UniProt ID | MSA1_YEAST | |
---|---|---|
UniProt AC | Q08471 | |
Protein Name | G1-specific transcription factors activator MSA1 | |
Gene Name | MSA1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 629 | |
Subcellular Localization | ||
Protein Description | Activator of G1-specific transcription factors, MBF and SBF. Promotes both the timing of G1-specific gene transcription and cell cycle initiation. Associates with SBF- and MBF-regulated target promoters and this binding is maximal during the G1 phase, prior to maximum budding. Affects cell cycle initiation by advancing the timing of transcription of G1-specific genes. Overexpression advances the timing of SBF-dependent transcription and budding. Depletion delays both indicators of cell cycle initiation.. | |
Protein Sequence | MDKSMIKKRGRPPITKDYPNPLQSPMAHSSMQVQKQGPHSFAKPLMKVGQSSPSPNKRRLSIDHHHNLAATTRKGRYRGVLLSTPTKKSSTNGSTPISTPSSNDSYNNTVFSETRKTFLQSSPPIMTSSPAFQKKNDYMFPSQEQFKLSLTITESGKAVIAGSLPFSPSSKSSHLMNNNNKKIMQNEKIHKGSKKNAPKFEKRRILSLLKQMKNEKYCDTDTLPEAPPAKPSRSDIIDTELPTIIETSASPIGSARNNNILLSQPPQSPPSSAQLKPPSTPKSSLQFRMGFTPNVALNSVSLSDTISKSTNAVGASNNNNQNGNSISNIADANTLLTLTNSPGVFLSPRNKMLPKSTTASNEQQQEFVFKFSSGDPLLLTDDADGNWPEMLFNVSNTPRRQKCFNTPPSWINFGSPGLFSPPRSSNVMVNGTTVATASDSGNVHRQLQAQLEAQVQVQSQSNSPTQRQQQQRQFQIPPPHINMNSSPPQINIASPPHQSMSRVSSIYFNKEKTTTGVANMLGNTKSENLQPPANLFTAAHGPSTPRNQEFQLPTLIECTPLIQQTMNGSLGTKYIPGTSISNSATPNLHGFPVGTGKAPSSFDDSLKQNPYSNKQDDARTALKRLIDDQ | |
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 |
---|---|---|---|---|---|
51 | Phosphorylation | PLMKVGQSSPSPNKR HHHHCCCCCCCCCCC | 37.98 | 27717283 | |
52 | Phosphorylation | LMKVGQSSPSPNKRR HHHCCCCCCCCCCCC | 22.85 | 19684113 | |
54 | Phosphorylation | KVGQSSPSPNKRRLS HCCCCCCCCCCCCCC | 42.95 | 19684113 | |
121 | Phosphorylation | TRKTFLQSSPPIMTS HHHHHHHCCCCCCCC | 47.13 | 21082442 | |
122 | Phosphorylation | RKTFLQSSPPIMTSS HHHHHHCCCCCCCCC | 23.02 | 21551504 | |
163 | Phosphorylation | GKAVIAGSLPFSPSS CCEEEEECCCCCCCH | 24.69 | 28889911 | |
167 | Phosphorylation | IAGSLPFSPSSKSSH EEECCCCCCCHHHHH | 23.18 | 21551504 | |
169 | Phosphorylation | GSLPFSPSSKSSHLM ECCCCCCCHHHHHHC | 49.56 | 28132839 | |
170 | Phosphorylation | SLPFSPSSKSSHLMN CCCCCCCHHHHHHCC | 39.68 | 28132839 | |
234 | Phosphorylation | PPAKPSRSDIIDTEL CCCCCCHHHCCCCCC | 37.18 | 28889911 | |
250 | Phosphorylation | TIIETSASPIGSARN CEEECCCCCCCCCCC | 19.47 | 28889911 | |
254 | Phosphorylation | TSASPIGSARNNNIL CCCCCCCCCCCCCCC | 25.44 | 28132839 | |
263 | Phosphorylation | RNNNILLSQPPQSPP CCCCCCCCCCCCCCC | 36.88 | 28132839 | |
268 | Phosphorylation | LLSQPPQSPPSSAQL CCCCCCCCCCCCCCC | 44.55 | 19684113 | |
271 | Phosphorylation | QPPQSPPSSAQLKPP CCCCCCCCCCCCCCC | 41.51 | 19684113 | |
272 | Phosphorylation | PPQSPPSSAQLKPPS CCCCCCCCCCCCCCC | 26.30 | 28889911 | |
279 | Phosphorylation | SAQLKPPSTPKSSLQ CCCCCCCCCCCCCEE | 66.91 | 23749301 | |
280 | Phosphorylation | AQLKPPSTPKSSLQF CCCCCCCCCCCCEEE | 40.27 | 28889911 | |
395 | Phosphorylation | PEMLFNVSNTPRRQK CHHHEECCCCCCHHH | 35.77 | 21440633 | |
505 | Phosphorylation | QSMSRVSSIYFNKEK CCHHCCEEEEECCCC | 20.60 | 24909858 | |
513 | Phosphorylation | IYFNKEKTTTGVANM EEECCCCCCCCHHHH | 30.59 | 29136822 | |
514 | Phosphorylation | YFNKEKTTTGVANML EECCCCCCCCHHHHH | 32.40 | 29136822 | |
515 | Phosphorylation | FNKEKTTTGVANMLG ECCCCCCCCHHHHHC | 34.59 | 29136822 | |
524 | Phosphorylation | VANMLGNTKSENLQP HHHHHCCCCCCCCCC | 33.86 | 28889911 | |
537 | Phosphorylation | QPPANLFTAAHGPST CCCCCEECCCCCCCC | 26.54 | 28132839 | |
543 | Phosphorylation | FTAAHGPSTPRNQEF ECCCCCCCCCCCCCC | 56.49 | 22369663 | |
544 | Phosphorylation | TAAHGPSTPRNQEFQ CCCCCCCCCCCCCCC | 29.42 | 22369663 | |
601 | Phosphorylation | GTGKAPSSFDDSLKQ CCCCCCCCCCHHHHH | 31.47 | 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 MSA1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MSA1_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 MSA1_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SWI4_YEAST | SWI4 | physical | 18160399 | |
MBP1_YEAST | MBP1 | physical | 18160399 | |
ACH1_YEAST | ACH1 | genetic | 20093466 | |
BEM2_YEAST | BEM2 | genetic | 20093466 | |
MAD1_YEAST | MAD1 | genetic | 20093466 | |
MAD2_YEAST | MAD2 | genetic | 20093466 | |
ELF1_YEAST | ELF1 | genetic | 20093466 | |
ZRC1_YEAST | ZRC1 | genetic | 20093466 | |
EOS1_YEAST | EOS1 | genetic | 20093466 | |
MSB4_YEAST | MSB4 | genetic | 20093466 | |
YPK9_YEAST | YPK9 | genetic | 20093466 | |
CHL1_YEAST | CHL1 | genetic | 20093466 | |
YP089_YEAST | YPR089W | genetic | 20093466 | |
KAR3_YEAST | KAR3 | genetic | 20093466 | |
RNQ1_YEAST | RNQ1 | genetic | 22529103 | |
TEC1_YEAST | TEC1 | physical | 24732795 | |
STE12_YEAST | STE12 | physical | 24732795 | |
MBP1_YEAST | MBP1 | physical | 24732795 | |
MSA2_YEAST | MSA2 | genetic | 24732795 | |
TPS2_YEAST | TPS2 | genetic | 27708008 | |
BEM2_YEAST | BEM2 | genetic | 27708008 | |
ELF1_YEAST | ELF1 | genetic | 27708008 | |
VAC14_YEAST | VAC14 | genetic | 27708008 | |
PEX12_YEAST | PEX12 | genetic | 27708008 | |
ZRC1_YEAST | ZRC1 | genetic | 27708008 | |
OCA2_YEAST | OCA2 | genetic | 27708008 | |
CHL1_YEAST | CHL1 | genetic | 27708008 | |
KAR3_YEAST | KAR3 | genetic | 27708008 |
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-167; SER-234 ANDSER-601, AND MASS SPECTROMETRY. |