dbPTM

CRYAB_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CRYAB_RAT
UniProt AC	P23928
Protein Name	Alpha-crystallin B chain
Gene Name	Cryab
Organism	Rattus norvegicus (Rat).
Sequence Length	175
Subcellular Localization	Cytoplasm . Nucleus . Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. Localizes at the Z-bands and the intercalated disk in cardiomyocytes.
Protein Description	May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions..
Protein Sequence	MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEMRMEKDRFSVNLDVKHFSPEELKVKVLGDVIEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MDIAIHHP -------CCCEECCC	8.31	-
19	Phosphorylation	RPFFPFHSPSRLFDQ CCCCCCCCHHHHHHH	25.58	23991683
21	Phosphorylation	FFPFHSPSRLFDQFF CCCCCCHHHHHHHHH	44.63	23991683
22	Methylation	FPFHSPSRLFDQFFG CCCCCHHHHHHHHHH	42.64	-
45	Phosphorylation	FSTATSLSPFYLRPP CCCCCCCCCCCCCCH	16.84	9774459
50	Methylation	SLSPFYLRPPSFLRA CCCCCCCCCHHHHCC	29.69	-
59	Phosphorylation	PSFLRAPSWIDTGLS HHHHCCCHHHHCCHH	35.36	23991683
63	Phosphorylation	RAPSWIDTGLSEMRM CCCHHHHCCHHHHHC	30.78	23991683
82	Acetylation	FSVNLDVKHFSPEEL EEEEEECCCCCHHHH	38.30	22902405
90	Acetylation	HFSPEELKVKVLGDV CCCHHHHEEEEEEEE	43.20	22902405
92	Acetylation	SPEELKVKVLGDVIE CHHHHEEEEEEEEEE	30.10	26302492
103	Acetylation	DVIEVHGKHEERQDE EEEEECCCCCHHCCC	32.72	22902405
139	Phosphorylation	TITSSLSSDGVLTVN EEEECCCCCCEEEEC	43.61	22108457
166	Acetylation	IPITREEKPAVTAAP CCCCCCCCCCCCCCC	33.26	22902405
170	O-linked_Glycosylation	REEKPAVTAAPKK-- CCCCCCCCCCCCC--	21.14	23543138
174	Acetylation	PAVTAAPKK------ CCCCCCCCC------	67.40	22902405

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
45	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
45	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CRYAB_RAT !!

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 CRYAB_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of CRYAB_RAT !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of CRYAB_RAT

Related Literatures of Post-Translational Modification

O-linked Glycosylation
Reference	PubMed
"Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin."; Roquemore E.P., Chevrier M.R., Cotter R.J., Hart G.W.; Biochemistry 35:3578-3586(1996). Cited for: GLYCOSYLATION AT THR-170.	8639509 [Abstract]