| UniProt ID | SPP41_YEAST | |
|---|---|---|
| UniProt AC | P38904 | |
| Protein Name | Protein SPP41 | |
| Gene Name | SPP41 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1435 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Negative regulator of PRP3 and PRP4 genes.. | |
| Protein Sequence | MAYDEDDGEINFNELVGNLLSSHNQEGQEEGEVQGGEQEGDDFEKIYPTSENIEPKHPDDSQHMHNSPDQNIEIPHFVDEEDELVSVVANAVQNIDDEQAKPENHLENGSEHVTSDTADDNHEKEQQQEWAHILQQEILKSDGEPLRENTERRVSTSQHHPSQRTDDALDQDDENLRMAILESLQELNTNEEEEKEPEKHEHAAPNDKLSSKKSSKKKKKDKSKNRESSKDKSSKKSKSSSHSKKHAKDRNKEKQSKPTNNENTLDLSNILENLIHENDNAAIDTAKQTVDIQDNSHTDNTNNEDVEAQALVEATLKAFENELLSSAPTEEPSQEQSIGPVSSRKAVEPPRKPTADDIPLAMLQAFKPKKRPPQEKKKTKSKTSKAASTANKSPASESTSKKKKKKKTVKESNKSQEAYEDDEFSRILADMVNQVVNTSLKETSTHTATQDNKLESESDFTSPVQSQYTTEDASTANDDSLDLNQIMQNAMAMVFQNQNDDEFDENIVEDFNRGLGDLSVSDLLPHDNLSRMEKKSVPKSSSKSEKKTAISRRASKKASRDASSVELTEVPSKPKKPSKTEVSLEKKLRKKYVSIANEAASVARKKRWAKNKELKEKEKLERQTAREERRHKKKLEKQRLAEEQEELKKIVERGPPYPPDLRLTKSGKPKKPYRRWTPEELLKRSQEAEKPRKVKKERKKKEKKMKVPSSALKKIPLFNFVKGNVQPSARHRLNDIEGSLSTIGLHKSPDGVRRILSRPKSEDHEWPLSDSSASQNYDAHLKTVVHKEKIPFHPPWTIPSQPPFALPVARRKKIPNIKKYRKRTNNSFRVSKEGTASTRNRILPAILLPIINTLKAAAKSQTAAGATPEEARKRLATIIQHAKSTVIRAALQARKNSMQAAHSKGTTTELATTASRMKNPLKMIPIFNTSRVKQQLDKQLPARSAGTEISSSESPDKATPDPHSNSTIAGHTLKGVTTPIKIEDSDANVPPVSIAVSTIEPSQDKLELTKRAESVEPVENNVETAKETQSVQEIKENVGTKASEEVTLTEDKTNGDPKNEKRILIESPVEKTDKKKPGEKIATDLNEDASLSDKKDGDEKSTLHSDAAQLTGNEPDSVNTTTGKPKLIDVSLKPLNEAKPKIPIIFPLKRPQIKPEVSVINLVQNLVNTKIPEIKNESVDLGSNITDILSSTITNILPEITATDVKNYQYEDENVKYLKKTPRQVLNLDGLVPPSGRCITKAKRVRRIKKLSADATTAPEADGKANSESITYTFDIPSPEEVQSKRSVVLKFAKARLTEAELSCLKKEINNVRKRRWREMNSTKNWEYDVKSRLKKRANAFFGEGESETKSKWIEERFQEKVSQEKYKDRLETTETQANNTKIVIDDKEILNILAVNMNNLNKARCIEKDIQESFREEKLASLQPKKKRKKSILH | |
| 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 |
|---|---|---|---|---|---|
| 155 | Phosphorylation | ENTERRVSTSQHHPS CCCCCCCCCCCCCCC | 22.11 | 28889911 | |
| 157 | Phosphorylation | TERRVSTSQHHPSQR CCCCCCCCCCCCCCC | 21.73 | 28132839 | |
| 165 | Phosphorylation | QHHPSQRTDDALDQD CCCCCCCCCCCCCCC | 30.51 | 28889911 | |
| 329 | Phosphorylation | ELLSSAPTEEPSQEQ HHHCCCCCCCCCCCC | 53.34 | 24961812 | |
| 333 | Phosphorylation | SAPTEEPSQEQSIGP CCCCCCCCCCCCCCC | 50.02 | 24961812 | |
