| UniProt ID | MLP2_YEAST | |
|---|---|---|
| UniProt AC | P40457 | |
| Protein Name | Protein MLP2 | |
| Gene Name | MLP2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1679 | |
| Subcellular Localization | Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Nuclear periphery, excluded from nuclear envelope adjacent to nucleolus. | |
| Protein Description | Involved together with the closely related MLP1 in the structural and functional organization of perinuclear chromatin. MLP1/MLP2 associate with the nuclear pore complex and form filamentous structures along the nuclear periphery. According to PubMed:11862215 some telomeres are tethered to the nuclear periphery through MLP1/MLP2, probably mediated by YKU70/YKU80 (HDF1/HDF2) heterodimer and show perinuclear location dependent silencing. According to PubMed:12490156 MLP1 and MLP2 are involved in telomere length regulation but not silencing or telomere anchoring. MLP2 plays a role in the incorporation of components into the spindle pole body. MLP2 is also involved in double-strand break repair, probably also mediated by the YKU70/YKU80 (HDF1/HDF2) heterodimer.. | |
| Protein Sequence | MEDKISEFLNVPFESLQGVTYPVLRKLYKKIAKFERSEEEVTKLNVLVDEIKSQYYSRISKLKQLLDESSEQKNTAKEELNGLKDQLNEERSRYRREIDALKKQLHVSHEAMREVNDEKRVKEEYDIWQSRDQGNDSLNDDLNKENKLLRRKLMEMENILQRCKSNAISLQLKYDTSVQEKELMLQSKKLIEEKLSSFSKKTLTEEVTKSSHVENLEEKLYQMQSNYESVFTYNKFLLNQNKQLSQSVEEKVLEMKNLKDTASVEKAEFSKEMTLQKNMNDLLRSQLTSLEKDCSLRAIEKNDDNSCRNPEHTDVIDELIDTKLRLEKSKNECQRLQNIVMDCTKEEEATMTTSAVSPTVGKLFSDIKVLKRQLIKERNQKFQLQNQLEDFILELEHKTPELISFKERTKSLEHELKRSTELLETVSLTKRKQEREITSLRQKINGCEANIHSLVKQRLDLARQVKLLLLNTSAIQETASPLSQDELISLRKILESSNIVNENDSQAIITERLVEFSNVNELQEKNVELLNCIRILADKLENYEGKQDKTLQKVENQTIKEAKDAIIELENINAKMETRINILLRERDSYKLLASTEENKANTNSVTSMEAAREKKIRELEAELSSTKVENSAIIQNLRKELLIYKKSQCKKKTTLEDFENFKGLAKEKERMLEEAIDHLKAELEKQKSWVPSYIHVEKERASTELSQSRIKIKSLEYEISKLKKETASFIPTKESLTRDFEQCCKEKKELQMRLKESEISHNENKMDFSSKEGQYKAKIKELENNLERLRSDLQSKIQEIESIRSCKDSQLKWAQNTIDDTEMKMKSLLTELSNKETTIEKLSSEIENLDKELRKTKFQYKFLDQNSDASTLEPTLRKELEQIQVQLKDANSQIQAYEEIISSNENALIELKNELAKTKENYDAKIELEKKEKWAREEDLSRLRGELGEIRALQPKLKEGALHFVQQSEKLRNEVERIQKMIEKIEKMSTIVQLCKKKEMSQYQSTMKENKDLSELVIRLEKDAADCQAELTKTKSSLYSAQDLLDKHERKWMEEKADYERELISNIEQTESLRVENSVLIEKVDDTAANNGDKDHLKLVSLFSNLRHERNSLETKLTTCKRELAFVKQKNDSLEKTINDLQRTQTLSEKEYQCSAVIIDEFKDITKEVTQVNILKENNAILQKSLKNVTEKNREIYKQLNDRQEEISRLQRDLIQTKEQVSINSNKILVYESEMEQCKQRYQDLSQQQKDAQKKDIEKLTNEISDLKGKLSSAENANADLENKFNRLKKQAHEKLDASKKQQAALTNELNELKAIKDKLEQDLHFENAKVIDLDTKLKAHELQSEDVSRDHEKDTYRTLMEEIESLKKELQIFKTANSSSDAFEKLKVNMEKEKDRIIDERTKEFEKKLQETLNKSTSSEAEYSKDIETLKKEWLKEYEDETLRRIKEAEENLKKRIRLPSEERIQKIISKRKEELEEEFRKKLKENAGSLTFLDNKGSGEDAEEELWNSPSKGNSERPSAVAGFINQKNLKPQEQLKNVKNDVSFNDSQSMVTNKENNIVDSSAAGNKAIPTFSFGKPFFSSNTSSLQSFQNPFTASQSNINTNAPLRTLNIQPEVAVKAAINFSNVTDLTNNSTDGAKITEIGSTSKRPIESGTSSDPDTKKVKESPANDQASNE | |
