Open ValWood opened 1 week ago
Lipidation IMPORTED???
We're not loading the Lipidation data. Here's a sample of what it looks like. There are only 51 genes from UniProt that have this field:
LIPID 485; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255"
LIPID 202; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250|UniProtKB:P62745"
LIPID 404; /note="S-farnesyl cysteine"; /evidence="ECO:0000250"
LIPID 116; /note="Phosphatidylethanolamine amidated glycine"; /evidence="ECO:0000250|UniProtKB:P38182"
LIPID 182; /note="S-farnesyl cysteine"; /evidence="ECO:0000250"
LIPID 203; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250|UniProtKB:P36586"; LIPID 205; /note="S-geranylgeranyl cysteine"; /evi…
LIPID 216; /note="S-farnesyl cysteine"; /evidence="ECO:0000250"
LIPID 202; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000269|PubMed:1597466"; LIPID 203; /note="S-geranylgeranyl cysteine"; /evide…
LIPID 199; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250"; LIPID 201; /note="S-geranylgeranyl cysteine"; /evidence="ECO:000025…
LIPID 213; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000269|PubMed:1597466"; LIPID 214; /note="S-geranylgeranyl cysteine"; /evide…
LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000250"; LIPID 3; /note="S-palmitoyl cysteine"; /evidence="ECO:0000250"
LIPID 189; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250"
LIPID 2; /note="N-myristoyl glycine"; /evidence="ECO:0000269|PubMed:14722091"
LIPID 199; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250"
LIPID 197; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250"
LIPID 200; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250"
LIPID 199; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255"
LIPID 206; /note="S-geranylgeranyl cysteine"; /evidence="ECO:0000250|UniProtKB:P36586"; LIPID 208; /note="S-geranylgeranyl cysteine"; /evi…
LIPID 516; /note="GPI-anchor amidated serine"; /evidence="ECO:0000255"
(Moved from https://github.com/pombase/pombase-chado/issues/52)
- Modified residue What does this provide??? how does it differ from Post-translational modification
- Post-translational modification What does this provide??? how does it differ from Modified residue
Here is a sample of the "Modified residue" data:
SPAC144.13c; │ MOD_RES 62; /note="Phosphoserine"; /evidence="ECO:0000269|PubMed:10921878"
SPBC428.11; │ MOD_RES 210; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P06721"
SPAC22A12.07c; │ MOD_RES 451; /note="Phosphothreonine"; /evidence="ECO:0000269|PubMed:18257517"
SPAC23C4.08; │ MOD_RES 202; /note="Cysteine methyl ester"; /evidence="ECO:0000250|UniProtKB:P62745"
SPAC2F3.09; │ MOD_RES 377; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250|UniProtKB:P18079"
SPAC31G5.15; │ MOD_RES 912; /note="Pyruvic acid (Ser); by autocatalysis"; /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
SPBC428.02c; │ MOD_RES 256; /note="N6-(pyridoxal phosphate)lysine"; /evidence="ECO:0000250"
SPAC10F6.09c; │ MOD_RES 105; /note="N6-acetyllysine"; /evidence="ECO:0000250"
And here is a sample of the "Post-translational modification" data. It seems to be free text notes. Some are quite long:
SPBP16F5.04; │ PTM: Autoubiquitinated at Cys-90; undergoes 'Lys-48'-linked polyubiquitination, which leads to proteasome-dependent protein degradation. {ECO:0000250|UniProtKB:Q02159}.
SPAC144.13c; │ PTM: Phosphorylated by cdc2-cdc13-CDK complex. This targets srw1 for proteolysis which in turn promotes cdc13 turnover. Dephosphorylated during G1 arrest. {ECO:0000269|PubMed:10921878, ECO:0000269|PubMed:18257517}.
SPAC11E3.13c; │ PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
SPAC14C4.09; │ PTM: Not glycosylated.
SPAC17A5.04c; │ PTM: Glycosylated. {ECO:0000269|PubMed:14871934}.
SPAC17G6.12; │ PTM: Neddylated; enhancing the ubiquitin-ligase activity. {ECO:0000250|UniProtKB:P47050}.
SPAC19G12.14; │ PTM: Phosphorylated by casein kinase I. Phosphorylation inactivates the enzyme. {ECO:0000269|PubMed:9873063}.
SPAC20G4.03c; │ PTM: Autophosphorylated.
SPAC22A12.08c; │ PTM: [Isoform 1]: Proteolytically cleaved, presumably during its import into the mitochondrion by mitochondrial processing peptidase. {ECO:0000269|PubMed:29958934}.
SPAC23C4.08; │ PTM: Palmitoylated by the erf2-erf4 complex. {ECO:0000269|PubMed:23843742}.
SPCC962.02c; │ PTM: Phosphorylated by ark1. {ECO:0000269|PubMed:11950927}.
SPAC31G5.15; │ PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the c…
SPAC31G5.18c; │ PTM: The N-terminal UBL (ubiquitin-like) propeptide is cleaved at Gly-84 by the deubiquitinating enzymes ubp5 and ubp15; the resulting mature sde2 associates with spliceosomes. {ECO:0000269|PubMed:28947618, ECO:0000269|PubMed:36095128}.; PTM: Polyubiquitinated; ubiquitination is partially dependent on ubr11. {ECO:0000269|PubMed:28947618}.
SPAC3A11.08; │ PTM: Neddylated; enhancing the ubiquitin-ligase activity. {ECO:0000250|UniProtKB:P47050}.
SPAC56E4.06c; │ PTM: Cleaved by autocatalysis into a large and a small subunit. {ECO:0000250}.
SPAC6B12.11; │ PTM: Phosphorylated by cdc2 at the onset of S-phase. {ECO:0000269|PubMed:11937031, ECO:0000269|PubMed:18257517}.
SPAC9E9.11; │ PTM: The N-terminus is blocked. {ECO:0000269|PubMed:10438489}.
SPBC16E9.18; │ PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the c…
SPBC30D10.10c; │ PTM: Phosphorylation at Thr-1972 in the ATP-binding region by AKT1 strongly reduces kinase activity. {ECO:0000269|PubMed:24247430}.
(Moved from #52)
We're not loading the Lipidation data.
Moved to pombase/pombase-chado#1220 and now done.
It would be good to know what these include so we can see if they are useful