| UniProt ID | SMC4_YEAST | |
|---|---|---|
| UniProt AC | Q12267 | |
| Protein Name | Structural maintenance of chromosomes protein 4 | |
| Gene Name | SMC4 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1418 | |
| 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 | MSDSPLSKRQKRKSAQEPELSLDQGDAEEDSQVENRVNLSENTPEPDLPALEASYSKSYTPRKLVLSSGENRYAFSQPTNSTTTSLHVPNLQPPKTSSRGRDHKSYSQSPPRSPGRSPTRRLELLQLSPVKNSRVELQKIYDRHQSSSKQQSRLFINELVLENFKSYAGKQVVGPFHTSFSAVVGPNGSGKSNVIDSMLFVFGFRANKMRQDRLSDLIHKSEAFPSLQSCSVAVHFQYVIDESSGTSRIDEEKPGLIITRKAFKNNSSKYYINEKESSYTEVTKLLKNEGIDLDHKRFLILQGEVENIAQMKPKAEKESDDGLLEYLEDIIGTANYKPLIEERMGQIENLNEVCLEKENRFEIVDREKNSLESGKETALEFLEKEKQLTLLRSKLFQFKLLQSNSKLASTLEKISSSNKDLEDEKMKFQESLKKVDEIKAQRKEIKDRISSCSSKEKTLVLERRELEGTRVSLEERTKNLVSKMEKAEKTLKSTKHSISEAENMLEELRGQQTEHETEIKDLTQLLEKERSILDDIKLSLKDKTKNISAEIIRHEKELEPWDLQLQEKESQIQLAESELSLLEETQAKLKKNVETLEEKILAKKTHKQELQDLILDLKKKLNSLKDERSQGEKNFTSAHLKLKEMQKVLNAHRQRAMEARSSLSKAQNKSKVLTALSRLQKSGRINGFHGRLGDLGVIDDSFDVAISTACPRLDDVVVDTVECAQHCIDYLRKNKLGYARFILLDRLRQFNLQPISTPENVPRLFDLVKPKNPKFSNAFYSVLRDTLVAQNLKQANNVAYGKKRFRVVTVDGKLIDISGTMSGGGNHVAKGLMKLGTNQSDKVDDYTPEEVDKIERELSERENNFRVASDTVHEMEEELKKLRDHEPDLESQISKAEMEADSLASELTLAEQQVKEAEMAYVKAVSDKAQLNVVMKNLERLRGEYNDLQSETKTKKEKIKGLQDEIMKIGGIKLQMQNSKVESVCQKLDILVAKLKKVKSASKKSGGDVVKFQKLLQNSERDVELSSDELKVIEEQLKHTKLALAENDTNMNETLNLKVELKEQSEQLKEQMEDMEESINEFKSIEIEMKNKLEKLNSLLTYIKSEITQQEKGLNELSIRDVTHTLGMLDDNKMDSVKEDVKNNQELDQEYRSCETQDESEIKDAETSCDNYHPMNIDETSDEVSRGIPRLSEDELRELDVELIESKINELSYYVEETNVDIGVLEEYARRLAEFKRRKLDLNNAVQKRDEVKEQLGILKKKRFDEFMAGFNIISMTLKEMYQMITMGGNAELELVDSLDPFSEGVTFSVMPPKKSWRNITNLSGGEKTLSSLALVFALHKYKPTPLYVMDEIDAALDFRNVSIVANYIKERTKNAQFIVISLRNNMFELAQQLVGVYKRDNRTKSTTIKNIDILNRT | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSDSPLSKR ------CCCCCCCHH | 59.09 | 30377154 | |
| 2 | Acetylation | ------MSDSPLSKR ------CCCCCCCHH | 59.09 | 22814378 | |
| 4 | Phosphorylation | ----MSDSPLSKRQK ----CCCCCCCHHHH | 36.71 | 28152593 | |
| 7 | Phosphorylation | -MSDSPLSKRQKRKS -CCCCCCCHHHHHHH | 29.22 | 28889911 | |
| 8 | Acetylation | MSDSPLSKRQKRKSA CCCCCCCHHHHHHHC | 67.54 | 25381059 | |
