CRBB1_HUMAN - dbPTM
CRBB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRBB1_HUMAN
UniProt AC P53674
Protein Name Beta-crystallin B1
Gene Name CRYBB1
Organism Homo sapiens (Human).
Sequence Length 252
Subcellular Localization
Protein Description Crystallins are the dominant structural components of the vertebrate eye lens..
Protein Sequence MSQAAKASASATVAVNPGPDTKGKGAPPAGTSPSPGTTLAPTTVPITSAKAAELPPGNYRLVVFELENFQGRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLMSFRPIKMDAQEHKISLFEGANFKGNTIEIQGDDAPSLWVYGFSDRVGSVKVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQSLRRLRDKQWHLEGSFPVLATEPPK
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 Orthologous
Protein Cluster
2Acetylation------MSQAAKASA
------CCHHHHHCC
28.648626774
6Acetylation--MSQAAKASASATV
--CCHHHHHCCCCEE
45.9812060738
10PhosphorylationQAAKASASATVAVNP
HHHHHCCCCEEEECC
23.2122817900
12PhosphorylationAKASASATVAVNPGP
HHHCCCCEEEECCCC
13.4022817900
107PhosphorylationPWVAFEQSNFRGEMF
CEEEEECCCCCCEEE
30.6424719451
130PhosphorylationRWNTWSSSYRSDRLM
CCCCCCCCCCCCCEE
21.0322964224
131PhosphorylationWNTWSSSYRSDRLMS
CCCCCCCCCCCCEEE
18.9822964224
138PhosphorylationYRSDRLMSFRPIKMD
CCCCCEEEECEECCC
23.7724719451
160AcetylationLFEGANFKGNTIEIQ
EEECCCCCCCEEEEE
51.5712060738
163PhosphorylationGANFKGNTIEIQGDD
CCCCCCCEEEEECCC
28.76-
230MethylationQPQMQSLRRLRDKQW
HHHHHHHHHHHHCCC
40.61-
231MethylationPQMQSLRRLRDKQWH
HHHHHHHHHHHCCCC
39.09-
235MethylationSLRRLRDKQWHLEGS
HHHHHHHCCCCCCCC
49.1812060738

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

Oops, there are no upstream regulatory protein records of CRBB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRBB1_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 CRBB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of CRBB1_HUMAN !!

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611544Cataract 17, multiple types (CTRCT17)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRBB1_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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 SER-10 AND THR-12,ACETYLATION AT LYS-6 AND LYS-160, METHYLATION AT ARG-230; ARG-231 ANDLYS-235, SUSCEPTIBILITY TO OXIDATION, AND MASS SPECTROMETRY.
Methylation
ReferencePubMed
"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 SER-10 AND THR-12,ACETYLATION AT LYS-6 AND LYS-160, METHYLATION AT ARG-230; ARG-231 ANDLYS-235, SUSCEPTIBILITY TO OXIDATION, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-10 AND THR-12,ACETYLATION AT LYS-6 AND LYS-160, METHYLATION AT ARG-230; ARG-231 ANDLYS-235, SUSCEPTIBILITY TO OXIDATION, AND MASS SPECTROMETRY.

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