CRBA1_HUMAN - dbPTM
CRBA1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRBA1_HUMAN
UniProt AC P05813
Protein Name Beta-crystallin A3
Gene Name CRYBA1
Organism Homo sapiens (Human).
Sequence Length 215
Subcellular Localization
Protein Description Crystallins are the dominant structural components of the vertebrate eye lens..
Protein Sequence METQAEQQELETLPTTKMAQTNPTPGSLGPWKITIYDQENFQGKRMEFTSSCPNVSERSFDNVRSLKVESGAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKMTIFEKENFIGRQWEISDDYPSLQAMGWFNNEVGSMKIQSGAWVCYQYPGYRGYQYILECDHHGGDYKHWREWGSHAQTSQIQSIRRIQQ
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
1Acetylation-------METQAEQQ
-------CCCHHHHH
13.038999933
2 (in isoform 2)Acetylation-50.028999933
15PhosphorylationQELETLPTTKMAQTN
HHHHCCCCCCCCCCC
42.01-
44MethylationDQENFQGKRMEFTSS
ECCCCCCCEEEEECC
37.4817022627
82MethylationGYEHTSFCGQQFILE
CCEECCCCCCEEEEC
4.8815576560
82S-glutathionyl cysteineGYEHTSFCGQQFILE
CCEECCCCCCEEEEC
4.88-
82GlutathionylationGYEHTSFCGQQFILE
CCEECCCCCCEEEEC
4.8822833525
112PhosphorylationYHIERLMSFRPICSA
HHHHHHHHCCCCCCC
23.7724719451
117MethylationLMSFRPICSANHKES
HHHCCCCCCCCCCCC
3.3115576560
117GlutathionylationLMSFRPICSANHKES
HHHCCCCCCCCCCCC
3.3122833525
117S-glutathionyl cysteineLMSFRPICSANHKES
HHHCCCCCCCCCCCC
3.31-
122AcetylationPICSANHKESKMTIF
CCCCCCCCCCCEEEE
64.5912060738
125AcetylationSANHKESKMTIFEKE
CCCCCCCCEEEEEEC
40.9512060738
127PhosphorylationNHKESKMTIFEKENF
CCCCCCEEEEEECCC
26.6722817900
131AcetylationSKMTIFEKENFIGRQ
CCEEEEEECCCCCCC
47.4012060738
137MethylationEKENFIGRQWEISDD
EECCCCCCCEEECCC
33.35-
160PhosphorylationWFNNEVGSMKIQSGA
CCCCCCCCEEEECCC
23.2922817900
179PhosphorylationQYPGYRGYQYILECD
ECCCCCCEEEEEEEC
6.8022817900
181PhosphorylationPGYRGYQYILECDHH
CCCCCEEEEEEECCC
10.0522817900
185MethylationGYQYILECDHHGGDY
CEEEEEEECCCCCCC
5.6015576560
204PhosphorylationEWGSHAQTSQIQSIR
HCCCCCCHHHHHHHH
24.3121712546

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 CRBA1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRBA1_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 CRBA1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CRBA1_HUMANCRYBA1physical
19401464
CRBB1_HUMANCRYBB1physical
25416956
CRBB3_HUMANCRYBB3physical
25416956
RBPMS_HUMANRBPMSphysical
25416956
RHXF2_HUMANRHOXF2physical
25416956
CRBB1_HUMANCRYBB1physical
21516116

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
600881Cataract 10, multiple types (CTRCT10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRBA1_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-127 AND SER-160,ACETYLATION AT LYS-122; LYS-125 AND LYS-131, METHYLATION AT ARG-137,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-127 AND SER-160,ACETYLATION AT LYS-122; LYS-125 AND LYS-131, METHYLATION AT ARG-137,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-127 AND SER-160,ACETYLATION AT LYS-122; LYS-125 AND LYS-131, METHYLATION AT ARG-137,SUSCEPTIBILITY TO OXIDATION, AND MASS SPECTROMETRY.

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