MitoProteome Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins

MT000152

UniProt Annotations

Entry Information

Gene Name	crystallin, alpha B
Protein Entry	CRYAB_HUMAN
UniProt ID	P02511
Species	Human

Comments

Comment type	Description
Disease	Cardiomyopathy, dilated 1II (CMD1II) [MIM:615184]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death. {ECO:0000269\|PubMed:16483541, ECO:0000269\|PubMed:16793013}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Disease	Cataract 16, multiple types (CTRCT16) [MIM:613763]: An opacification of the crystalline lens of the eye that frequently results in visual impairment or blindness. Opacities vary in morphology, are often confined to a portion of the lens, and may be static or progressive. In general, the more posteriorly located and dense an opacity, the greater the impact on visual function. CTRCT16 includes posterior polar cataract, among others. Posterior polar cataract is a subcapsular opacity, usually disk-shaped, located at the back of the lens. {ECO:0000269\|PubMed:11577372}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Disease	Myopathy, myofibrillar, 2 (MFM2) [MIM:608810]: A neuromuscular disorder that results in weakness of the proximal and distal limb muscles, weakness of the neck, velopharynx and trunk muscles, hypertrophic cardiomyopathy, and cataract in a subset of patients. {ECO:0000269\|PubMed:14681890, ECO:0000269\|PubMed:21920752, ECO:0000269\|PubMed:9731540}. Note=The disease is caused by mutations affecting the gene represented in this entry.
Disease	Myopathy, myofibrillar, fatal infantile hypertonic, alpha-B crystallin-related (MFMFIH-CRYAB) [MIM:613869]: A muscular dystrophy with onset in the first weeks of life after a normal neonatal period. Affected infants show rapidly progressive muscular rigidity of the trunk and limbs associated with increasing respiratory difficulty resulting in death before age 3 years. {ECO:0000269\|PubMed:21337604}. Note=The disease is caused by mutations affecting the gene represented in this entry.
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.
Interaction	Self; NbExp=4; IntAct=EBI-739060, EBI-739060; P02489:CRYAA; NbExp=7; IntAct=EBI-739060, EBI-6875961; P05813:CRYBA1; NbExp=2; IntAct=EBI-739060, EBI-7043337; P07315:CRYGC; NbExp=3; IntAct=EBI-739060, EBI-6875941; P04792:HSPB1; NbExp=2; IntAct=EBI-739060, EBI-352682; Q9UJY1:HSPB8; NbExp=2; IntAct=EBI-739060, EBI-739074; Q3UBX0:Tmem109 (xeno); NbExp=2; IntAct=EBI-739060, EBI-2366300;
Mass Spectrometry	Mass=20199; Method=Electrospray; Range=1-175; Evidence={ECO:0000269\|PubMed:10930324, ECO:0000269\|PubMed:8175657};
Mass Spectrometry	Mass=20201; Method=Electrospray; Range=1-175; Evidence={ECO:0000269\|PubMed:10930324, ECO:0000269\|PubMed:8175657};
Mass Spectrometry	Mass=20278; Method=Electrospray; Range=1-175; Note=With 1 phosphate group.; Evidence={ECO:0000269\|PubMed:10930324, ECO:0000269\|PubMed:8175657};
Mass Spectrometry	Mass=20281; Method=Electrospray; Range=1-175; Note=With 1 phosphate group.; Evidence={ECO:0000269\|PubMed:10930324, ECO:0000269\|PubMed:8175657};
Mass Spectrometry	Mass=20360; Method=Electrospray; Range=1-175; Note=With 2 phosphate groups.; Evidence={ECO:0000269\|PubMed:8175657};
Similarity	Belongs to the small heat shock protein (HSP20) family. {ECO:0000255\|PROSITE-ProRule:PRU00285}.
Subcellular Location	Cytoplasm {ECO:0000269\|PubMed:19464326}. Nucleus {ECO:0000269\|PubMed:19464326}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles.
Subunit	Heteropolymer composed of three CRYAA and one CRYAB subunits. Aggregates with homologous proteins, including the small heat shock protein HSPB1, to form large heteromeric complexes. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Interacts with HSPBAP1 and TTN/titin. {ECO:0000269\|PubMed:10751411, ECO:0000269\|PubMed:14676215, ECO:0000269\|PubMed:20836128, ECO:0000269\|PubMed:22890888}.
Tissue Specificity	Lens as well as other tissues.
Web Resource	Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CRYABID40156ch11q23.html";