UniProt ID | LRG1_YEAST | |
---|---|---|
UniProt AC | P35688 | |
Protein Name | Rho-GTPase-activating protein LRG1 | |
Gene Name | LRG1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1017 | |
Subcellular Localization | Cytoplasm. Bud. Bud neck. Localized to the bud site during bud formation and at the bud neck during cytokinesis. | |
Protein Description | Acts in signal transduction. Activates CDC42, RHO1 and RHO2. Negatively regulates 1,3-beta-glucan synthesis. May be responsible for the down-regulation of CDC42 during mating.. | |
Protein Sequence | MIQNSAGYRSLNTASPMTVQVKNQKKICARCNKLVIPDSQRTKTTLKALGKYYHESCFTCQDCQKPLKPKYFPYQVDKTSESILLCQYDYFRRHNLLCHVCDTPLRGLYYTAFGYRYDEEHFSCTICATPCGVKKCFMYGNQLYCKYHFLKYFSKRCKGCEFPISDQYIEFPKGEEIHCWHPECYGIHKYWHVNLAAETVGLQYLPKLEYNPNSGDKDINPTAYELDKQMQAFNFILSKTWSVLYRFEEEAASCISDMFQYLTSNDQLKGIESTGLLVLKIDCLFRGLDTLNLSTNKSMPVNSDQECIENNAMAASKYSKFPKNLSTKIMIYLQLLRKLGTENKNETITISSFMSVITGLAHFLKLLTRFGLYTALENNKLTHSVNPLLRFLREVEKNELFENNPFQYIKTPVNATDSCAGCNKYIQEECIQFYEHRWHIACFTCSSCHKNINPRSLTDPTFNKEKKKILCSHCSIDDPASVPGFKFVTKLAQLIFLLKIALVKSRTVMLKSKASNKVGRNSLQSTMLKEQTYIRTLNDIKRLRSRRESVRVTHNKQQARKSVILETAETDLNDPTKQGDSKNLVIQTDDPSSSQQVSTRENVFSNTKTLTLDDISRIVAAEQARELRPNAFAHFKKLKETDDETSNVVPKKSGVYYSELSTMELSMIRAISLSLLAGKQLISKTDPNYTSLVSMVFSNEKQVTGSFWNRMKIMMSMEPKKPITKTVFGAPLDVLCEKWGVDSDLGVGPVKIRIPIIIDELISSLRQMDMSVEGIFRKNGNIRRLRELTANIDSNPTEAPDFSKENAIQLSALLKKFIRELPQPILSTDLYELWIKAAKIDLEDEKQRVILLIYSLLPTYNRNLLEALLSFLHWTSSFSYIENEMGSKMDIHNLSTVITPNILYLRHKEISNDNVPDEPESGLVDSFAQNKGENYFLAIEIVDYLITHNEEMAMVPKFLMNLLKDVQLQKLDNYESINHFISTVMQSKTIDYSECDIKTPVTVKDSTTTVIQGEINK | |
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 |
---|---|---|---|---|---|
1 | Acetylation | -------MIQNSAGY -------CCCCCCCC | 33.30 | 22814378 | |
15 | Phosphorylation | YRSLNTASPMTVQVK CCCCCCCCCCEEEEC | 17.11 | 22369663 | |
18 | Phosphorylation | LNTASPMTVQVKNQK CCCCCCCEEEECCHH | 15.92 | 22369663 | |
269 | Acetylation | LTSNDQLKGIESTGL HCCCHHHCCHHHCCE | 52.81 | 25381059 | |
303 | Phosphorylation | NKSMPVNSDQECIEN CCCCCCCCCHHHHHH | 40.69 | 23749301 | |
512 | Phosphorylation | SRTVMLKSKASNKVG CCCCHHCCCCCCCCC | 29.50 | 27017623 | |
515 | Phosphorylation | VMLKSKASNKVGRNS CHHCCCCCCCCCHHH | 40.70 | 27017623 | |
522 | Phosphorylation | SNKVGRNSLQSTMLK CCCCCHHHHHHHHHH | 26.82 | 21440633 | |
