:23981774,
CC       ECO:0000269|PubMed:25044645, ECO:0000269|PubMed:7506602,
CC       ECO:0000269|PubMed:7564249, ECO:0000269|PubMed:7611293,
CC       ECO:0000269|PubMed:7635485, ECO:0000269|PubMed:7762555,
CC       ECO:0000269|PubMed:7849717, ECO:0000269|PubMed:7967489,
CC       ECO:0000269|PubMed:7981678, ECO:0000269|PubMed:8353501,
CC       ECO:0000269|PubMed:8528202, ECO:0000269|PubMed:8755636,
CC       ECO:0000269|PubMed:8803779, ECO:0000269|PubMed:8990018,
CC       ECO:0000269|PubMed:9156316, ECO:0000269|PubMed:9266356,
CC       ECO:0000269|PubMed:9361025, ECO:0000269|PubMed:9889017}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=CBS mutation database;
CC       URL="http://cbs.lf1.cuni.cz/index.php";
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DR   EMBL; L19501; AAA19874.1; -; mRNA.
DR   EMBL; X82166; CAA57656.1; -; mRNA.
DR   EMBL; L14577; AAA98524.1; -; mRNA.
DR   EMBL; X88562; CAA61252.1; -; Genomic_DNA.
DR   EMBL; X91910; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98811; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98812; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98813; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98814; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98815; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98816; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98817; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98818; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98819; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98820; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98821; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98822; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; X98823; CAA61252.1; JOINED; Genomic_DNA.
DR   EMBL; AF042836; AAC64684.1; -; Genomic_DNA.
DR   EMBL; AF042836; AAC64683.1; -; Genomic_DNA.
DR   EMBL; BT007154; AAP35818.1; -; mRNA.
DR   EMBL; AK313691; BAG36440.1; -; mRNA.
DR   EMBL; AP001630; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471079; EAX09508.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09509.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09510.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09511.1; -; Genomic_DNA.
DR   EMBL; CH471079; EAX09515.1; -; Genomic_DNA.
DR   EMBL; BC000440; AAH00440.1; -; mRNA.
DR   EMBL; BC007257; AAH07257.1; -; mRNA.
DR   EMBL; BC010242; AAH10242.1; -; mRNA.
DR   EMBL; BC011381; AAH11381.1; -; mRNA.
DR   CCDS; CCDS13693.1; -. [P35520-1]
DR   CCDS; CCDS82646.1; -. [P35520-1]
DR   CCDS; CCDS86979.1; -. [P35520-2]
DR   PIR; A55760; A55760.
DR   RefSeq; NP_000062.1; NM_000071.2. [P35520-1]
DR   RefSeq; NP_001171479.1; NM_001178008.2. [P35520-1]
DR   RefSeq; NP_001171480.1; NM_001178009.2. [P35520-1]
DR   RefSeq; NP_001307227.1; NM_001320298.1. [P35520-1]
DR   RefSeq; NP_001308002.1; NM_001321073.1. [P35520-1]
DR   RefSeq; XP_011528079.1; XM_011529777.1. [P35520-2]
DR   RefSeq; XP_011528083.1; XM_011529781.1.
DR   RefSeq; XP_011528084.1; XM_011529782.1.
DR   RefSeq; XP_011544396.1; XM_011546094.1.
DR   RefSeq; XP_011544397.1; XM_011546095.2.
DR   RefSeq; XP_011544399.1; XM_011546097.2.
DR   RefSeq; XP_011544400.1; XM_011546098.1.
DR   RefSeq; XP_011544401.1; XM_011546099.1.
DR   RefSeq; XP_016883700.1; XM_017028211.1.
DR   RefSeq; XP_016883701.1; XM_017028212.1.
DR   RefSeq; XP_016883702.1; XM_017028213.1.
DR   RefSeq; XP_016883703.1; XM_017028214.1.
DR   RefSeq; XP_016883704.1; XM_017028215.1.
DR   RefSeq; XP_016883705.1; XM_017028216.1.
DR   RefSeq; XP_016883706.1; XM_017028217.1.
DR   RefSeq; XP_016883707.1; XM_017028218.1.
DR   RefSeq; XP_016883978.1; XM_017028489.1.
DR   RefSeq; XP_016883979.1; XM_017028490.1.
DR   RefSeq; XP_016883980.1; XM_017028491.1. [P35520-1]
DR   RefSeq; XP_016883981.1; XM_017028492.1.
DR   PDB; 1JBQ; X-ray; 2.60 A; A/B/C/D/E/F=2-413.
DR   PDB; 1M54; X-ray; 2.90 A; A/B/C/D/E/F=44-406.
DR   PDB; 4COO; X-ray; 2.00 A; A/B=1-551.
DR   PDB; 4L0D; X-ray; 2.97 A; A/B=1-551.
DR   PDB; 4L27; X-ray; 3.39 A; A/B/C/D=2-551.
DR   PDB; 4L28; X-ray; 2.63 A; A/B/C/D=2-551.
DR   PDB; 4L3V; X-ray; 3.63 A; A/B/C=2-551.
DR   PDB; 4PCU; X-ray; 3.58 A; A/B=1-551.
DR   PDB; 4UUU; X-ray; 1.71 A; A/B=406-547.
DR   PDB; 5MMS; X-ray; 2.80 A; A/B/C/D/E/F=1-408.
DR   PDBsum; 1JBQ; -.
DR   PDBsum; 1M54; -.
DR   PDBsum; 4COO; -.
DR   PDBsum; 4L0D; -.
DR   PDBsum; 4L27; -.
DR   PDBsum; 4L28; -.
DR   PDBsum; 4L3V; -.
DR   PDBsum; 4PCU; -.
DR   PDBsum; 4UUU; -.
DR   PDBsum; 5MMS; -.
DR   AlphaFoldDB; P35520; -.
DR   SMR; P35520; -.
DR   BioGRID; 107321; 129.
DR   BioGRID; 3195666; 10.
DR   IntAct; P35520; 42.
DR   MINT; P35520; -.
DR   BindingDB; P35520; -.
DR   ChEMBL; CHEMBL3399911; -.
DR   DrugBank; DB00118; Ademetionine.
DR   DrugBank; DB00151; Cysteine.
DR   DrugBank; DB00114; Pyridoxal phosphate.
DR   DrugBank; DB00133; Serine.
DR   DrugCentral; P35520; -.
DR   GuidetoPHARMACOLOGY; 1443; -.
DR   GlyGen; P35520; 2 sites, 2 O-linked glycans (2 sites).
DR   iPTMnet; P35520; -.
DR   PhosphoSitePlus; P35520; -.
DR   SwissPalm; P35520; -.
DR   BioMuta; CBS; -.
DR   DMDM; 543959; -.
DR   EPD; P35520; -.
DR   jPOST; P35520; -.
DR   MassIVE; P35520; -.
DR   MaxQB; P35520; -.
DR   PRIDE; P35520; -.
DR   ProteomicsDB; 55074; -. [P35520-1]
DR   ProteomicsDB; 55075; -. [P35520-2]
DR   Antibodypedia; 768; 495 antibodies from 37 providers.
DR   DNASU; 875; -.
DR   Ensembl; ENST00000352178.9; ENSP00000344460.5; ENSG00000160200.18. [P35520-1]
DR   Ensembl; ENST00000359624.7; ENSP00000352643.3; ENSG00000160200.18. [P35520-1]
DR   Ensembl; ENST00000398158.5; ENSP00000381225.1; ENSG00000160200.18. [P35520-1]
DR   Ensembl; ENST00000398165.8; ENSP00000381231.4; ENSG00000160200.18. [P35520-1]
DR   GeneID; 102724560; -.
DR   GeneID; 875; -.
DR   KEGG; hsa:102724560; -.
DR   KEGG; hsa:875; -.
DR   MANE-Select; ENST00000398165.8; ENSP00000381231.4; NM_000071.3; NP_000062.1.
DR   UCSC; uc002zct.3; human. [P35520-1]
DR   CTD; 875; -.
DR   DisGeNET; 102724560; -.
DR   DisGeNET; 875; -.
DR   GeneCards; CBS; -.
DR   GeneReviews; CBS; -.
DR   HGNC; HGNC:1550; CBS.
DR   HPA; ENSG00000160200; Tissue enhanced (liver, pancreas).
DR   MalaCards; CBS; -.
DR   MIM; 236200; phenotype.
DR   MIM; 613381; gene.
DR   neXtProt; NX_P35520; -.
DR   OpenTargets; ENSG00000160200; -.
DR   OpenTargets; ENSG00000274276; -.
DR   Orphanet; 394; Classic homocystinuria.
DR   PharmGKB; PA26123; -.
DR   VEuPathDB; HostDB:ENSG00000160200; -.
DR   GeneTree; ENSGT00510000047027; -.
DR   HOGENOM; CLU_021018_0_0_1; -.
DR   InParanoid; P35520; -.
DR   OMA; IEITMDT; -.
DR   OrthoDB; 1016546at2759; -.
DR   PhylomeDB; P35520; -.
DR   TreeFam; TF300784; -.
DR   BioCyc; MetaCyc:HS08461-MON; -.
DR   BRENDA; 4.2.1.22; 2681.
DR   PathwayCommons; P35520; -.
DR   Reactome; R-HSA-1614603; Cysteine formation from homocysteine.
DR   Reactome; R-HSA-2408508; Metabolism of ingested SeMet, Sec, MeSec into H2Se.
DR   SABIO-RK; P35520; -.
DR   SignaLink; P35520; -.
DR   SIGNOR; P35520; -.
DR   UniPathway; UPA00136; UER00201.
DR   BioGRID-ORCS; 102724560; 0 hits in 13 CRISPR screens.
DR   BioGRID-ORCS; 875; 11 hits in 1080 CRISPR screens.
DR   ChiTaRS; CBS; human.
DR   EvolutionaryTrace; P35520; -.
DR   GeneWiki; Cystathionine_beta_synthase; -.
DR   Pharos; P35520; Tchem.
DR   PRO; PR:P35520; -.
DR   Proteomes; UP000005640; Chromosome 21.
DR   RNAct; P35520; protein.
DR   Bgee; ENSG00000160200; Expressed in right lobe of liver and 95 other tissues.
DR   ExpressionAtlas; P35520; baseline and differential.
DR   Genevisible; P35520; HS.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0070025; F:carbon monoxide binding; IDA:BHF-UCL.
DR   GO; GO:0004122; F:cystathionine beta-synthase activity; IDA:UniProtKB.
DR   GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR   GO; GO:0020037; F:heme binding; IDA:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0072341; F:modified amino acid binding; IDA:UniProtKB.
DR   GO; GO:0070026; F:nitric oxide binding; IDA:BHF-UCL.
DR   GO; GO:0050421; F:nitrite reductase (NO-forming) activity; IDA:BHF-UCL.
DR   GO; GO:0019825; F:oxygen binding; IDA:BHF-UCL.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IDA:BHF-UCL.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR   GO; GO:0097746; P:blood vessel diameter maintenance; IEA:Ensembl.
DR   GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
DR   GO; GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0021587; P:cerebellum morphogenesis; IEA:Ensembl.
DR   GO; GO:0019344; P:cysteine biosynthetic process; IDA:BHF-UCL.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   GO; GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
DR   GO; GO:0042262; P:DNA protection; IMP:BHF-UCL.
DR   GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR   GO; GO:0043418; P:homocysteine catabolic process; IDA:UniProtKB.
DR   GO; GO:0050667; P:homocysteine metabolic process; IDA:UniProtKB.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0019448; P:L-cysteine catabolic process; IDA:UniProtKB.
DR   GO; GO:0006565; P:L-serine catabolic process; IDA:UniProtKB.
DR   GO; GO:0006563; P:L-serine metabolic process; IDA:UniProtKB.
DR   GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0043506; P:regulation of JUN kinase activity; IEA:Ensembl.
DR   GO; GO:0010749; P:regulation of nitric oxide mediated signal transduction; IEA:Ensembl.
DR   GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
DR   GO; GO:0006801; P:superoxide metabolic process; IEA:Ensembl.
DR   GO; GO:0019346; P:transsulfuration; IEA:Ensembl.
DR   CDD; cd04608; CBS_pair_CBS; 1.
DR   DisProt; DP01976; -.
DR   Gene3D; 3.10.580.10; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR046353; CBS_C.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR005857; Cysta_beta_synth.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SMART; SM00116; CBS; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   TIGRFAMs; TIGR01137; cysta_beta; 1.
DR   PROSITE; PS51371; CBS; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Alternative splicing;
KW   Amino-acid biosynthesis; CBS domain; Cysteine biosynthesis; Cytoplasm;
KW   Disease variant; Heme; Iron; Isopeptide bond; Lyase; Metal-binding;
KW   Nucleus; Phosphoprotein; Pyridoxal phosphate; Reference proteome;
KW   Ubl conjugation.
FT   CHAIN           1..551
FT                   /note="Cystathionine beta-synthase"
FT                   /id="PRO_0000167133"
FT   DOMAIN          418..476
FT                   /note="CBS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         52
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:11483494,
FT                   ECO:0000269|PubMed:12173932"
FT   BINDING         65
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000269|PubMed:11483494,
FT                   ECO:0000269|PubMed:12173932"
FT   BINDING         149
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:11483494,
FT                   ECO:0000269|PubMed:12173932"
FT   BINDING         256..260
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:11483494,
FT                   ECO:0000269|PubMed:12173932"
FT   BINDING         349
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000269|PubMed:11483494,
FT                   ECO:0000269|PubMed:12173932"
FT   MOD_RES         27
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         119
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:11483494,
FT                   ECO:0000269|PubMed:12173932"
FT   MOD_RES         199
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   CROSSLNK        211
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO)"
FT                   /evidence="ECO:0000269|PubMed:17087506"
FT   VAR_SEQ         518
FT                   /note="Y -> SQDQAWAGVVGGPAD (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_001217"
FT   VARIANT         18
FT                   /note="R -> C (associated with 1/3 to 2/3 the enzyme
FT                   activity of the wild-type; dbSNP:rs201827340)"
FT                   /evidence="ECO:0000269|PubMed:16205833"
FT                   /id="VAR_046921"
FT   VARIANT         49
FT                   /note="P -> L (in CBSD; decreased expression; no effect on
FT                   cystathionine beta-synthase activity; increased
FT                   homotetramer formation; dbSNP:rs148865119)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653"
FT                   /id="VAR_008049"
FT   VARIANT         58
FT                   /note="R -> W (in CBSD; linked with V-114; 18% of activity;
FT                   dbSNP:rs555959266)"
FT                   /evidence="ECO:0000269|PubMed:10408774"
FT                   /id="VAR_008050"
FT   VARIANT         65
FT                   /note="H -> R (in CBSD; decreased cystathionine beta-
FT                   synthase activity; inhibited by AdoMet and AdoHcy;
FT                   decreased homotetramer formation; dbSNP:rs1191141364)"
FT                   /evidence="ECO:0000269|PubMed:11359213,
FT                   ECO:0000269|PubMed:20506325"
FT                   /id="VAR_021790"
FT   VARIANT         69
FT                   /note="A -> P (in dbSNP:rs17849313)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_046922"
FT   VARIANT         78
FT                   /note="P -> R (in CBSD; severe form; associated in cis with
FT                   N-102; decreased cystathionine beta-synthase activity;
FT                   decreased homotetramer formation; dbSNP:rs786204608)"
FT                   /evidence="ECO:0000269|PubMed:20506325,
FT                   ECO:0000269|PubMed:7981678"
FT                   /id="VAR_002171"
FT   VARIANT         85
FT                   /note="G -> R (in CBSD; loss of cystathionine beta-synthase
FT                   activity; dbSNP:rs863223435)"
FT                   /evidence="ECO:0000269|PubMed:12007221,
FT                   ECO:0000269|PubMed:23981774"
FT                   /id="VAR_008051"
FT   VARIANT         87
FT                   /note="T -> N (in CBSD; decreased cystathionine beta-
FT                   synthase activity; increased aggregation)"
FT                   /evidence="ECO:0000269|PubMed:23981774"
FT                   /id="VAR_074590"
FT   VARIANT         88
FT                   /note="P -> S (in CBSD)"
FT                   /evidence="ECO:0000269|PubMed:7762555"
FT                   /id="VAR_002172"
FT   VARIANT         101
FT                   /note="L -> P (in CBSD; common mutation in Irish
FT                   population; loss of activity; dbSNP:rs786204757)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:14635102, ECO:0000269|PubMed:9889017"
FT                   /id="VAR_021791"
FT   VARIANT         102
FT                   /note="K -> N (in CBSD; associated in cis with R-78;
FT                   decreased cystathionine beta-synthase activity; decreased
FT                   homotetramer formation; dbSNP:rs786204609)"
FT                   /evidence="ECO:0000269|PubMed:20506325,
FT                   ECO:0000269|PubMed:7981678"
FT                   /id="VAR_002173"
FT   VARIANT         102
FT                   /note="K -> Q (in dbSNP:rs34040148)"
FT                   /evidence="ECO:0000269|PubMed:11013450"
FT                   /id="VAR_008052"
FT   VARIANT         109
FT                   /note="C -> R (in CBSD; loss of activity;
FT                   dbSNP:rs778220779)"
FT                   /evidence="ECO:0000269|PubMed:12124992"
FT                   /id="VAR_021792"
FT   VARIANT         114
FT                   /note="A -> V (in CBSD; mild form; when linked with W-58
FT                   severe form; decreased cystathionine beta-synthase
FT                   activity; decreases homotetramer formation by promoting
FT                   formation of larger aggregates; dbSNP:rs121964964)"
FT                   /evidence="ECO:0000269|PubMed:11359213,
FT                   ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:8353501"
FT                   /id="VAR_002174"
