| UniProt ID | ATR_YEAST | |
|---|---|---|
| UniProt AC | P38111 | |
| Protein Name | Serine/threonine-protein kinase MEC1 | |
| Gene Name | MEC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 2368 | |
| Subcellular Localization | Nucleus. Localizes to nuclear DNA repair foci in response to DNA double strand breaks. The recruitment to DNA lesion sites requires its interaction with LCD1 and the presence of the RPA complex on DNA. | |
| Protein Description | Serine/threonine protein kinase which activates checkpoint signaling upon genotoxic stresses such as ionizing radiation (IR), ultraviolet light (UV), or DNA replication stalling, thereby acting as a DNA damage sensor. Recognizes the substrate consensus sequence [ST]-Q. Recruited in complex with protein LCD1 by the single-strand-binding protein complex RPA to DNA lesions in order to initiate the DNA repair by homologous recombination, after the MRX-complex and TEL1 are displaced. Phosphorylates LCD1 and RPA2, a subunit of RPA, involved in DNA replication, repair and recombination. Phosphorylates RAD9, CHK1 and RAD53, which leads to the activation of the CHK1 and RAD53 kinases involved in DNA damage repair cascade. Phosphorylates histone H2A to form H2AS128ph (gamma-H2A) at sites of DNA damage, also involved in the regulation of DNA damage response mechanism. Phosphorylates also SLX4 and RTT107 which are proteins involved in genome stability. Required for cell growth and meiotic recombination.. | |
| Protein Sequence | MESHVKYLDELILAIKDLNSGVDSKVQIKKVPTDPSSSQEYAKSLKILNTLIRNLKDQRRNNIMKNDTIFSKTVSALALLLEYNPFLLVMKDSNGNFEIQRLIDDFLNISVLNYDNYHRIWFMRRKLGSWCKACVEFYGKPAKFQLTAHFENTMNLYEQALTEVLLGKTELLKFYDTLKGLYILLYWFTSEYSTFGNSIAFLDSSLGFTKFDFNFQRLIRIVLYVFDSCELAALEYAEIQLKYISLVVDYVCNRTISTALDAPALVCCEQLKFVLTTMHHFLDNKYGLLDNDPTMAKGILRLYSLCISNDFSKCFVDHFPIDQWADFSQSEHFPFTQLTNKALSIVYFDLKRRSLPVEALKYDNKFNIWVYQSEPDSSLKNVTSPFDDRYKQLEKLRLLVLKKFNKTERGTLLKYRVNQLSPGFFQRAGNDFKLILNEASVSIQTCFKTNNITRLTSWTVILGRLACLESEKFSGTLPNSTKDMDNWYVCHLCDIEKTGNPFVRINPNRPEAAGKSEIFRILHSNFLSHPNIDEFSESLLSGILFSLHRIFSHFQPPKLTDGNGQINKSFKLVQKCFMNSNRYLRLLSTRIIPLFNISDSHNSEDEHTATLIKFLQSQKLPVVKENLVIAWTQLTLTTSNDVFDTLLLKLIDIFNSDDYSLRIMMTLQIKNMAKILKKTPYQLLSPILPVLLRQLGKNLVERKVGFQNLIELLGYSSKTILDIFQRYIIPYAIIQYKSDVLSEIAKIMCDGDTSLINQMKVNLLKKNSRQIFAVALVKHGLFSLDILETLFLNRAPTFDKGYITAYLPDYKTLAEITKLYKNSVTKDASDSENANMILCSLRFLITNFEKDKRHGSKYKNINNWTDDQEQAFQKKLQDNILGIFQVFSSDIHDVEGRTTYYEKLRVINGISFLIIYAPKKSIISALAQISICLQTGLGLKEVRYEAFRCWHLLVRHLNDEELSTVIDSLIAFILQKWSEFNGKLRNIVYSILDTLIKEKSDLILKLKPYTTLALVGKPELGILARDGQFARMVNKIRSTTDLIPIFANNLKSSNKYVINQNLDDIEVYLRRKQTERSIDFTPKKVGQTSDITLVLGALLDTSHKFRNLDKDLCEKCAKCISMIGVLDVTKHEFKRTTYSENEVYDLNDSVQTIKFLIWVINDILVPAFWQSENPSKQLFVALVIQESLKYCGLSSESWDMNHKELYPNEAKLWEKFNSVSKTTIYPLLSSLYLAQSWKEYVPLKYPSNNFKEGYKIWVKRFTLDLLKTGTTENHPLHVFSSLIREDDGSLSNFLLPYISLDIIIKAEKGTPYADILNGIIIEFDSIFTCNLEGMNNLQVDSLRMCYESIFRVFEYCKKWATEFKQNYSKLHGTFIIKDTKTTNMLLRIDEFLRTTPSDLLAQRSLETDSFERSALYLEQCYRQNPHDKNQNGQLLKNLQITYEEIGDIDSLDGVLRTFATGNLVSKIEELQYSENWKLAQDCFNVLGKFSDDPKTTTRMLKSMYDHQLYSQIISNSSFHSSDGKISLSPDVKEWYSIGLEAANLEGNVQTLKNWVEQIESLRNIDDREVLLQYNIAKALIAISNEDPLRTQKYIHNSFRLIGTNFITSSKETTLLKKQNLLMKLHSLYDLSFLSSAKDKFEYKSNTTILDYRMERIGADFVPNHYILSMRKSFDQLKMNEQADADLGKTFFTLAQLARNNARLDIASESLMHCLERRLPQAELEFAEILWKQGENDRALKIVQEIHEKYQENSSVNARDRAAVLLKFTEWLDLSNNSASEQIIKQYQDIFQIDSKWDKPYYSIGLYYSRLLERKKAEGYITNGRFEYRAISYFLLAFEKNTAKVRENLPKVITFWLDIAAASISEAPGNRKEMLSKATEDICSHVEEALQHCPTYIWYFVLTQLLSRLLHSHQSSAQIIMHILLSLAVEYPSHILWYITALVNSNSSKRVLRGKHILEKYRQHSQNPHDLVSSALDLTKALTRVCLQDVKSITSRSGKSLEKDFKFDMNVAPSAMVVPVRKNLDIISPLESNSMRGYQPFRPVVSIIRFGSSYKVFSSLKKPKQLNIIGSDGNIYGIMCKKEDVRQDNQYMQFATTMDFLLSKDIASRKRSLGINIYSVLSLREDCGILEMVPNVVTLRSILSTKYESLKIKYSLKSLHDRWQHTAVDGKLEFYMEQVDKFPPILYQWFLENFPDPINWFNARNTYARSYAVMAMVGHILGLGDRHCENILLDIQTGKVLHVDFDCLFEKGKRLPVPEIVPFRLTPNLLDALGIIGTEGTFKKSSEVTLALMRKNEVALMNVIETIMYDRNMDHSIQKALKVLRNKIRGIDPQDGLVLSVAGQTETLIQEATSEDNLSKMYIGWLPFW | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 33 | Phosphorylation | VQIKKVPTDPSSSQE CEEEECCCCCCCCHH | 64.63 | 20377248 | |
| 36 | Phosphorylation | KKVPTDPSSSQEYAK EECCCCCCCCHHHHH | 45.49 | 28889911 | |
| 37 | Phosphorylation | KVPTDPSSSQEYAKS ECCCCCCCCHHHHHH | 41.24 | 20377248 | |
| 38 | Phosphorylation | VPTDPSSSQEYAKSL CCCCCCCCHHHHHHH | 31.22 | 20190278 | |
| 189 | Phosphorylation | YILLYWFTSEYSTFG HHHHHHHCCCCCCCC | 13.40 | 27017623 | |
| 193 | Phosphorylation | YWFTSEYSTFGNSIA HHHCCCCCCCCCHHH | 17.13 | 27017623 | |
| 194 | Phosphorylation | WFTSEYSTFGNSIAF HHCCCCCCCCCHHHH | 34.36 | 27017623 | |
| 336 | Phosphorylation | QSEHFPFTQLTNKAL CCCCCCHHHHHCCHH | 23.94 | 14595109 | |
| 1802 | Phosphorylation | KWDKPYYSIGLYYSR CCCCCCEEHHHHHHH | 12.34 | 28889911 | |
| 1994 | Phosphorylation | QDVKSITSRSGKSLE HHHHHHHCCCCCCCH | 23.84 | 28889911 | |
| 1996 | Phosphorylation | VKSITSRSGKSLEKD HHHHHCCCCCCCHHC | 50.79 | 19779198 | |
| 2102 | Phosphorylation | TTMDFLLSKDIASRK HHHHHHHCCHHHHCC | 30.35 | 27017623 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 38 | S | Phosphorylation | Kinase | ATM/ATR | - | GPS |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ATR_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 ATR_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 SER-37 AND SER-38, 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-38, AND MASSSPECTROMETRY. | |
