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 | ||
|
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MASDHQTQA ------CCCCCCCCC | 24.54 | 8443605 | |
3 | Phosphorylation | -----MASDHQTQAG -----CCCCCCCCCC | 34.04 | 29978859 | |
7 | Phosphorylation | -MASDHQTQAGKPQS -CCCCCCCCCCCCCC | 19.57 | 29978859 | |
11 | Methylation | DHQTQAGKPQSLNPK CCCCCCCCCCCCCCE | 42.79 | 17022627 | |
14 | Phosphorylation | TQAGKPQSLNPKIII CCCCCCCCCCCEEEE | 38.34 | 29978859 | |
42 | Methylation | NGPCPNLKETGVEKA CCCCCCHHHHCCEEC | 60.93 | 23161681 | |
68 | Methylation | GYEQANCKGEQFVFE CCEECCCCCCEEEEE | 66.35 | 12060738 | |
76 | Acetylation | GEQFVFEKGEYPRWD CCEEEEECCCCCCCC | 45.65 | 12060738 | |
91 | Phosphorylation | SWTSSRRTDSLSSLR CCCCCCCCCCCHHCC | 28.91 | - | |
93 | Phosphorylation | TSSRRTDSLSSLRPI CCCCCCCCCHHCCCE | 29.54 | 22167270 | |
95 | Phosphorylation | SRRTDSLSSLRPIKV CCCCCCCHHCCCEEE | 31.14 | 22167270 | |
96 | Phosphorylation | RRTDSLSSLRPIKVD CCCCCCHHCCCEEEC | 33.42 | 22167270 | |
104 | Phosphorylation | LRPIKVDSQEHKIIL CCCEEECCCCCEEEE | 40.22 | - | |
118 | Phosphorylation | LYENPNFTGKKMEII EEECCCCCCCEEEEE | 55.52 | 22817900 | |
120 | Methylation | ENPNFTGKKMEIIDD ECCCCCCCEEEEECC | 45.98 | 12060738 | |
121 | Methylation | NPNFTGKKMEIIDDD CCCCCCCEEEEECCC | 43.01 | 23161681 | |
121 | Acetylation | NPNFTGKKMEIIDDD CCCCCCCEEEEECCC | 43.01 | 12060738 | |
174 | Phosphorylation | EKGDYKDSSDFGAPH HCCCCCCCCCCCCCC | 27.88 | 29083192 | |
175 | Phosphorylation | KGDYKDSSDFGAPHP CCCCCCCCCCCCCCH | 47.28 | 29083192 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CRBB2_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CRYAA_HUMAN | CRYAA | physical | 11700327 | |
CRYAB_HUMAN | CRYAB | physical | 11700327 | |
CRGC_HUMAN | CRYGC | physical | 11700327 | |
CRBB2_HUMAN | CRYBB2 | physical | 11700327 | |
HSPB1_HUMAN | HSPB1 | physical | 11700327 | |
CRYAB_HUMAN | CRYAB | physical | 16274233 |
Kegg Disease | ||||||
---|---|---|---|---|---|---|
There are no disease associations of PTM sites. | ||||||
OMIM Disease | ||||||
601547 | Cataract 3, multiple types (CTRCT3) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |