UniProt ID | SMC2_YEAST | |
---|---|---|
UniProt AC | P38989 | |
Protein Name | Structural maintenance of chromosomes protein 2 | |
Gene Name | SMC2 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1170 | |
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 | Central component 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.. | |
Protein Sequence | MKVEELIIDGFKSYATRTVITDWDPQFNAITGLNGSGKSNILDAICFVLGIASMSTVRASSLQDLIYKRGQAGVTKASVTIVFDNTDKSNSPIGFTNSPQISVTRQVVLGGTSKYLINGHRAPQQSVLQLFQSVQLNINNPNFLIMQGKITKVLNMKPSEILSLIEEAAGTKMFEDRREKAERTMSKKETKLQENRTLLTEEIEPKLEKLRNEKRMFLEFQSTQTDLEKTERIVVSYEYYNIKHKHTSIRETLENGETRMKMLNEFVKKTSEEIDSLNEDVEEIKLQKEKELHKEGTISKLENKENGLLNEISRLKTSLSIKVENLNDTTEKSKALESEIASSSAKLIEKKSAYANTEKDYKMVQEQLSKQRDLYKRKEELVSTLTTGISSTGAADGGYNAQLAKAKTELNEVSLAIKKSSMKMELLKKELLTIEPKLKEATKDNELNVKHVKQCQETCDKLRARLVEYGFDPSRIKDLKQREDKLKSHYYQTCKNSEYLKRRVTNLEFNYTKPYPNFEASFVHGVVGQLFQIDNDNIRYATALQTCAGGRLFNVVVQDSQTATQLLERGRLRKRVTIIPLDKIYTRPISSQVLDLAKKIAPGKVELAINLIRFDESITKAMEFIFGNSLICEDPETAKKITFHPKIRARSITLQGDVYDPEGTLSGGSRNTSESLLVDIQKYNQIQKQIETIQADLNHVTEELQTQYATSQKTKTIQSDLNLSLHKLDLAKRNLDANPSSQIIARNEEILRDIGECENEIKTKQMSLKKCQEEVSTIEKDMKEYDSDKGSKLNELKKELKLLAKELEEQESESERKYDLFQNLELETEQLSSELDSNKTLLHNHLKSIESLKLENSDLEGKIRGVEDDLVTVQTELNEEKKRLMDIDDELNELETLIKKKQDEKKSSELELQKLVHDLNKYKSNTNNMEKIIEDLRQKHEFLEDFDLVRNIVKQNEGIDLDTYRERSKQLNEKFQELRKKVNPNIMNMIENVEKKEAALKTMIKTIEKDKMKIQETISKLNEYKRETLVKTWEKVTLDFGNIFADLLPNSFAKLVPCEGKDVTQGLEVKVKLGNIWKESLIELSGGQRSLIALSLIMALLQFRPAPMYILDEVDAALDLSHTQNIGHLIKTRFKGSQFIVVSLKEGMFANANRVFRTRFQDGTSVVSIM | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
67 | Phosphorylation | SSLQDLIYKRGQAGV HHHHHHHHHCCCCCC | 11.26 | 28132839 | |
390 | Phosphorylation | STLTTGISSTGAADG HHHHHCCCCCCCCCC | 24.16 | 27017623 | |
391 | Phosphorylation | TLTTGISSTGAADGG HHHHCCCCCCCCCCC | 29.01 | 27017623 | |
399 | Phosphorylation | TGAADGGYNAQLAKA CCCCCCCHHHHHHHH | 16.92 | 27017623 | |
505 | Phosphorylation | EYLKRRVTNLEFNYT HHHHHHHCEEECCCC | 32.07 | 28889911 | |
590 | Phosphorylation | KIYTRPISSQVLDLA HHCCCCCCHHHHHHH | 19.87 | 27017623 | |
629 | Phosphorylation | MEFIFGNSLICEDPE HHHHHCCCCCCCCHH | 21.35 | 27017623 | |
642 | Phosphorylation | PETAKKITFHPKIRA HHHHHHCEECHHHCC | 25.44 | 27017623 | |
741 | Phosphorylation | NLDANPSSQIIARNE CCCCCCHHHHHHCCH | 27.01 | 27214570 | |
907 | Phosphorylation | KKQDEKKSSELELQK HHHCHHCCCHHHHHH | 39.86 | 30377154 | |
1005 | Acetylation | AALKTMIKTIEKDKM HHHHHHHHHHHHHHH | 32.40 | 25381059 | |
1085 | Phosphorylation | KESLIELSGGQRSLI HHHHECCCCCHHHHH | 28.25 | 28889911 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of SMC2_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMC2_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 SMC2_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-1085, AND MASSSPECTROMETRY. |