CYTB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CYTB_HUMAN
• UniProt AC: P04080
• Protein Name: Cystatin-B
• Gene Name: CSTB
• Organism: Homo sapiens (Human).
• Sequence Length: 98
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B..
• Protein Sequence: MMCGAPSATQPATAETQHIADQVRSQLEEKENKKFPVFKAVSFKSQVVAGTNYFIKVHVGDEDFVHLRVFQSLPHENKPLTLSNYQTNKAKHDELTYF

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MMCGAPSA -------CCCCCCCC	4.53	22223895
7	Phosphorylation	-MMCGAPSATQPATA -CCCCCCCCCCCCCH	43.33	28450419
7	O-linked_Glycosylation	-MMCGAPSATQPATA -CCCCCCCCCCCCCH	43.33	30379171
9	Phosphorylation	MCGAPSATQPATAET CCCCCCCCCCCCHHH	39.15	28450419
9	O-linked_Glycosylation	MCGAPSATQPATAET CCCCCCCCCCCCHHH	39.15	30379171
13	Phosphorylation	PSATQPATAETQHIA CCCCCCCCHHHHHHH	31.54	28450419
13	O-linked_Glycosylation	PSATQPATAETQHIA CCCCCCCCHHHHHHH	31.54	30379171
16	Phosphorylation	TQPATAETQHIADQV CCCCCHHHHHHHHHH	24.00	20068231
16	O-linked_Glycosylation	TQPATAETQHIADQV CCCCCHHHHHHHHHH	24.00	30379171
25	O-linked_Glycosylation	HIADQVRSQLEEKEN HHHHHHHHHHHHHHH	40.02	30379171
34	Acetylation	LEEKENKKFPVFKAV HHHHHHCCCCEEEEE	67.49	26051181
39	Acetylation	NKKFPVFKAVSFKSQ HCCCCEEEEEEEECE	48.38	25953088
39	Ubiquitination	NKKFPVFKAVSFKSQ HCCCCEEEEEEEECE	48.38	21890473
44	Acetylation	VFKAVSFKSQVVAGT EEEEEEEECEEEECC	32.26	25825284
44	Ubiquitination	VFKAVSFKSQVVAGT EEEEEEEECEEEECC	32.26	21890473
45	Phosphorylation	FKAVSFKSQVVAGTN EEEEEEECEEEECCC	26.63	26356563
51	Phosphorylation	KSQVVAGTNYFIKVH ECEEEECCCEEEEEE	19.60	28152594
53	Phosphorylation	QVVAGTNYFIKVHVG EEEECCCEEEEEEEC	13.40	28152594
68	Methylation	DEDFVHLRVFQSLPH CCCEEEEEEEECCCC	16.60	-
72	Phosphorylation	VHLRVFQSLPHENKP EEEEEEECCCCCCCC	32.19	24719451
78	Acetylation	QSLPHENKPLTLSNY ECCCCCCCCCEEECC	38.12	23954790
78	Ubiquitination	QSLPHENKPLTLSNY ECCCCCCCCCEEECC	38.12	19608861
81	Phosphorylation	PHENKPLTLSNYQTN CCCCCCCEEECCCCC	36.35	24719451
83	Phosphorylation	ENKPLTLSNYQTNKA CCCCCEEECCCCCCC	28.40	28152594
85	Phosphorylation	KPLTLSNYQTNKAKH CCCEEECCCCCCCCC	17.22	24719451
87	Phosphorylation	LTLSNYQTNKAKHDE CEEECCCCCCCCCCC	28.46	28152594
91	Ubiquitination	NYQTNKAKHDELTYF CCCCCCCCCCCCCCC	53.88	19608861
91	Acetylation	NYQTNKAKHDELTYF CCCCCCCCCCCCCCC	53.88	23236377
91	Malonylation	NYQTNKAKHDELTYF CCCCCCCCCCCCCCC	53.88	26320211
96	Phosphorylation	KAKHDELTYF----- CCCCCCCCCC-----	22.34	23403867
97	Phosphorylation	AKHDELTYF------ CCCCCCCCC------	21.66	25159151

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

Oops, there are no upstream regulatory protein records of CYTB_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CYTB_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CYTB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CATH_HUMAN	CTSH	physical	11514663
CATB_HUMAN	CTSB	physical	11514663
CYTC_HUMAN	CST3	physical	1996959
METK2_HUMAN	MAT2A	physical	22939629
NUDC_HUMAN	NUDC	physical	22939629
FLNB_HUMAN	FLNB	physical	22939629
SC24A_HUMAN	SEC24A	physical	22939629
SARNP_HUMAN	SARNP	physical	22863883
GSTT1_HUMAN	GSTT1	physical	26344197
PDCD6_HUMAN	PDCD6	physical	26344197

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 254800: Epilepsy, progressive myoclonic 1 (EPM1)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
PubMed: 19413330

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78 AND LYS-91, AND MASSSPECTROMETRY.
PubMed: 19608861

Phosphorylation

"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-97, AND MASSSPECTROMETRY.
PubMed: 19534553