| UniProt ID | STU2_YEAST | |
|---|---|---|
| UniProt AC | P46675 | |
| Protein Name | Protein STU2 | |
| Gene Name | STU2 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 888 | |
| Subcellular Localization | Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Cytoplasm, cytoskeleton, spindle . Chromosome, centromere, kinetochore . Localizes primarily to the spindle pole body (SPB) and to a lesser extent along spindle microtubules. | |
| Protein Description | Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. May play a role in the attachment, organization, and/or dynamics of microtubule ends at the spindle pole body. Stabilizes both cytoplasmic and nuclear microtubules. Promotes mitotic spindle elongation in anaphase. Has microtubule polymerase activity by accelerating microtubule growth and inhibiting catastrophe. The polymerase activity is proposed to involve a tethering mechanism at the microtubule plus end: a curved, longitudinally microtubule lattice-associated tubulin heterodimer (that cannot be incorporated into the microtubule lattice) is bound via one TOG domain while the other TOG domain binds to an unpolymerized tubulin heterodimer leading to lateral association of these tubulin heterdimers; polymerization-induced straightening of the tubulin heterodimer releases the polymerase. [PubMed: 11309422] | |
| Protein Sequence | MSGEEEVDYTTLPLEERLTYKLWKARLEAYKELNQLFRNSVGDISRDDNIQIYWRDPTLFAQYITDSNVVAQEQAIVALNSLIDAFASSSLKNAHNITLISTWTPLLVEKGLTSSRATTKTQSMSCILSLCGLDTSITQSVELVIPFFEKKLPKLIAAAANCVYELMAAFGLTNVNVQTFLPELLKHVPQLAGHGDRNVRSQTMNLIVEIYKVTGNNSDLLEEILFKKLKPIQVKDLHKLFAKVGDEPSSSKMLFEWEKRELEKKRSQEEEARKRKSILSNDEGEYQIDKDGDTLMGMETDMPPSKQQSGVQIDTFSMLPEETILDKLPKDFQERITSSKWKDRVEALEEFWDSVLSQTKKLKSTSQNYSNLLGIYGHIIQKDANIQAVALAAQSVELICDKLKTPGFSKDYVSLVFTPLLDRTKEKKPSVIEAIRKALLTICKYYDPLASSGRNEDMLKDILEHMKHKTPQIRMECTQLFNASMKEEKDGYSTLQRYLKDEVVPIVIQIVNDTQPAIRTIGFESFAILIKIFGMNTFVKTLEHLDNLKRKKIEETVKTLPNFSIASGSTHSTIETNKQTGPMENKFLLKKSSVLPSKRVASSPLRNDNKSKVNPIGSVASASKPSMVAANNKSRVLLTSKSLATPKNVVANSTDKNEKLIEEYKYRLQKLQNDEMIWTKERQSLLEKMNNTENYKIEMIKENEMLREQLKEAQSKLNEKNIQLRSKEIDVNKLSDRVLSLENELRNMEIELDRNKKRNDTNLQSMGTISSYSIPSSTVSSNYGVKSLSSALPFKEEEDVRRKEDVNYERRSSESIGDLPHRVNSLNIRPYRKNGTGVSSVSDDLDIDFNDSFASEESYKRAAAVTSTLKARIEKMKAKSRREGTTRT | |
| 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 | ------MSGEEEVDY ------CCCCCCCCC | 55.71 | 28152593 | |
| 121 | Phosphorylation | SSRATTKTQSMSCIL CCCCCHHHHCHHHHH | 24.63 | 27017623 | |
| 123 | Phosphorylation | RATTKTQSMSCILSL CCCHHHHCHHHHHHH | 20.21 | 27017623 | |
| 129 | Phosphorylation | QSMSCILSLCGLDTS HCHHHHHHHCCCCCC | 11.16 | 27017623 | |
| 135 | Phosphorylation | LSLCGLDTSITQSVE HHHCCCCCCHHCCCH | 27.37 | 27017623 | |
| 136 | Phosphorylation | SLCGLDTSITQSVEL HHCCCCCCHHCCCHH | 24.25 | 27017623 | |
| 249 | Phosphorylation | AKVGDEPSSSKMLFE HHHCCCCCHHHHHHH | 45.24 | 19823750 | |
| 250 | Phosphorylation | KVGDEPSSSKMLFEW HHCCCCCHHHHHHHH | 44.70 | 21551504 | |
| 251 | Phosphorylation | VGDEPSSSKMLFEWE HCCCCCHHHHHHHHH | 26.82 | 17287358 | |
| 277 | Phosphorylation | EEARKRKSILSNDEG HHHHHHHHHHCCCCC | 32.56 | 25521595 | |
