UniProt ID | CBF3A_YEAST | |
---|---|---|
UniProt AC | P32504 | |
Protein Name | Centromere DNA-binding protein complex CBF3 subunit A | |
Gene Name | CBF2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 956 | |
Subcellular Localization | Nucleus . Chromosome, centromere . Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body . Spindle midzone during anaphase B. | |
Protein Description | Acts as a component of the centromere DNA-binding protein complex CBF3, which is essential for chromosome segregation and movement of centromeres along microtubules. CBF3 is required for the recruitment of other kinetochore complexes to CEN DNA. It plays a role in the attachment of chromosomes to the spindle and binds selectively to a highly conserved DNA sequence called CDEIII, found in centromers and in several promoters.. | |
Protein Sequence | MRSSILFLLKLMKIMDVQQQQEAMSSEDRFQELVDSLKPRTAHQYKTYYTKYIQWCQLNQIIPTPEDNSVNSVPYKDLPISAELIHWFLLDTLITDDKPGEKREETEDLDEEEENSFKIATLKKIIGSLNFLSKLCKVHENPNANIDTKYLESVTKLHTHWIDSQKAITTNETNNTNTQVLCPPLLKVSLNLWNPETNHLSEKFFKTCSEKLRFLVDFQLRSYLNLSFEERSKIRFGSLKLGKRDRDAIIYHKVTHSAEKKDTPGHHQLLALLPQDCPFICPQTTLAAYLYLRFYGIPSVSKGDGFPNLNADENGSLLQDIPILRGKSLTTYPREETFSNYYTTVFRYCHLPYKRREYFNKCNLVYPTWDEDTFRTFFNEENHGNWLEQPEAFAFPDKIPFDFKKIMNFKSPYTSYSTNAKKDPFPPPKDLLVQIFPEIDEYKRHDYEGLSQNSRDFLDLMEVLRERFLSNLPWIYKFFPNHDIFQDPIFGNSDFQSYFNDKTIHSKGSPILSFDILPGFNKIYKNKTNFYSLLIERPSQLTFASSHNPDTHPTQKQESEGPLQMSQLDTTQLNELLKQQSFEYVQFQTLSNFQILLSVFNKIFEKLEMKKSSRGYILHQLNLFKITLDERIKKSKIDDADKFIRDNQPIKKEENIVNEDGPNTSRRTKRPKQIRLLSIADSSDESSTEDSNVFKKDGESIEDGAYGENEDENDSEMQEQLKSMINELINSKISTFLRDQMDQFELKINALLDKILEEKVTRIIEQKLGSHTGKFSTLKRPQLYMTEEHNVGFDMEVPKKLRTSGKYAETVKDNDDHQAMSTTASPSPEQDQEAKSYTDEQEFMLDKSIDSIEGIILEWFTPNAKYANQCVHSMNKSGNKSWRANCEALYKERKSIVEFYIYLVNHESLDRYKAVDICEKLRDQNEGSFSRLAKFLRKWRHDHQNSFDGLLVYLSN | |
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 |
---|---|---|---|---|---|
106 | Phosphorylation | PGEKREETEDLDEEE CCCCCCCCCCCCHHH | 30.00 | 21551504 | |
211 | Acetylation | FFKTCSEKLRFLVDF HHHHHHHHHHHHHHH | 28.77 | 25381059 | |
411 | Phosphorylation | KKIMNFKSPYTSYST HHHHCCCCCCCCCCC | 20.99 | 28889911 | |
413 | Phosphorylation | IMNFKSPYTSYSTNA HHCCCCCCCCCCCCC | 18.53 | 28889911 | |
415 | Phosphorylation | NFKSPYTSYSTNAKK CCCCCCCCCCCCCCC | 15.96 | 28889911 | |
416 | Phosphorylation | FKSPYTSYSTNAKKD CCCCCCCCCCCCCCC | 16.24 | 28889911 | |
506 | Phosphorylation | FNDKTIHSKGSPILS HCCCCCCCCCCCCEE | 34.56 | 28889911 | |
509 | Phosphorylation | KTIHSKGSPILSFDI CCCCCCCCCCEEEEE | 16.71 | 28889911 | |
