| UniProt ID | SCC1_YEAST | |
|---|---|---|
| UniProt AC | Q12158 | |
| Protein Name | Sister chromatid cohesion protein 1 | |
| Gene Name | MCD1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 566 | |
| Subcellular Localization | Nucleus . Chromosome . Chromosome, centromere . Associates with chromatin. Before prophase it is scattered along chromosome arms. During prophase, most of cohesin complexes dissociate from chromatin except at centromeres, where cohesin complexes rema | |
| Protein Description | Cleavable component of the cohesin complex involved in chromosome cohesion during cell cycle. 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 metaphase-anaphase transition, this protein is cleaved by ESP1 and dissociates from chromatin, allowing sister chromatids to segregate.. | |
| Protein Sequence | MVTENPQRLTVLRLATNKGPLAQIWLASNMSNIPRGSVIQTHIAESAKEIAKASGCDDESGDNEYITLRTSGELLQGIVRVYSKQATFLLTDIKDTLTKISMLFKTSQKMTSTVNRLNTVTRVHQLMLEDAVTEREVLVTPGLEFLDDTTIPVGLMAQENSMERKVQGAAPWDTSLEVGRRFSPDEDFEHNNLSSMNLDFDIEEGPITSKSWEEGTRQSSRNFDTHENYIQDDDFPLDDAGTIGWDLGITEKNDQNNDDDDNSVEQGRRLGESIMSEEPTDFGFDLDIEKEAPAGNIDTITDAMTESQPKQTGTRRNSKLLNTKSIQIDEETENSESIASSNTYKEERSNNLLTPQPTNFTTKRLWSEITESMSYLPDPILKNFLSYESLKKRKIHNGREGSIEEPELNVSLNLTDDVISNAGTNDNSFNELTDNMSDFVPIDAGLNEAPFPEENIIDAKTRNEQTTIQTEKVRPTPGEVASKAIVQMAKILRKELSEEKEVIFTDVLKSQANTEPENITKREASRGFFDILSLATEGCIGLSQTEAFGNIKIDAKPALFERFINA | |
| 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 |
|---|---|---|---|---|---|
| 52 | Ubiquitination | ESAKEIAKASGCDDE HHHHHHHHHHCCCCC | 49.06 | 23749301 | |
| 105 | Acetylation | TKISMLFKTSQKMTS HHHHHHHHCCHHHHH | 43.22 | 25381059 | |
| 109 | Ubiquitination | MLFKTSQKMTSTVNR HHHHCCHHHHHHHHH | 43.86 | 23749301 | |
| 109 | Acetylation | MLFKTSQKMTSTVNR HHHHCCHHHHHHHHH | 43.86 | 25381059 | |
| 112 | Phosphorylation | KTSQKMTSTVNRLNT HCCHHHHHHHHHHHH | 27.19 | 30377154 | |
| 119 | Phosphorylation | STVNRLNTVTRVHQL HHHHHHHHHHHHHHH | 28.04 | 20190278 | |
| 161 | Phosphorylation | GLMAQENSMERKVQG CCCCCCCCCHHHHCC | 22.67 | 28889911 | |
| 165 | Sumoylation | QENSMERKVQGAAPW CCCCCHHHHCCCCCC | 26.13 | - | |
| 174 | Phosphorylation | QGAAPWDTSLEVGRR CCCCCCCCCCCCCCC | 31.20 | 22890988 | |
| 175 | Phosphorylation | GAAPWDTSLEVGRRF CCCCCCCCCCCCCCC | 21.76 | 22369663 | |
| 194 | Phosphorylation | DFEHNNLSSMNLDFD CCCCCCCCCCCCCEE | 29.66 | 21440633 | |
| 195 | Phosphorylation | FEHNNLSSMNLDFDI CCCCCCCCCCCCEEC | 18.17 | 21440633 | |
| 210 | Acetylation | EEGPITSKSWEEGTR CCCCCCCCCHHCCCC | 51.44 | 11864574 | |
| 263 | Phosphorylation | NNDDDDNSVEQGRRL CCCCCCCHHHHHHHH | 33.74 | 19823750 | |
| 273 | Phosphorylation | QGRRLGESIMSEEPT HHHHHHHHHHCCCCC | 23.07 | 21440633 | |
| 276 | Phosphorylation | RLGESIMSEEPTDFG HHHHHHHCCCCCCCC | 36.82 | 19823750 | |
| 280 | Phosphorylation | SIMSEEPTDFGFDLD HHHCCCCCCCCCCCE | 47.44 | 19823750 | |
| 290 | Sumoylation | GFDLDIEKEAPAGNI CCCCEECCCCCCCCC | 60.55 | - | |
| 299 | Phosphorylation | APAGNIDTITDAMTE CCCCCCCHHHHHHHC | 23.21 | 27017623 | |
| 305 | Phosphorylation | DTITDAMTESQPKQT CHHHHHHHCCCCCCC | 33.92 | 30377154 | |
| 307 | Phosphorylation | ITDAMTESQPKQTGT HHHHHHCCCCCCCCC | 42.49 | 25752575 | |
| 319 | Acetylation | TGTRRNSKLLNTKSI CCCCCCCHHCCCCEE | 61.62 | 24489116 | |
| 325 | Phosphorylation | SKLLNTKSIQIDEET CHHCCCCEEECCCCC | 20.07 | 21551504 | |
| 332 | Phosphorylation | SIQIDEETENSESIA EEECCCCCCCCCCHH | 38.12 | 21551504 | |
| 349 | Phosphorylation | NTYKEERSNNLLTPQ CCCCCHHHCCCCCCC | 33.09 | 25752575 | |
| 354 | Phosphorylation | ERSNNLLTPQPTNFT HHHCCCCCCCCCCCC | 24.04 | 11864574 | |
| 358 | Phosphorylation | NLLTPQPTNFTTKRL CCCCCCCCCCCHHHH | 37.40 | 21551504 | |
| 370 | Phosphorylation | KRLWSEITESMSYLP HHHHHHHHHHHHCCC | 20.25 | 21551504 | |
| 372 | Phosphorylation | LWSEITESMSYLPDP HHHHHHHHHHCCCCH | 12.36 | 21551504 | |
| 460 | Sumoylation | EENIIDAKTRNEQTT HHHCCCCCCCCCCCE | 44.24 | - | |
| 461 | Phosphorylation | ENIIDAKTRNEQTTI HHCCCCCCCCCCCEE | 40.21 | 27017623 | |
| 466 | Phosphorylation | AKTRNEQTTIQTEKV CCCCCCCCEEEEEEC | 21.49 | 23749301 | |
| 467 | Phosphorylation | KTRNEQTTIQTEKVR CCCCCCCEEEEEECC | 15.69 | 23749301 | |
| 476 | Phosphorylation | QTEKVRPTPGEVASK EEEECCCCCHHHHHH | 33.10 | 27017623 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SCC1_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 SCC1_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Eco1 is a novel acetyltransferase that can acetylate proteinsinvolved in cohesion."; Ivanov D., Schleiffer A., Eisenhaber F., Mechtler K., Haering C.H.,Nasmyth K.; Curr. Biol. 12:323-328(2002). Cited for: ACETYLATION AT LYS-210, AND MUTAGENESIS OF LYS-210; LYS-252; LYS-290;LYS-310; LYS-319 AND LYS-324. | |
| 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-161; THR-174; SER-175;SER-307 AND THR-354, 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-263, AND MASSSPECTROMETRY. | |
