UniProt ID | LCP5_YEAST | |
---|---|---|
UniProt AC | P40079 | |
Protein Name | U3 small nucleolar ribonucleoprotein protein LCP5 | |
Gene Name | LCP5 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 357 | |
Subcellular Localization | Nucleus, nucleolus. | |
Protein Description | Component of the U3 small nucleolar ribonucleoprotein. Required for the early cleavages at sites A0, A1 and A2 of the pre-ribosomal RNA. Participates in ribosome biogenesis.. | |
Protein Sequence | MSELNALLKDINGSLTATSESLERLSGIYSNSATDEIPESNQLHEHLFYDAKKPAEKVSLLSLKNGSMLGYINSLLMLIGNRLDDECKDPSAMDARERSIQHRVVLERGVKPLEKKLAYQLDKLTRAYVKMEKEYKDAEKRALEKSTLVNHSGNDDSEDDESSEDEIAYRPNTSGIINTNKKSSAYRVEETAKQENGEENDDNETGVYKPPKITAVLPPQQTHFEDRFDAREHKDRSNKSRMQAMEEYIRESSDQPDWSASIGADIVNHGRGGIKSLRDTEKERRVTSFEEDNFTRLNITNKAEKRKQKQRERNARMNVIGGEDFGIFSSKRKLEDSTSRRGAKKTRSAWDRAQRRL | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MSELNALLK ------CHHHHHHHH | 51.28 | 22814378 | |
2 | Phosphorylation | ------MSELNALLK ------CHHHHHHHH | 51.28 | 29136822 | |
14 | Phosphorylation | LLKDINGSLTATSES HHHHHCCCCEECHHH | 20.33 | 29136822 | |
16 | Phosphorylation | KDINGSLTATSESLE HHHCCCCEECHHHHH | 29.59 | 29136822 | |
18 | Phosphorylation | INGSLTATSESLERL HCCCCEECHHHHHHH | 28.00 | 29136822 | |
19 | Phosphorylation | NGSLTATSESLERLS CCCCEECHHHHHHHH | 23.79 | 29136822 | |
21 | Phosphorylation | SLTATSESLERLSGI CCEECHHHHHHHHCC | 34.98 | 29136822 | |
123 | Acetylation | KLAYQLDKLTRAYVK HHHHHHHHHHHHHHH | 61.42 | 24489116 | |
146 | Phosphorylation | EKRALEKSTLVNHSG HHHHHHHHCCCCCCC | 20.00 | 21440633 | |
147 | Phosphorylation | KRALEKSTLVNHSGN HHHHHHHCCCCCCCC | 45.88 | 21440633 | |
152 | Phosphorylation | KSTLVNHSGNDDSED HHCCCCCCCCCCCCC | 33.80 | 22890988 | |
157 | Phosphorylation | NHSGNDDSEDDESSE CCCCCCCCCCCCCCH | 45.87 | 22890988 | |
162 | Phosphorylation | DDSEDDESSEDEIAY CCCCCCCCCHHHHCC | 46.12 | 22890988 | |
163 | Phosphorylation | DSEDDESSEDEIAYR CCCCCCCCHHHHCCC | 47.20 | 22890988 | |
169 | Phosphorylation | SSEDEIAYRPNTSGI CCHHHHCCCCCCCCC | 32.06 | 19795423 | |
173 | Phosphorylation | EIAYRPNTSGIINTN HHCCCCCCCCCCCCC | 30.89 | 19795423 | |
174 | Phosphorylation | IAYRPNTSGIINTNK HCCCCCCCCCCCCCC | 34.34 | 19795423 | |
179 | Phosphorylation | NTSGIINTNKKSSAY CCCCCCCCCCCCCCE | 37.70 | 19795423 | |
191 | Phosphorylation | SAYRVEETAKQENGE CCEEHHHHHHHHCCC | 26.16 | 25704821 | |
252 | Phosphorylation | MEEYIRESSDQPDWS HHHHHHHCCCCCCCC | 29.39 | 30377154 | |
253 | Phosphorylation | EEYIRESSDQPDWSA HHHHHHCCCCCCCCH | 35.20 | 30377154 | |
275 | Acetylation | NHGRGGIKSLRDTEK CCCCCCCHHHCCCHH | 46.87 | 25381059 | |
276 | Phosphorylation | HGRGGIKSLRDTEKE CCCCCCHHHCCCHHH | 27.07 | 30377154 | |
287 | Phosphorylation | TEKERRVTSFEEDNF CHHHHCCCCCCCCCC | 26.36 | 23749301 | |
288 | Phosphorylation | EKERRVTSFEEDNFT HHHHCCCCCCCCCCH | 28.01 | 25533186 | |
329 | Phosphorylation | GEDFGIFSSKRKLED CCCCCCCCCCCCCCC | 32.79 | 30377154 | |
331 | Acetylation | DFGIFSSKRKLEDST CCCCCCCCCCCCCCC | 52.97 | 25381059 | |
333 | Acetylation | GIFSSKRKLEDSTSR CCCCCCCCCCCCCCH | 61.02 | 25381059 |
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 LCP5_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LCP5_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 LCP5_YEAST !! |
Kegg Drug | ||||||
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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 SER-14 AND SER-288, AND MASSSPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND MASSSPECTROMETRY. |