Search Results
Overview
| Uniprot ID | P35520 |
|---|---|
| Protein Name | Cystathionine beta-synthase |
| Gene Name | CBS |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 25 | RSGPHSAKGSLEKGS |
| 30 | SAKGSLEKGSPEDKE |
Function
Hydro-lyase catalyzing the first step of the transsulfuration pathway, where the hydroxyl group of L-serine is displaced by L-homocysteine in a beta-replacement reaction to form L-cystathionine, the precursor of L-cysteine. This catabolic route allows the elimination of L-methionine and the toxic metabolite L-homocysteine (PubMed:20506325, PubMed:23974653, PubMed:23981774). Also involved in the production of hydrogen sulfide, a gasotransmitter with signaling and cytoprotective effects on neurons (By similarity)
Protein Sequence
10
MPSETPQAEV
20
GPTGCPHRSG
30
PHSAKGSLEK
40
GSPEDKEAKE
50
PLWIRPDAPS
60
RCTWQLGRPA
70
SESPHHHTAP
80
AKSPKILPDI
90
LKKIGDTPMV
100
RINKIGKKFG
110
LKCELLAKCE
120
FFNAGGSVKD
130
RISLRMIEDA
140
ERDGTLKPGD
150
TIIEPTSGNT
160
GIGLALAAAV
170
RGYRCIIVMP
180
EKMSSEKVDV
190
LRALGAEIVR
200
TPTNARFDSP
210
ESHVGVAWRL
220
KNEIPNSHIL
230
DQYRNASNPL
240
AHYDTTADEI
250
LQQCDGKLDM
260
LVASVGTGGT
270
ITGIARKLKE
280
KCPGCRIIGV
290
DPEGSILAEP
300
EELNQTEQTT
310
YEVEGIGYDF
320
IPTVLDRTVV
330
DKWFKSNDEE
340
AFTFARMLIA
350
QEGLLCGGSA
360
GSTVAVAVKA
370
AQELQEGQRC
380
VVILPDSVRN
390
YMTKFLSDRW
400
MLQKGFLKEE
410
DLTEKKPWWW
420
HLRVQELGLS
430
APLTVLPTIT
440
CGHTIEILRE
450
KGFDQAPVVD
460
EAGVILGMVT
470
LGNMLSSLLA
480
GKVQPSDQVG
490
KVIYKQFKQI
500
RLTDTLGRLS
510
HILEMDHFAL
520
VVHEQIQYHS
530
TGKSSQRQMV
540
FGVVTAIDLL
550
NFVAAQERDQ
K
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0070025 | carbon monoxide binding |
| Molecular Function | GO:0004122 | cystathionine beta-synthase activity |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0020037 | heme binding |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0072341 | modified amino acid binding |
| Molecular Function | GO:0070026 | nitric oxide binding |
| Molecular Function | GO:0050421 | nitrite reductase (NO-forming) activity |
| Molecular Function | GO:0019825 | oxygen binding |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0030170 | pyridoxal phosphate binding |
| Molecular Function | GO:1904047 | S-adenosyl-L-methionine binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0071456 | cellular response to hypoxia |
| Biological Process | GO:0042262 | DNA protection |
| Biological Process | GO:0043418 | homocysteine catabolic process |
| Biological Process | GO:0050667 | homocysteine metabolic process |
| Biological Process | GO:0070814 | hydrogen sulfide biosynthetic process |
| Biological Process | GO:0019344 | L-cysteine biosynthetic process |
| Biological Process | GO:0006535 | L-cysteine biosynthetic process from L-serine |
| Biological Process | GO:0019343 | L-cysteine biosynthetic process via L-cystathionine |
| Biological Process | GO:0019448 | L-cysteine catabolic process |
| Biological Process | GO:0006565 | L-serine catabolic process |
| Biological Process | GO:0006563 | L-serine metabolic process |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:0031667 | response to nutrient levels |
| Biological Process | GO:0019346 | transsulfuration |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.