CRBB2_HUMAN - dbPTM
CRBB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRBB2_HUMAN
UniProt AC P43320
Protein Name Beta-crystallin B2
Gene Name CRYBB2
Organism Homo sapiens (Human).
Sequence Length 205
Subcellular Localization
Protein Description Crystallins are the dominant structural components of the vertebrate eye lens..
Protein Sequence MASDHQTQAGKPQSLNPKIIIFEQENFQGHSHELNGPCPNLKETGVEKAGSVLVQAGPWVGYEQANCKGEQFVFEKGEYPRWDSWTSSRRTDSLSSLRPIKVDSQEHKIILYENPNFTGKKMEIIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGLQYLLEKGDYKDSSDFGAPHPQVQSVRRIRDMQWHQRGAFHPSN
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------MASDHQTQA
------CCCCCCCCC
24.548443605
3Phosphorylation-----MASDHQTQAG
-----CCCCCCCCCC
34.0429978859
7Phosphorylation-MASDHQTQAGKPQS
-CCCCCCCCCCCCCC
19.5729978859
11MethylationDHQTQAGKPQSLNPK
CCCCCCCCCCCCCCE
42.7917022627
14PhosphorylationTQAGKPQSLNPKIII
CCCCCCCCCCCEEEE
38.3429978859
42MethylationNGPCPNLKETGVEKA
CCCCCCHHHHCCEEC
60.9323161681
68MethylationGYEQANCKGEQFVFE
CCEECCCCCCEEEEE
66.3512060738
76AcetylationGEQFVFEKGEYPRWD
CCEEEEECCCCCCCC
45.6512060738
91PhosphorylationSWTSSRRTDSLSSLR
CCCCCCCCCCCHHCC
28.91-
93PhosphorylationTSSRRTDSLSSLRPI
CCCCCCCCCHHCCCE
29.5422167270
95PhosphorylationSRRTDSLSSLRPIKV
CCCCCCCHHCCCEEE
31.1422167270
96PhosphorylationRRTDSLSSLRPIKVD
CCCCCCHHCCCEEEC
33.4222167270
104PhosphorylationLRPIKVDSQEHKIIL
CCCEEECCCCCEEEE
40.22-
118PhosphorylationLYENPNFTGKKMEII
EEECCCCCCCEEEEE
55.5222817900
120MethylationENPNFTGKKMEIIDD
ECCCCCCCEEEEECC
45.9812060738
121MethylationNPNFTGKKMEIIDDD
CCCCCCCEEEEECCC
43.0123161681
121AcetylationNPNFTGKKMEIIDDD
CCCCCCCEEEEECCC
43.0112060738
174PhosphorylationEKGDYKDSSDFGAPH
HCCCCCCCCCCCCCC
27.8829083192
175PhosphorylationKGDYKDSSDFGAPHP
CCCCCCCCCCCCCCH
47.2829083192

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 CRBB2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRBB2_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 CRBB2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRYAA_HUMANCRYAAphysical
11700327
CRYAB_HUMANCRYABphysical
11700327
CRGC_HUMANCRYGCphysical
11700327
CRBB2_HUMANCRYBB2physical
11700327
HSPB1_HUMANHSPB1physical
11700327
CRYAB_HUMANCRYABphysical
16274233

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601547Cataract 3, multiple types (CTRCT3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRBB2_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 THR-118, ACETYLATION ATLYS-76 AND LYS-121, METHYLATION AT LYS-42; LYS-68 AND LYS-121,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 THR-118, ACETYLATION ATLYS-76 AND LYS-121, METHYLATION AT LYS-42; LYS-68 AND LYS-121,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 THR-118, ACETYLATION ATLYS-76 AND LYS-121, METHYLATION AT LYS-42; LYS-68 AND LYS-121,SUSCEPTIBILITY TO OXIDATION, AND MASS SPECTROMETRY.

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