UniProt ID | DHH1_YEAST | |
---|---|---|
UniProt AC | P39517 | |
Protein Name | ATP-dependent RNA helicase DHH1 {ECO:0000305} | |
Gene Name | DHH1 {ECO:0000303|PubMed:8511971} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 506 | |
Subcellular Localization | Cytoplasm, P-body . | |
Protein Description | ATP-dependent RNA helicase involved in mRNA turnover, and more specifically in mRNA decapping by activating the decapping enzyme DCP1. [PubMed: 11780629] | |
Protein Sequence | MGSINNNFNTNNNSNTDLDRDWKTALNIPKKDTRPQTDDVLNTKGNTFEDFYLKRELLMGIFEAGFEKPSPIQEEAIPVAITGRDILARAKNGTGKTAAFVIPTLEKVKPKLNKIQALIMVPTRELALQTSQVVRTLGKHCGISCMVTTGGTNLRDDILRLNETVHILVGTPGRVLDLASRKVADLSDCSLFIMDEADKMLSRDFKTIIEQILSFLPPTHQSLLFSATFPLTVKEFMVKHLHKPYEINLMEELTLKGITQYYAFVEERQKLHCLNTLFSKLQINQAIIFCNSTNRVELLAKKITDLGYSCYYSHARMKQQERNKVFHEFRQGKVRTLVCSDLLTRGIDIQAVNVVINFDFPKTAETYLHRIGRSGRFGHLGLAINLINWNDRFNLYKIEQELGTEIAAIPATIDKSLYVAENDETVPVPFPIEQQSYHQQAIPQQQLPSQQQFAIPPQQHHPQFMVPPSHQQQQAYPPPQMPSQQGYPPQQEHFMAMPPGQSQPQY | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Phosphorylation | -----MGSINNNFNT -----CCCCCCCCCC | 22.35 | 22369663 | |
10 | Phosphorylation | SINNNFNTNNNSNTD CCCCCCCCCCCCCCC | 34.87 | 22369663 | |
14 | Phosphorylation | NFNTNNNSNTDLDRD CCCCCCCCCCCCCCH | 43.14 | 22369663 | |
16 | Phosphorylation | NTNNNSNTDLDRDWK CCCCCCCCCCCCHHH | 37.45 | 22369663 | |
30 | Acetylation | KTALNIPKKDTRPQT HHHHCCCCCCCCCCC | 60.53 | 25381059 | |
54 | 2-Hydroxyisobutyrylation | TFEDFYLKRELLMGI CHHHHHHHHHHHHHH | 32.23 | - | |
54 | Acetylation | TFEDFYLKRELLMGI CHHHHHHHHHHHHHH | 32.23 | 24489116 | |
54 | Succinylation | TFEDFYLKRELLMGI CHHHHHHHHHHHHHH | 32.23 | 23954790 | |
107 | Acetylation | FVIPTLEKVKPKLNK EEECCHHHHCCCCCC | 59.68 | 24489116 | |
109 | Acetylation | IPTLEKVKPKLNKIQ ECCHHHHCCCCCCCC | 47.72 | 24489116 | |
318 | 2-Hydroxyisobutyrylation | YYSHARMKQQERNKV HHHHHHHHHHHHHHH | 43.19 | - | |
324 | Acetylation | MKQQERNKVFHEFRQ HHHHHHHHHHHHHHH | 53.12 | 22865919 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of DHH1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DHH1_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of DHH1_YEAST !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16, AND MASSSPECTROMETRY. |