UniProt ID | NCB2_YEAST | |
---|---|---|
UniProt AC | Q92317 | |
Protein Name | Negative cofactor 2 complex subunit beta | |
Gene Name | NCB2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 146 | |
Subcellular Localization | Nucleus . | |
Protein Description | Component of the NC2 complex which represses RNA polymerase II transcription through binding to SPT15/TBP and thereby inhibiting the assembly of the preinitiation complex. The NC2 complex may also mediate transcriptional activation from TATA-driven promoters through association with SPT15/TBP.. | |
Protein Sequence | MAGDSDNVSLPKATVQKMISEILDQDLMFTKDAREIIINSGIEFIMILSSMASEMADNEAKKTIAPEHVIKALEELEYNEFIPFLEEILLNFKGSQKVKETRDSKFKKSGLSEEELLRQQEELFRQSRSRLHHNSVSDPVKSEDSS | |
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 |
---|---|---|---|---|---|
5 | Phosphorylation | ---MAGDSDNVSLPK ---CCCCCCCCCCCH | 30.11 | 30377154 | |
9 | Phosphorylation | AGDSDNVSLPKATVQ CCCCCCCCCCHHHHH | 45.25 | 30377154 | |
109 | Phosphorylation | RDSKFKKSGLSEEEL CCHHHHHCCCCHHHH | 45.62 | 22369663 | |
112 | Phosphorylation | KFKKSGLSEEELLRQ HHHHCCCCHHHHHHH | 46.62 | 22369663 | |
127 | Phosphorylation | QEELFRQSRSRLHHN HHHHHHHHHHHHCCC | 28.15 | 24961812 | |
129 | Phosphorylation | ELFRQSRSRLHHNSV HHHHHHHHHHCCCCC | 44.43 | 22369663 | |
135 | Phosphorylation | RSRLHHNSVSDPVKS HHHHCCCCCCCCCCC | 20.74 | 22369663 | |
137 | Phosphorylation | RLHHNSVSDPVKSED HHCCCCCCCCCCCCC | 35.70 | 22369663 | |
141 | Sumoylation | NSVSDPVKSEDSS-- CCCCCCCCCCCCC-- | 54.22 | - | |
142 | Phosphorylation | SVSDPVKSEDSS--- CCCCCCCCCCCC--- | 47.04 | 22369663 | |
145 | Phosphorylation | DPVKSEDSS------ CCCCCCCCC------ | 33.62 | 22369663 | |
146 | Phosphorylation | PVKSEDSS------- CCCCCCCC------- | 57.47 | 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 NCB2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NCB2_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 NCB2_YEAST !! |
Kegg Drug | ||||||
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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-112; SER-135; SER-142;SER-145 AND SER-146, 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-145, AND MASSSPECTROMETRY. | |
"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-135; SER-137 ANDSER-142, AND MASS SPECTROMETRY. | |
"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-135 AND SER-145, ANDMASS SPECTROMETRY. |