| 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 |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MEDKISEFLNVPF --CCCHHHHHHCCCH | 28.21 | 28889911 | |
| 21 | Phosphorylation | ESLQGVTYPVLRKLY HHHCCCCHHHHHHHH | 6.74 | 19779198 | |
| 69 | Phosphorylation | LKQLLDESSEQKNTA HHHHHHHCHHHHHHH | 38.55 | 21440633 | |
| 70 | Phosphorylation | KQLLDESSEQKNTAK HHHHHHCHHHHHHHH | 41.84 | 21440633 | |
| 75 | Phosphorylation | ESSEQKNTAKEELNG HCHHHHHHHHHHHHH | 46.25 | 28889911 | |
| 137 | Phosphorylation | SRDQGNDSLNDDLNK CCCCCCCCCCCCCHH | 32.83 | 23749301 | |
| 147 | Acetylation | DDLNKENKLLRRKLM CCCHHHHHHHHHHHH | 50.41 | 24489116 | |
| 261 | Phosphorylation | EMKNLKDTASVEKAE HHCCCCCCCCHHHHH | 21.17 | 27017623 | |
| 270 | Phosphorylation | SVEKAEFSKEMTLQK CHHHHHHHHHHHHHH | 21.15 | 27017623 | |
| 357 | Phosphorylation | TMTTSAVSPTVGKLF CCCCCCCCHHHHHHH | 17.99 | 23749301 | |
| 368 | Acetylation | GKLFSDIKVLKRQLI HHHHHHHHHHHHHHH | 46.64 | 24489116 | |
| 505 | Phosphorylation | NIVNENDSQAIITER CCCCCCCCHHHHHHH | 32.85 | 30377154 | |
| 539 | Acetylation | CIRILADKLENYEGK HHHHHHHHHHCCCCC | 52.68 | 24489116 | |
| 608 | Phosphorylation | ANTNSVTSMEAAREK CCCCCCCHHHHHHHH | 16.69 | 23749301 | |
| 663 | Acetylation | LEDFENFKGLAKEKE HHHHHHHHHHHHHHH | 65.68 | 24489116 | |
| 689 | Phosphorylation | AELEKQKSWVPSYIH HHHHHHHCCCCCEEE | 30.71 | 28889911 | |
| 694 | Phosphorylation | QKSWVPSYIHVEKER HHCCCCCEEECCHHH | 6.75 | 28889911 | |
| 699 | Acetylation | PSYIHVEKERASTEL CCEEECCHHHHCCHH | 51.95 | 24489116 | |
| 707 | Phosphorylation | ERASTELSQSRIKIK HHHCCHHCHHHHHHH | 21.63 | 27017623 | |
| 722 | Acetylation | SLEYEISKLKKETAS HHHHHHHHHHHHHHH | 70.73 | 24489116 | |
| 862 | Acetylation | RKTKFQYKFLDQNSD HHHHHHHHHCCCCCC | 28.77 | 24489116 | |
| 1007 | Phosphorylation | EMSQYQSTMKENKDL HHHHHHHHHHHCCCH | 19.41 | 23749301 | |
| 1015 | Phosphorylation | MKENKDLSELVIRLE HHHCCCHHHHHHHHH | 38.73 | 28889911 | |
| 1035 | Phosphorylation | CQAELTKTKSSLYSA HHHHHHCCHHHHHCH | 30.81 | 21126336 | |
| 1048 | Acetylation | SAQDLLDKHERKWME CHHHHHHHHHHHHHH | 47.54 | 24489116 | |
| 1079 | Phosphorylation | ESLRVENSVLIEKVD HCCEEECCEEEEEEC | 12.56 | 30377154 | |
| 1102 | Phosphorylation | KDHLKLVSLFSNLRH HHHHHHHHHHHHHHH | 33.85 | 30377154 | |
