UniProt ID | MOB1_YEAST | |
---|---|---|
UniProt AC | P40484 | |
Protein Name | DBF2 kinase activator protein MOB1 | |
Gene Name | MOB1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 314 | |
Subcellular Localization | Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Bud neck. Chromosome, centromere. Localizes predominantly to the cytoplasmic surface of the spindle pole body during anaphase and to a ring at the bud neck | |
Protein Description | Functions as an activator subunit for the DBF2 protein kinase. Binds to DBF2, which is required for the phosphorylation and activation of DBF2 by the upstream kinase CDC15 in late anaphase. DBF2-MOB1 is part of the mitotic exit network (MEN) signaling cascade, which regulates release from the nucleus and activity of phosphatase CDC14. Required for inactivation of mitotic cyclin-dependent kinase for exit from mitosis, cytokinesis and G1 gene transcription.. | |
Protein Sequence | MSFLQNFHISPGQTIRSTRGFKWNTANAANNAGSVSPTKATPHNNTINGNNNNANTINNRADFTNNPVNGYNESDHGRMSPVLTTPKRHAPPPEQLQNVTDFNYTPSHQKPFLQPQAGTTVTTHQDIKQIVEMTLGSEGVLNQAVKLPRGEDENEWLAVHCVDFYNQINMLYGSITEFCSPQTCPRMIATNEYEYLWAFQKGQPPVSVSAPKYVECLMRWCQDQFDDESLFPSKVTGTFPEGFIQRVIQPILRRLFRVYAHIYCHHFNEILELNLQTVLNTSFRHFCLFAQEFELLRPADFGPLLELVMELRDR | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MSFLQNFHI ------CCCCCCCCC | 34.36 | 22369663 | |
10 | Phosphorylation | FLQNFHISPGQTIRS CCCCCCCCCCCCCCC | 17.89 | 22369663 | |
14 | Phosphorylation | FHISPGQTIRSTRGF CCCCCCCCCCCCCCC | 25.03 | 29734811 | |
17 | Phosphorylation | SPGQTIRSTRGFKWN CCCCCCCCCCCCCCC | 20.71 | 19823750 | |
18 | Phosphorylation | PGQTIRSTRGFKWNT CCCCCCCCCCCCCCC | 25.59 | 19823750 | |
22 | Acetylation | IRSTRGFKWNTANAA CCCCCCCCCCCCCCC | 42.21 | 22865919 | |
25 | Phosphorylation | TRGFKWNTANAANNA CCCCCCCCCCCCCCC | 21.85 | 22890988 | |
34 | Phosphorylation | NAANNAGSVSPTKAT CCCCCCCCCCCCCCC | 19.60 | 22369663 | |
36 | Phosphorylation | ANNAGSVSPTKATPH CCCCCCCCCCCCCCC | 28.66 | 22369663 | |
38 | Phosphorylation | NAGSVSPTKATPHNN CCCCCCCCCCCCCCC | 26.29 | 22369663 | |
41 | Phosphorylation | SVSPTKATPHNNTIN CCCCCCCCCCCCCCC | 27.00 | 28889911 | |
46 | Phosphorylation | KATPHNNTINGNNNN CCCCCCCCCCCCCCC | 22.57 | 23749301 | |
56 | Phosphorylation | GNNNNANTINNRADF CCCCCCCCCCCCHHC | 23.75 | 23749301 | |
64 | Phosphorylation | INNRADFTNNPVNGY CCCCHHCCCCCCCCC | 34.33 | 22369663 | |
71 | Phosphorylation | TNNPVNGYNESDHGR CCCCCCCCCCCCCCC | 15.56 | 22369663 | |
74 | Phosphorylation | PVNGYNESDHGRMSP CCCCCCCCCCCCCCC | 31.13 | 22369663 | |
80 | Phosphorylation | ESDHGRMSPVLTTPK CCCCCCCCCCCCCCC | 15.53 | 22369663 | |
84 | Phosphorylation | GRMSPVLTTPKRHAP CCCCCCCCCCCCCCC | 41.09 | 22369663 | |
85 | Phosphorylation | RMSPVLTTPKRHAPP CCCCCCCCCCCCCCC | 23.74 | 22369663 | |
100 | Phosphorylation | PEQLQNVTDFNYTPS HHHHCCCCCCCCCCC | 42.28 | 24961812 | |
104 | Phosphorylation | QNVTDFNYTPSHQKP CCCCCCCCCCCCCCC | 21.74 | 28889911 | |
105 | Phosphorylation | NVTDFNYTPSHQKPF CCCCCCCCCCCCCCC | 21.30 | 28889911 | |
107 | Phosphorylation | TDFNYTPSHQKPFLQ CCCCCCCCCCCCCCC | 30.65 | 24961812 | |
119 | Phosphorylation | FLQPQAGTTVTTHQD CCCCCCCCEEECHHH | 22.55 | 19779198 | |
120 | Phosphorylation | LQPQAGTTVTTHQDI CCCCCCCEEECHHHH | 18.22 | 21440633 | |
137 | Phosphorylation | IVEMTLGSEGVLNQA HHHHHHCCCCHHCHH | 34.00 | 28889911 | |
229 | Phosphorylation | QDQFDDESLFPSKVT HHHCCCCCCCCCCCC | 42.16 | 28889911 |
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 MOB1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MOB1_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 MOB1_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-34; SER-36; THR-38;SER-80; THR-85 AND SER-137, AND MASS 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-80, AND MASSSPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80 AND THR-85, AND MASSSPECTROMETRY. |