FT   VARIANT         116
FT                   /note="G -> R (in CBSD; dbSNP:rs760214620)"
FT                   /evidence="ECO:0000269|PubMed:8803779"
FT                   /id="VAR_008053"
FT   VARIANT         121
FT                   /note="R -> C (in CBSD; dbSNP:rs775992753)"
FT                   /id="VAR_008054"
FT   VARIANT         121
FT                   /note="R -> H (in CBSD; dbSNP:rs770095972)"
FT                   /id="VAR_008055"
FT   VARIANT         121
FT                   /note="R -> L (in CBSD; mild form; dbSNP:rs770095972)"
FT                   /id="VAR_008056"
FT   VARIANT         125
FT                   /note="R -> P (in CBSD)"
FT                   /evidence="ECO:0000269|PubMed:11553052"
FT                   /id="VAR_046923"
FT   VARIANT         125
FT                   /note="R -> Q (in CBSD; severe form; when linked with D-131
FT                   moderate form; loss of cystathionine beta-synthase
FT                   activity; decreased homotetramer formation;
FT                   dbSNP:rs781444670)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:7762555,
FT                   ECO:0000269|PubMed:7849717"
FT                   /id="VAR_002175"
FT   VARIANT         125
FT                   /note="R -> W (in CBSD; exhibits an activity lower than 4%
FT                   of the wild-type enzyme; absent capacity to form multimeric
FT                   quaternary structure; dbSNP:rs886057100)"
FT                   /evidence="ECO:0000269|PubMed:12815602,
FT                   ECO:0000269|PubMed:16429402"
FT                   /id="VAR_008057"
FT   VARIANT         126
FT                   /note="M -> V (in CBSD; loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:10408774"
FT                   /id="VAR_008058"
FT   VARIANT         128
FT                   /note="E -> D (in CBSD; dbSNP:rs374593242)"
FT                   /id="VAR_008059"
FT   VARIANT         131
FT                   /note="E -> D (in CBSD; linked with Q-125; loss of
FT                   activity; dbSNP:rs1555875351)"
FT                   /evidence="ECO:0000269|PubMed:7849717"
FT                   /id="VAR_002176"
FT   VARIANT         139
FT                   /note="G -> R (in CBSD; mild form; dbSNP:rs121964965)"
FT                   /evidence="ECO:0000269|PubMed:7611293"
FT                   /id="VAR_008060"
FT   VARIANT         143
FT                   /note="I -> M (in CBSD; 4% of activity; stable;
FT                   dbSNP:rs370167302)"
FT                   /evidence="ECO:0000269|PubMed:15146473"
FT                   /id="VAR_021793"
FT   VARIANT         144
FT                   /note="E -> K (in CBSD; loss of cystathionine beta-synthase
FT                   activity; impaired stimulation by AdoMet and AdoHcy;
FT                   decreased homotetramer formation; dbSNP:rs121964966)"
FT                   /evidence="ECO:0000269|PubMed:10215408,
FT                   ECO:0000269|PubMed:11359213, ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:7611293,
FT                   ECO:0000269|PubMed:9156316"
FT                   /id="VAR_002177"
FT   VARIANT         145
FT                   /note="P -> L (in CBSD; dbSNP:rs121964963)"
FT                   /evidence="ECO:0000269|PubMed:8353501"
FT                   /id="VAR_002178"
FT   VARIANT         148
FT                   /note="G -> R (in CBSD; loss of cystathionine beta-synthase
FT                   activity; impaired stimulation by AdoMet and AdoHcy; loss
FT                   of homotetramer formation; dbSNP:rs755952006)"
FT                   /evidence="ECO:0000269|PubMed:15146473,
FT                   ECO:0000269|PubMed:16429402, ECO:0000269|PubMed:20506325"
FT                   /id="VAR_008061"
FT   VARIANT         151..159
FT                   /note="Missing (in CBSD)"
FT                   /id="VAR_008063"
FT   VARIANT         151
FT                   /note="G -> R (in CBSD; dbSNP:rs373782713)"
FT                   /id="VAR_008062"
FT   VARIANT         152
FT                   /note="I -> M (in CBSD; severe form)"
FT                   /id="VAR_008064"
FT   VARIANT         154
FT                   /note="L -> Q (in CBSD; protein expression is comparable to
FT                   wild-type; significant decrease of enzyme activity)"
FT                   /evidence="ECO:0000269|PubMed:16205833"
FT                   /id="VAR_046924"
FT   VARIANT         155
FT                   /note="A -> T (in CBSD; complete loss of activity; severely
FT                   affects homotetramer formation by promoting formation of
FT                   larger aggregates; dbSNP:rs1429138569)"
FT                   /evidence="ECO:0000269|PubMed:11359213"
FT                   /id="VAR_008065"
FT   VARIANT         155
FT                   /note="A -> V (in CBSD; protein expression is comparable to
FT                   wild-type; significant decrease of enzyme activity)"
FT                   /evidence="ECO:0000269|PubMed:16205833"
FT                   /id="VAR_046925"
FT   VARIANT         165
FT                   /note="C -> Y (in CBSD; severe form; protein expression is
FT                   comparable to wild-type; loss of cystathionine beta-
FT                   synthase activity; no effect on homotetramer formation;
FT                   dbSNP:rs1347651454)"
FT                   /evidence="ECO:0000269|PubMed:10215408,
FT                   ECO:0000269|PubMed:11359213, ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:7635485"
FT                   /id="VAR_002179"
FT   VARIANT         168
FT                   /note="V -> A (in CBSD)"
FT                   /evidence="ECO:0000269|PubMed:15993874"
FT                   /id="VAR_046926"
FT   VARIANT         168
FT                   /note="V -> M (in CBSD; dbSNP:rs121964970)"
FT                   /evidence="ECO:0000269|PubMed:8528202"
FT                   /id="VAR_002180"
FT   VARIANT         173
FT                   /note="M -> V (in CBSD; presents 40% of the wild-type
FT                   activity; highly reduced capacity to form multimeric
FT                   quaternary structure)"
FT                   /evidence="ECO:0000269|PubMed:16429402"
FT                   /id="VAR_046927"
FT   VARIANT         173
FT                   /note="Missing (in CBSD; loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:21520339"
FT                   /id="VAR_066098"
FT   VARIANT         176
FT                   /note="E -> K (in CBSD; severe form; loss of cystathionine
FT                   beta-synthase activity; inhibited by AdoMet; severely
