CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018521
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cystathionine beta-synthase 
Protein Synonyms/Alias
 Beta-thionase; Serine sulfhydrase 
Gene Name
 Cbs 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
25HLDMHSEKRQLEKGPubiquitination[1]
30SEKRQLEKGPSGDKDubiquitination[1]
69HYHTVLTKSPKILPDubiquitination[1]
72TVLTKSPKILPDILRubiquitination[1]
80ILPDILRKIGNTPMVubiquitination[1]
116FNAGGSVKDRISLRMubiquitination[1]
134AERAGNLKPGDTIIEubiquitination[1]
158LALAAAVKGYRCIIVubiquitination[1]
169CIIVMPEKMSMEKVDubiquitination[1]
174PEKMSMEKVDVLRALubiquitination[1]
208VGVAWRLKNEIPNSHubiquitination[1]
319LDRAVVDKWFKSNDEubiquitination[1]
322AVVDKWFKSNDEDSFubiquitination[1]
381SVRNYMSKFLSDKWMubiquitination[1]
386MSKFLSDKWMLQKGFubiquitination[1]
391SDKWMLQKGFMKEELubiquitination[1]
395MLQKGFMKEELSVKRubiquitination[1]
401MKEELSVKRPWWWRLubiquitination[1]
477RPSDEVCKVLYKQFKacetylation[2]
477RPSDEVCKVLYKQFKubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] Calorie restriction and SIRT3 trigger global reprogramming of the mitochondrial protein acetylome.
 Hebert AS, Dittenhafer-Reed KE, Yu W, Bailey DJ, Selen ES, Boersma MD, Carson JJ, Tonelli M, Balloon AJ, Higbee AJ, Westphall MS, Pagliarini DJ, Prolla TA, Assadi-Porter F, Roy S, Denu JM, Coon JJ.
 Mol Cell. 2013 Jan 10;49(1):186-99. [PMID: 23201123] 
Functional Description
 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). 
Sequence Annotation
 DOMAIN 414 474 CBS.
 REGION 253 257 Pyridoxal phosphate binding (By
 METAL 49 49 Iron (heme axial ligand) (By similarity).
 METAL 62 62 Iron (heme axial ligand) (By similarity).
 BINDING 146 146 Pyridoxal phosphate (By similarity).
 BINDING 346 346 Pyridoxal phosphate (By similarity).
 MOD_RES 116 116 N6-(pyridoxal phosphate)lysine (By
 CROSSLNK 208 208 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 Alternative splicing; Amino-acid biosynthesis; CBS domain; Complete proteome; Cysteine biosynthesis; Cytoplasm; Heme; Iron; Isopeptide bond; Lyase; Metal-binding; Nucleus; Pyridoxal phosphate; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 561 AA 
Protein Sequence
MPSGTSQCED GSAGGFQHLD MHSEKRQLEK GPSGDKDRVW IRPDTPSRCT WQLGRAMADS 60
PHYHTVLTKS PKILPDILRK IGNTPMVRIN KISKNAGLKC ELLAKCEFFN AGGSVKDRIS 120
LRMIEDAERA GNLKPGDTII EPTSGNTGIG LALAAAVKGY RCIIVMPEKM SMEKVDVLRA 180
LGAEIVRTPT NARFDSPESH VGVAWRLKNE IPNSHILDQY RNASNPLAHY DDTAEEILQQ 240
CDGKLDMLVA SAGTGGTITG IARKLKEKCP GCKIIGVDPE GSILAEPEEL NQTEQTAYEV 300
EGIGYDFIPT VLDRAVVDKW FKSNDEDSFA FARMLIAQEG LLCGGSSGSA MAVAVKAARE 360
LQEGQRCVVI LPDSVRNYMS KFLSDKWMLQ KGFMKEELSV KRPWWWRLRV QELSLSAPLT 420
VLPTVTCEDT IAILREKGFD QAPVVNESGA ILGMVTLGNM LSSLLAGKVR PSDEVCKVLY 480
KQFKPIHLTD TLGTLSHILE MDHFALVVHE QIQSRDQAWS GVVGGPTDCS NGMSSKQQMV 540
FGVVTAIDLL NFVAAREQTQ T 561 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005730; C:nucleolus; IEA:Compara.
 GO:0004122; F:cystathionine beta-synthase activity; IMP:MGI.
 GO:0020037; F:heme binding; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0072341; F:modified amino acid binding; IEA:Compara.
 GO:0030170; F:pyridoxal phosphate binding; IEA:Compara.
 GO:0001974; P:blood vessel remodeling; IMP:MGI.
 GO:0060351; P:cartilage development involved in endochondral bone morphogenesis; IMP:MGI.
 GO:0071456; P:cellular response to hypoxia; IEA:Compara.
 GO:0021587; P:cerebellum morphogenesis; IMP:MGI.
 GO:0019344; P:cysteine biosynthetic process; IMP:MGI.
 GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
 GO:0019343; P:cysteine biosynthetic process via cystathionine; IEA:InterPro.
 GO:0001958; P:endochondral ossification; IMP:MGI.
 GO:0043418; P:homocysteine catabolic process; IEA:Compara.
 GO:0050667; P:homocysteine metabolic process; IMP:MGI.
 GO:0070814; P:hydrogen sulfide biosynthetic process; ISS:UniProtKB.
 GO:0019448; P:L-cysteine catabolic process; IEA:Compara.
 GO:0006565; P:L-serine catabolic process; IEA:Compara.
 GO:0060135; P:maternal process involved in female pregnancy; IMP:MGI.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0050880; P:regulation of blood vessel size; IMP:MGI.
 GO:0030823; P:regulation of cGMP metabolic process; IMP:MGI.
 GO:0043506; P:regulation of JUN kinase activity; IMP:MGI.
 GO:0051593; P:response to folic acid; IMP:MGI.
 GO:0006801; P:superoxide metabolic process; IMP:MGI.
 GO:0019346; P:transsulfuration; IEA:Compara. 
Interpro
 IPR001216; Cys_synth_BS.
 IPR005857; Cysta_beta_synth.
 IPR000644; Cysta_beta_synth_core.
 IPR001926; Trp_syn_b_sub_like_PLP_eny_SF. 
Pfam
 PF00571; CBS
 PF00291; PALP 
SMART
 SM00116; CBS 
PROSITE
 PS51371; CBS
 PS00901; CYS_SYNTHASE 
PRINTS