| UniProt ID | SHS1_YEAST | |
|---|---|---|
| UniProt AC | Q07657 | |
| Protein Name | Seventh homolog of septin 1 | |
| Gene Name | SHS1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 551 | |
| Subcellular Localization |
Membrane Peripheral membrane protein. Bud neck . Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate (By similarity).. |
|
| Protein Description | Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 min before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.. | |
| Protein Sequence | MSTASTPPINLFRRKKEHKRGITYTMLLCGPAGTGKTAFANNLLETKIFPHKYQYGKSNASISSNPEVKVIAPTKVVSFNSKNGIPSYVSEFDPMRANLEPGITITSTSLELGGNKDQGKPEMNEDDTVFFNLIMTHGIGENLDDSLCSEEVMSYLEQQFDIVLAEETRIKRNPRFEDTRVHVALYFIEPTGHGLREVDVELMKSISKYTNVLPIITRADSFTKEELTQFRKNIMFDVERYNVPIYKFEVDPEDDDLESMEENQALASLQPFAIITSDTRDSEGRYVREYPWGIISIDDDKISDLKVLKNVLFGSHLQEFKDTTQNLLYENYRSEKLSSVANAEEIGPNSTKRQSNAPSLSNFASLISTGQFNSSQTLANNLRADTPRNQVSGNFKENEYEDNGEHDSAENEQEMSPVRQLGREIKQENENLIRSIKTESSPKFLNSPDLPERTKLRNISETVPYVLRHERILARQQKLEELEAQSAKELQKRIQELERKAHELKLREKLINQNKLNGSSSSINSLQQSTRSQIKKNDTYTDLASIASGRD | |
| 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 | ------MSTASTPPI ------CCCCCCCCC | 32.45 | 28152593 | |
| 2 | Acetylation | ------MSTASTPPI ------CCCCCCCCC | 32.45 | 22814378 | |
| 3 | Phosphorylation | -----MSTASTPPIN -----CCCCCCCCCC | 24.27 | 28152593 | |
| 5 | Phosphorylation | ---MSTASTPPINLF ---CCCCCCCCCCHH | 41.35 | 28152593 | |
| 6 | Phosphorylation | --MSTASTPPINLFR --CCCCCCCCCCHHH | 30.53 | 18431499 | |
| 23 | Phosphorylation | KEHKRGITYTMLLCG HHHCCCCEEEEEEEC | 18.76 | 28889911 | |
| 52 | Ubiquitination | ETKIFPHKYQYGKSN CCCCCCCCCCCCCCC | 34.00 | 22817900 | |
| 57 | Acetylation | PHKYQYGKSNASISS CCCCCCCCCCCCCCC | 35.29 | 21984913 | |
| 57 | Ubiquitination | PHKYQYGKSNASISS CCCCCCCCCCCCCCC | 35.29 | 23749301 | |
| 58 | Phosphorylation | HKYQYGKSNASISSN CCCCCCCCCCCCCCC | 33.01 | 23749301 | |
| 61 | Phosphorylation | QYGKSNASISSNPEV CCCCCCCCCCCCCCC | 27.53 | 22369663 | |
| 63 | Phosphorylation | GKSNASISSNPEVKV CCCCCCCCCCCCCEE | 22.90 | 18431499 | |
| 64 | Phosphorylation | KSNASISSNPEVKVI CCCCCCCCCCCCEEE | 55.52 | 22369663 | |
| 69 | Acetylation | ISSNPEVKVIAPTKV CCCCCCCEEECCEEE | 26.68 | 24489116 | |
| 78 | Phosphorylation | IAPTKVVSFNSKNGI ECCEEEEEEECCCCC | 23.00 | 30377154 | |
| 82 | Acetylation | KVVSFNSKNGIPSYV EEEEEECCCCCCCCC | 61.37 | 21984913 | |
| 204 | Acetylation | EVDVELMKSISKYTN HHCHHHHHHHHHHCC | 58.21 | 21984913 | |
| 208 | Acetylation | ELMKSISKYTNVLPI HHHHHHHHHCCCHHE | 55.19 | 24489116 | |
| 217 | Phosphorylation | TNVLPIITRADSFTK CCCHHEEECCCCCCH | 22.11 | 21440633 | |
| 221 | Phosphorylation | PIITRADSFTKEELT HEEECCCCCCHHHHH | 33.55 | 17563356 | |
| 224 | Acetylation | TRADSFTKEELTQFR ECCCCCCHHHHHHHH | 47.37 | 24489116 | |