FT                   decreases homotetramer formation by promoting formation of
FT                   larger aggregates; dbSNP:rs762065361)"
FT                   /evidence="ECO:0000269|PubMed:11359213,
FT                   ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:9266356"
FT                   /id="VAR_008066"
FT   VARIANT         180
FT                   /note="V -> A (in CBSD; decreased cystathionine beta-
FT                   synthase activity; decreases homotetramer formation;
FT                   dbSNP:rs1555875010)"
FT                   /evidence="ECO:0000269|PubMed:20506325"
FT                   /id="VAR_008067"
FT   VARIANT         191
FT                   /note="T -> M (in CBSD; moderate and severe forms; loss of
FT                   cystathionine beta-synthase activity; absent capacity to
FT                   form multimeric quaternary structure; dbSNP:rs121964973)"
FT                   /evidence="ECO:0000269|PubMed:12815602,
FT                   ECO:0000269|PubMed:15993874, ECO:0000269|PubMed:16429402,
FT                   ECO:0000269|PubMed:20506325"
FT                   /id="VAR_008068"
FT   VARIANT         198
FT                   /note="D -> V (in CBSD)"
FT                   /id="VAR_008069"
FT   VARIANT         200
FT                   /note="P -> L (in CBSD; dbSNP:rs758712880)"
FT                   /evidence="ECO:0000269|PubMed:21520339"
FT                   /id="VAR_066099"
FT   VARIANT         224
FT                   /note="R -> H (in CBSD; dbSNP:rs761647392)"
FT                   /evidence="ECO:0000269|PubMed:8528202"
FT                   /id="VAR_002181"
FT   VARIANT         226
FT                   /note="A -> T (in CBSD; presents 20% of the wild-type
FT                   activity; dramatically reduced capacity to form multimeric
FT                   quaternary structure; dbSNP:rs763835246)"
FT                   /evidence="ECO:0000269|PubMed:14635102,
FT                   ECO:0000269|PubMed:16429402"
FT                   /id="VAR_008070"
FT   VARIANT         228
FT                   /note="N -> K (in CBSD; loss of cystathionine beta-synthase
FT                   activity; decreased homotetramer formation;
FT                   dbSNP:rs1464223176)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:15146473, ECO:0000269|PubMed:20506325,
FT                   ECO:0000269|PubMed:9889017"
FT                   /id="VAR_021794"
FT   VARIANT         228
FT                   /note="N -> S (in CBSD; has significantly decreased levels
FT                   of enzyme activity; dbSNP:rs1555874803)"
FT                   /evidence="ECO:0000269|PubMed:14635102"
FT                   /id="VAR_046928"
FT   VARIANT         231
FT                   /note="A -> P (in CBSD; has significantly decreased levels
FT                   of enzyme activity)"
FT                   /evidence="ECO:0000269|PubMed:14635102"
FT                   /id="VAR_046929"
FT   VARIANT         234
FT                   /note="D -> N (in CBSD; decreased cystathionine beta-
FT                   synthase activity; changed localization; decreased
FT                   interaction with pyridoxal 5'-phosphate; no effect on
FT                   homotetramer formation; dbSNP:rs773734233)"
FT                   /evidence="ECO:0000269|PubMed:23981774"
FT                   /id="VAR_008071"
FT   VARIANT         234
FT                   /note="Missing (in CBSD; protein expression is comparable
FT                   to wild-type; significant decrease of enzyme activity)"
FT                   /evidence="ECO:0000269|PubMed:16205833"
FT                   /id="VAR_046930"
FT   VARIANT         239
FT                   /note="E -> K (in CBSD)"
FT                   /id="VAR_002182"
FT   VARIANT         247..256
FT                   /note="Missing (in CBSD)"
FT                   /evidence="ECO:0000269|PubMed:15365998"
FT                   /id="VAR_046931"
FT   VARIANT         257
FT                   /note="T -> M (in CBSD; moderate to severe form; protein
FT                   expression is comparable to wild-type; significant decrease
FT                   of enzyme activity; dbSNP:rs758236584)"
FT                   /evidence="ECO:0000269|PubMed:16205833,
FT                   ECO:0000269|PubMed:7762555"
FT                   /id="VAR_002183"
FT   VARIANT         262
FT                   /note="T -> M (in CBSD; moderate form; dbSNP:rs149119723)"
FT                   /evidence="ECO:0000269|PubMed:9361025,
FT                   ECO:0000269|PubMed:9889017"
FT                   /id="VAR_008072"
FT   VARIANT         262
FT                   /note="T -> R (in CBSD; severe form; loss of cystathionine
FT                   beta-synthase activity; loss of homotetramer formation)"
FT                   /evidence="ECO:0000269|PubMed:11013450,
FT                   ECO:0000269|PubMed:20506325"
FT                   /id="VAR_021795"
FT   VARIANT         266
FT                   /note="R -> G (in CBSD)"
FT                   /id="VAR_008073"
FT   VARIANT         266
FT                   /note="R -> K (in CBSD; mild form; decreased cystathionine
FT                   beta-synthase activity; decreased homotetramer formation;
FT                   no effect on heme-binding; decreased stability;
FT                   dbSNP:rs121964969)"
FT                   /evidence="ECO:0000269|PubMed:20506325,
FT                   ECO:0000269|PubMed:22738154, ECO:0000269|PubMed:9361025"
FT                   /id="VAR_008074"
FT   VARIANT         269
FT                   /note="Missing (in CBSD; loss of expression)"
FT                   /evidence="ECO:0000269|PubMed:23974653"
FT                   /id="VAR_074591"
FT   VARIANT         270
FT                   /note="Missing (in CBSD)"
FT                   /id="VAR_008075"
FT   VARIANT         275
FT                   /note="C -> Y (in CBSD; severe form; exhibits an activity
FT                   lower than 4% of the wild-type enzyme; absent capacity to
FT                   form multimeric quaternary structure)"
FT                   /evidence="ECO:0000269|PubMed:12815602,
FT                   ECO:0000269|PubMed:16429402"
FT                   /id="VAR_021796"
FT   VARIANT         278
FT                   /note="I -> S (in CBSD; loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:21520339"
FT                   /id="VAR_066100"
FT   VARIANT         278
FT                   /note="I -> T (in CBSD; mild to severe form; common
FT                   mutation; decreased expression; loss of cystathionine beta-
FT                   synthase activity; impaired stimulation by AdoMet and
