Search Results

Overview

Uniprot IDP02511
Protein NameAlpha-crystallin B chain
Gene NameCRYAB
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
103 DVIEVHGKHEERQDE
150 LTVNGPRKQVSGPER
166 IPITREEKPAVTAAP
174 PAVTAAPKK******
82 FSVNLDVKHFSPEEL
90 HFSPEELKVKVLGDV
92 SPEELKVKVLGDVIE

Function

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. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity)

Protein Sequence

10 MDIAIHHPWI 20 RRPFFPFHSP 30 SRLFDQFFGE 40 HLLESDLFPT 50 STSLSPFYLR 60 PPSFLRAPSW 70 FDTGLSEMRL 80 EKDRFSVNLD 90 VKHFSPEELK 100 VKVLGDVIEV 110 HGKHEERQDE 120 HGFISREFHR 130 KYRIPADVDP 140 LTITSSLSSD 150 GVLTVNGPRK 160 QVSGPERTIP 170 ITREEKPAVT AAPKK

Gene Ontology

Classification GO ID Description
Cellular Component GO:0032432 actin filament bundle
Cellular Component GO:0030424 axon
Cellular Component GO:0097512 cardiac myofibril
Cellular Component GO:0009986 cell surface
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0043197 dendritic spine
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005764 lysosome
Cellular Component GO:0031430 M band
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0043204 perikaryon
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0032991 protein-containing complex
Cellular Component GO:0097060 synaptic membrane
Cellular Component GO:0030018 Z disc
Molecular Function GO:0001540 amyloid-beta binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0046872 metal ion binding
Molecular Function GO:0008017 microtubule binding
Molecular Function GO:0042803 protein homodimerization activity
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0005212 structural constituent of eye lens
Molecular Function GO:0005198 structural molecule activity
Molecular Function GO:0051082 unfolded protein binding
Biological Process GO:0071480 cellular response to gamma radiation
Biological Process GO:0031109 microtubule polymerization or depolymerization
Biological Process GO:0006936 muscle contraction
Biological Process GO:1905907 negative regulation of amyloid fibril formation
Biological Process GO:0043066 negative regulation of apoptotic process
Biological Process GO:0030308 negative regulation of cell growth
Biological Process GO:0045892 negative regulation of DNA-templated transcription
Biological Process GO:0032387 negative regulation of intracellular transport
Biological Process GO:0031333 negative regulation of protein-containing complex assembly
Biological Process GO:2000378 negative regulation of reactive oxygen species metabolic process
Biological Process GO:0006457 protein folding
Biological Process GO:0042026 protein refolding
Biological Process GO:0050821 protein stabilization
Biological Process GO:0043067 regulation of programmed cell death
Biological Process GO:0032355 response to estradiol
Biological Process GO:0009408 response to heat
Biological Process GO:0042542 response to hydrogen peroxide
Biological Process GO:0051403 stress-activated MAPK cascade

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[3] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.