| UniProt ID | CND1_YEAST | |
|---|---|---|
| UniProt AC | Q06156 | |
| Protein Name | Condensin complex subunit 1 | |
| Gene Name | YCS4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1176 | |
| Subcellular Localization | Nucleus . Chromosome . Nuclear throughout the cell cycle. During mitosis, most of the condensin complex is associated with the chromatin. At the onset of prophase, condensin associates with chromosome arms and to chromosome condensation. At anaphase, | |
| 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 | MSGFSLSEYLTKFQTTDRESYPRLQDPSRELNVIIDQLAVSPEQIDASPDSLEALIDLCHDFPHLTPKLQTQLSYLISSSLSNLSKDIKANLSSNVNFTEIGGLIPQWKRHLEEYGYLIQVLLTFLQDELHKVSSQSTNLNRSAKNSKNDSANVELFKRDCNQMENLLESITKLLEINLSKIFQTTPEKDLFIGLFTRPLFVLLEIEPVTKVSSLKMFIQRILAMCVKNHGQSSSIQSSLMTNLTYFLHLSVFNAELLKLLNDEYNYPQLTEDILKEISTRVFNAKDTTGPKAISNFLIKLSELSPGIMLRQMNLVITLLNNSSITLRCSVVEACGNIVAELAQDPQTMEHYKQQIAVLIELLEERFQDSNPYVRTKAIQGCSKICDLSSKFNKSKAKFTSLAVRSLQDRSSLVRRNSVKLLSKLLLKHPFKAIHGSQLRLSEWEEYLKGSESQLNSTLKKVESQETLNDTIERSLIEEEVEQDEGQCRTELEGSFNKSAELSRIENEVENINATNTSVLMKLKLMIVYYKDAISFIKEIHKSIELISNLLFSKNRNEVLESMDFLVLADAFDIELSEFGIKKMLHLVWMKGTNDEGTSISVHLIECYKQLFLTAPDSCNMQEKAAHIAKNLINLSIGASIADLASLEQLLGMMYEQKLIDQHVINILWAIYNSASKASMQKEQNVNNRDSEKGFSKEQIHGSIIILGMLSLADNEIALKGLESLLNIGLGAVGLKDLTLCRYSCLALERMVPKRSTIITKAINQELEDVAVKKLYAIIINYTKDNEYYPMCEQALSALFTISSKPDILATDLIREKTMMTFGKPEEEDSILSLEQSSRVVSLSQLLFIVGQVAIKTLVYLEKCEAEFKKRKIEAETRNGKVKNQGADVTNTTQDNGGDKELEMIGGTNEDDFTDAIQFVKENELLFGEKSILGKFCPIVEEIVSNSSRFSDPMLQRTATLCLEKLMCLSSKYCEKSLPLLITVMEKSPDPTIRSNAVLGLGDMAVCFNNLVDENTDYLYRRLHDENLMVQRTCLMTVTFLILAGQVKVKGQLGEMAKCLDNPDQGISDMCRLFFTELASKDNAIYNGFIDIFSNLSSDDLLGKESFKKIIKFLLTFIDKERHQKQLNEKLVGRLRKCETQKQWDDIAFVLNNLPYKNEDVTALLEQGFKVVSAKE | |
| 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 |
|---|---|---|---|---|---|
| 9 | Phosphorylation | SGFSLSEYLTKFQTT CCCCHHHHHHHHCCC | 19.12 | 28132839 | |
| 74 | Phosphorylation | PKLQTQLSYLISSSL HHHHHHHHHHHHHHH | 14.21 | 28889911 | |
| 75 | Phosphorylation | KLQTQLSYLISSSLS HHHHHHHHHHHHHHH | 19.35 | 28889911 | |
| 78 | Phosphorylation | TQLSYLISSSLSNLS HHHHHHHHHHHHCCC | 15.98 | 28889911 | |
| 82 | Phosphorylation | YLISSSLSNLSKDIK HHHHHHHHCCCHHHH | 37.36 | 28889911 | |
| 85 | Phosphorylation | SSSLSNLSKDIKANL HHHHHCCCHHHHHHC | 32.31 | 28889911 | |
| 370 | Phosphorylation | LEERFQDSNPYVRTK HHHHHCCCCCHHHHH | 28.99 | 28889911 | |
| 406 | Phosphorylation | FTSLAVRSLQDRSSL HHHHHHHHHHCHHHH | 24.63 | 28889911 | |
| 437 | Phosphorylation | PFKAIHGSQLRLSEW CCHHHCCCCCCHHHH | 16.33 | 30377154 | |
| 464 | Phosphorylation | STLKKVESQETLNDT HHHHHHHCHHHHHHH | 35.98 | 17563356 | |
| 467 | Phosphorylation | KKVESQETLNDTIER HHHHCHHHHHHHHHH | 24.19 | 23749301 | |
| 471 | Phosphorylation | SQETLNDTIERSLIE CHHHHHHHHHHHHHH | 24.54 | 19481522 | |
| 475 | Phosphorylation | LNDTIERSLIEEEVE HHHHHHHHHHHHHHH | 22.40 | 27214570 | |
| 490 | Phosphorylation | QDEGQCRTELEGSFN CCCCCCHHHHHCCCC | 53.18 | 19779198 | |
| 495 | Phosphorylation | CRTELEGSFNKSAEL CHHHHHCCCCCHHHH | 19.10 | 25704821 | |
| 499 | Phosphorylation | LEGSFNKSAELSRIE HHCCCCCHHHHHHHH | 28.25 | 23749301 | |
| 503 | Phosphorylation | FNKSAELSRIENEVE CCCHHHHHHHHHHHH | 23.79 | 28889911 | |
| 691 | Phosphorylation | QNVNNRDSEKGFSKE HCCCCCHHCCCCCHH | 37.66 | 21551504 | |
| 830 | Phosphorylation | GKPEEEDSILSLEQS CCCHHHCCCCCHHHH | 28.80 | 25752575 | |
| 833 | Phosphorylation | EEEDSILSLEQSSRV HHHCCCCCHHHHHCC | 28.34 | 23749301 | |
| 860 | Phosphorylation | VAIKTLVYLEKCEAE HHHHHHHHHHHHHHH | 16.56 | 26447709 | |
| 890 | Phosphorylation | KNQGADVTNTTQDNG CCCCCCCCCCCCCCC | 27.65 | 27717283 | |
| 892 | Phosphorylation | QGADVTNTTQDNGGD CCCCCCCCCCCCCCC | 19.23 | 28889911 | |
| 893 | Phosphorylation | GADVTNTTQDNGGDK CCCCCCCCCCCCCCC | 35.67 | 28889911 | |
| 931 | Phosphorylation | ELLFGEKSILGKFCP CCCCCCCCHHHHHCH | 20.81 | 19481522 | |
| 983 | Phosphorylation | KSLPLLITVMEKSPD HHHCEEEEEEECCCC | 17.48 | 21551504 |
| 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 CND1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CND1_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 CND1_YEAST !! | ||||||
| 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-464, AND MASSSPECTROMETRY. | |
| "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-464, AND MASSSPECTROMETRY. | |
