CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001967
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha-crystallin A chain 
Protein Synonyms/Alias
 Heat shock protein beta-4; HspB4; Alpha-crystallin A chain, short form 
Gene Name
 CRYAA 
Gene Synonyms/Alias
 CRYA1; HSPB4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
11TIQHPWFKRTLGPFYmethylation[1]
70EVRSDRDKFVIFLDVacetylation[2, 3, 4]
78FVIFLDVKHFSPEDLacetylation[3]
88SPEDLTVKVQDDFVEacetylation[3]
88SPEDLTVKVQDDFVEmethylation[3, 5]
99DFVEIHGKHNERQDDacetylation[4]
145MLTFCGPKIQTGLDAacetylation[3]
Reference
 [1] Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility?
 Wilmarth PA, Tanner S, Dasari S, Nagalla SR, Riviere MA, Bafna V, Pevzner PA, David LL.
 J Proteome Res. 2006 Oct;5(10):2554-66. [PMID: 17022627]
 [2] In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin.
 Lin PP, Barry RC, Smith DL, Smith JB.
 Protein Sci. 1998 Jun;7(6):1451-7. [PMID: 9655350]
 [3] Shotgun identification of protein modifications from protein complexes and lens tissue.
 MacCoss MJ, McDonald WH, Saraf A, Sadygov R, Clark JM, Tasto JJ, Gould KL, Wolters D, Washburn M, Weiss A, Clark JI, Yates JR 3rd.
 Proc Natl Acad Sci U S A. 2002 Jun 11;99(12):7900-5. [PMID: 12060738]
 [4] Acetylation of αA-crystallin in the human lens: effects on structure and chaperone function.
 Nagaraj RH, Nahomi RB, Shanthakumar S, Linetsky M, Padmanabha S, Pasupuleti N, Wang B, Santhoshkumar P, Panda AK, Biswas A.
 Biochim Biophys Acta. 2012 Feb;1822(2):120-9. [PMID: 22120592]
 [5] Update on activities at the Universal Protein Resource (UniProt) in 2013.
 e="String">UniProt Consortium.
 Nucleic Acids Res. 2013 Jan;41(Database issue):D43-7. [PMID: 23161681
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 79 79 Zinc.
 METAL 107 107 Zinc.
 METAL 115 115 Zinc.
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 70 70 N6-acetyllysine.
 MOD_RES 99 99 N6-acetyllysine.
 MOD_RES 101 101 Deamidated asparagine; partial.
 MOD_RES 122 122 Phosphoserine.
 CARBOHYD 162 162 O-linked (GlcNAc) (By similarity).
 DISULFID 131 142  
Keyword
 Acetylation; Cataract; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Disulfide bond; Eye lens protein; Glycoprotein; Metal-binding; Nucleus; Oxidation; Phosphoprotein; Polymorphism; Reference proteome; Sensory transduction; Vision; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 173 AA 
Protein Sequence
MDVTIQHPWF KRTLGPFYPS RLFDQFFGEG LFEYDLLPFL SSTISPYYRQ SLFRTVLDSG 60
ISEVRSDRDK FVIFLDVKHF SPEDLTVKVQ DDFVEIHGKH NERQDDHGYI SREFHRRYRL 120
PSNVDQSALS CSLSADGMLT FCGPKIQTGL DATHAERAIP VSREEKPTSA PSS 173 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0005212; F:structural constituent of eye lens; IEA:UniProtKB-KW.
 GO:0051082; F:unfolded protein binding; IMP:UniProtKB.
 GO:0007015; P:actin filament organization; IEA:Compara.
 GO:0060561; P:apoptotic process involved in morphogenesis; IEA:Compara.
 GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Compara.
 GO:0070309; P:lens fiber cell morphogenesis; IEA:Compara.
 GO:0000072; P:M phase specific microtubule process; IEA:Compara.
 GO:0007005; P:mitochondrion organization; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
 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; IDA:HGNC.
 GO:0030307; P:positive regulation of cell growth; IEA:Compara.
 GO:0001934; P:positive regulation of protein phosphorylation; IEA:Compara.
 GO:0006457; P:protein folding; IEA:Compara.
 GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
 GO:0042493; P:response to drug; IEA:Compara.
 GO:0051384; P:response to glucocorticoid stimulus; IEA:Compara.
 GO:0042542; P:response to hydrogen peroxide; IEA:Compara.
 GO:0001666; P:response to hypoxia; IEA:Compara.
 GO:0010288; P:response to lead ion; IEA:Compara.
 GO:0070141; P:response to UV-A; IEA:Compara.
 GO:0007021; P:tubulin complex assembly; IEA:Compara.
 GO:0007601; P:visual perception; IMP:UniProtKB. 
Interpro
 IPR002068; a-crystallin/Hsp20_dom.
 IPR001436; Alpha-crystallin/HSP.
 IPR012274; Alpha-crystallin_A.
 IPR003090; Alpha-crystallin_N.
 IPR008978; HSP20-like_chaperone. 
Pfam
 PF00525; Crystallin
 PF00011; HSP20 
SMART
  
PROSITE
 PS01031; HSP20 
PRINTS
 PR00299; ACRYSTALLIN.