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Q91WT9

- CBS_MOUSE

UniProt

Q91WT9 - CBS_MOUSE

Protein

Cystathionine beta-synthase

Gene

Cbs

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    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.By similarity

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi49 – 491Iron (heme axial ligand)By similarity
    Metal bindingi62 – 621Iron (heme axial ligand)By similarity
    Binding sitei146 – 1461Pyridoxal phosphateBy similarity
    Binding sitei346 – 3461Pyridoxal phosphateBy similarity

    GO - Molecular functioni

    1. adenyl nucleotide binding Source: InterPro
    2. cystathionine beta-synthase activity Source: MGI
    3. heme binding Source: Ensembl
    4. metal ion binding Source: UniProtKB-KW
    5. modified amino acid binding Source: Ensembl
    6. pyridoxal phosphate binding Source: Ensembl

    GO - Biological processi

    1. blood vessel remodeling Source: MGI
    2. cartilage development involved in endochondral bone morphogenesis Source: MGI
    3. cellular response to hypoxia Source: Ensembl
    4. cerebellum morphogenesis Source: MGI
    5. cysteine biosynthetic process Source: MGI
    6. cysteine biosynthetic process from serine Source: InterPro
    7. cysteine biosynthetic process via cystathionine Source: InterPro
    8. endochondral ossification Source: MGI
    9. homocysteine catabolic process Source: Ensembl
    10. homocysteine metabolic process Source: MGI
    11. hydrogen sulfide biosynthetic process Source: UniProtKB
    12. L-cysteine catabolic process Source: Ensembl
    13. L-serine catabolic process Source: Ensembl
    14. maternal process involved in female pregnancy Source: MGI
    15. negative regulation of apoptotic process Source: Ensembl
    16. regulation of blood vessel size Source: MGI
    17. regulation of cGMP metabolic process Source: MGI
    18. regulation of JUN kinase activity Source: MGI
    19. response to folic acid Source: MGI
    20. superoxide metabolic process Source: MGI
    21. transsulfuration Source: Ensembl

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Cysteine biosynthesis

    Keywords - Ligandi

    Heme, Iron, Metal-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    ReactomeiREACT_198986. Cysteine formation from homocysteine.
    UniPathwayiUPA00136; UER00201.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cystathionine beta-synthase (EC:4.2.1.22)
    Alternative name(s):
    Beta-thionase
    Serine sulfhydrase
    Gene namesi
    Name:Cbs
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 17

    Organism-specific databases

    MGIiMGI:88285. Cbs.

    Subcellular locationi

    Nucleus By similarity. Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. nucleolus Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 561560Cystathionine beta-synthasePRO_0000262592Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei116 – 1161N6-(pyridoxal phosphate)lysineBy similarity
    Cross-linki208 – 208Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

    Post-translational modificationi

    Binds covalently to a heme group through a thiolate ligand.By similarity

    Keywords - PTMi

    Isopeptide bond, Ubl conjugation

    Proteomic databases

    MaxQBiQ91WT9.
    PaxDbiQ91WT9.
    PRIDEiQ91WT9.

    PTM databases

    PhosphoSiteiQ91WT9.

    Expressioni

    Gene expression databases

    ArrayExpressiQ91WT9.
    BgeeiQ91WT9.
    CleanExiMM_CBS.
    GenevestigatoriQ91WT9.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    DIPiDIP-60823N.
    IntActiQ91WT9. 1 interaction.
    MINTiMINT-4121506.
    STRINGi10090.ENSMUSP00000066878.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91WT9.
    SMRiQ91WT9. Positions 40-558.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini414 – 47461CBSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni253 – 2575Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Contains 1 CBS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    CBS domain

    Phylogenomic databases

    eggNOGiCOG0031.
    GeneTreeiENSGT00510000047027.
    HOGENOMiHOG000217392.
    HOVERGENiHBG000918.
    InParanoidiQ91WT9.
    KOiK01697.
    OMAiEEIWTQT.
    OrthoDBiEOG7J70F1.
    PhylomeDBiQ91WT9.
    TreeFamiTF300784.

    Family and domain databases

    InterProiIPR000644. CBS_dom.
    IPR005857. Cysta_beta_synth.
    IPR001216. P-phosphate_BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view]
    PfamiPF00571. CBS. 1 hit.
    PF00291. PALP. 1 hit.
    [Graphical view]
    SMARTiSM00116. CBS. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    TIGRFAMsiTIGR01137. cysta_beta. 1 hit.
    PROSITEiPS51371. CBS. 1 hit.
    PS00901. CYS_SYNTHASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q91WT9-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MPSGTSQCED GSAGGFQHLD MHSEKRQLEK GPSGDKDRVW IRPDTPSRCT    50
    WQLGRAMADS PHYHTVLTKS PKILPDILRK IGNTPMVRIN KISKNAGLKC 100
    ELLAKCEFFN AGGSVKDRIS LRMIEDAERA GNLKPGDTII EPTSGNTGIG 150
    LALAAAVKGY RCIIVMPEKM SMEKVDVLRA LGAEIVRTPT NARFDSPESH 200
    VGVAWRLKNE IPNSHILDQY RNASNPLAHY DDTAEEILQQ CDGKLDMLVA 250
    SAGTGGTITG IARKLKEKCP GCKIIGVDPE GSILAEPEEL NQTEQTAYEV 300
    EGIGYDFIPT VLDRAVVDKW FKSNDEDSFA FARMLIAQEG LLCGGSSGSA 350
    MAVAVKAARE LQEGQRCVVI LPDSVRNYMS KFLSDKWMLQ KGFMKEELSV 400
    KRPWWWRLRV QELSLSAPLT VLPTVTCEDT IAILREKGFD QAPVVNESGA 450
    ILGMVTLGNM LSSLLAGKVR PSDEVCKVLY KQFKPIHLTD TLGTLSHILE 500
    MDHFALVVHE QIQSRDQAWS GVVGGPTDCS NGMSSKQQMV FGVVTAIDLL 550
    NFVAAREQTQ T 561
    Length:561
    Mass (Da):61,544
    Last modified:January 23, 2007 - v3
    Checksum:i072CF81AFE10372E
    GO
    Isoform 2 (identifier: Q91WT9-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:547
    Mass (Da):60,193
    Checksum:i5DC0F6E3DAED8461
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei514 – 52815SRDQA…GGPTD → Y in isoform 2. 2 PublicationsVSP_021790Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK077669 mRNA. Translation: BAC36943.1.
    BC013472 mRNA. Translation: AAH13472.1.
    BC013480 mRNA. Translation: AAH13480.1.
    BC026595 mRNA. Translation: AAH26595.1.
    CCDSiCCDS28609.1. [Q91WT9-1]
    CCDS28610.1. [Q91WT9-2]
    RefSeqiNP_001258282.1. NM_001271353.1. [Q91WT9-2]
    NP_659104.1. NM_144855.3. [Q91WT9-1]
    NP_835742.1. NM_178224.3. [Q91WT9-2]
    XP_006523612.1. XM_006523549.1. [Q91WT9-1]
    XP_006523613.1. XM_006523550.1. [Q91WT9-1]
    XP_006523614.1. XM_006523551.1. [Q91WT9-1]
    UniGeneiMm.206417.
    Mm.486781.

