dbPTM

CBS_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CBS_HUMAN
UniProt AC	P35520
Protein Name	Cystathionine beta-synthase {ECO:0000305}
Gene Name	CBS
Organism	Homo sapiens (Human).
Sequence Length	551
Subcellular Localization	Cytoplasm . Nucleus .
Protein Description	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: 23981774]
Protein Sequence	MPSETPQAEVGPTGCPHRSGPHSAKGSLEKGSPEDKEAKEPLWIRPDAPSRCTWQLGRPASESPHHHTAPAKSPKILPDILKKIGDTPMVRINKIGKKFGLKCELLAKCEFFNAGGSVKDRISLRMIEDAERDGTLKPGDTIIEPTSGNTGIGLALAAAVRGYRCIIVMPEKMSSEKVDVLRALGAEIVRTPTNARFDSPESHVGVAWRLKNEIPNSHILDQYRNASNPLAHYDTTADEILQQCDGKLDMLVASVGTGGTITGIARKLKEKCPGCRIIGVDPEGSILAEPEELNQTEQTTYEVEGIGYDFIPTVLDRTVVDKWFKSNDEEAFTFARMLIAQEGLLCGGSAGSTVAVAVKAAQELQEGQRCVVILPDSVRNYMTKFLSDRWMLQKGFLKEEDLTEKKPWWWHLRVQELGLSAPLTVLPTITCGHTIEILREKGFDQAPVVDEAGVILGMVTLGNMLSSLLAGKVQPSDQVGKVIYKQFKQIRLTDTLGRLSHILEMDHFALVVHEQIQYHSTGKSSQRQMVFGVVTAIDLLNFVAAQERDQK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MPSETPQAEV -----CCCCCCCCCC	53.45	25627689
5	Phosphorylation	---MPSETPQAEVGP ---CCCCCCCCCCCC	25.66	25159151
15	Glutathionylation	AEVGPTGCPHRSGPH CCCCCCCCCCCCCCC	2.56	22555962
19	Phosphorylation	PTGCPHRSGPHSAKG CCCCCCCCCCCCCCC	54.35	19413330
23	Phosphorylation	PHRSGPHSAKGSLEK CCCCCCCCCCCCCCC	34.51	20068231
27	Phosphorylation	GPHSAKGSLEKGSPE CCCCCCCCCCCCCCC	32.42	20068231
27 (in isoform 2)	Phosphorylation	-	32.42	21406692
32	Phosphorylation	KGSLEKGSPEDKEAK CCCCCCCCCCCCCCC	35.86	29255136
50	Phosphorylation	WIRPDAPSRCTWQLG EECCCCCCCCCEECC	41.53	20873877
61	Phosphorylation	WQLGRPASESPHHHT EECCCCCCCCCCCCC	41.09	20873877
63	Phosphorylation	LGRPASESPHHHTAP CCCCCCCCCCCCCCC	27.34	20873877
68	Phosphorylation	SESPHHHTAPAKSPK CCCCCCCCCCCCCCC	29.94	27732954
72	Ubiquitination	HHHTAPAKSPKILPD CCCCCCCCCCCCHHH	67.25	29901268
73	Phosphorylation	HHTAPAKSPKILPDI CCCCCCCCCCCHHHH	33.27	20873877
75	Ubiquitination	TAPAKSPKILPDILK CCCCCCCCCHHHHHH	65.06	29967540
82	Ubiquitination	KILPDILKKIGDTPM CCHHHHHHHHCCCCC	42.55	29967540
82 (in isoform 2)	Ubiquitination	-	42.55	-
83	Ubiquitination	ILPDILKKIGDTPMV CHHHHHHHHCCCCCE	48.77	29967540
87	Phosphorylation	ILKKIGDTPMVRINK HHHHHCCCCCEEEEC	14.20	24702127
98	Ubiquitination	RINKIGKKFGLKCEL EEECHHHHHCCCHHH	39.18	29967540
102 (in isoform 2)	Ubiquitination	-	26.49	-
102	Ubiquitination	IGKKFGLKCELLAKC HHHHHCCCHHHHHCC	26.49	-
106	Ubiquitination	FGLKCELLAKCEFFN HCCCHHHHHCCCEEC	1.68	29967540
109	S-nitrosylation	KCELLAKCEFFNAGG CHHHHHCCCEECCCC	4.60	24105792
117	Phosphorylation	EFFNAGGSVKDRISL CEECCCCCHHHHEEE	25.69	20068231
119	Ubiquitination	FNAGGSVKDRISLRM ECCCCCHHHHEEEEE	42.88	-
119	N6-(pyridoxal phosphate)lysine	FNAGGSVKDRISLRM ECCCCCHHHHEEEEE	42.88	-
119 (in isoform 2)	Ubiquitination	-	42.88	-
119	Other	FNAGGSVKDRISLRM ECCCCCHHHHEEEEE	42.88	11483494
137 (in isoform 2)	Ubiquitination	-	46.95	-
137	Ubiquitination	AERDGTLKPGDTIIE HHHCCCCCCCCEEEE	46.95	-
165	Glutathionylation	AAVRGYRCIIVMPEK HHHCCCEEEEECCCC	1.55	22555962