FT                   AdoHcy; severely affects homotetramer formation by
FT                   promoting formation of larger aggregates; dbSNP:rs5742905)"
FT                   /evidence="ECO:0000269|PubMed:11013450,
FT                   ECO:0000269|PubMed:11359213, ECO:0000269|PubMed:12007221,
FT                   ECO:0000269|PubMed:12124992, ECO:0000269|PubMed:1301198,
FT                   ECO:0000269|PubMed:14635102, ECO:0000269|PubMed:15146473,
FT                   ECO:0000269|PubMed:15993874, ECO:0000269|PubMed:20506325,
FT                   ECO:0000269|PubMed:21240075, ECO:0000269|PubMed:23974653,
FT                   ECO:0000269|PubMed:7506602, ECO:0000269|PubMed:7611293,
FT                   ECO:0000269|PubMed:8528202, ECO:0000269|PubMed:8803779,
FT                   ECO:0000269|PubMed:9156316, ECO:0000269|PubMed:9266356,
FT                   ECO:0000269|PubMed:9361025, ECO:0000269|PubMed:9889017"
FT                   /id="VAR_002184"
FT   VARIANT         281
FT                   /note="D -> N (in CBSD; loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:21520339"
FT                   /id="VAR_066101"
FT   VARIANT         288
FT                   /note="A -> P (in CBSD)"
FT                   /evidence="ECO:0000269|PubMed:15365998"
FT                   /id="VAR_046932"
FT   VARIANT         288
FT                   /note="A -> T (in CBSD; protein expression is comparable to
FT                   wild-type; significant decrease of enzyme activity;
FT                   dbSNP:rs141502207)"
FT                   /evidence="ECO:0000269|PubMed:16205833"
FT                   /id="VAR_046933"
FT   VARIANT         290
FT                   /note="P -> L (in CBSD; dbSNP:rs760912339)"
FT                   /evidence="ECO:0000269|PubMed:7564249,
FT                   ECO:0000269|PubMed:8803779"
FT                   /id="VAR_002185"
FT   VARIANT         302
FT                   /note="E -> K (in CBSD; no effect on cystathionine beta-
FT                   synthase activity; inhibited by AdoHcy and impaired
FT                   activation by AdoMet; no effect on homotetramer formation;
FT                   dbSNP:rs779270933)"
FT                   /evidence="ECO:0000269|PubMed:10408774,
FT                   ECO:0000269|PubMed:12124992, ECO:0000269|PubMed:20506325"
FT                   /id="VAR_008076"
FT   VARIANT         305
FT                   /note="G -> R (in CBSD; loss of cystathionine beta-synthase
FT                   activity; no effect on homotetramer formation)"
FT                   /evidence="ECO:0000269|PubMed:20506325"
FT                   /id="VAR_008077"
FT   VARIANT         307
FT                   /note="G -> S (in CBSD; moderate to severe form; linked
FT                   with D-534; common mutation; loss of cystathionine beta-
FT                   synthase activity; impaired stimulation by AdoMet and
FT                   AdoHcy; no effect on homotetramer formation;
FT                   dbSNP:rs121964962)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:14635102, ECO:0000269|PubMed:20506325,
FT                   ECO:0000269|PubMed:7506602, ECO:0000269|PubMed:8528202,
FT                   ECO:0000269|PubMed:9266356, ECO:0000269|PubMed:9361025,
FT                   ECO:0000269|PubMed:9889017"
FT                   /id="VAR_002186"
FT   VARIANT         320
FT                   /note="V -> A (in CBSD; has 36% of wild-type enzyme
FT                   activity; dbSNP:rs781567152)"
FT                   /evidence="ECO:0000269|PubMed:14635102,
FT                   ECO:0000269|PubMed:9361025"
FT                   /id="VAR_008078"
FT   VARIANT         321
FT                   /note="D -> V (in CBSD; loss of activity)"
FT                   /evidence="ECO:0000269|PubMed:21520339"
FT                   /id="VAR_066102"
FT   VARIANT         331
FT                   /note="A -> E (in CBSD; dbSNP:rs777919630)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:9156316"
FT                   /id="VAR_008079"
FT   VARIANT         331
FT                   /note="A -> V (in CBSD; dbSNP:rs777919630)"
FT                   /evidence="ECO:0000269|PubMed:8528202"
FT                   /id="VAR_002187"
FT   VARIANT         336
FT                   /note="R -> C (in CBSD; protein expression is comparable to
FT                   wild-type; loss of activity; absent capacity to form
FT                   multimeric quaternary structure; dbSNP:rs398123151)"
FT                   /evidence="ECO:0000269|PubMed:10408774,
FT                   ECO:0000269|PubMed:12124992, ECO:0000269|PubMed:12815602,
FT                   ECO:0000269|PubMed:16205833, ECO:0000269|PubMed:16429402,
FT                   ECO:0000269|PubMed:21240075"
FT                   /id="VAR_002188"
FT   VARIANT         336
FT                   /note="R -> H (in CBSD; mild form; no effect on expression;
FT                   exhibits an activity lower than 4% of the wild-type enzyme;
FT                   altered stimulation by AdoMet; absent capacity to form
FT                   multimeric quaternary structure; dbSNP:rs760417941)"
FT                   /evidence="ECO:0000269|PubMed:16429402,
FT                   ECO:0000269|PubMed:23974653"
FT                   /id="VAR_008080"
FT   VARIANT         338
FT                   /note="L -> P (in CBSD; severe form; exhibits an activity
FT                   lower than 4% of the wild-type enzyme; absent capacity to
FT                   form multimeric quaternary structure)"
FT                   /evidence="ECO:0000269|PubMed:12815602,
FT                   ECO:0000269|PubMed:16429402"
FT                   /id="VAR_021797"
FT   VARIANT         347
FT                   /note="G -> S (in CBSD; protein expression is comparable to
FT                   wild-type; loss of activity; dbSNP:rs771298943)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:16205833"
FT                   /id="VAR_021798"
FT   VARIANT         349
FT                   /note="S -> N (in CBSD; severe form; exhibits an activity
FT                   lower than 4% of the wild-type enzyme; absent capacity to
FT                   form multimeric quaternary structure)"
FT                   /evidence="ECO:0000269|PubMed:12815602,
FT                   ECO:0000269|PubMed:16429402"
FT                   /id="VAR_021799"
FT   VARIANT         352
FT                   /note="S -> N (in CBSD)"
FT                   /id="VAR_008081"
FT   VARIANT         353
FT                   /note="T -> M (in CBSD; protein expression is comparable to
FT                   wild-type; significant decrease of enzyme activity;