| 280 | Phosphorylation | RKRKSILSNDEGEYQ HHHHHHHCCCCCCEE | 40.33 | 22890988 | |
| 294 | Phosphorylation | QIDKDGDTLMGMETD EECCCCCEEEEEECC | 24.95 | 21440633 | |
| 300 | Phosphorylation | DTLMGMETDMPPSKQ CEEEEEECCCCCCCC | 28.80 | 21440633 | |
| 315 | Phosphorylation | QSGVQIDTFSMLPEE CCCCEEECCCCCCHH | 21.17 | 30377154 | |
| 478 | Phosphorylation | PQIRMECTQLFNASM HHHHHHHHHHHHHHH | 18.26 | 30377154 | |
| 484 | Phosphorylation | CTQLFNASMKEEKDG HHHHHHHHHHCCCCC | 31.34 | 30377154 | |
| 592 | Phosphorylation | NKFLLKKSSVLPSKR CCEEEECCCCCCCCC | 24.88 | 30377154 | |
| 602 | Phosphorylation | LPSKRVASSPLRNDN CCCCCCCCCCCCCCC | 29.63 | 29136822 | |
| 603 | Phosphorylation | PSKRVASSPLRNDNK CCCCCCCCCCCCCCC | 20.44 | 19823750 | |
| 618 | Phosphorylation | SKVNPIGSVASASKP CCCCCCCHHHCCCCC | 18.41 | 29136822 | |
| 621 | Phosphorylation | NPIGSVASASKPSMV CCCCHHHCCCCCCEE | 30.80 | 23749301 | |
| 623 | Phosphorylation | IGSVASASKPSMVAA CCHHHCCCCCCEEEC | 42.47 | 29136822 | |
| 626 | Phosphorylation | VASASKPSMVAANNK HHCCCCCCEEECCCC | 29.62 | 23749301 | |
| 634 | Phosphorylation | MVAANNKSRVLLTSK EEECCCCCCEEEEEC | 29.73 | 28889911 | |
| 695 | Phosphorylation | KMNNTENYKIEMIKE HHCCCCCHHHEEHHH | 13.70 | 27017623 | |
| 740 | Phosphorylation | KLSDRVLSLENELRN HHHHHHHHHHHHHHH | 30.68 | 30377154 | |
| 765 | Phosphorylation | RNDTNLQSMGTISSY CCCCCCCCCCEEEEC | 23.50 | 27017623 | |
| 768 | Phosphorylation | TNLQSMGTISSYSIP CCCCCCCEEEECCCC | 14.72 | 27017623 | |
| 770 | Phosphorylation | LQSMGTISSYSIPSS CCCCCEEEECCCCCC | 24.06 | 27017623 | |
| 771 | Phosphorylation | QSMGTISSYSIPSST CCCCEEEECCCCCCC | 21.03 | 27017623 | |
| 772 | Phosphorylation | SMGTISSYSIPSSTV CCCEEEECCCCCCCC | 12.11 | 27017623 | |
| 783 | Phosphorylation | SSTVSSNYGVKSLSS CCCCCCCCCCCCHHH | 25.83 | 27017623 | |
| 787 | Phosphorylation | SSNYGVKSLSSALPF CCCCCCCCHHHCCCC | 30.95 | 23749301 | |
| 808 | Phosphorylation | RRKEDVNYERRSSES HCHHHCCCCHHCCCC | 15.63 | 24961812 | |
| 812 | Phosphorylation | DVNYERRSSESIGDL HCCCCHHCCCCCCCC | 44.68 | 22369663 | |
| 813 | Phosphorylation | VNYERRSSESIGDLP CCCCHHCCCCCCCCC | 33.29 | 22369663 | |
| 815 | Phosphorylation | YERRSSESIGDLPHR CCHHCCCCCCCCCCC | 33.54 | 22369663 | |
| 825 | Phosphorylation | DLPHRVNSLNIRPYR CCCCCCCCCCCCCCC | 21.67 | 27214570 | |
| 866 | Phosphorylation | YKRAAAVTSTLKARI HHHHHHHHHHHHHHH | 15.97 | 30377154 | |
| 867 | Phosphorylation | KRAAAVTSTLKARIE HHHHHHHHHHHHHHH | 25.74 | 30377154 |
| 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 STU2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of STU2_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 STU2_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-2; SER-603; SER-812;SER-813; SER-815 AND SER-825, 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-603; SER-812 ANDSER-813, AND MASS SPECTROMETRY. | |
| "Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry."; Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.; Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251 AND SER-603, ANDMASS 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-813, AND MASSSPECTROMETRY. | |
