| UniProt ID | CND2_YEAST | |
|---|---|---|
| UniProt AC | P38170 | |
| Protein Name | Condensin complex subunit 2 | |
| Gene Name | BRN1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 754 | |
| 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 chro | |
| 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 | MTTQLRYENNDDDERVEYNLFTNRSTMMANFEEWIKMATDNKINSRNSWNFALIDYFYDLDVLKDGENNINFQKASATLDGCIKIYSSRVDSVTTETGKLLSGLAQRKTNGASNGDDSNGGNGEGLGGDSDEANIEIDPLTGMPISNDPDVNNTRRRVYNRVLETTLVEFETIKMKELDQELIIDPLFKKALVDFDEGGAKSLLLNTLNIDNTARVIFDASIKDTQNVGQGKLQRKEEELIERDSLVDDENEPSQSLISTRNDSTVNDSVISAPSMEDEILSLGMDFIKFDQIAVCEISGSIEQLRNVVEDINQAKDFIENVNNRFDNFLTEEELQAAVPDNAEDDSDGFDMGMQQELCYPDENHDNTSHDEQDDDNVNSTTGSIFEKDLMAYFDENLNRNWRGREHWKVRNFKKANLVNKESDLLEETRTTIGDTTDKNTTDDKSMDTKKKHKQKKVLEIDFFKTDDSFEDKVFASKGRTKIDMPIKNRKNDTHYLLPDDFHFSTDRITRLFIKPGQKMSLFSHRKHTRGDVSSGLFEKSTVSANHSNNDIPTIADEHFWADNYERKEQEEKEKEQSKEVGDVVGGALDNPFEDDMDGVDFNQAFEGTDDNEEASVKLDLQDDEDHKFPIRENKVTYSRVSKKVDVRRLKKNVWRSINNLIQEHDSRKNREQSSNDSETHTEDESTKELKFSDIIQGISKMYSDDTLKDISTSFCFICLLHLANEHGLQITHTENYNDLIVNYEDLATTQAAS | |
| 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 |
|---|---|---|---|---|---|
| 42 | Ubiquitination | IKMATDNKINSRNSW HHHHHCCCCCCCCCC | 46.18 | 23749301 | |
| 74 | Ubiquitination | ENNINFQKASATLDG CCCCCHHHHHEEHHH | 39.92 | 23749301 | |
| 92 | Phosphorylation | IYSSRVDSVTTETGK EEECCCCEEEHHHHH | 20.64 | 19481522 | |
| 102 | Phosphorylation | TETGKLLSGLAQRKT HHHHHHHHHHHHCCC | 42.04 | 30377154 | |
| 166 | Phosphorylation | YNRVLETTLVEFETI HHHHHHHEEEEEEEE | 21.30 | 19481522 | |
| 202 | Phosphorylation | FDEGGAKSLLLNTLN CCCCCCHHHEEHHCC | 24.58 | 19481522 | |
| 245 | Phosphorylation | EELIERDSLVDDENE HHHHHHCCCCCCCCC | 36.19 | 25704821 | |
| 254 | Phosphorylation | VDDENEPSQSLISTR CCCCCCCCHHCEECC | 26.65 | 23749301 | |
| 256 | Phosphorylation | DENEPSQSLISTRND CCCCCCHHCEECCCC | 31.82 | 27214570 | |
| 264 | Phosphorylation | LISTRNDSTVNDSVI CEECCCCCCCCCCCC | 37.49 | 28889911 | |
| 269 | Phosphorylation | NDSTVNDSVISAPSM CCCCCCCCCCCCCCH | 19.02 | 28889911 | |
| 423 | Phosphorylation | ANLVNKESDLLEETR HCCCCCCHHHHHHHC | 34.86 | 30377154 | |
| 432 | Phosphorylation | LLEETRTTIGDTTDK HHHHHCCCCCCCCCC | 21.48 | 19481522 | |
| 436 | Phosphorylation | TRTTIGDTTDKNTTD HCCCCCCCCCCCCCC | 31.51 | 23749301 | |
| 437 | Phosphorylation | RTTIGDTTDKNTTDD CCCCCCCCCCCCCCC | 50.11 | 27017623 | |
| 469 | Phosphorylation | DFFKTDDSFEDKVFA EEEECCCCHHCHHHH | 33.09 | 28889911 | |
| 529 | Phosphorylation | LFSHRKHTRGDVSSG CCCCCCCCCCCCCCC | 39.11 | 19823750 | |
| 534 | Phosphorylation | KHTRGDVSSGLFEKS CCCCCCCCCCCCCCC | 24.35 | 23749301 | |
| 535 | Phosphorylation | HTRGDVSSGLFEKST CCCCCCCCCCCCCCE | 39.09 | 23749301 | |
| 541 | Phosphorylation | SSGLFEKSTVSANHS CCCCCCCCEEECCCC | 27.18 | 24961812 | |
| 542 | Phosphorylation | SGLFEKSTVSANHSN CCCCCCCEEECCCCC | 29.55 | 28889911 | |
| 544 | Phosphorylation | LFEKSTVSANHSNND CCCCCEEECCCCCCC | 24.36 | 20377248 | |
| 548 | Phosphorylation | STVSANHSNNDIPTI CEEECCCCCCCCCCC | 36.82 | 20377248 | |
| 554 | Phosphorylation | HSNNDIPTIADEHFW CCCCCCCCCHHHCCC | 29.18 | 19481522 | |
| 639 | Phosphorylation | RENKVTYSRVSKKVD CCCCCCCCCCCCCCC | 19.48 | 27017623 | |
| 674 | Phosphorylation | SRKNREQSSNDSETH HHHCHHCCCCCCCCC | 26.76 | 23749301 | |
| 675 | Phosphorylation | RKNREQSSNDSETHT HHCHHCCCCCCCCCC | 44.33 | 19779198 | |
| 678 | Phosphorylation | REQSSNDSETHTEDE HHCCCCCCCCCCCCC | 48.96 | 23749301 | |
| 680 | Phosphorylation | QSSNDSETHTEDEST CCCCCCCCCCCCCHH | 37.74 | 23749301 | |
| 682 | Phosphorylation | SNDSETHTEDESTKE CCCCCCCCCCCHHHH | 53.18 | 17563356 | |
| 700 | Phosphorylation | SDIIQGISKMYSDDT HHHHHHHHHHCCCCC | 20.42 | 19481522 |
| 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 CND2_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of CND2_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 CND2_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-256, 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 THR-682, AND MASSSPECTROMETRY. | |