177 (in isoform 2)	Ubiquitination	-	45.76	-
177	Ubiquitination	PEKMSSEKVDVLRAL CCCCCHHHHHHHHHH	45.76	-
190	Methylation	ALGAEIVRTPTNARF HHCCCEECCCCCCCC	40.42	-
191	Phosphorylation	LGAEIVRTPTNARFD HCCCEECCCCCCCCC	24.46	21964256
193	Phosphorylation	AEIVRTPTNARFDSP CCEECCCCCCCCCCC	40.68	21964256
199	Phosphorylation	PTNARFDSPESHVGV CCCCCCCCCCCCHHH	28.05	11013450
202	Phosphorylation	ARFDSPESHVGVAWR CCCCCCCCCHHHHHH	27.19	29978859
211	Ubiquitination	VGVAWRLKNEIPNSH HHHHHHCCCCCCCCH	43.91	29967540
211 (in isoform 2)	Ubiquitination	-	43.91	-
211	Sumoylation	VGVAWRLKNEIPNSH HHHHHHCCCCCCCCH	43.91	17087506
211	Sumoylation	VGVAWRLKNEIPNSH HHHHHHCCCCCCCCH	43.91	-
217	Ubiquitination	LKNEIPNSHILDQYR CCCCCCCCHHHHHHH	13.42	29967540
223	Nitration	NSHILDQYRNASNPL CCHHHHHHHCCCCCC	12.90	-
227	Phosphorylation	LDQYRNASNPLAHYD HHHHHCCCCCCCCCC	42.39	-
254	Phosphorylation	KLDMLVASVGTGGTI CCCEEEEECCCCHHH	17.38	23663014
257	Phosphorylation	MLVASVGTGGTITGI EEEEECCCCHHHHHH	30.22	23663014
260	Phosphorylation	ASVGTGGTITGIARK EECCCCHHHHHHHHH	19.40	23663014
262	Phosphorylation	VGTGGTITGIARKLK CCCCHHHHHHHHHHH	23.52	23663014
279	Ubiquitination	CPGCRIIGVDPEGSI CCCCEEEEECCCCCC	18.53	32015554
289	Ubiquitination	PEGSILAEPEELNQT CCCCCCCCHHHHCCC	50.20	21890473
293	Ubiquitination	ILAEPEELNQTEQTT CCCCHHHHCCCCCCE	5.69	22817900
322	Ubiquitination	LDRTVVDKWFKSNDE CCHHHHHHHHHCCHH	42.81	29967540
322 (in isoform 2)	Ubiquitination	-	42.81	-
325 (in isoform 2)	Ubiquitination	-	47.43	-
325	Ubiquitination	TVVDKWFKSNDEEAF HHHHHHHHCCHHHHH	47.43	21890473
329	Ubiquitination	KWFKSNDEEAFTFAR HHHHCCHHHHHHHHH	56.31	22817900
336	Methylation	EEAFTFARMLIAQEG HHHHHHHHHHHHHCC	19.09	-
370	Glutathionylation	ELQEGQRCVVILPDS HHHCCCEEEEECCHH	1.89	22555962
376	Ubiquitination	RCVVILPDSVRNYMT EEEEECCHHHHHHHH	57.21	29967540
381	Phosphorylation	LPDSVRNYMTKFLSD CCHHHHHHHHHHHHH	8.80	23403867
383	Phosphorylation	DSVRNYMTKFLSDRW HHHHHHHHHHHHHHH	14.32	23403867
384 (in isoform 2)	Ubiquitination	-	27.98	-
384	Ubiquitination	SVRNYMTKFLSDRWM HHHHHHHHHHHHHHH	27.98	32015554
387	Phosphorylation	NYMTKFLSDRWMLQK HHHHHHHHHHHHHHC	28.41	23403867
389	Methylation	MTKFLSDRWMLQKGF HHHHHHHHHHHHCCC	19.82	-
394 (in isoform 1)	Ubiquitination	-	47.90	21890473
394	Ubiquitination	SDRWMLQKGFLKEED HHHHHHHCCCCCHHH	47.90	22817900
394 (in isoform 2)	Ubiquitination	-	47.90	21890473
398	Sumoylation	MLQKGFLKEEDLTEK HHHCCCCCHHHCCCC	57.72	-
398	Ubiquitination	MLQKGFLKEEDLTEK HHHCCCCCHHHCCCC	57.72	22817900
398	Sumoylation	MLQKGFLKEEDLTEK HHHCCCCCHHHCCCC	57.72	-
411	Ubiquitination	EKKPWWWHLRVQELG CCCCCEEEEHHHHHC	7.05	21890473
415	Ubiquitination	WWWHLRVQELGLSAP CEEEEHHHHHCCCCC	33.49	22817900
428	Phosphorylation	APLTVLPTITCGHTI CCEEEECCCCCCCHH	25.43	22210691
431	Glutathionylation	TVLPTITCGHTIEIL EEECCCCCCCHHHHH	3.12	22555962
434	O-linked_Glycosylation	PTITCGHTIEILREK CCCCCCCHHHHHHHC	12.94	OGP
434	Phosphorylation	PTITCGHTIEILREK CCCCCCCHHHHHHHC	12.94	22210691
481	Ubiquitination	QPSDQVGKVIYKQFK CCHHHHHHHHHHHHH	26.97	29967540
