Reviewed, UniProtKB/Swiss-Prot Q91WT9 (CBS_MOUSE)

Names and origin

Protein names

Recommended name:
    Cystathionine beta-synthase
    EC=4.2.1.22
Alternative name(s):
    Serine sulfhydrase
    Beta-thionase

Gene names

Name:

Cbs

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	561 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	L-serine + L-homocysteine = L-cystathionine + H2O.
Cofactor	Pyridoxal phosphate By similarity.
Pathway	Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine from L-homocysteine and L-serine: step 1/2.
Subunit structure	Homotetramer By similarity.
Subcellular location	Nucleus By similarity. Cytoplasm By similarity.
Post-translational modification	Binds covalently to a heme group through a thiolate ligand By similarity.
Sequence similarities	Belongs to the cysteine synthase/cystathionine beta-synthase family. Contains 1 CBS domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Cysteine biosynthesis
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Domain	CBS domain
Ligand	Heme Iron Metal-binding Pyridoxal phosphate
Molecular function	Lyase
PTM	Isopeptide bond Ubl conjugation
Gene Ontology (GO)
Biological process	cysteine biosynthetic process from serine Inferred from electronic annotation. Source: InterPro cysteine biosynthetic process via cystathionine Inferred from electronic annotation. Source: InterPro endochondral ossification Inferred from mutant phenotype. Source: MGI homocysteine metabolic process Inferred from mutant phenotype. Source: MGI regulation of JUN kinase activity Inferred from mutant phenotype. Source: MGI response to folic acid Inferred from mutant phenotype. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	cystathionine beta-synthase activity Inferred from mutant phenotype. Source: MGI iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q91WT9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q91WT9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     514-528: SRDQAWSGVVGGPTD → Y

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 561	560	Cystathionine beta-synthase		PRO_0000262592
Regions
	Domain	414 – 474	61	CBS
	Region	253 – 257	5	Pyridoxal phosphate binding By similarity
Sites
	Metal binding	49	1	Iron (heme axial ligand) By similarity
	Metal binding	62	1	Iron (heme axial ligand) By similarity
	Binding site	146	1	Pyridoxal phosphate By similarity
	Binding site	346	1	Pyridoxal phosphate By similarity
Amino acid modifications
	Modified residue	116	1	N6-(pyridoxal phosphate)lysine By similarity
	Cross-link	208		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	514 – 528	15	SRDQA…GGPTD → Y in isoform 2.		VSP_021790

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 072CF81AFE10372E	FASTA	561	61,544
	10 20 30 40 50 60 MPSGTSQCED GSAGGFQHLD MHSEKRQLEK GPSGDKDRVW IRPDTPSRCT WQLGRAMADS 70 80 90 100 110 120 PHYHTVLTKS PKILPDILRK IGNTPMVRIN KISKNAGLKC ELLAKCEFFN AGGSVKDRIS 130 140 150 160 170 180 LRMIEDAERA GNLKPGDTII EPTSGNTGIG LALAAAVKGY RCIIVMPEKM SMEKVDVLRA 190 200 210 220 230 240 LGAEIVRTPT NARFDSPESH VGVAWRLKNE IPNSHILDQY RNASNPLAHY DDTAEEILQQ 250 260 270 280 290 300 CDGKLDMLVA SAGTGGTITG IARKLKEKCP GCKIIGVDPE GSILAEPEEL NQTEQTAYEV 310 320 330 340 350 360 EGIGYDFIPT VLDRAVVDKW FKSNDEDSFA FARMLIAQEG LLCGGSSGSA MAVAVKAARE 370 380 390 400 410 420 LQEGQRCVVI LPDSVRNYMS KFLSDKWMLQ KGFMKEELSV KRPWWWRLRV QELSLSAPLT 430 440 450 460 470 480 VLPTVTCEDT IAILREKGFD QAPVVNESGA ILGMVTLGNM LSSLLAGKVR PSDEVCKVLY 490 500 510 520 530 540 KQFKPIHLTD TLGTLSHILE MDHFALVVHE QIQSRDQAWS GVVGGPTDCS NGMSSKQQMV 550 560 FGVVTAIDLL NFVAAREQTQ T
	Isoform 2. Checksum: 5DC0F6E3DAED8461	FASTA	547	60,193
	10 20 30 40 50 60 MPSGTSQCED GSAGGFQHLD MHSEKRQLEK GPSGDKDRVW IRPDTPSRCT WQLGRAMADS 70 80 90 100 110 120 PHYHTVLTKS PKILPDILRK IGNTPMVRIN KISKNAGLKC ELLAKCEFFN AGGSVKDRIS 130 140 150 160 170 180 LRMIEDAERA GNLKPGDTII EPTSGNTGIG LALAAAVKGY RCIIVMPEKM SMEKVDVLRA 190 200 210 220 230 240 LGAEIVRTPT NARFDSPESH VGVAWRLKNE IPNSHILDQY RNASNPLAHY DDTAEEILQQ 250 260 270 280 290 300 CDGKLDMLVA SAGTGGTITG IARKLKEKCP GCKIIGVDPE GSILAEPEEL NQTEQTAYEV 310 320 330 340 350 360 EGIGYDFIPT VLDRAVVDKW FKSNDEDSFA FARMLIAQEG LLCGGSSGSA MAVAVKAARE 370 380 390 400 410 420 LQEGQRCVVI LPDSVRNYMS KFLSDKWMLQ KGFMKEELSV KRPWWWRLRV QELSLSAPLT 430 440 450 460 470 480 VLPTVTCEDT IAILREKGFD QAPVVNESGA ILGMVTLGNM LSSLLAGKVR PSDEVCKVLY 490 500 510 520 530 540 KQFKPIHLTD TLGTLSHILE MDHFALVVHE QIQYCSNGMS SKQQMVFGVV TAIDLLNFVA AREQTQT