525 | Phosphorylation | VGRNSLQSTMLKEQT CCHHHHHHHHHHHHH | 22.52 | 21440633 | |
526 | Phosphorylation | GRNSLQSTMLKEQTY CHHHHHHHHHHHHHH | 17.35 | 27017623 | |
562 | Phosphorylation | NKQQARKSVILETAE CHHHHHHEEEEEEEC | 14.61 | 21551504 | |
567 | Phosphorylation | RKSVILETAETDLND HHEEEEEEECCCCCC | 26.75 | 30377154 | |
582 | Ubiquitination | PTKQGDSKNLVIQTD CCCCCCCCCEEEECC | 60.07 | 23749301 | |
588 | Phosphorylation | SKNLVIQTDDPSSSQ CCCEEEECCCCCCCC | 31.11 | 30377154 | |
593 | Phosphorylation | IQTDDPSSSQQVSTR EECCCCCCCCCCCCC | 37.24 | 23749301 | |
605 | Phosphorylation | STRENVFSNTKTLTL CCCCCCCCCCCEEEH | 39.03 | 24603354 | |
607 | Phosphorylation | RENVFSNTKTLTLDD CCCCCCCCCEEEHHH | 24.98 | 26447709 | |
609 | Phosphorylation | NVFSNTKTLTLDDIS CCCCCCCEEEHHHHH | 23.96 | 26447709 | |
611 | Phosphorylation | FSNTKTLTLDDISRI CCCCCEEEHHHHHHH | 33.11 | 26447709 | |
641 | Phosphorylation | HFKKLKETDDETSNV HHHHHHCCCCCCCCC | 47.35 | 27717283 | |
645 | Phosphorylation | LKETDDETSNVVPKK HHCCCCCCCCCCCCC | 32.37 | 27017623 | |
646 | Phosphorylation | KETDDETSNVVPKKS HCCCCCCCCCCCCCC | 26.11 | 23749301 | |
771 | Phosphorylation | SLRQMDMSVEGIFRK HHHHCCCCHHHHHHC | 16.86 | 30377154 | |
811 | Phosphorylation | KENAIQLSALLKKFI HHHHHHHHHHHHHHH | 10.65 | 30377154 | |
895 | Phosphorylation | KMDIHNLSTVITPNI CEECCCHHHCCCCCE | 26.41 | 28889911 | |
896 | Phosphorylation | MDIHNLSTVITPNIL EECCCHHHCCCCCEE | 21.06 | 28889911 | |
974 | Phosphorylation | QLQKLDNYESINHFI CHHHCCCHHHHHHHH | 15.66 | 28889911 | |
982 | Phosphorylation | ESINHFISTVMQSKT HHHHHHHHHHHCCCC | 17.63 | 28889911 | |
983 | Phosphorylation | SINHFISTVMQSKTI HHHHHHHHHHCCCCC | 18.38 | 28889911 | |
987 | Phosphorylation | FISTVMQSKTIDYSE HHHHHHCCCCCCCCC | 17.42 | 28889911 | |
993 | Phosphorylation | QSKTIDYSECDIKTP CCCCCCCCCCCCCCC | 28.18 | 23749301 | |
998 | Ubiquitination | DYSECDIKTPVTVKD CCCCCCCCCCEEECC | 33.26 | 23749301 | |
999 | Phosphorylation | YSECDIKTPVTVKDS CCCCCCCCCEEECCC | 24.27 | 23749301 | |
1002 | Phosphorylation | CDIKTPVTVKDSTTT CCCCCCEEECCCCCE | 24.04 | 21551504 |
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 LRG1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of LRG1_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 LRG1_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-562, AND MASSSPECTROMETRY. |