Cryab | ENSRNOG00000010524 | NCBI 25420

Details for: Cryab

Gene ID: 25420

Symbol: Cryab

Ensembl ID: ENSRNOG00000010524

Description: crystallin, alpha B

Associated with

Cellular responses to stimuli
(R-RNO-8953897)
Cellular responses to stress
(R-RNO-2262752)
Cellular response to heat stress
(R-RNO-3371556)
Hsf1-dependent transactivation
(R-RNO-3371571)
Actin filament bundle
(GO:0032432)
Amyloid-beta binding
(GO:0001540)
Apoptotic process involved in morphogenesis
(GO:0060561)
Axon
(GO:0030424)
Camera-type eye development
(GO:0043010)
Cardiac myofibril
(GO:0097512)
Cell surface
(GO:0009986)
Cellular response to gamma radiation
(GO:0071480)
Contractile fiber
(GO:0043292)
Cytoplasm
(GO:0005737)
Cytoskeletal protein binding
(GO:0008092)
Cytosol
(GO:0005829)
Dendritic spine
(GO:0043197)
Extracellular region
(GO:0005576)
I band
(GO:0031674)
Identical protein binding
(GO:0042802)
Lens development in camera-type eye
(GO:0002088)
Lysosome
(GO:0005764)
M band
(GO:0031430)
Metal ion binding
(GO:0046872)
Microtubule binding
(GO:0008017)
Microtubule polymerization or depolymerization
(GO:0031109)
Mitochondrion
(GO:0005739)
Muscle organ development
(GO:0007517)
Negative regulation of amyloid fibril formation
(GO:1905907)
Negative regulation of apoptotic process
(GO:0043066)
Negative regulation of cell growth
(GO:0030308)
Negative regulation of dna-templated transcription
(GO:0045892)
Negative regulation of gene expression
(GO:0010629)
Negative regulation of intracellular transport
(GO:0032387)
Negative regulation of protein-containing complex assembly
(GO:0031333)
Negative regulation of reactive oxygen species metabolic process
(GO:2000378)
Nucleus
(GO:0005634)
Perikaryon
(GO:0043204)
Plasma membrane
(GO:0005886)
Protein-containing complex
(GO:0032991)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Protein folding
(GO:0006457)
Protein homodimerization activity
(GO:0042803)
Protein refolding
(GO:0042026)
Protein stabilization
(GO:0050821)
Regulation of programmed cell death
(GO:0043067)
Response to estradiol
(GO:0032355)
Response to heat
(GO:0009408)
Response to hydrogen peroxide
(GO:0042542)
Response to hypoxia
(GO:0001666)
Stress-activated mapk cascade
(GO:0051403)
Structural constituent of eye lens
(GO:0005212)
Structural molecule activity
(GO:0005198)
Synaptic membrane
(GO:0097060)
Tubulin complex assembly
(GO:0007021)
Unfolded protein binding
(GO:0051082)
Z disc
(GO:0030018)

Other Information

Proteins

Alpha-crystallin B chain

Genular Protein ID: 416295971

Symbol: CRYAB_RAT

Name: Alpha-crystallin B chain

UniProtKB Accession Codes:

P23928 Q6LDR2

Database IDs:

Citations:

PubMed ID: 2176207

Title: Multiple mRNAs of rat brain alpha-crystallin B chain result from alternative transcriptional initiation.

PubMed ID: 2176207

DOI: 10.1016/s0021-9258(18)45689-x

PubMed ID: 1765091

Title: Alpha B-crystallin exists as an independent protein in the heart and in the lens.

PubMed ID: 1765091

DOI: 10.1111/j.1432-1033.1991.tb16432.x

PubMed ID: 1764082

Title: Early changes of alpha B-crystallin mRNA in rat skeletal muscle to mechanical tension and denervation.

PubMed ID: 1764082

DOI: 10.1016/0006-291x(91)92083-v

PubMed ID: 1783614

Title: Alpha B-crystallin in skeletal muscle: purification and localization.

PubMed ID: 1783614

DOI: 10.1093/oxfordjournals.jbchem.a123665

PubMed ID: 2912453

Title: Alpha-B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues.

PubMed ID: 2912453

DOI: 10.1016/s0006-291x(89)80215-3

PubMed ID: 8282729

Title: Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles.

PubMed ID: 8282729

DOI: 10.1093/oxfordjournals.jbchem.a124184

PubMed ID: 8639509

Title: Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin.

PubMed ID: 8639509

DOI: 10.1021/bi951918j

PubMed ID: 10751411

Title: Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27.

PubMed ID: 10751411

DOI: 10.1074/jbc.m001981200

PubMed ID: 16641100

Title: Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites.

PubMed ID: 16641100

DOI: 10.1073/pnas.0600895103

PubMed ID: 22673903

Title: Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.

PubMed ID: 22673903

DOI: 10.1038/ncomms1871

Sequence Information:

Length: 175
Mass: 20089
Checksum: AB66796291518B9B
Sequence:

MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFST ATSLSPFYLR PPSFLRAPSW 
IDTGLSEMRM EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR 
KYRIPADVDP LTITSSLSSD GVLTVNGPRK QASGPERTIP ITREEKPAVT AAPKK

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Cryab

Associated with

Other Information

Multiple mRNAs of rat brain alpha-crystallin B chain result from alternative transcriptional initiation. PubMed ID: 2176207

Alpha B-crystallin exists as an independent protein in the heart and in the lens. PubMed ID: 1765091

Early changes of alpha B-crystallin mRNA in rat skeletal muscle to mechanical tension and denervation. PubMed ID: 1764082

Alpha B-crystallin in skeletal muscle: purification and localization. PubMed ID: 1783614

Alpha-B subunit of lens-specific protein alpha-crystallin is present in other ocular and non-ocular tissues. PubMed ID: 2912453

Physiological and pathological changes in levels of the two small stress proteins, HSP27 and alpha B crystallin, in rat hindlimb muscles. PubMed ID: 8282729

Dynamic O-GlcNAcylation of the small heat shock protein alpha B-crystallin. PubMed ID: 8639509

Identification and characterization of a novel protein from Sertoli cells, PASS1, that associates with mammalian small stress protein hsp27. PubMed ID: 10751411

Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites. PubMed ID: 16641100

Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues. PubMed ID: 22673903