| 1285 | Acetylation | ANADLENKFNRLKKQ HCHHHHHHHHHHHHH | 34.34 | 24489116 | |
| 1380 | Phosphorylation | QIFKTANSSSDAFEK HHHHHCCCCCHHHHH | 28.84 | 30377154 | |
| 1381 | Phosphorylation | IFKTANSSSDAFEKL HHHHCCCCCHHHHHH | 31.85 | 28889911 | |
| 1382 | Phosphorylation | FKTANSSSDAFEKLK HHHCCCCCHHHHHHC | 32.55 | 30377154 | |
| 1418 | Phosphorylation | LQETLNKSTSSEAEY HHHHHCCCCCCCHHH | 32.23 | 21440633 | |
| 1420 | Phosphorylation | ETLNKSTSSEAEYSK HHHCCCCCCCHHHHH | 33.02 | 30377154 | |
| 1421 | Phosphorylation | TLNKSTSSEAEYSKD HHCCCCCCCHHHHHH | 40.70 | 21440633 | |
| 1463 | Phosphorylation | KKRIRLPSEERIQKI HHHCCCCCHHHHHHH | 57.59 | 23749301 | |
| 1492 | Phosphorylation | KLKENAGSLTFLDNK HHHHHHCCCEECCCC | 23.09 | 22369663 | |
| 1494 | Phosphorylation | KENAGSLTFLDNKGS HHHHCCCEECCCCCC | 24.69 | 22369663 | |
| 1501 | Phosphorylation | TFLDNKGSGEDAEEE EECCCCCCCCCHHHH | 40.39 | 22369663 | |
| 1512 | Phosphorylation | AEEELWNSPSKGNSE HHHHHHCCCCCCCCC | 20.97 | 22369663 | |
| 1514 | Phosphorylation | EELWNSPSKGNSERP HHHHCCCCCCCCCCH | 53.68 | 25521595 | |
| 1518 | Phosphorylation | NSPSKGNSERPSAVA CCCCCCCCCCHHHHH | 43.58 | 21440633 | |
| 1522 | Phosphorylation | KGNSERPSAVAGFIN CCCCCCHHHHHHHHC | 41.41 | 28889911 | |
| 1547 | Phosphorylation | KNVKNDVSFNDSQSM HCCCCCCCCCCHHHC | 22.61 | 30377154 | |
| 1551 | Phosphorylation | NDVSFNDSQSMVTNK CCCCCCCHHHCCCCC | 25.84 | 30377154 | |
| 1577 | Phosphorylation | NKAIPTFSFGKPFFS CCCCCCCCCCCCCCC | 35.25 | 21551504 | |
| 1637 | Phosphorylation | VTDLTNNSTDGAKIT CHHCCCCCCCCCEEE | 29.91 | 30377154 | |
| 1656 | Phosphorylation | TSKRPIESGTSSDPD CCCCCCCCCCCCCCC | 48.36 | 21440633 | |
| 1658 | Phosphorylation | KRPIESGTSSDPDTK CCCCCCCCCCCCCCC | 34.04 | 27717283 | |
| 1659 | Phosphorylation | RPIESGTSSDPDTKK CCCCCCCCCCCCCCC | 35.95 | 28889911 | |
| 1660 | Phosphorylation | PIESGTSSDPDTKKV CCCCCCCCCCCCCCC | 53.66 | 17563356 | |
| 1670 | Phosphorylation | DTKKVKESPANDQAS CCCCCCCCCCCCCCC | 24.48 | 25521595 | |
| 1677 | Phosphorylation | SPANDQASNE----- CCCCCCCCCC----- | 35.54 | 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 MLP2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MLP2_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 MLP2_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-1659 AND SER-1670, ANDMASS SPECTROMETRY. | |
| "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-1660, AND MASSSPECTROMETRY. | |
| "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 SER-1512, AND MASSSPECTROMETRY. | |