    Genome annotation databases

    EnsembliENSMUST00000067801; ENSMUSP00000066878; ENSMUSG00000024039. [Q91WT9-1]
    ENSMUST00000078509; ENSMUSP00000077597; ENSMUSG00000024039. [Q91WT9-2]
    ENSMUST00000118504; ENSMUSP00000113209; ENSMUSG00000024039. [Q91WT9-2]
    GeneIDi12411.
    KEGGimmu:12411.
    UCSCiuc008bvl.1. mouse. [Q91WT9-1]
    uc008bvm.1. mouse. [Q91WT9-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK077669 mRNA. Translation: BAC36943.1 .
    BC013472 mRNA. Translation: AAH13472.1 .
    BC013480 mRNA. Translation: AAH13480.1 .
    BC026595 mRNA. Translation: AAH26595.1 .
    CCDSi CCDS28609.1. [Q91WT9-1 ]
    CCDS28610.1. [Q91WT9-2 ]
    RefSeqi NP_001258282.1. NM_001271353.1. [Q91WT9-2 ]
    NP_659104.1. NM_144855.3. [Q91WT9-1 ]
    NP_835742.1. NM_178224.3. [Q91WT9-2 ]
    XP_006523612.1. XM_006523549.1. [Q91WT9-1 ]
    XP_006523613.1. XM_006523550.1. [Q91WT9-1 ]
    XP_006523614.1. XM_006523551.1. [Q91WT9-1 ]
    UniGenei Mm.206417.
    Mm.486781.

    3D structure databases

    ProteinModelPortali Q91WT9.
    SMRi Q91WT9. Positions 40-558.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-60823N.
    IntActi Q91WT9. 1 interaction.
    MINTi MINT-4121506.
    STRINGi 10090.ENSMUSP00000066878.

    PTM databases

    PhosphoSitei Q91WT9.

    Proteomic databases

    MaxQBi Q91WT9.
    PaxDbi Q91WT9.
    PRIDEi Q91WT9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000067801 ; ENSMUSP00000066878 ; ENSMUSG00000024039 . [Q91WT9-1 ]
    ENSMUST00000078509 ; ENSMUSP00000077597 ; ENSMUSG00000024039 . [Q91WT9-2 ]
    ENSMUST00000118504 ; ENSMUSP00000113209 ; ENSMUSG00000024039 . [Q91WT9-2 ]
    GeneIDi 12411.
    KEGGi mmu:12411.
    UCSCi uc008bvl.1. mouse. [Q91WT9-1 ]
    uc008bvm.1. mouse. [Q91WT9-2 ]

    Organism-specific databases

    CTDi 875.
    MGIi MGI:88285. Cbs.

    Phylogenomic databases

    eggNOGi COG0031.
    GeneTreei ENSGT00510000047027.
    HOGENOMi HOG000217392.
    HOVERGENi HBG000918.
    InParanoidi Q91WT9.
    KOi K01697.
    OMAi EEIWTQT.
    OrthoDBi EOG7J70F1.
    PhylomeDBi Q91WT9.
    TreeFami TF300784.

    Enzyme and pathway databases

    UniPathwayi UPA00136 ; UER00201 .
    Reactomei REACT_198986. Cysteine formation from homocysteine.

    Miscellaneous databases

    ChiTaRSi CBS. mouse.
    NextBioi 281194.
    PROi Q91WT9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q91WT9.
    Bgeei Q91WT9.
    CleanExi MM_CBS.
    Genevestigatori Q91WT9.

    Family and domain databases

    InterProi IPR000644. CBS_dom.
    IPR005857. Cysta_beta_synth.
    IPR001216. P-phosphate_BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00571. CBS. 1 hit.
    PF00291. PALP. 1 hit.
    [Graphical view ]
    SMARTi SM00116. CBS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    TIGRFAMsi TIGR01137. cysta_beta. 1 hit.
    PROSITEi PS51371. CBS. 1 hit.
    PS00901. CYS_SYNTHASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [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.

    Entry informationi

    Entry nameiCBS_MOUSE
    AccessioniPrimary (citable) accession number: Q91WT9
    Secondary accession number(s): Q91WU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 105 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3