References

[1]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Strain: C57BL/6J.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK077669 mRNA. Translation: BAC36943.1. BC013472 mRNA. Translation: AAH13472.1. BC013480 mRNA. Translation: AAH13480.1. BC026595 mRNA. Translation: AAH26595.1.
IPI	IPI00128378. IPI00269811.
RefSeq	NP_659104.1. NP_835742.1.
UniGene	Mm.206417
3D structure databases
HSSP	HSSP built from PDB template 1M54 based on UniProtKB P35520.
SMR	Q91WT9. Positions 40-396.
ModBase	Search...
Protein-protein interaction databases
STRING	Q91WT9.
Proteomic databases
PRIDE	Q91WT9.
Genome annotation databases
Ensembl	ENSMUST00000067801; ENSMUSP00000066878; ENSMUSG00000024039; Mus musculus. [Genome view] ENSMUST00000078509; ENSMUSP00000077597; ENSMUSG00000024039; Mus musculus. [Genome view]
GeneID	12411.
KEGG	mmu:12411.
NMPDR	fig|10090.3.peg.2592.
UCSC	uc008bvl.1. mouse. uc008bvm.1. mouse.
Organism-specific databases
CTD	12411.
MGI	MGI:88285. Cbs.
Phylogenomic databases
HOVERGEN	Q91WT9.
OMA	FLSDRWM.
Enzyme and pathway databases
BRENDA	4.2.1.22. 244.
Gene expression databases
ArrayExpress	Q91WT9.
Bgee	Q91WT9.
CleanEx	MM_CBS.
Genevestigator	Q91WT9.
GermOnline	ENSMUSG00000024039. Mus musculus.
Family and domain databases
InterPro	IPR001216. Cys_synth_BS. IPR005857. Cysta_beta_synth. IPR000644. Cysta_beta_synth_core. IPR001926. PyrdxlP-dep_enz_bsu. [Graphical view]
Pfam	PF00571. CBS. 1 hit. PF00291. PALP. 1 hit. [Graphical view]
SMART	SM00116. CBS. 1 hit. [Graphical view]
TIGRFAMs	TIGR01137. cysta_beta. 1 hit.
PROSITE	PS51371. CBS. 1 hit. PS00901. CYS_SYNTHASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	281194.
SOURCE	Search...

Entry information

Entry name

CBS_MOUSE

Accession

Primary (citable) accession number: Q91WT9
Secondary accession number(s): Q91WU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	January 23, 2007
Last modified:	November 3, 2009
This is version 59 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)