CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001968
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha-crystallin B chain 
Protein Synonyms/Alias
 Alpha(B)-crystallin 
Gene Name
 CRYAB 
Gene Synonyms/Alias
 CRYA2 
Created Date
 July 27, 2013 
Organism
 Bos taurus (Bovine) 
NCBI Taxa ID
 9913 
Lysine Modification
Position
Peptide
Type
References
90HFSPEELKVKVLGDVglycation[1]
92SPEELKVKVLGDVIEglycation[1]
103DVIEVHGKHEERQDEglycation[2]
150LTVNGPRKQASGPERglycation[2]
166IPITREEKPAVTAAPglycation[3]
Reference
 [1] Site selectivity in the glycation of alpha A- and alpha B-crystallins by glucose.
 Abraham EC, Cherian M, Smith JB.
 Biochem Biophys Res Commun. 1994 Jun 30;201(3):1451-6. [PMID: 7912928]
 [2] Quantification of post-translationally modified peptides of bovine alpha-crystallin using tandem mass tags and electron transfer dissociation.
 Viner RI, Zhang T, Second T, Zabrouskov V.
 J Proteomics. 2009 Jul 21;72(5):874-85. [PMID: 19245863]
 [3] Role of the specifically targeted lysine residues in the glycation dependent loss of chaperone activity of alpha A- and alpha B-crystallins.
 Abraham EC, Huaqian J, Aziz A, Kumarasamy A, Datta P.
 Mol Cell Biochem. 2008 Mar;310(1-2):235-9. [PMID: 18158587
Functional 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. 
Sequence Annotation
 METAL 104 104 Zinc (By similarity).
 METAL 111 111 Zinc (By similarity).
 METAL 119 119 Zinc (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 19 19 Phosphoserine.
 MOD_RES 22 22 Omega-N-methylated arginine (By
 MOD_RES 45 45 Phosphoserine.
 MOD_RES 50 50 Omega-N-methylated arginine (By
 MOD_RES 59 59 Phosphoserine.
 MOD_RES 92 92 N6-acetyllysine; alternate (By
 MOD_RES 166 166 N6-acetyllysine (By similarity).
 CARBOHYD 90 90 N-linked (Glc) (glycation) (Probable).
 CARBOHYD 92 92 N-linked (Glc) (glycation); alternate  
Keyword
 Acetylation; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Eye lens protein; Glycation; Glycoprotein; Metal-binding; Methylation; Nucleus; Oxidation; Phosphoprotein; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 175 AA 
Protein Sequence
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPA STSLSPFYLR PPSFLRAPSW 60
IDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR 120
KYRIPADVDP LAITSSLSSD GVLTVNGPRK QASGPERTIP ITREEKPAVT AAPKK 175 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0030018; C:Z disc; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
 GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Compara.
 GO:0002088; P:lens development in camera-type eye; IEA:Compara.
 GO:0007517; P:muscle organ development; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; ISS:AgBase.
 GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Compara.
 GO:0010629; P:negative regulation of gene expression; IEA:Compara.
 GO:0032387; P:negative regulation of intracellular transport; ISS:AgBase.
 GO:0051260; P:protein homooligomerization; IEA:Compara.
 GO:0042542; P:response to hydrogen peroxide; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0007021; P:tubulin complex assembly; IEA:Compara. 
Interpro
 IPR002068; a-crystallin/Hsp20_dom.
 IPR001436; Alpha-crystallin/HSP.
 IPR012273; Alpha-crystallin_B.
 IPR003090; Alpha-crystallin_N.
 IPR008978; HSP20-like_chaperone. 
Pfam
 PF00525; Crystallin
 PF00011; HSP20 
SMART
  
PROSITE
 PS01031; HSP20 
PRINTS
 PR00299; ACRYSTALLIN.