| 337 | Phosphorylation | EEPSQEQSIGPVSSR CCCCCCCCCCCCCCC | 28.85 | 24961812 | |
| 342 | Phosphorylation | EQSIGPVSSRKAVEP CCCCCCCCCCCCCCC | 27.79 | 24961812 | |
| 343 | Phosphorylation | QSIGPVSSRKAVEPP CCCCCCCCCCCCCCC | 37.73 | 24961812 | |
| 393 | Phosphorylation | AASTANKSPASESTS HHHHHCCCCCCCCCC | 26.04 | 23749301 | |
| 519 | Phosphorylation | NRGLGDLSVSDLLPH HHCCCCCCHHHCCCC | 25.06 | 22369663 | |
| 521 | Phosphorylation | GLGDLSVSDLLPHDN CCCCCCHHHCCCCCC | 21.11 | 29688323 | |
| 530 | Phosphorylation | LLPHDNLSRMEKKSV CCCCCCHHHHHHHCC | 35.52 | 29688323 | |
| 559 | Phosphorylation | RRASKKASRDASSVE HHHHHHHCCCCCCCC | 39.30 | 21440633 | |
| 563 | Phosphorylation | KKASRDASSVELTEV HHHCCCCCCCCEECC | 38.92 | 22369663 | |
| 564 | Phosphorylation | KASRDASSVELTEVP HHCCCCCCCCEECCC | 22.72 | 22369663 | |
| 592 | Phosphorylation | EKKLRKKYVSIANEA HHHHHHHHHHHHHHH | 11.49 | 23749301 | |
| 601 | Phosphorylation | SIANEAASVARKKRW HHHHHHHHHHHHHHH | 24.29 | 23749301 | |
| 668 | Ubiquitination | LRLTKSGKPKKPYRR CCCCCCCCCCCCCCC | 61.83 | 23749301 | |
| 709 | Phosphorylation | EKKMKVPSSALKKIP HHCCCCCHHHHHCCC | 31.09 | 28889911 | |
| 713 | Acetylation | KVPSSALKKIPLFNF CCCHHHHHCCCCCHH | 48.66 | 25381059 | |
| 739 | Phosphorylation | RLNDIEGSLSTIGLH HHHCCCCCCHHCCCC | 13.32 | 28889911 | |
| 741 | Phosphorylation | NDIEGSLSTIGLHKS HCCCCCCHHCCCCCC | 21.48 | 28889911 | |
| 748 | Phosphorylation | STIGLHKSPDGVRRI HHCCCCCCCCHHHHH | 19.92 | 28889911 | |
| 761 | Phosphorylation | RILSRPKSEDHEWPL HHHCCCCCCCCCCCC | 51.44 | 22369663 | |
| 769 | Phosphorylation | EDHEWPLSDSSASQN CCCCCCCCCCCCCCC | 31.22 | 22369663 | |
| 771 | Phosphorylation | HEWPLSDSSASQNYD CCCCCCCCCCCCCHH | 25.16 | 20377248 | |
| 772 | Phosphorylation | EWPLSDSSASQNYDA CCCCCCCCCCCCHHH | 36.61 | 20377248 | |
| 774 | Phosphorylation | PLSDSSASQNYDAHL CCCCCCCCCCHHHHH | 22.40 | 22369663 | |
| 777 | Phosphorylation | DSSASQNYDAHLKTV CCCCCCCHHHHHCCE | 13.58 | 21440633 | |
| 859 | Ubiquitination | NTLKAAAKSQTAAGA HHHHHHHHHHCCCCC | 38.07 | 23749301 | |
| 929 | Phosphorylation | KMIPIFNTSRVKQQL HHEECCCHHHHHHHH | 13.73 | 30377154 | |
| 944 | Phosphorylation | DKQLPARSAGTEISS HHCCCCHHCCCCCCC | 32.91 | 28889911 | |
| 947 | Phosphorylation | LPARSAGTEISSSES CCCHHCCCCCCCCCC | 29.84 | 22369663 | |
| 950 | Phosphorylation | RSAGTEISSSESPDK HHCCCCCCCCCCCCC | 22.91 | 23749301 | |
| 951 | Phosphorylation | SAGTEISSSESPDKA HCCCCCCCCCCCCCC | 43.73 | 22369663 | |
| 952 | Phosphorylation | AGTEISSSESPDKAT CCCCCCCCCCCCCCC | 34.99 | 22369663 | |
| 954 | Phosphorylation | TEISSSESPDKATPD CCCCCCCCCCCCCCC | 40.10 | 22369663 | |
| 977 | Phosphorylation | GHTLKGVTTPIKIED CCCCCCCCCCEEECC | 35.21 | 21440633 | |
| 978 | Phosphorylation | HTLKGVTTPIKIEDS CCCCCCCCCEEECCC | 22.17 | 29734811 | |
| 981 | Sumoylation | KGVTTPIKIEDSDAN CCCCCCEEECCCCCC | 41.04 | 15166219 | |
| 981 | Sumoylation | KGVTTPIKIEDSDAN CCCCCCEEECCCCCC | 41.04 | - | |
| 985 | Phosphorylation | TPIKIEDSDANVPPV CCEEECCCCCCCCCC | 26.32 | 21440633 | |
| 1014 | Phosphorylation | ELTKRAESVEPVENN HHHHHHHHCCCCCCC | 30.69 | 22369663 | |
| 1067 | Phosphorylation | EKRILIESPVEKTDK CCEEEEECCCCCCCC | 27.53 | 25521595 | |
| 1090 | Phosphorylation | TDLNEDASLSDKKDG CCCCCCCCCCCCCCC | 40.50 | 24961812 | |
| 1092 | Phosphorylation | LNEDASLSDKKDGDE CCCCCCCCCCCCCCC | 44.91 | 21440633 | |
| 1105 | Phosphorylation | DEKSTLHSDAAQLTG CCCCCCCHHHHHHHC | 31.86 | 23749301 | |
| 1149 | Acetylation | IPIIFPLKRPQIKPE CCEEEECCCCCCCCC | 63.37 | 25381059 | |
| 1154 | Sumoylation | PLKRPQIKPEVSVIN ECCCCCCCCCCCHHH | 29.85 | - | |
| 1154 | Sumoylation | PLKRPQIKPEVSVIN ECCCCCCCCCCCHHH | 29.85 | 15166219 | |
| 1158 | Phosphorylation | PQIKPEVSVINLVQN CCCCCCCCHHHHHHH | 18.67 | 21440633 | |
| 1252 | Phosphorylation | VRRIKKLSADATTAP HHHHHHHCCCCCCCC | 32.74 | 27214570 |
| 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 SPP41_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPP41_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 SPP41_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-564; SER-1014 ANDSER-1067, 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-519; SER-563 ANDSER-1014, 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-1067, AND MASSSPECTROMETRY. | |
| Sumoylation | |
| Reference | PubMed |
| "Global analyses of sumoylated proteins in Saccharomyces cerevisiae.Induction of protein sumoylation by cellular stresses."; Zhou W., Ryan J.J., Zhou H.; J. Biol. Chem. 279:32262-32268(2004). Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-981 AND LYS-1154, AND MASSSPECTROMETRY. | |
