UniProt ID | ELM1_YEAST | |
---|---|---|
UniProt AC | P32801 | |
Protein Name | Serine/threonine-protein kinase ELM1 | |
Gene Name | ELM1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 640 | |
Subcellular Localization | ||
Protein Description | Important role in G1 events required for bud emergence and septin organization. Coordinates cell growth and cell division at G2/M, essential for efficient cytokinesis and for regulation of SWE1.. | |
Protein Sequence | MSPRQLIPTLIPEWAPLSQQSCIREDELDSPPITPTSQTSSFGSSFSQQKPTYSTIIGENIHTILDEIRPYVKKITVSDQDKKTINQYTLGVSAGSGQFGYVRKAYSSTLGKVVAVKIIPKKPWNAQQYSVNQVMRQIQLWKSKGKITTNMSGNEAMRLMNIEKCRWEIFAASRLRNNVHIVRLIECLDSPFSESIWIVTNWCSLGELQWKRDDDEDILPQWKKIVISNCSVSTFAKKILEDMTKGLEYLHSQGCIHRDIKPSNILLDEEEKVAKLSDFGSCIFTPQSLPFSDANFEDCFQRELNKIVGTPAFIAPELCHLGNSKRDFVTDGFKLDIWSLGVTLYCLLYNELPFFGENEFETYHKIIEVSLSSKINGNTLNDLVIKRLLEKDVTLRISIQDLVKVLSRDQPIDSRNHSQISSSSVNPVRNEGPVRRFFGRLLTKKGKKKTSGKGKDKVLVSATSKVTPSIHIDEEPDKECFSTTVLRSSPDSSDYCSSLGEEAIQVTDFLDTFCRSNESLPNLTVNNDKQNSDMKTDRSESSSHSSLKIPTPIKAMIRLKSSPKENGNRTHINCSQDKPSSPLMDRTVGKRTVNNSGARKLAHSSNILNFKAYINSEDSDIRETVEDVKTYLNFADNGQI | |
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 |
---|---|---|---|---|---|
148 | Phosphorylation | WKSKGKITTNMSGNE HHCCCCEEECCCHHH | 18.66 | 22369663 | |
149 | Phosphorylation | KSKGKITTNMSGNEA HCCCCEEECCCHHHH | 32.19 | 22369663 | |
152 | Phosphorylation | GKITTNMSGNEAMRL CCEEECCCHHHHHHH | 40.30 | 22369663 | |
414 | Phosphorylation | SRDQPIDSRNHSQIS CCCCCCCCCCCCCCC | 35.38 | 28889911 | |
461 | Phosphorylation | GKDKVLVSATSKVTP CCCEEEEEECCCCCC | 22.97 | 30377154 | |
467 | Phosphorylation | VSATSKVTPSIHIDE EEECCCCCCCCCCCC | 18.30 | 27717283 | |
469 | Phosphorylation | ATSKVTPSIHIDEEP ECCCCCCCCCCCCCC | 19.89 | 28889911 | |
516 | Phosphorylation | FLDTFCRSNESLPNL HHHHHHCCCCCCCCC | 46.24 | 22369663 | |
519 | Phosphorylation | TFCRSNESLPNLTVN HHHCCCCCCCCCEEC | 54.07 | 22369663 | |
524 | Phosphorylation | NESLPNLTVNNDKQN CCCCCCCEECCCCCC | 28.03 | 22369663 | |
541 | Phosphorylation | MKTDRSESSSHSSLK CCCCCCCCCCCCCCC | 38.09 | 21440633 | |
542 | Phosphorylation | KTDRSESSSHSSLKI CCCCCCCCCCCCCCC | 28.19 | 21440633 | |
543 | Phosphorylation | TDRSESSSHSSLKIP CCCCCCCCCCCCCCC | 36.35 | 21440633 | |
545 | Phosphorylation | RSESSSHSSLKIPTP CCCCCCCCCCCCCCC | 39.04 | 21440633 | |
546 | Phosphorylation | SESSSHSSLKIPTPI CCCCCCCCCCCCCCC | 28.40 | 21440633 | |
551 | Phosphorylation | HSSLKIPTPIKAMIR CCCCCCCCCCHHHEE | 40.91 | 28889911 | |
561 | Phosphorylation | KAMIRLKSSPKENGN HHHEEECCCCCCCCC | 57.37 | 30377154 | |
562 | Phosphorylation | AMIRLKSSPKENGNR HHEEECCCCCCCCCC | 38.10 | 24930733 | |
570 | Phosphorylation | PKENGNRTHINCSQD CCCCCCCCEEECCCC | 30.98 | 19779198 | |
580 | Phosphorylation | NCSQDKPSSPLMDRT ECCCCCCCCCCCCCC | 50.78 | 29136822 | |
581 | Phosphorylation | CSQDKPSSPLMDRTV CCCCCCCCCCCCCCC | 30.49 | 29136822 | |
596 | Phosphorylation | GKRTVNNSGARKLAH CCCCCCCHHHHHHCH | 28.73 | 28889911 | |
616 | Phosphorylation | NFKAYINSEDSDIRE CEEEECCCCCCCHHH | 32.97 | 30377154 | |
619 | Phosphorylation | AYINSEDSDIRETVE EECCCCCCCHHHHHH | 30.77 | 30377154 |
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 ELM1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ELM1_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 ELM1_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-152 AND SER-519, ANDMASS SPECTROMETRY. |