CRBB3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CRBB3_HUMAN
• UniProt AC: P26998
• Protein Name: Beta-crystallin B3
• Gene Name: CRYBB3
• Organism: Homo sapiens (Human).
• Sequence Length: 211
• Protein Description: Crystallins are the dominant structural components of the vertebrate eye lens..
• Protein Sequence: MAEQHGAPEQAAAGKSHGDLGGSYKVILYELENFQGKRCELSAECPSLTDSLLEKVGSIQVESGPWLAFESRAFRGEQFVLEKGDYPRWDAWSNSRDSDSLLSLRPLNIDSPHHKLHLFENPAFSGRKMEIVDDDVPSLWAHGFQDRVASVRAINGTWVGYEFPGYRGRQYVFERGEYRHWNEWDASQPQLQSVRRIRDQKWHKRGRFPSS

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	-------MAEQHGAP -------CCHHHCCH	9.27	8999933
2	Acetylation	------MAEQHGAPE ------CCHHHCCHH	25.75	-
29	Phosphorylation	GSYKVILYELENFQG CCEEEEEEEEECCCC	13.82	22817900
51	Phosphorylation	ECPSLTDSLLEKVGS CCCCCCHHHHHHHCC	29.62	24719451
103	Phosphorylation	RDSDSLLSLRPLNID CCCCCCCCCCCCCCC	27.85	24719451
128	Acetylation	NPAFSGRKMEIVDDD CCCCCCCEEEEECCC	44.39	12060738
128	Methylation	NPAFSGRKMEIVDDD CCCCCCCEEEEECCC	44.39	12060738
150	Phosphorylation	GFQDRVASVRAINGT CCHHHEEEEEEECCE	14.85	24719451

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

Oops, there are no upstream regulatory protein records of CRBB3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CRBB3_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 CRBB3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TAB1_HUMAN	TAB1	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 609741: Cataract 22, multiple types (CTRCT22)
• 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

"Shotgun identification of protein modifications from proteincomplexes and lens tissue.";
MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M.,Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I.,Yates J.R. III;
Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, ACETYLATION ATLYS-128, METHYLATION AT LYS-128, SUSCEPTIBILITY TO OXIDATION, AND MASSSPECTROMETRY.
PubMed: 12060738

Methylation

"Shotgun identification of protein modifications from proteincomplexes and lens tissue.";
MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M.,Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I.,Yates J.R. III;
Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, ACETYLATION ATLYS-128, METHYLATION AT LYS-128, SUSCEPTIBILITY TO OXIDATION, AND MASSSPECTROMETRY.
PubMed: 12060738

Phosphorylation

"Shotgun identification of protein modifications from proteincomplexes and lens tissue.";
MacCoss M.J., McDonald W.H., Saraf A., Sadygov R., Clark J.M.,Tasto J.J., Gould K.L., Wolters D., Washburn M., Weiss A., Clark J.I.,Yates J.R. III;
Proc. Natl. Acad. Sci. U.S.A. 99:7900-7905(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, ACETYLATION ATLYS-128, METHYLATION AT LYS-128, SUSCEPTIBILITY TO OXIDATION, AND MASSSPECTROMETRY.
PubMed: 12060738