Pterin-4-alpha-carbinolamine dehydratase 2 (PCBD2)
The protein contains 130 amino acids for an estimated molecular weight of 14365 Da.
Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2 (By similarity).', 'Regulates the dimerization of homeodomain protein HNF-1-alpha and enhances its transcriptional activity. (updated: April 1, 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.
(right-click above to access to more options from the contextual menu)
No binding partner found
The reference OMIM entry for this protein is 609836
Pterin-4-alpha-carbinolamine dehydratase 2; pcbd2
Dimerization cofactor of hepatocyte nuclear factor 1-alpha 2; dcoh2
Dimerization cofactor of hepatocyte nuclear factor 1 from muscle; dcohm
CLONING
Using MIRK (DYRK1B; 604556) as bait in a yeast 2-hybrid screen of a human skeletal muscle cDNA library, Lim et al. (2002) identified PCBD2, which they called DCOHM, encoding a deduced 103-amino acid protein. The DCOHM protein shares 78% sequence identity with DCOH (PCBD1; 126090). Rose et al. (2004) identified the mouse homolog and determined the high-resolution crystal structure of Dcoh2. Dcoh1 and Dcoh2 dimers adopt the same fold, and their structural differences are confined largely to the protein surfaces and tetramer interface.GENE FUNCTION
Using coimmunoprecipitation studies and GST pull-down assays, Lim et al. (2002) confirmed the interaction of MIRK and DCOHM. DCOH stabilizes HNF1-alpha (142410) as a dimer and enhances its transcriptional activity. Using a reporter gene construct, Lim et al. (2002) showed that DCOHM has a similar activity. In GST pull-down assays, Lim et al. (2002) found that DCOHM, MIRK, and HNF1-alpha form a complex, and that a direct interaction between MIRK and HNF1-alpha can occur in the absence of DCOHM. Lim et al. (2002) concluded that MIRK binds to DCOHM in a DCOHM/HNF1-alpha tetramer, enabling it to bind and phosphorylate HNF1-alpha. Rose et al. (2004) compared the properties of mouse Dcoh1 with those of Dcoh2. Like Dcoh1, Dcoh2 forms a tetramer, displays pterin-4-alpha-carbinolamine dehydratase activity, and binds Hnf1-alpha in vitro and in vivo. Deletion mutant experiments demonstrated that Dcoh2 binds to the N-terminal dimerization domain of Hnf1-alpha. Unlike the hyperstable Dcoh1 tetramer, Dcoh2 readily disproportionates and forms a 2:2 complex with Hnf1-alpha in vitro. Rose et al. (2004) measured the exchange of monomers in preformed Hnf1-alpha dimers and found that both Dcoh1 and Dcoh2 stabilize Hnf1-alpha dimers.MAPPING
By sequence analysis, Rose et al. (2004) mapped the DCOHM gene to chromosome 5q31.2. ... 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
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 609836 was added.