| 259 | Phosphorylation | PEDDDLESMEENQAL CCCCCHHHHHHHHHH | 38.50 | 18431499 | |
| 321 | Ubiquitination | GSHLQEFKDTTQNLL CHHHHHHHHHHHHHH | 54.11 | 23749301 | |
| 350 | Phosphorylation | AEEIGPNSTKRQSNA HHHHCCCCCCCCCCC | 38.14 | 18431499 | |
| 351 | Phosphorylation | EEIGPNSTKRQSNAP HHHCCCCCCCCCCCC | 36.57 | 18431499 | |
| 352 | Ubiquitination | EIGPNSTKRQSNAPS HHCCCCCCCCCCCCC | 48.54 | 23749301 | |
| 352 | Acetylation | EIGPNSTKRQSNAPS HHCCCCCCCCCCCCC | 48.54 | 21984913 | |
| 355 | Phosphorylation | PNSTKRQSNAPSLSN CCCCCCCCCCCCHHH | 38.70 | 22369663 | |
| 359 | Phosphorylation | KRQSNAPSLSNFASL CCCCCCCCHHHHHHH | 41.86 | 22369663 | |
| 361 | Phosphorylation | QSNAPSLSNFASLIS CCCCCCHHHHHHHHH | 33.95 | 22369663 | |
| 365 | Phosphorylation | PSLSNFASLISTGQF CCHHHHHHHHHCCCC | 23.30 | 22369663 | |
| 368 | Phosphorylation | SNFASLISTGQFNSS HHHHHHHHCCCCCCC | 31.60 | 22369663 | |
| 369 | Phosphorylation | NFASLISTGQFNSSQ HHHHHHHCCCCCCCH | 28.19 | 18431499 | |
| 374 | Phosphorylation | ISTGQFNSSQTLANN HHCCCCCCCHHHHHH | 25.72 | 22369663 | |
| 375 | Phosphorylation | STGQFNSSQTLANNL HCCCCCCCHHHHHHC | 28.43 | 20377248 | |
| 377 | Phosphorylation | GQFNSSQTLANNLRA CCCCCCHHHHHHCCC | 29.77 | 22369663 | |
| 386 | Phosphorylation | ANNLRADTPRNQVSG HHHCCCCCCCCCCCC | 24.14 | 18431499 | |
| 392 | Phosphorylation | DTPRNQVSGNFKENE CCCCCCCCCCCCCCC | 20.46 | 29136822 | |
| 400 | Phosphorylation | GNFKENEYEDNGEHD CCCCCCCCCCCCCCC | 39.92 | 22890988 | |
| 408 | Phosphorylation | EDNGEHDSAENEQEM CCCCCCCCHHHHHHH | 39.11 | 22369663 | |
| 416 | Phosphorylation | AENEQEMSPVRQLGR HHHHHHHHHHHHHHH | 21.35 | 22369663 | |
| 426 | Sumoylation | RQLGREIKQENENLI HHHHHHHHHHCHHHH | 46.97 | - | |
| 426 | Ubiquitination | RQLGREIKQENENLI HHHHHHHHHHCHHHH | 46.97 | 23749301 | |
| 426 | Sumoylation | RQLGREIKQENENLI HHHHHHHHHHCHHHH | 46.97 | - | |
| 435 | Phosphorylation | ENENLIRSIKTESSP HCHHHHHHHCCCCCC | 22.80 | 23749301 | |
| 437 | Ubiquitination | ENLIRSIKTESSPKF HHHHHHHCCCCCCCH | 47.70 | - | |
| 437 | Sumoylation | ENLIRSIKTESSPKF HHHHHHHCCCCCCCH | 47.70 | - | |
| 437 | Sumoylation | ENLIRSIKTESSPKF HHHHHHHCCCCCCCH | 47.70 | - | |
| 438 | Phosphorylation | NLIRSIKTESSPKFL HHHHHHCCCCCCCHH | 39.16 | 19684113 | |
| 440 | Phosphorylation | IRSIKTESSPKFLNS HHHHCCCCCCCHHCC | 58.11 | 28152593 | |
| 441 | Phosphorylation | RSIKTESSPKFLNSP HHHCCCCCCCHHCCC | 26.36 | 18431499 | |
| 443 | Acetylation | IKTESSPKFLNSPDL HCCCCCCCHHCCCCC | 65.51 | 24489116 | |
| 447 | Phosphorylation | SSPKFLNSPDLPERT CCCCHHCCCCCCHHH | 23.18 | 22369663 | |
| 454 | Phosphorylation | SPDLPERTKLRNISE CCCCCHHHCCCCHHH | 32.54 | 18431499 | |
| 460 | Phosphorylation | RTKLRNISETVPYVL HHCCCCHHHHHHHHH | 30.66 | 22369663 | |
| 462 | Phosphorylation | KLRNISETVPYVLRH CCCCHHHHHHHHHHH | 21.71 | 22890988 | |