532 | Phosphorylation | KNKTNFYSLLIERPS CCCCCCHHHEECCHH | 16.74 | 22890988 | |
556 | Sumoylation | PDTHPTQKQESEGPL CCCCCCCCCCCCCCC | 59.52 | - | |
559 | Phosphorylation | HPTQKQESEGPLQMS CCCCCCCCCCCCCHH | 45.41 | 21551504 | |
566 | Phosphorylation | SEGPLQMSQLDTTQL CCCCCCHHHCCHHHH | 18.03 | 28889911 | |
651 | Sumoylation | IRDNQPIKKEENIVN HHCCCCCCCHHHCCC | 61.90 | - | |
664 | Phosphorylation | VNEDGPNTSRRTKRP CCCCCCCCCCCCCCC | 27.09 | 29688323 | |
665 | Phosphorylation | NEDGPNTSRRTKRPK CCCCCCCCCCCCCCC | 26.80 | 23749301 | |
668 | Phosphorylation | GPNTSRRTKRPKQIR CCCCCCCCCCCCEEE | 30.23 | 21551504 | |
678 | Phosphorylation | PKQIRLLSIADSSDE CCEEEEEEECCCCCC | 21.96 | 19795423 | |
682 | Phosphorylation | RLLSIADSSDESSTE EEEEECCCCCCCCCC | 30.57 | 19795423 | |
683 | Phosphorylation | LLSIADSSDESSTED EEEECCCCCCCCCCC | 46.04 | 19795423 | |
686 | Phosphorylation | IADSSDESSTEDSNV ECCCCCCCCCCCCCC | 47.77 | 19795423 | |
687 | Phosphorylation | ADSSDESSTEDSNVF CCCCCCCCCCCCCCC | 33.49 | 19795423 | |
688 | Phosphorylation | DSSDESSTEDSNVFK CCCCCCCCCCCCCCC | 53.76 | 19795423 | |
691 | Phosphorylation | DESSTEDSNVFKKDG CCCCCCCCCCCCCCC | 28.76 | 19795423 | |
700 | Phosphorylation | VFKKDGESIEDGAYG CCCCCCCCCCCCCCC | 36.49 | 25704821 | |
706 | Phosphorylation | ESIEDGAYGENEDEN CCCCCCCCCCCCCCC | 30.42 | 28889911 | |
715 | Phosphorylation | ENEDENDSEMQEQLK CCCCCCHHHHHHHHH | 46.69 | 23749301 | |
774 | Acetylation | KLGSHTGKFSTLKRP HHCCCCCCCCCCCCC | 36.98 | 25381059 | |
779 | Sumoylation | TGKFSTLKRPQLYMT CCCCCCCCCCEEEEE | 63.22 | - | |
806 | Acetylation | KKLRTSGKYAETVKD HHHCCCCCCEEECCC | 40.84 | 22865919 | |
821 | Phosphorylation | NDDHQAMSTTASPSP CCCCCCCCCCCCCCH | 26.14 | 20377248 | |
822 | Phosphorylation | DDHQAMSTTASPSPE CCCCCCCCCCCCCHH | 17.19 | 28889911 | |
823 | Phosphorylation | DHQAMSTTASPSPEQ CCCCCCCCCCCCHHH | 20.17 | 21551504 | |
825 | Phosphorylation | QAMSTTASPSPEQDQ CCCCCCCCCCHHHHH | 24.66 | 20377248 | |
827 | Phosphorylation | MSTTASPSPEQDQEA CCCCCCCCHHHHHHH | 38.28 | 20377248 | |
836 | Phosphorylation | EQDQEAKSYTDEQEF HHHHHHHHCCHHHHH | 40.07 | 22369663 | |
837 | Phosphorylation | QDQEAKSYTDEQEFM HHHHHHHCCHHHHHH | 19.94 | 22890988 | |
838 | Phosphorylation | DQEAKSYTDEQEFML HHHHHHCCHHHHHHH | 39.90 | 22890988 | |
890 | Phosphorylation | RANCEALYKERKSIV HHHHHHHHHHHHHHH | 20.18 | 28889911 |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CBF3A_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 CBF3A_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-566; TYR-837 ANDTYR-890, AND MASS SPECTROMETRY. |