481 (in isoform 2)	Ubiquitination	-	26.97	-
481	Acetylation	QPSDQVGKVIYKQFK CCHHHHHHHHHHHHH	26.97	66727057
485 (in isoform 2)	Ubiquitination	-	37.83	-
485	Ubiquitination	QVGKVIYKQFKQIRL HHHHHHHHHHHHHCC	37.83	-
525	Phosphorylation	YHSTGKSSQRQMVFG HHCCCCCHHHHHHHH	32.63	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
227	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS
525	S	Phosphorylation	Kinase	PRKG1	Q13976	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CBS_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of CBS_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VTA1_HUMAN	VTA1	physical	16189514
FXR2_HUMAN	FXR2	physical	16189514
HID1_HUMAN	HID1	physical	16189514
CBS_HUMAN	CBS	physical	16189514
CBS_HUMAN	CBS	physical	11483494
CBS_HUMAN	CBS	physical	11173483
HSP26_YEAST	HSP26	genetic	20066033
CBS_HUMAN	CBS	physical	21900206
CBS_HUMAN	CBS	physical	19447967
GPSM1_HUMAN	GPSM1	physical	23718855
DAXX_HUMAN	DAXX	physical	21988832
UGPA_HUMAN	UGP2	physical	21988832
GON7_HUMAN	C14orf142	physical	22863883
ERO1A_HUMAN	ERO1L	physical	22863883
GOPC_HUMAN	GOPC	physical	22863883
GPN1_HUMAN	GPN1	physical	22863883
HSF1_HUMAN	HSF1	physical	22863883
IPO4_HUMAN	IPO4	physical	22863883
IREB2_HUMAN	IREB2	physical	22863883
LRSM1_HUMAN	LRSAM1	physical	22863883
PARP6_HUMAN	PARP6	physical	22863883
PDLI5_HUMAN	PDLIM5	physical	22863883
RD23B_HUMAN	RAD23B	physical	22863883
SRP14_HUMAN	SRP14	physical	22863883
SAE2_HUMAN	UBA2	physical	22863883
UBA5_HUMAN	UBA5	physical	22863883
PIAS1_HUMAN	PIAS1	physical	17087506
PIAS3_HUMAN	PIAS3	physical	17087506
UBC9_HUMAN	UBE2I	physical	17087506
RANB9_HUMAN	RANBP9	physical	17087506
CBX4_HUMAN	CBX4	physical	17087506
CBS_HUMAN	CBS	physical	25416956
ECHP_HUMAN	EHHADH	physical	25416956
TBA8_HUMAN	EHHADH	physical	25416956
PIN1_HUMAN	PIN1	physical	25416956
AAKG1_HUMAN	PRKAG1	physical	25416956
PSA1_HUMAN	PSMA1	physical	25416956
UBC9_HUMAN	UBE2I	physical	25416956
UBS3A_HUMAN	UBASH3A	physical	25416956
AP1B1_HUMAN	AP1B1	physical	26344197
SYCC_HUMAN	CARS	physical	26344197
CGL_HUMAN	CTH	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
SYIC_HUMAN	IARS	physical	26344197
NMD3_HUMAN	NMD3	physical	26344197
SYQ_HUMAN	QARS	physical	26344197
SC24B_HUMAN	SEC24B	physical	26344197
SC31A_HUMAN	SEC31A	physical	26344197
UBE3B_HUMAN	UBE3B	physical	26344197
CBS_HUMAN	CBS	physical	21516116
TRAP1_HUMAN	TRAP1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
236200	Cystathionine beta-synthase deficiency (CBSD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00151	L-Cysteine
DB00133	L-Serine
DB00118	S-Adenosylmethionine

Regulatory Network of CBS_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.	19413330 [Abstract]
Sumoylation
Reference	PubMed
"Human cystathionine beta-synthase is a target for sumoylation."; Kabil O., Zhou Y., Banerjee R.; Biochemistry 45:13528-13536(2006). Cited for: SUMOYLATION AT LYS-211, AND SUBCELLULAR LOCATION.	17087506 [Abstract]