Cystatin-B (CSTB)
The protein contains 98 amino acids for an estimated molecular weight of 11140 Da.
This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| EPM1 |
Biological Process
Adult locomotory behavior
Negative regulation of endopeptidase activity
Negative regulation of peptidase activity
Negative regulation of proteolysis
Neutrophil degranulation
Regulation of apoptotic process
The reference OMIM entry for this protein is 254800
Myoclonic epilepsy of unverricht and lundborg
Uld
Epilepsy, progressive myoclonic, 1a; epm1a
Epilepsy, progressive myoclonic, 1; epm1
Progressive myoclonic epilepsy; pme
Baltic myoclonic epilepsy
A number sign (#) is used with this entry because myoclonic epilepsy of Unverricht and Lundborg (ULD), also known as progressive myoclonic epilepsy-1A (EPM1A), is caused by mutation in the cystatin B gene (CSTB; 601145) on chromosome 21q22.
DESCRIPTION
Myoclonic epilepsy of Unverricht and Lundborg is an autosomal recessive disorder characterized by onset of neurodegeneration between 6 and 13 years of age. Although it is considered a progressive myoclonic epilepsy, it differs from other forms in that is appears to be progressive only in adolescence, with dramatic worsening of myoclonus and ataxia in the first 6 years after onset. The disease stabilizes in early adulthood, and myoclonus and ataxia may even improve, and there is minimal to no cognitive decline (summary by Ramachandran et al., 2009). - Genetic Heterogeneity of Progressive Myoclonic Epilepsy Progressive myoclonic epilepsy refers to a clinically and genetically heterogeneous group of neurodegenerative disorders, usually with debilitating symptoms, although severity varies. See also EPM1B (612437), caused by mutation in the PRICKLE1 gene (608500); Lafora disease (EPM2A/B; 254780), caused by mutation in either the EPM2A (607566) or the NHLRC1 (608072) gene; EPM3 (611726), caused by mutation in the KCTD7 gene (611725); EPM4 (254900), caused by mutation in the SCARB2 gene (602257); EPM5 (613832), caused by mutation in the PRICKLE2 gene (608501); EPM6 (614018), caused by mutation in the GOSR2 gene (604027); and EPM7 (616187), caused by mutation in the KCNC1 gene (176258). Other disorders characterized by progressive myoclonic epilepsy include the neuronal ceroid lipofuscinoses (see, e.g., CLN1; 256730); sialidosis (256550); MERFF (545000); and DRPLA (125370), among others (reviews by Ramachandran et al., 2009 and Mendonca de Siqueira, 2010).CLINICAL FEATURES
Unverricht (1891, 1895) and Lundborg (1903) first reported a type of progressive myoclonic epilepsy common in Finland. Onset of the disorder occurred around age 10 years, and was characterized by progressive myoclonus resulting in incapacitation, but only mild mental deterioration. Histological studies of the brain showed 'degenerative' changes without inclusion bodies. Severity and survival were variable (Norio and Koskiniemi, 1979). Eldridge et al. (1981, 1983) referred to this disorder as the 'Baltic type' of myoclonic epilepsy because the descriptions first by Unverricht and then by Lundborg were in families from Estonia and Eastern Sweden and subsequent patients were found in Finland. Eldridge et al. (1983) found 15 families in the United States. The 27 affected members had the following features starting at about age 10 years: stimulus- and photo-sensitive and occasionally violent myoclonus, usually worse upon waking; generalized tonic-clonic seizures, sometimes associated with absence attacks; and light-sensitive, generally synchronous, spike-and-wave discharges on EEG that preceded clinical manifestations. Necropsy showed marked loss of Purkinje cells of the cerebellum, but no inclusion bodies. Phenytoin was associated with progressive motor and intellectual deterioration, marked ataxia, and even death. Treatment with valproic acid was associated with marked improvement. Contrary to myoclonic epilepsy with Lafora bodies, intelligence in this form was only slightly affected and psychotic symptoms were not found. In addition, Lafora body disease is invariably fatal. Kyllerman et al. (1991) describe ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 254800 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed