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Q91WT9 (CBS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cystathionine beta-synthase

EC=4.2.1.22
Alternative name(s):
Beta-thionase
Serine sulfhydrase
Gene names
Name:Cbs
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length561 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Pyridoxal phosphate 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 processAmino-acid biosynthesis
Cysteine biosynthesis
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainCBS domain
   LigandHeme
Iron
Metal-binding
Pyridoxal phosphate
   Molecular functionLyase
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-cysteine catabolic process

Inferred from electronic annotation. Source: Ensembl

L-serine catabolic process

Inferred from electronic annotation. Source: Ensembl

blood vessel remodeling

Inferred from mutant phenotype PubMed 12433838. Source: MGI

cartilage development involved in endochondral bone morphogenesis

Inferred from mutant phenotype PubMed 15622513. Source: MGI

cellular response to hypoxia

Inferred from electronic annotation. Source: Ensembl

cerebellum morphogenesis

Inferred from mutant phenotype PubMed 16160063. Source: MGI

cysteine biosynthetic process

Inferred from mutant phenotype PubMed 15030387. Source: MGI

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 PubMed 15622513. Source: MGI

homocysteine catabolic process

Inferred from electronic annotation. Source: Ensembl

homocysteine metabolic process

Inferred from mutant phenotype PubMed 10953023PubMed 10993757PubMed 15131763PubMed 15555590PubMed 15622513PubMed 15916860PubMed 16226235PubMed 18541157PubMed 7878023. Source: MGI

hydrogen sulfide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

maternal process involved in female pregnancy

Inferred from mutant phenotype PubMed 16984962. Source: MGI

negative regulation of apoptotic process

Inferred from electronic annotation. Source: Ensembl

regulation of JUN kinase activity

Inferred from mutant phenotype PubMed 15030387. Source: MGI

regulation of blood vessel size

Inferred from mutant phenotype PubMed 10953023. Source: MGI

regulation of cGMP metabolic process

Inferred from mutant phenotype PubMed 10953023. Source: MGI

response to folic acid

Inferred from mutant phenotype PubMed 10993757. Source: MGI

superoxide metabolic process

Inferred from mutant phenotype PubMed 10953023. Source: MGI

transsulfuration

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionadenyl nucleotide binding

Inferred from electronic annotation. Source: InterPro

cystathionine beta-synthase activity

Inferred from mutant phenotype PubMed 10953023PubMed 7878023. Source: MGI

heme binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

modified amino acid binding

Inferred from electronic annotation. Source: Ensembl

pyridoxal phosphate binding

Inferred from electronic annotation. Source: Ensembl

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 561560Cystathionine beta-synthase
PRO_0000262592

Regions

Domain414 – 47461CBS
Region253 – 2575Pyridoxal phosphate binding By similarity

Sites

Metal binding491Iron (heme axial ligand) By similarity
Metal binding621Iron (heme axial ligand) By similarity
Binding site1461Pyridoxal phosphate By similarity
Binding site3461Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue1161N6-(pyridoxal phosphate)lysine By similarity
Cross-link208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence514 – 52815SRDQA…GGPTD → Y in isoform 2.
VSP_021790

Sequences

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

Last modified January 23, 2007. Version 3.
Checksum: 072CF81AFE10372E

FASTA56161,544
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5DC0F6E3DAED8461
Show »

FASTA54760,193

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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK077669 mRNA. Translation: BAC36943.1.
BC013472 mRNA. Translation: AAH13472.1.
BC013480 mRNA. Translation: AAH13480.1.
BC026595 mRNA. Translation: AAH26595.1.
RefSeqNP_001258282.1. NM_001271353.1.
NP_659104.1. NM_144855.3.
NP_835742.1. NM_178224.3.
XP_006523612.1. XM_006523549.1.
XP_006523613.1. XM_006523550.1.
XP_006523614.1. XM_006523551.1.
UniGeneMm.206417.
Mm.486781.

3D structure databases

ProteinModelPortalQ91WT9.
SMRQ91WT9. Positions 40-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ91WT9. 1 interaction.
MINTMINT-4121506.
STRING10090.ENSMUSP00000066878.

PTM databases

PhosphoSiteQ91WT9.

Proteomic databases

PaxDbQ91WT9.
PRIDEQ91WT9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000067801; ENSMUSP00000066878; ENSMUSG00000024039. [Q91WT9-1]
ENSMUST00000078509; ENSMUSP00000077597; ENSMUSG00000024039. [Q91WT9-2]
ENSMUST00000118504; ENSMUSP00000113209; ENSMUSG00000024039. [Q91WT9-2]
GeneID12411.
KEGGmmu:12411.
UCSCuc008bvl.1. mouse. [Q91WT9-1]
uc008bvm.1. mouse. [Q91WT9-2]

Organism-specific databases

CTD875.
MGIMGI:88285. Cbs.

Phylogenomic databases

eggNOGCOG0031.
GeneTreeENSGT00510000047027.
HOGENOMHOG000217392.
HOVERGENHBG000918.
InParanoidQ91WT9.
KOK01697.
OMADADSFEM.
OrthoDBEOG7J70F1.
PhylomeDBQ91WT9.
TreeFamTF300784.

Enzyme and pathway databases

UniPathwayUPA00136; UER00201.

Gene expression databases

ArrayExpressQ91WT9.
BgeeQ91WT9.
CleanExMM_CBS.
GenevestigatorQ91WT9.

Family and domain databases

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

Other

ChiTaRSCBS. mouse.
NextBio281194.
PROQ91WT9.
SOURCESearch...

Entry information

Entry nameCBS_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot