UniProt ID | CBF5_YEAST | |
---|---|---|
UniProt AC | P33322 | |
Protein Name | H/ACA ribonucleoprotein complex subunit CBF5 | |
Gene Name | CBF5 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 483 | |
Subcellular Localization | Nucleus, nucleolus . Chromosome, centromere . Cytoplasm, cytoskeleton . | |
Protein Description | Catalytic subunit of H/ACA small nucleolar ribonucleoprotein (H/ACA snoRNP) complex, which catalyzes pseudouridylation of rRNA. [PubMed: 10523634] | |
Protein Sequence | MSKEDFVIKPEAAGASTDTSEWPLLLKNFDKLLVRSGHYTPIPAGSSPLKRDLKSYISSGVINLDKPSNPSSHEVVAWIKRILRCEKTGHSGTLDPKVTGCLIVCIDRATRLVKSQQGAGKEYVCIVRLHDALKDEKDLGRSLENLTGALFQRPPLISAVKRQLRVRTIYESNLIEFDNKRNLGVFWASCEAGTYMRTLCVHLGMLLGVGGHMQELRRVRSGALSENDNMVTLHDVMDAQWVYDNTRDESYLRSIIQPLETLLVGYKRIVVKDSAVNAVCYGAKLMIPGLLRYEEGIELYDEIVLITTKGEAIAVAIAQMSTVDLASCDHGVVASVKRCIMERDLYPRRWGLGPVAQKKKQMKADGKLDKYGRVNENTPEQWKKEYVPLDNAEQSTSSSQETKETEEEPKKAKEDSLIKEVETEKEEVKEDDSKKEKKEKKDKKEKKEKKEKKDKKEKKEKKEKKRKSEDGDSEEKKSKKSKK | |
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 | ------MSKEDFVIK ------CCHHHEEEC | 44.76 | 24961812 | |
3 | Acetylation | -----MSKEDFVIKP -----CCHHHEEECH | 61.06 | 24489116 | |
3 | Ubiquitination | -----MSKEDFVIKP -----CCHHHEEECH | 61.06 | 24961812 | |
9 | Ubiquitination | SKEDFVIKPEAAGAS CHHHEEECHHHCCCC | 31.35 | 23749301 | |
9 | Acetylation | SKEDFVIKPEAAGAS CHHHEEECHHHCCCC | 31.35 | 24489116 | |
31 | Acetylation | LLLKNFDKLLVRSGH HHHHCHHHHEECCCC | 39.31 | 24489116 | |
31 | Ubiquitination | LLLKNFDKLLVRSGH HHHHCHHHHEECCCC | 39.31 | 23749301 | |
36 | Phosphorylation | FDKLLVRSGHYTPIP HHHHEECCCCCCCCC | 23.57 | 21440633 | |
39 | Phosphorylation | LLVRSGHYTPIPAGS HEECCCCCCCCCCCC | 20.10 | 28889911 | |
40 | Phosphorylation | LVRSGHYTPIPAGSS EECCCCCCCCCCCCC | 14.74 | 22890988 | |
46 | Phosphorylation | YTPIPAGSSPLKRDL CCCCCCCCCCCHHHH | 30.78 | 22369663 | |
47 | Phosphorylation | TPIPAGSSPLKRDLK CCCCCCCCCCHHHHH | 33.08 | 22369663 | |
50 | Ubiquitination | PAGSSPLKRDLKSYI CCCCCCCHHHHHHHH | 47.45 | 23749301 | |
50 | Succinylation | PAGSSPLKRDLKSYI CCCCCCCHHHHHHHH | 47.45 | 23954790 | |
50 | Acetylation | PAGSSPLKRDLKSYI CCCCCCCHHHHHHHH | 47.45 | 24489116 | |
54 | Ubiquitination | SPLKRDLKSYISSGV CCCHHHHHHHHHCCC | 45.56 | 17644757 | |
66 | Ubiquitination | SGVINLDKPSNPSSH CCCCCCCCCCCCCHH | 54.21 | 17644757 | |
80 | Ubiquitination | HEVVAWIKRILRCEK HHHHHHHHHHHCCHH | 23.76 | 23749301 | |
80 | Acetylation | HEVVAWIKRILRCEK HHHHHHHHHHHCCHH | 23.76 | 24489116 | |
87 | Ubiquitination | KRILRCEKTGHSGTL HHHHCCHHCCCCCCC | 64.53 | 23749301 | |
114 | Ubiquitination | DRATRLVKSQQGAGK EHHHHHHHHCCCCCC | 47.33 | 23749301 | |
121 | Ubiquitination | KSQQGAGKEYVCIVR HHCCCCCCCEEEEEE | 45.39 | 23749301 | |
134 | Ubiquitination | VRLHDALKDEKDLGR EEHHHHHCCCHHHHH | 66.61 | 15699485 | |
134 | Acetylation | VRLHDALKDEKDLGR EEHHHHHCCCHHHHH | 66.61 | 22865919 | |
137 | Ubiquitination | HDALKDEKDLGRSLE HHHHCCCHHHHHHHH | 69.27 | 22106047 | |
161 | Acetylation | PPLISAVKRQLRVRT CHHHHHHHHHHHHHH | 33.86 | 24489116 | |
161 | Ubiquitination | PPLISAVKRQLRVRT CHHHHHHHHHHHHHH | 33.86 | 23749301 | |
180 | Acetylation | NLIEFDNKRNLGVFW CCEEECCCCCEEEEE | 44.50 | 24489116 | |
180 | Ubiquitination | NLIEFDNKRNLGVFW CCEEECCCCCEEEEE | 44.50 | 23749301 | |
254 | Phosphorylation | RDESYLRSIIQPLET CCHHHHHHHHHHHHH | 22.81 | 21440633 | |
267 | Ubiquitination | ETLLVGYKRIVVKDS HHHHCCCEEEEECHH | 29.71 | 23749301 | |
272 | Ubiquitination | GYKRIVVKDSAVNAV CCEEEEECHHHHHHH | 34.76 | 23749301 | |
284 | Ubiquitination | NAVCYGAKLMIPGLL HHHHHCCCHHCCCCC | 33.94 | 17644757 | |
358 | Ubiquitination | GLGPVAQKKKQMKAD CCCHHHHHHHHHHCC | 52.80 | 17644757 | |
359 | Ubiquitination | LGPVAQKKKQMKADG CCHHHHHHHHHHCCC | 35.84 | 17644757 | |
370 | Ubiquitination | KADGKLDKYGRVNEN HCCCCCCCCCCCCCC | 61.10 | 15699485 | |
371 | Phosphorylation | ADGKLDKYGRVNENT CCCCCCCCCCCCCCC | 15.16 | 21440633 | |
378 | Phosphorylation | YGRVNENTPEQWKKE CCCCCCCCHHHHHHH | 23.25 | 22369663 | |
383 | Ubiquitination | ENTPEQWKKEYVPLD CCCHHHHHHHCCCCC | 35.11 | 17644757 | |
384 | Ubiquitination | NTPEQWKKEYVPLDN CCHHHHHHHCCCCCC | 51.85 | 23749301 | |
384 | Acetylation | NTPEQWKKEYVPLDN CCHHHHHHHCCCCCC | 51.85 | 24489116 | |
386 | Phosphorylation | PEQWKKEYVPLDNAE HHHHHHHCCCCCCHH | 19.08 | 22890988 | |
395 | Phosphorylation | PLDNAEQSTSSSQET CCCCHHHCCCCCCCC | 23.05 | 22369663 | |
396 | Phosphorylation | LDNAEQSTSSSQETK CCCHHHCCCCCCCCC | 32.11 | 22369663 | |
397 | Phosphorylation | DNAEQSTSSSQETKE CCHHHCCCCCCCCCC | 32.99 | 25521595 | |
398 | Phosphorylation | NAEQSTSSSQETKET CHHHCCCCCCCCCCC | 35.81 | 22369663 | |
399 | Phosphorylation | AEQSTSSSQETKETE HHHCCCCCCCCCCCC | 31.63 | 22369663 | |
402 | Phosphorylation | STSSSQETKETEEEP CCCCCCCCCCCCCCC | 26.92 | 22369663 | |
403 | Acetylation | TSSSQETKETEEEPK CCCCCCCCCCCCCCH | 62.98 | 24489116 | |
403 | Ubiquitination | TSSSQETKETEEEPK CCCCCCCCCCCCCCH | 62.98 | 17644757 | |
405 | Phosphorylation | SSQETKETEEEPKKA CCCCCCCCCCCCHHH | 50.70 | 22369663 | |
416 | Phosphorylation | PKKAKEDSLIKEVET CHHHHHHHHHHHHHH | 32.84 | 25521595 | |
423 | Phosphorylation | SLIKEVETEKEEVKE HHHHHHHHHHHHHHC | 58.49 | 25521595 | |
468 | Phosphorylation | KKEKKRKSEDGDSEE HHHHHHHCCCCCHHH | 44.98 | 27717283 | |
473 | Phosphorylation | RKSEDGDSEEKKSKK HHCCCCCHHHHHHHH | 53.86 | 27214570 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
399 | S | Phosphorylation | Kinase | ATM/ATR | - | GPS |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CBF5_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 CBF5_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-47; THR-378; THR-396;SER-397; SER-398; SER-399 AND THR-402, 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 THR-378; SER-399 ANDTHR-405, 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-47 AND THR-378, 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 THR-378, AND MASSSPECTROMETRY. |