UniProt ID | SIS2_YEAST | |
---|---|---|
UniProt AC | P36024 | |
Protein Name | Phosphopantothenoylcysteine decarboxylase subunit SIS2 | |
Gene Name | SIS2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 562 | |
Subcellular Localization | Nucleus. Cytoplasm. | |
Protein Description | Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis. Acts as an inhibitory subunit of protein phosphatase PPZ1, which is involved in many cellular processes such as G1-S transition or salt tolerance. Also modulates the expression of the ENA1 ATPase.. | |
Protein Sequence | MTAVASTSGKQDADHNQSIECPRFSRGQKEILLDHEDAKGKDSIINSPVSGRQSISPTLSNATTTTTKSIMNATGTSGAVVSNTPEPGLKRVPAVTFSDLKQQQKQDSLTQLKNDSERTKSPNSNPAPVSNSIPGNHAVIPNHTNTSRTTQLSGSPLVNEMKDYDPKKKDSALKIVDTMKPDKIMATSTPISRENNKVTAKAPTSITLRKEDAQDQANNVSGQINVRSTPEETPVKQSVIPSIIPKRENSKNLDPRLPQDDGKLHVLFGATGSLSVFKIKPMIKKLEEIYGRDRISIQVILTQSATQFFEQRYTKKIIKSSEKLNKMSQYESTPATPVTPTPGQCNMAQVVELPPHIQLWTDQDEWDAWKQRTDPVLHIELRRWADILVVAPLTANTLSKIALGLCDNLLTSVIRAWNPSYPILLAPSMVSSTFNSMMTKKQLQTIKEEMSWVTVFKPSEKVMDINGDIGLGGMMDWNEIVNKIVMKLGGYPKNNEEEDDDEDEEEDDDEEEDTEDKNENNNDDDDDDDDDDDDDDDDDDDDDDDDEDEDEAETPGIIDKHQ | |
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 |
---|---|---|---|---|---|
18 | Phosphorylation | QDADHNQSIECPRFS CCCCCCCCCCCCCCC | 26.18 | 23749301 | |
43 | Phosphorylation | EDAKGKDSIINSPVS HHHCCCCCCCCCCCC | 28.93 | 22369663 | |
47 | Phosphorylation | GKDSIINSPVSGRQS CCCCCCCCCCCCCCC | 19.10 | 22369663 | |
50 | Phosphorylation | SIINSPVSGRQSISP CCCCCCCCCCCCCCC | 31.48 | 22369663 | |
54 | Phosphorylation | SPVSGRQSISPTLSN CCCCCCCCCCCCCCC | 24.55 | 22369663 | |
56 | Phosphorylation | VSGRQSISPTLSNAT CCCCCCCCCCCCCCC | 19.65 | 22369663 | |
58 | Phosphorylation | GRQSISPTLSNATTT CCCCCCCCCCCCCCC | 35.71 | 22369663 | |
60 | Phosphorylation | QSISPTLSNATTTTT CCCCCCCCCCCCCCC | 27.22 | 22369663 | |
63 | Phosphorylation | SPTLSNATTTTTKSI CCCCCCCCCCCCHHH | 29.00 | 22369663 | |
64 | Phosphorylation | PTLSNATTTTTKSIM CCCCCCCCCCCHHHH | 21.53 | 22369663 | |
65 | Phosphorylation | TLSNATTTTTKSIMN CCCCCCCCCCHHHHH | 28.28 | 22369663 | |
66 | Phosphorylation | LSNATTTTTKSIMNA CCCCCCCCCHHHHHC | 30.09 | 22369663 | |
67 | Phosphorylation | SNATTTTTKSIMNAT CCCCCCCCHHHHHCC | 22.24 | 22369663 | |
69 | Phosphorylation | ATTTTTKSIMNATGT CCCCCCHHHHHCCCC | 25.61 | 28152593 | |
74 | Phosphorylation | TKSIMNATGTSGAVV CHHHHHCCCCCCCEE | 35.67 | 27017623 | |
76 | Phosphorylation | SIMNATGTSGAVVSN HHHHCCCCCCCEECC | 21.45 | 30377154 | |
77 | Phosphorylation | IMNATGTSGAVVSNT HHHCCCCCCCEECCC | 26.54 | 30377154 | |
82 | Phosphorylation | GTSGAVVSNTPEPGL CCCCCEECCCCCCCC | 28.52 | 22369663 | |
84 | Phosphorylation | SGAVVSNTPEPGLKR CCCEECCCCCCCCCC | 22.86 | 22369663 | |
96 | Phosphorylation | LKRVPAVTFSDLKQQ CCCCCEEEHHHHHHH | 21.37 | 30377154 | |