| 465 | Phosphorylation | NISETVPYVLRHERI CHHHHHHHHHHHHHH | 14.05 | 22369663 | |
| 478 | Ubiquitination | RILARQQKLEELEAQ HHHHHHHHHHHHHHH | 49.91 | 23749301 | |
| 478 | Acetylation | RILARQQKLEELEAQ HHHHHHHHHHHHHHH | 49.91 | 24489116 | |
| 486 | Phosphorylation | LEELEAQSAKELQKR HHHHHHHHHHHHHHH | 48.64 | 30377154 | |
| 488 | Acetylation | ELEAQSAKELQKRIQ HHHHHHHHHHHHHHH | 65.29 | 21984913 | |
| 488 | Ubiquitination | ELEAQSAKELQKRIQ HHHHHHHHHHHHHHH | 65.29 | 23749301 | |
| 515 | Acetylation | EKLINQNKLNGSSSS HHHHHCCCCCCCCHH | 33.30 | 24489116 | |
| 519 | Phosphorylation | NQNKLNGSSSSINSL HCCCCCCCCHHHHHH | 26.44 | 22369663 | |
| 520 | Phosphorylation | QNKLNGSSSSINSLQ CCCCCCCCHHHHHHH | 29.51 | 22369663 | |
| 521 | Phosphorylation | NKLNGSSSSINSLQQ CCCCCCCHHHHHHHH | 36.61 | 25521595 | |
| 522 | Phosphorylation | KLNGSSSSINSLQQS CCCCCCHHHHHHHHH | 27.95 | 22369663 | |
| 525 | Phosphorylation | GSSSSINSLQQSTRS CCCHHHHHHHHHHHH | 26.36 | 22369663 | |
| 529 | Phosphorylation | SINSLQQSTRSQIKK HHHHHHHHHHHHHHC | 16.90 | 18431499 | |
| 530 | Phosphorylation | INSLQQSTRSQIKKN HHHHHHHHHHHHHCC | 29.96 | 18431499 | |
| 532 | Phosphorylation | SLQQSTRSQIKKNDT HHHHHHHHHHHCCCC | 36.02 | 22369663 | |
| 536 | Acetylation | STRSQIKKNDTYTDL HHHHHHHCCCCHHHH | 62.78 | 21984913 | |
| 536 | Ubiquitination | STRSQIKKNDTYTDL HHHHHHHCCCCHHHH | 62.78 | 23749301 | |
| 539 | Phosphorylation | SQIKKNDTYTDLASI HHHHCCCCHHHHHHH | 37.40 | 22369663 | |
| 540 | Phosphorylation | QIKKNDTYTDLASIA HHHCCCCHHHHHHHH | 10.91 | 22369663 | |
| 541 | Phosphorylation | IKKNDTYTDLASIAS HHCCCCHHHHHHHHC | 26.99 | 22369663 | |
| 545 | Phosphorylation | DTYTDLASIASGRD- CCHHHHHHHHCCCC- | 26.45 | 22369663 | |
| 548 | Phosphorylation | TDLASIASGRD---- HHHHHHHCCCC---- | 32.46 | 22369663 |
| 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 SHS1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SHS1_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 SHS1_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 THR-23; SER-63; SER-64;SER-221; SER-374; SER-408; SER-416; SER-447; SER-519; SER-520;SER-521; SER-522; SER-525; THR-539; TYR-540; THR-541; SER-545 ANDSER-548, 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-221; SER-408; SER-416;THR-539; SER-545 AND SER-548, AND MASS SPECTROMETRY. | |
| "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-416; SER-447; SER-519;SER-525; SER-545 AND SER-548, AND MASS SPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; SER-460 ANDTHR-539, AND MASS SPECTROMETRY. | |
| Sumoylation | |
| Reference | PubMed |
| "Cell cycle-regulated attachment of the ubiquitin-related protein SUMOto the yeast septins."; Johnson E.S., Blobel G.; J. Cell Biol. 147:981-994(1999). Cited for: SUMOYLATION AT LYS-426 AND LYS-437, AND MUTAGENESIS OF LYS-426 ANDLYS-437. | |