FT                   dbSNP:rs121964972)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:14635102, ECO:0000269|PubMed:16205833,
FT                   ECO:0000269|PubMed:9156316"
FT                   /id="VAR_008082"
FT   VARIANT         354
FT                   /note="V -> M (in CBSD; dbSNP:rs267606146)"
FT                   /id="VAR_008083"
FT   VARIANT         355
FT                   /note="A -> P (in CBSD; dbSNP:rs1192581453)"
FT                   /evidence="ECO:0000269|PubMed:9889017"
FT                   /id="VAR_021800"
FT   VARIANT         361
FT                   /note="A -> T (in CBSD; dbSNP:rs745764562)"
FT                   /evidence="ECO:0000269|PubMed:11553052"
FT                   /id="VAR_046934"
FT   VARIANT         369
FT                   /note="R -> C (in CBSD; when linked with C-491 severe form;
FT                   decreased cystathionine beta-synthase activity; decreased
FT                   homotetramer formation; dbSNP:rs117687681)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:9361025"
FT                   /id="VAR_008084"
FT   VARIANT         369
FT                   /note="R -> H (in CBSD; dbSNP:rs11700812)"
FT                   /id="VAR_002189"
FT   VARIANT         370
FT                   /note="C -> Y (in CBSD; dbSNP:rs757920190)"
FT                   /evidence="ECO:0000269|PubMed:10462600"
FT                   /id="VAR_008085"
FT   VARIANT         371
FT                   /note="V -> M (in CBSD; dbSNP:rs372010465)"
FT                   /evidence="ECO:0000269|PubMed:12124992,
FT                   ECO:0000269|PubMed:7635485"
FT                   /id="VAR_002190"
FT   VARIANT         376
FT                   /note="D -> N (in CBSD; has significantly decreased levels
FT                   of enzyme activity; dbSNP:rs1170128038)"
FT                   /evidence="ECO:0000269|PubMed:14635102"
FT                   /id="VAR_046935"
FT   VARIANT         379
FT                   /note="R -> Q (in CBSD; exhibits an activity lower than 4%
FT                   of the wild-type enzyme; absent capacity to form multimeric
FT                   quaternary structure; dbSNP:rs763036586)"
FT                   /evidence="ECO:0000269|PubMed:12815602,
FT                   ECO:0000269|PubMed:16429402"
FT                   /id="VAR_021801"
FT   VARIANT         379
FT                   /note="R -> W (in CBSD; dbSNP:rs769080151)"
FT                   /evidence="ECO:0000269|PubMed:15365998"
FT                   /id="VAR_046936"
FT   VARIANT         384
FT                   /note="K -> E (in CBSD; severe form; dbSNP:rs121964967)"
FT                   /evidence="ECO:0000269|PubMed:8990018"
FT                   /id="VAR_002191"
FT   VARIANT         384
FT                   /note="K -> N (in CBSD; moderate form)"
FT                   /id="VAR_008086"
FT   VARIANT         391
FT                   /note="M -> I (in CBSD)"
FT                   /id="VAR_008087"
FT   VARIANT         422
FT                   /note="P -> L (in CBSD; changed cystathionine beta-synthase
FT                   activity; impaired stimulation by AdoMet; does not affect
FT                   homotetramer formation; dbSNP:rs28934892)"
FT                   /evidence="ECO:0000269|PubMed:12007221,
FT                   ECO:0000269|PubMed:20506325"
FT                   /id="VAR_021802"
FT   VARIANT         427
FT                   /note="P -> L (in CBSD; no effect on cystathionine beta-
FT                   synthase activity; altered stimulation by AdoMet;
FT                   dbSNP:rs863223434)"
FT                   /evidence="ECO:0000269|PubMed:23974653,
FT                   ECO:0000269|PubMed:25044645"
FT                   /id="VAR_074592"
FT   VARIANT         434
FT                   /note="T -> N (in CBSD; dbSNP:rs1555872506)"
FT                   /id="VAR_008088"
FT   VARIANT         435
FT                   /note="I -> T (in CBSD; no effect on cystathionine beta-
FT                   synthase activity; impaired stimulation by AdoMet and
FT                   AdoHcy; does not affect homotetramer formation)"
FT                   /evidence="ECO:0000269|PubMed:12007221,
FT                   ECO:0000269|PubMed:20506325"
FT                   /id="VAR_008089"
FT   VARIANT         439
FT                   /note="R -> Q (in CBSD; no effect on cystathionine beta-
FT                   synthase activity; increased homotetramer formation;
FT                   dbSNP:rs756467921)"
FT                   /evidence="ECO:0000269|PubMed:10462600,
FT                   ECO:0000269|PubMed:12124992, ECO:0000269|PubMed:20506325,
FT                   ECO:0000269|PubMed:9156316"
FT                   /id="VAR_008090"
FT   VARIANT         444
FT                   /note="D -> N (in CBSD; decreased expression; no effect on
FT                   cystathionine beta-synthase activity; altered stimulation
FT                   by AdoMet; increased homotetramer formation;
FT                   dbSNP:rs28934891)"
FT                   /evidence="ECO:0000269|PubMed:12007221,
FT                   ECO:0000269|PubMed:20506325, ECO:0000269|PubMed:23974653,
FT                   ECO:0000269|PubMed:25044645, ECO:0000269|PubMed:8755636"
FT                   /id="VAR_002192"
FT   VARIANT         446
FT                   /note="A -> S (in CBSD)"
FT                   /evidence="ECO:0000269|PubMed:21520339"
FT                   /id="VAR_066103"
FT   VARIANT         449
FT                   /note="V -> G (in CBSD; no effect on cystathionine beta-
FT                   synthase activity; altered stimulation by AdoMet)"
FT                   /evidence="ECO:0000269|PubMed:25044645"
FT                   /id="VAR_074593"
FT   VARIANT         454
FT                   /note="V -> E (in CBSD)"
FT                   /evidence="ECO:0000269|PubMed:8528202"
FT                   /id="VAR_002193"
FT   VARIANT         456
FT                   /note="L -> P (in CBSD; severe; exhibits an activity lower
FT                   than 4% of the wild-type enzyme; absent capacity to form
FT                   multimeric quaternary structure)"
FT                   /evidence="ECO:0000269|PubMed:12815602,
FT                   ECO:0000269|PubMed:16429402"
FT                   /id="VAR_021803"
FT   VARIANT         466
FT                   /note="S -> L (in CBSD; increased cystathionine beta-
FT                   synthase activity; impaired stimulation by AdoMet and
FT                   AdoHcy; decreased homotetramer formation;
FT                   dbSNP:rs121964971)"
FT                   /evidence="ECO:0000269|PubMed:12007221,
