Serine hydroxymethyltransferase, cytosolic (SHMT1)
The protein contains 483 amino acids for an estimated molecular weight of 53083 Da.
Interconversion of serine and glycine (PubMed:8505317, PubMed:24698160). (updated: Oct. 25, 2017)
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.
- 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.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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 |
|---|---|
| dbSNP:rs7215148 | |
| dbSNP:rs1979277 |
Biological Process
Carnitine biosynthetic process
Cellular nitrogen compound metabolic process
Cellular response to leukemia inhibitory factor
Cellular response to tetrahydrofolate
DTMP biosynthetic process
Folic acid metabolic process
Glycine biosynthetic process from serine
Glycine metabolic process
L-serine catabolic process
L-serine metabolic process
Negative regulation of translation
One-carbon metabolic process
Protein homotetramerization
Protein tetramerization
Purine nucleobase biosynthetic process
Small molecule metabolic process
Tetrahydrofolate interconversion
Tetrahydrofolate metabolic process
Vitamin metabolic process
Water-soluble vitamin metabolic process
Molecular Function
Amino acid binding
Cobalt ion binding
Glycine hydroxymethyltransferase activity
Identical protein binding
L-allo-threonine aldolase activity
MRNA 5'-UTR binding
Protein homodimerization activity
Pyridoxal phosphate binding
Serine binding
Small molecule binding
Translation repressor activity, mRNA regulatory element binding
Zinc ion binding
The reference OMIM entry for this protein is 182144
Serine hydroxymethyltransferase, cytosolic; shmt1
Serine hydroxymethyltransferase (SHMT), a pyridoxal phosphate-containing enzyme, catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. Some eukaryotic cells, including human cells, contain both cytosolic and mitochondrial forms of SHMT (summary by Garrow et al., 1993).
CLONING
Garrow et al. (1993) cloned human cDNAs for cytosolic and mitochondrial SHMT (SHMT2; 138450) by functional complementation of an Escherichia coli glyA mutant with a human cDNA library. The cDNA for the cytosolic enzyme encoded a 483-residue protein of M(r) 53,020. The deduced protein sequence shared 63% identity with that of the SHMT2 protein.MAPPING
By isotopic in situ hybridization, Garrow et al. (1993) assigned the cytosolic and mitochondrial SHMT genes to 17p11.2 and 12q13, respectively. The high degree of nucleotide sequence identity between the 2 isozymes as well as the presence of keratin genes in both chromosomal regions was consistent with these regions of chromosomes 12 and 17 having arisen by a duplication event. - Pseudogene Byrne et al. (1996) described an SHMT pseudogene with 90% identity to SHMT cDNA. By fluorescence in situ hybridization, they mapped the pseudogene to 1p33-p32.3.GENE FUNCTION
Folate-dependent one-carbon metabolism is critical for the synthesis of numerous cellular constituents required for cell growth, and SHMT is central to this process. Elsea et al. (1995) found that the SHMT1 gene maps to the critical interval for Smith-Magenis syndrome (SMS; 182290) on 17p11.2. They found that the gene spans approximately 40 kb. It was found to be deleted in all 26 SMS patients examined by PCR, fluorescence in situ hybridization, and/or Southern analysis. Furthermore, haploinsufficiency was indicated by the fact that SHMT enzyme activity in patient lymphoblasts was approximately 50% that of unaffected parent lymphoblasts. They suggested that haploinsufficiency may play a role in the SMS phenotype and that this finding may point to possible therapeutic interventions. ... More on the omim web site
Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 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 182144 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed