UniProt ID | YP247_YEAST | |
---|---|---|
UniProt AC | Q12523 | |
Protein Name | WD repeat-containing protein YPL247C | |
Gene Name | YPL247C | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 523 | |
Subcellular Localization | Cytoplasm . Nucleus . | |
Protein Description | ||
Protein Sequence | MDPFHNGNKRSSISFGSSQRQPYNKNNYLSGTNGPSSAAQDQGRGPSPFGMSGNTTNGGNSKRNSGCDLSATYYASRSPMYSPLDFSPPVFSPNHSQLQQARGYAANIPVVSNLMNPSMASVCEYQSHYPLFGLDWSADDYVCLGSYKEDSRNKLQVLHSNDLLSWESVVDADVVYPVSKIQWVPSQLYPRKLATCSDSLRIWSVSPEERQFQEQINLSLCKYNRQHPANPAAADDMKVIGTFPPITSFDWNTVDTNLIISSSIDTTCIVWDLQSSHYVKTQLIAHDSEVFDVRFLTKSTQLFASCGGDGSVRVFDLRSLAHSTIIYEPPSSSVSGATAGTITPSSKGSDALLRLEPSPYDPNVLATFAADSNKIIILDMRNPESPILNLQGHGSSVNGIKWHPTKRNVLLSCGDDCQVLYWDLNSSFMEINAAGSKSPSIHGTSLEDPDGDTEMTDGGAGSGLNEDPLSLNNNSKQVCKTLETPNMMYANKTQEINNIAWRPQRGDWFGCVSGKKFQNVRVL | |
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 |
---|---|---|---|---|---|
9 | Acetylation | DPFHNGNKRSSISFG CCCCCCCCCCCCCCC | 55.87 | 25381059 | |
11 | Phosphorylation | FHNGNKRSSISFGSS CCCCCCCCCCCCCCC | 33.36 | 22369663 | |
12 | Phosphorylation | HNGNKRSSISFGSSQ CCCCCCCCCCCCCCC | 26.70 | 22369663 | |
14 | Phosphorylation | GNKRSSISFGSSQRQ CCCCCCCCCCCCCCC | 26.04 | 22369663 | |
17 | Phosphorylation | RSSISFGSSQRQPYN CCCCCCCCCCCCCCC | 22.68 | 30377154 | |
28 | Phosphorylation | QPYNKNNYLSGTNGP CCCCCCCCCCCCCCC | 16.19 | 22369663 | |
30 | Phosphorylation | YNKNNYLSGTNGPSS CCCCCCCCCCCCCCH | 32.96 | 22369663 | |
32 | Phosphorylation | KNNYLSGTNGPSSAA CCCCCCCCCCCCHHH | 33.36 | 22369663 | |
36 | Phosphorylation | LSGTNGPSSAAQDQG CCCCCCCCHHHHCCC | 33.73 | 22369663 | |
37 | Phosphorylation | SGTNGPSSAAQDQGR CCCCCCCHHHHCCCC | 30.66 | 22369663 | |
47 | Phosphorylation | QDQGRGPSPFGMSGN HCCCCCCCCCCCCCC | 35.37 | 22369663 | |
52 | Phosphorylation | GPSPFGMSGNTTNGG CCCCCCCCCCCCCCC | 29.30 | 22369663 | |
55 | Phosphorylation | PFGMSGNTTNGGNSK CCCCCCCCCCCCCCC | 25.76 | 22369663 | |
56 | Phosphorylation | FGMSGNTTNGGNSKR CCCCCCCCCCCCCCC | 35.55 | 22369663 | |
61 | Phosphorylation | NTTNGGNSKRNSGCD CCCCCCCCCCCCCCC | 35.95 | 22369663 | |
65 | Phosphorylation | GGNSKRNSGCDLSAT CCCCCCCCCCCCCCE | 44.85 | 22369663 | |
70 | Phosphorylation | RNSGCDLSATYYASR CCCCCCCCCEEECCC | 12.81 | 28889911 | |
78 | Phosphorylation | ATYYASRSPMYSPLD CEEECCCCCCCCCCC | 16.12 | 22369663 | |
81 | Phosphorylation | YASRSPMYSPLDFSP ECCCCCCCCCCCCCC | 15.55 | 22369663 | |
82 | Phosphorylation | ASRSPMYSPLDFSPP CCCCCCCCCCCCCCC | 16.85 | 22369663 | |
87 | Phosphorylation | MYSPLDFSPPVFSPN CCCCCCCCCCCCCCC | 28.14 | 22369663 | |
96 | Phosphorylation | PVFSPNHSQLQQARG CCCCCCHHHHHHHHH | 38.95 | 19779198 | |
319 | Phosphorylation | VRVFDLRSLAHSTII EEEEEHHHCCEEEEE | 36.89 | 22369663 | |
323 | Phosphorylation | DLRSLAHSTIIYEPP EHHHCCEEEEEECCC | 18.72 | 22369663 | |
324 | Phosphorylation | LRSLAHSTIIYEPPS HHHCCEEEEEECCCC | 11.09 | 22369663 | |
335 | Phosphorylation | EPPSSSVSGATAGTI CCCCCCCCCCCCCEE | 25.34 | 22369663 | |
338 | Phosphorylation | SSSVSGATAGTITPS CCCCCCCCCCEECCC | 29.19 | 22369663 | |
341 | Phosphorylation | VSGATAGTITPSSKG CCCCCCCEECCCCCC | 21.15 | 22369663 | |
343 | Phosphorylation | GATAGTITPSSKGSD CCCCCEECCCCCCCC | 19.56 | 22369663 | |
345 | Phosphorylation | TAGTITPSSKGSDAL CCCEECCCCCCCCCE | 35.71 | 22369663 | |
346 | Phosphorylation | AGTITPSSKGSDALL CCEECCCCCCCCCEE | 42.09 | 22369663 | |
438 | Phosphorylation | INAAGSKSPSIHGTS ECCCCCCCCCCCCCC | 26.10 | 28889911 | |
440 | Phosphorylation | AAGSKSPSIHGTSLE CCCCCCCCCCCCCCC | 34.02 | 20377248 | |
444 | Phosphorylation | KSPSIHGTSLEDPDG CCCCCCCCCCCCCCC | 18.90 | 21440633 | |
445 | Phosphorylation | SPSIHGTSLEDPDGD CCCCCCCCCCCCCCC | 34.06 | 19779198 | |
481 | Phosphorylation | NSKQVCKTLETPNMM CCHHHHHHCCCCCCC | 25.38 | 27017623 | |
484 | Phosphorylation | QVCKTLETPNMMYAN HHHHHCCCCCCCCCC | 24.07 | 27017623 | |
489 | Phosphorylation | LETPNMMYANKTQEI CCCCCCCCCCCCEEE | 9.03 | 27017623 |
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 YP247_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YP247_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 YP247_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
HSP60_YEAST | HSP60 | physical | 16554755 | |
PP2B1_YEAST | CNA1 | physical | 24930733 | |
PP2B2_YEAST | CMP2 | physical | 24930733 |
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-12; SER-47; SER-65;THR-343 AND SER-438, 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-65, AND MASSSPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND MASSSPECTROMETRY. |