101 | Acetylation | AVTFSDLKQQQKQDS EEEHHHHHHHHHHHH | 51.56 | 24489116 | |
108 | Phosphorylation | KQQQKQDSLTQLKND HHHHHHHHHHHHHCH | 30.72 | 22369663 | |
110 | Phosphorylation | QQKQDSLTQLKNDSE HHHHHHHHHHHCHHH | 35.49 | 22369663 | |
119 | Phosphorylation | LKNDSERTKSPNSNP HHCHHHCCCCCCCCC | 31.64 | 22369663 | |
121 | Phosphorylation | NDSERTKSPNSNPAP CHHHCCCCCCCCCCC | 28.80 | 22369663 | |
124 | Phosphorylation | ERTKSPNSNPAPVSN HCCCCCCCCCCCCCC | 47.80 | 22369663 | |
130 | Phosphorylation | NSNPAPVSNSIPGNH CCCCCCCCCCCCCCC | 24.65 | 22369663 | |
144 | Phosphorylation | HAVIPNHTNTSRTTQ CCCCCCCCCCCCCEE | 47.00 | 21551504 | |
149 | Phosphorylation | NHTNTSRTTQLSGSP CCCCCCCCEECCCCC | 20.75 | 22369663 | |
150 | Phosphorylation | HTNTSRTTQLSGSPL CCCCCCCEECCCCCC | 26.80 | 22369663 | |
153 | Phosphorylation | TSRTTQLSGSPLVNE CCCCEECCCCCCHHH | 27.66 | 22369663 | |
155 | Phosphorylation | RTTQLSGSPLVNEMK CCEECCCCCCHHHCC | 16.22 | 22369663 | |
180 | Acetylation | LKIVDTMKPDKIMAT CHHHHCCCCCCEEEE | 52.75 | 24489116 | |
183 | Acetylation | VDTMKPDKIMATSTP HHCCCCCCEEEECCC | 42.80 | 24489116 | |
187 | Phosphorylation | KPDKIMATSTPISRE CCCCEEEECCCCCCC | 18.76 | 22369663 | |
188 | Phosphorylation | PDKIMATSTPISREN CCCEEEECCCCCCCC | 23.73 | 22369663 | |
189 | Phosphorylation | DKIMATSTPISRENN CCEEEECCCCCCCCC | 21.93 | 22369663 | |
192 | Phosphorylation | MATSTPISRENNKVT EEECCCCCCCCCEEE | 34.44 | 22369663 | |
199 | Phosphorylation | SRENNKVTAKAPTSI CCCCCEEEEECCCEE | 24.85 | 19823750 | |
205 | Phosphorylation | VTAKAPTSITLRKED EEEECCCEEEEEHHH | 16.71 | 21551504 | |
221 | Phosphorylation | QDQANNVSGQINVRS HHHHHCCCCEEECCC | 27.40 | 21440633 | |
228 | Phosphorylation | SGQINVRSTPEETPV CCEEECCCCCCCCCC | 43.99 | 29136822 | |
229 | Phosphorylation | GQINVRSTPEETPVK CEEECCCCCCCCCCC | 24.93 | 29136822 | |
233 | Phosphorylation | VRSTPEETPVKQSVI CCCCCCCCCCCCHHC | 31.55 | 29136822 | |
320 | Phosphorylation | YTKKIIKSSEKLNKM HHHHHHHCHHHHHHH | 33.06 | 29136822 | |
321 | Phosphorylation | TKKIIKSSEKLNKMS HHHHHHCHHHHHHHH | 33.48 | 30377154 | |
421 | Phosphorylation | IRAWNPSYPILLAPS HHHHCCCCCEEECHH | 8.78 | 28132839 | |
491 | Phosphorylation | IVMKLGGYPKNNEEE HHHHHCCCCCCCCCC | 14.83 | 21551504 | |
514 | Phosphorylation | DDDEEEDTEDKNENN CCCCCCCCCCCCCCC | 49.73 | 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 SIS2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SIS2_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 SIS2_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-47; SER-50; SER-54;SER-56 AND SER-155, 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-47; SER-50; SER-54 ANDSER-56, 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-47; SER-50 AND SER-54,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-56, AND MASSSPECTROMETRY. |