FT                   ECO:0000269|PubMed:20506325"
FT                   /id="VAR_008091"
FT   VARIANT         491
FT                   /note="R -> C (in CBSD; linked with C-369;
FT                   dbSNP:rs1339830457)"
FT                   /id="VAR_008092"
FT   VARIANT         500
FT                   /note="S -> L (in CBSD; no effect on cystathionine beta-
FT                   synthase activity; altered stimulation by AdoMet;
FT                   dbSNP:rs755106884)"
FT                   /evidence="ECO:0000269|PubMed:23974653,
FT                   ECO:0000269|PubMed:25044645"
FT                   /id="VAR_074594"
FT   VARIANT         526
FT                   /note="Q -> K (in CBSD; has significantly decreased levels
FT                   of enzyme activity)"
FT                   /evidence="ECO:0000269|PubMed:14635102"
FT                   /id="VAR_046937"
FT   VARIANT         534
FT                   /note="V -> D (in CBSD; linked with S-307)"
FT                   /id="VAR_008093"
FT   VARIANT         539
FT                   /note="L -> S (in CBSD; loss of cystathionine beta-synthase
FT                   activity; impaired stimulation by AdoMet and AdoHcy; loss
FT                   of homotetramer formation; dbSNP:rs121964968)"
FT                   /evidence="ECO:0000269|PubMed:20506325,
FT                   ECO:0000269|PubMed:8990018"
FT                   /id="VAR_002194"
FT   VARIANT         540
FT                   /note="L -> Q (in CBSD; no effect on cystathionine beta-
FT                   synthase activity; altered stimulation by AdoMet)"
FT                   /evidence="ECO:0000269|PubMed:23974653,
FT                   ECO:0000269|PubMed:25044645"
FT                   /id="VAR_074595"
FT   VARIANT         548
FT                   /note="R -> Q (presents 60% of the wild-type activity;
FT                   highly reduced capacity to form multimeric quaternary
FT                   structure; dbSNP:rs150828989)"
FT                   /evidence="ECO:0000269|PubMed:16429402"
FT                   /id="VAR_046938"
FT   MUTAGEN         272
FT                   /note="C->A: Reduced heme content and cystathionine beta-
FT                   synthase activity."
FT                   /evidence="ECO:0000269|PubMed:12173932"
FT   MUTAGEN         275
FT                   /note="C->S: Reduced heme content and cystathionine beta-
FT                   synthase activity."
FT                   /evidence="ECO:0000269|PubMed:12173932"
FT   CONFLICT        58
FT                   /note="R -> P (in Ref. 4; CAA61252)"
FT                   /evidence="ECO:0000305"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          75..79
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           80..82
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          83..85
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          89..91
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           95..98
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          103..109
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           110..112
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          113..117
FT                   /evidence="ECO:0007829|PDB:4L0D"
FT   HELIX           119..132
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          141..145
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           149..161
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          164..170
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           175..183
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          187..191
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:5MMS"
FT   STRAND          197..199
FT                   /evidence="ECO:0007829|PDB:4L27"
FT   HELIX           203..213
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          217..219
FT                   /evidence="ECO:0007829|PDB:4L28"
FT   TURN            222..224
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           227..234
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           236..243
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   TURN            244..246
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          249..254
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          256..258
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           259..271
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          272..274
FT                   /evidence="ECO:0007829|PDB:1M54"
FT   STRAND          276..282
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          288..290
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           291..294
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           317..319
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          322..326
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           328..342
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           348..360
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           361..363
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   STRAND          369..374
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           378..381
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   TURN            382..386
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           388..393
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   HELIX           399..404
FT                   /evidence="ECO:0007829|PDB:4COO"
FT   TURN            408..411
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   HELIX           414..417
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   HELIX           431..441
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   STRAND          444..449
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   STRAND          455..460
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   HELIX           461..469
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   HELIX           479..482
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   STRAND          489..491
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   HELIX           496..505
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   STRAND          509..515
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   STRAND          526..534
FT                   /evidence="ECO:0007829|PDB:4UUU"
FT   HELIX           536..544
FT                   /evidence="ECO:0007829|PDB:4UUU"
SQ   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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