UniProt ID | CND3_YEAST | |
---|---|---|
UniProt AC | Q06680 | |
Protein Name | Condensin complex subunit 3 | |
Gene Name | YCG1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1035 | |
Subcellular Localization | Nucleus. Cytoplasm. Chromosome. In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromos | |
Protein Description | Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. The condensin complex probably also plays a role during interphase.. | |
Protein Sequence | MQDPDGIDINTKIFNSVAEVFQKAQGSYAGHRKHIAVLKKIQSKAVEQGYEDAFNFWFDKLVTKILPLKKNEIIGDRIVKLVAAFIASLERELILAKKQNYKLTNDEEGIFSRFVDQFIRHVLRGVESPDKNVRFRVLQLLAVIMDNIGEIDESLFNLLILSLNKRIYDREPTVRIQAVFCLTKFQDEEQTEHLTELSDNEENFEATRTLVASIQNDPSAEVRRAAMLNLINDNNTRPYILERARDVNIVNRRLVYSRILKSMGRKCFDDIEPHIFDQLIEWGLEDRELSVRNACKRLIAHDWLNALDGDLIELLEKLDVSRSSVCVKAIEALFQSRPDILSKIKFPESIWKDFTVEIAFLFRAIYLYCLDNNITEMLEENFPEASKLSEHLNHYILLRYHHNDISNDSQSHFDYNTLEFIIEQLSIAAERYDYSDEVGRRSMLTVVRNMLALTTLSEPLIKIGIRVMKSLSINEKDFVTMAIEIINDIRDDDIEKQEQEEKIKSKKINRRNETSVDEEDENGTHNDEVNEDEEDDNISSFHSAVENLVQGNGNVSESDIINNLPPEKEASSATIVLCLTRSSYMLELVNTPLTENILIASLMDTLITPAVRNTAPNIRELGVKNLGLCCLLDVKLAIDNMYILGMCVSKGNASLKYIALQVIVDIFSVHGNTVVDGEGKVDSISLHKIFYKVLKNNGLPECQVIAAEGLCKLFLADVFTDDDLFETLVLSYFSPINSSNEALVQAFAFCIPVYCFSHPAHQQRMSRTAADILLRLCVLWDDLQSSVIPEVDREAMLKPNIIFQQLLFWTDPRNLVNQTGSTKKDTVQLTFLIDVLKIYAQIEKKEIKKMIITNINAIFLSSEQDYSTLKELLEYSDDIAENDNLDNVSKNALDKLRNNLNSLIEEINERSETQTKDENNTANDQYSSILGNSFNKSSNDTIEHAADITDGNNTELTKTTVNISAVDNTTEQSNSRKRTRSEAEQIDTSKNLENMSIQDTSTVAKNVSFVLPDEKSDAMSIDEEDKDSESFSEVC | |
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 |
---|---|---|---|---|---|
16 | Phosphorylation | INTKIFNSVAEVFQK CCHHHHHHHHHHHHH | 16.38 | 19481522 | |
191 | Phosphorylation | KFQDEEQTEHLTELS HCCCHHHHHHHHHCC | 28.75 | 23749301 | |
195 | Phosphorylation | EEQTEHLTELSDNEE HHHHHHHHHCCCCHH | 36.47 | 23607784 | |
198 | Phosphorylation | TEHLTELSDNEENFE HHHHHHCCCCHHHHH | 31.96 | 17330950 | |
207 | Phosphorylation | NEENFEATRTLVASI CHHHHHHHHHHHHHH | 19.59 | 23607784 | |
862 | Phosphorylation | INAIFLSSEQDYSTL CHHHHCCCCCCHHHH | 41.23 | 27017623 | |
866 | Phosphorylation | FLSSEQDYSTLKELL HCCCCCCHHHHHHHH | 11.84 | 27017623 | |
867 | Phosphorylation | LSSEQDYSTLKELLE CCCCCCHHHHHHHHH | 35.24 | 27017623 | |
868 | Phosphorylation | SSEQDYSTLKELLEY CCCCCHHHHHHHHHC | 35.30 | 27017623 | |
902 | Phosphorylation | KLRNNLNSLIEEINE HHHHHHHHHHHHHHH | 33.61 | 21440633 | |
