| Type | Description |
|---|---|
| Definition | crystallin alpha A |
| Date | Results | Publications |
|---|---|---|
| 2016-11-05 12:14:00 | Data show that both green and red light wavelengths induce structural changes in betaL-crystalline. | 26656181 |
| 2014-10-11 11:00:00 | For moderate O-GlcNAcylation on bovine crystalline alpha, the preferred amino acids were Pro > Ala > Gly at position -2, Ala > Thr >Val > Lys > Pro at position -1, and Ala > Gly > Arg > Glu at position +2. | 24760753 |
| 2013-06-01 10:02:00 | We show that proteases with the potential to generate alphaA-66-80 peptide are present in bovine and human lenses. | 23410823 |
| 2011-09-03 10:41:00 | These results show that between pH 7 and 10 the protein undergoes a reversible thermal transition. | 21445944 |
| 2011-06-04 10:51:00 | alpha-crystallin is characterized by homogeneous distribution of scattering density in the domains inaccessible for water penetration | 21314599 |
| Type | IDs |
|---|---|
| Gene |
UniProtKB-ID:
CRYAA_BOVIN
UniprotKB:
P02470
UniParc:
UPI0000128370
EMBL:
M26142
Ensembl:
ENSBTAG00000003134
KO:
bta:281718
|
| Nucleutide sequences |
EMBL-CDS:
AAA30471.1
Ensembl_TRS:
ENSBTAT00000004073
|
| Protein sequencees |
Ensembl_PRO:
ENSBTAP00000004073
RefSeq:
NP_776714.1
|
| Others |
UniRef100:
UniRef100_P02470
UniRef90:
UniRef90_P02470
UniRef50:
UniRef50_P02470
UniGene:
Bt.397
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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