UniProt ID | LCB1_YEAST | |
---|---|---|
UniProt AC | P25045 | |
Protein Name | Serine palmitoyltransferase 1 | |
Gene Name | LCB1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 558 | |
Subcellular Localization |
Cytoplasm. Endoplasmic reticulum membrane Multi-pass membrane protein. |
|
Protein Description | Component of serine palmitoyltransferase (SPT), which catalyzes the committed step in the synthesis of sphingolipids, the condensation of serine with palmitoyl CoA to form the long chain base 3-ketosphinganine.. | |
Protein Sequence | MAHIPEVLPKSIPIPAFIVTTSSYLWYYFNLVLTQIPGGQFIVSYIKKSHHDDPYRTTVEIGLILYGIIYYLSKPQQKKSLQAQKPNLSPQEIDALIEDWEPEPLVDPSATDEQSWRVAKTPVTMEMPIQNHITITRNNLQEKYTNVFNLASNNFLQLSATEPVKEVVKTTIKNYGVGACGPAGFYGNQDVHYTLEYDLAQFFGTQGSVLYGQDFCAAPSVLPAFTKRGDVIVADDQVSLPVQNALQLSRSTVYYFNHNDMNSLECLLNELTEQEKLEKLPAIPRKFIVTEGIFHNSGDLAPLPELTKLKNKYKFRLFVDETFSIGVLGATGRGLSEHFNMDRATAIDITVGSMATALGSTGGFVLGDSVMCLHQRIGSNAYCFSACLPAYTVTSVSKVLKLMDSNNDAVQTLQKLSKSLHDSFASDDSLRSYVIVTSSPVSAVLHLQLTPAYRSRKFGYTCEQLFETMSALQKKSQTNKFIEPYEEEEKFLQSIVDHALINYNVLITRNTIVLKQETLPIVPSLKICCNAAMSPEELKNACESVKQSILACCQESNK | |
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 |
---|---|---|---|---|---|
121 | Phosphorylation | QSWRVAKTPVTMEMP HCEEEEECCEEEEEC | 17.16 | 17330950 | |
143 | Ubiquitination | TRNNLQEKYTNVFNL ECCCHHHHHHHHHHH | 44.40 | 17644757 | |
165 | Ubiquitination | LSATEPVKEVVKTTI EECCCCHHHHHHHHH | 56.35 | 17644757 | |
169 | Ubiquitination | EPVKEVVKTTIKNYG CCHHHHHHHHHHHCC | 45.16 | 17644757 | |
251 | Phosphorylation | NALQLSRSTVYYFNH HHHHHHCCEEEEECC | 20.88 | 28889911 | |
252 | Phosphorylation | ALQLSRSTVYYFNHN HHHHHCCEEEEECCC | 16.06 | 28889911 | |
272 | Phosphorylation | ECLLNELTEQEKLEK HHHHHHHCHHHHHHC | 29.46 | 28889911 | |
286 | Ubiquitination | KLPAIPRKFIVTEGI CCCCCCCCEEEEECC | 33.80 | 17644757 | |
308 | Ubiquitination | APLPELTKLKNKYKF CCCHHHHHCCCCEEE | 70.82 | 17644757 | |
398 | Ubiquitination | YTVTSVSKVLKLMDS EEHHCHHHHHHHHCC | 49.81 | 17644757 | |
401 | Ubiquitination | TSVSKVLKLMDSNND HCHHHHHHHHCCCCH | 44.76 | 23749301 | |
401 | Acetylation | TSVSKVLKLMDSNND HCHHHHHHHHCCCCH | 44.76 | 24489116 | |
415 | Acetylation | DAVQTLQKLSKSLHD HHHHHHHHHHHHHHH | 58.82 | 24489116 | |
457 | Ubiquitination | TPAYRSRKFGYTCEQ CHHHHHHCCCCCHHH | 44.37 | 17644757 | |
470 | Phosphorylation | EQLFETMSALQKKSQ HHHHHHHHHHHHHHH | 32.99 | 21440633 | |
474 | Ubiquitination | ETMSALQKKSQTNKF HHHHHHHHHHHCCCC | 56.07 | 17644757 | |
475 | Ubiquitination | TMSALQKKSQTNKFI HHHHHHHHHHCCCCC | 34.53 | 17644757 | |
518 | Phosphorylation | TIVLKQETLPIVPSL EEEECCCCCCCCCHH | 35.03 | 19795423 | |
524 | Phosphorylation | ETLPIVPSLKICCNA CCCCCCCHHHHHHCC | 31.25 | 19823750 | |
539 | Ubiquitination | AMSPEELKNACESVK CCCHHHHHHHHHHHH | 45.86 | 23749301 |
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 LCB1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LCB1_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 LCB1_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-121, AND MASSSPECTROMETRY. |