| UniProt ID | SMC1_YEAST | |
|---|---|---|
| UniProt AC | P32908 | |
| Protein Name | Structural maintenance of chromosomes protein 1 | |
| Gene Name | SMC1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1225 | |
| Subcellular Localization | Nucleus. Chromosome. Associates with chromatin. Before prophase it is scattered along chromosome arms. At anaphase, the MCD1 subunit of the cohesin complex is cleaved, leading to the dissociation of the complex from chromosomes, allowing chromosome s | |
| Protein Description | Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate.. | |
| Protein Sequence | MGRLVGLELSNFKSYRGVTKVGFGESNFTSIIGPNGSGKSNMMDAISFVLGVRSNHLRSNILKDLIYRGVLNDENSDDYDNEGAASSNPQSAYVKAFYQKGNKLVELMRIISRNGDTSYKIDGKTVSYKDYSIFLENENILIKAKNFLVFQGDVEQIAAQSPVELSRMFEEVSGSIQYKKEYEELKEKIEKLSKSATESIKNRRRIHGELKTYKEGINKNEEYRKQLDKKNELQKFQALWQLYHLEQQKEELTDKLSALNSEISSLKGKINNEMKSLQRSKSSFVKESAVISKQKSKLDYIFKDKEKLVSDLRLIKVPQQAAGKRISHIEKRIESLQKDLQRQKTYVERFETQLKVVTRSKEAFEEEIKQSARNYDKFKLNENDLKTYNCLHEKYLTEGGSILEEKIAVLNNDKREIQEELERFNKRADISKRRITEELSITGEKLDTQLNDLRVSLNEKNALHTERLHELKKLQSDIESANNQEYDLNFKLRETLVKIDDLSANQRETMKERKLRENIAMLKRFFPGVKGLVHDLCHPKKEKYGLAVSTILGKNFDSVIVENLTVAQECIAFLKKQRAGTASFIPLDTIETELPTLSLPDSQDYILSINAIDYEPEYEKAMQYVCGDSIICNTLNIAKDLKWKKGIRGKLVTIEGALIHKAGLMTGGISGDANNRWDKEEYQSLMSLKDKLLIQIDELSNGQRSNSIRAREVENSVSLLNSDIANLRTQVTQQKRSLDENRLEIKYHNDLIEKEIQPKITELKKKLDDLENTKDNLVKEKEALQNNIFKEFTSKIGFTIKEYENHSGELMRQQSKELQQLQKQILTVENKLQFETDRLSTTQRRYEKAQKDLENAQVEMKSLEEQEYAIEMKIGSIESKLEEHKNHLDELQKKFVTKQSELNSSEDILEDMNSNLQVLKRERDGIKEDIEKFDLERVTALKNCKISNINIPISSETTIDDLPISSTDNEAITISNSIDINYKGLPKKYKENNTDSARKELEQKIHEVEEILNELQPNARALERYDEAEGRFEVINNETEQLKAEEKKILNQFLKIKKKRKELFEKTFDYVSDHLDAIYRELTKNPNSNVELAGGNASLTIEDEDEPFNAGIKYHATPPLKRFKDMEYLSGGEKTVAALALLFAINSYQPSPFFVLDEVDAALDITNVQRIAAYIRRHRNPDLQFIVISLKNTMFEKSDALVGVYRQQQENSSKIITLDLSNYAE | |
| 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 |
|---|---|---|---|---|---|
| 40 | Phosphorylation | GPNGSGKSNMMDAIS CCCCCCCCCHHHHHH | 33.22 | 21126336 | |
| 59 | Phosphorylation | VRSNHLRSNILKDLI HCCHHHHHHHHHHHH | 34.28 | 27017623 | |
| 63 | Acetylation | HLRSNILKDLIYRGV HHHHHHHHHHHHHHC | 46.84 | 24489116 | |
| 76 | Phosphorylation | GVLNDENSDDYDNEG HCCCCCCCCCCCCCC | 29.79 | 20377248 | |
| 79 | Phosphorylation | NDENSDDYDNEGAAS CCCCCCCCCCCCCCC | 26.17 | 21440633 | |
| 86 | Phosphorylation | YDNEGAASSNPQSAY CCCCCCCCCCCCHHH | 30.07 | 22369663 | |
| 87 | Phosphorylation | DNEGAASSNPQSAYV CCCCCCCCCCCHHHH | 48.04 | 22369663 | |
| 91 | Phosphorylation | AASSNPQSAYVKAFY CCCCCCCHHHHHHHH | 23.87 | 22369663 | |
| 93 | Phosphorylation | SSNPQSAYVKAFYQK CCCCCHHHHHHHHHH | 14.02 | 22369663 | |
| 100 | Ubiquitination | YVKAFYQKGNKLVEL HHHHHHHHCCHHHHH | 53.74 | 23749301 | |
| 161 | Phosphorylation | VEQIAAQSPVELSRM HHHHHHCCHHHHHHH | 26.62 | 27214570 | |
| 186 | Acetylation | KKEYEELKEKIEKLS HHHHHHHHHHHHHHH | 61.31 | 25381059 | |
| 257 | Phosphorylation | EELTDKLSALNSEIS HHHHHHHHHHHHHHH | 36.13 | 19823750 | |
| 261 | Phosphorylation | DKLSALNSEISSLKG HHHHHHHHHHHHHHH | 36.84 | 19795423 | |
| 264 | Phosphorylation | SALNSEISSLKGKIN HHHHHHHHHHHHHHH | 26.10 | 19823750 | |
| 265 | Phosphorylation | ALNSEISSLKGKINN HHHHHHHHHHHHHHH | 39.50 | 19823750 | |
| 282 | Phosphorylation | KSLQRSKSSFVKESA HHHHHHHHHHHHHHH | 30.20 | 30377154 | |
| 297 | Acetylation | VISKQKSKLDYIFKD HHCCCHHHCCCHHCC | 53.03 | 24489116 | |
| 327 | Phosphorylation | QAAGKRISHIEKRIE HHCCHHHHHHHHHHH | 23.57 | 28889911 | |
| 401 | Phosphorylation | KYLTEGGSILEEKIA HHHCCCCCHHHHHHH | 34.55 | 27214570 | |
| 440 | Phosphorylation | RRITEELSITGEKLD HHCCHHHHCCCCCHH | 22.76 | 27017623 | |
| 442 | Phosphorylation | ITEELSITGEKLDTQ CCHHHHCCCCCHHHH | 35.59 | 27017623 | |
| 448 | Phosphorylation | ITGEKLDTQLNDLRV CCCCCHHHHHHHHHH | 45.45 | 27017623 | |
| 653 | Phosphorylation | GIRGKLVTIEGALIH CCCCEEEEEECHHHH | 24.61 | 19823750 | |
| 666 | Phosphorylation | IHKAGLMTGGISGDA HHCCCCCCCCCCCCC | 36.98 | 19823750 | |
| 670 | Phosphorylation | GLMTGGISGDANNRW CCCCCCCCCCCCCCC | 33.62 | 19823750 | |
| 1114 | Phosphorylation | PFNAGIKYHATPPLK CCCCCCCEECCCCCH | 8.51 | 27214570 | |
| 1117 | Phosphorylation | AGIKYHATPPLKRFK CCCCEECCCCCHHCC | 16.48 | 27214570 | |
| 1128 | Phosphorylation | KRFKDMEYLSGGEKT HHCCCHHHCCCCHHH | 10.26 | 19823750 | |
| 1130 | Phosphorylation | FKDMEYLSGGEKTVA CCCHHHCCCCHHHHH | 43.80 | 19823750 |
| 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 SMC1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMC1_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 SMC1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
| 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-327, AND MASSSPECTROMETRY. | |