911 | Phosphorylation | IEEINERSETQTKDE HHHHHHHCCCCCCCC | 38.53 | 25521595 | |
913 | Phosphorylation | EINERSETQTKDENN HHHHHCCCCCCCCCC | 42.67 | 19779198 | |
915 | Phosphorylation | NERSETQTKDENNTA HHHCCCCCCCCCCCC | 48.13 | 19823750 | |
921 | Phosphorylation | QTKDENNTANDQYSS CCCCCCCCCHHHHHH | 38.12 | 23749301 | |
933 | Phosphorylation | YSSILGNSFNKSSND HHHHHCCCCCCCCCC | 28.53 | 20190278 | |
937 | Phosphorylation | LGNSFNKSSNDTIEH HCCCCCCCCCCCCCC | 35.16 | 29734811 | |
938 | Phosphorylation | GNSFNKSSNDTIEHA CCCCCCCCCCCCCCC | 40.09 | 21551504 | |
941 | Phosphorylation | FNKSSNDTIEHAADI CCCCCCCCCCCCCCC | 32.30 | 21440633 | |
949 | Phosphorylation | IEHAADITDGNNTEL CCCCCCCCCCCCCEE | 38.10 | 21440633 | |
960 | Phosphorylation | NTELTKTTVNISAVD CCEEEEEEEEEEECC | 17.08 | 19481522 | |
964 | Phosphorylation | TKTTVNISAVDNTTE EEEEEEEEECCCCCC | 19.62 | 28889911 | |
969 | Phosphorylation | NISAVDNTTEQSNSR EEEECCCCCCCCCCC | 27.52 | 24961812 | |
979 | Phosphorylation | QSNSRKRTRSEAEQI CCCCCCCCHHHHHHC | 41.40 | 29136822 | |
981 | Phosphorylation | NSRKRTRSEAEQIDT CCCCCCHHHHHHCCC | 40.31 | 25521595 | |
988 | Phosphorylation | SEAEQIDTSKNLENM HHHHHCCCCCCCCCC | 43.14 | 23749301 | |
989 | Phosphorylation | EAEQIDTSKNLENMS HHHHCCCCCCCCCCC | 18.79 | 23749301 | |
996 | Phosphorylation | SKNLENMSIQDTSTV CCCCCCCCCCCHHHH | 28.78 | 20377248 | |
1000 | Phosphorylation | ENMSIQDTSTVAKNV CCCCCCCHHHHHHHC | 15.21 | 24961812 | |
1001 | Phosphorylation | NMSIQDTSTVAKNVS CCCCCCHHHHHHHCE | 29.22 | 20377248 | |
1002 | Phosphorylation | MSIQDTSTVAKNVSF CCCCCHHHHHHHCEE | 26.95 | 24961812 | |
1008 | Phosphorylation | STVAKNVSFVLPDEK HHHHHHCEEECCCCC | 21.02 | 25533186 | |
1016 | Phosphorylation | FVLPDEKSDAMSIDE EECCCCCCCCCCCCC | 28.67 | 21551504 | |
1020 | Phosphorylation | DEKSDAMSIDEEDKD CCCCCCCCCCCCCCC | 28.71 | 28889911 | |
1028 | Phosphorylation | IDEEDKDSESFSEVC CCCCCCCCCCHHCCC | 40.66 | 28889911 | |
1030 | Phosphorylation | EEDKDSESFSEVC-- CCCCCCCCHHCCC-- | 37.72 | 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 CND3_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CND3_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 CND3_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-198; SER-933; THR-979;SER-981 AND SER-1008, 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-198 AND SER-933, ANDMASS 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-981, AND MASSSPECTROMETRY. |