| 14 | Phosphorylation | SKRQKRKSAQEPELS CHHHHHHHCCCCCCC | 38.94 | 28889911 | |
| 21 | Phosphorylation | SAQEPELSLDQGDAE HCCCCCCCCCCCCHH | 28.39 | 28889911 | |
| 31 | Phosphorylation | QGDAEEDSQVENRVN CCCHHHHHHHHHHCC | 39.13 | 28889911 | |
| 40 | Phosphorylation | VENRVNLSENTPEPD HHHHCCCCCCCCCCC | 24.48 | 25752575 | |
| 43 | Phosphorylation | RVNLSENTPEPDLPA HCCCCCCCCCCCCHH | 25.61 | 24961812 | |
| 67 | Phosphorylation | TPRKLVLSSGENRYA CCCEEEECCCCCCEE | 28.90 | 21440633 | |
| 68 | Phosphorylation | PRKLVLSSGENRYAF CCEEEECCCCCCEEE | 46.06 | 21440633 | |
| 73 | Phosphorylation | LSSGENRYAFSQPTN ECCCCCCEEECCCCC | 24.47 | 23749301 | |
| 105 | Phosphorylation | SRGRDHKSYSQSPPR CCCCCCCCCCCCCCC | 26.96 | 22369663 | |
| 106 | Phosphorylation | RGRDHKSYSQSPPRS CCCCCCCCCCCCCCC | 18.61 | 22369663 | |
| 107 | Phosphorylation | GRDHKSYSQSPPRSP CCCCCCCCCCCCCCC | 31.13 | 22369663 | |
| 109 | Phosphorylation | DHKSYSQSPPRSPGR CCCCCCCCCCCCCCC | 30.82 | 22369663 | |
| 113 | Phosphorylation | YSQSPPRSPGRSPTR CCCCCCCCCCCCCCH | 37.16 | 22369663 | |
| 117 | Phosphorylation | PPRSPGRSPTRRLEL CCCCCCCCCCHHHHH | 36.22 | 22369663 | |
| 119 | Phosphorylation | RSPGRSPTRRLELLQ CCCCCCCCHHHHHHH | 29.66 | 22369663 | |
| 128 | Phosphorylation | RLELLQLSPVKNSRV HHHHHHCCCCCCCHH | 18.06 | 22369663 | |
| 139 | Acetylation | NSRVELQKIYDRHQS CCHHHHHHHHHHHCC | 56.72 | 25381059 | |
| 147 | Phosphorylation | IYDRHQSSSKQQSRL HHHHHCCCCHHHHHH | 34.68 | 28889911 | |
| 148 | Phosphorylation | YDRHQSSSKQQSRLF HHHHCCCCHHHHHHH | 39.47 | 28889911 | |
| 152 | Phosphorylation | QSSSKQQSRLFINEL CCCCHHHHHHHHHHH | 28.58 | 28889911 | |
| 278 | Phosphorylation | YINEKESSYTEVTKL ECCCCCCCHHHHHHH | 36.85 | 27214570 | |
| 528 | Acetylation | DLTQLLEKERSILDD HHHHHHHHHHHHHHH | 59.40 | 22865919 | |
| 605 | Phosphorylation | EKILAKKTHKQELQD HHHHCHHHCHHHHHH | 33.33 | 19795423 | |
| 623 | Phosphorylation | DLKKKLNSLKDERSQ HHHHHHHHHHHHHHH | 47.43 | 28889911 | |
| 809 | Phosphorylation | KKRFRVVTVDGKLID CCCEEEEEECCEEEE | 15.26 | 29136822 | |
| 818 | Phosphorylation | DGKLIDISGTMSGGG CCEEEEECCCCCCCC | 25.18 | 21551504 | |
| 820 | Phosphorylation | KLIDISGTMSGGGNH EEEEECCCCCCCCCH | 11.02 | 29136822 | |
| 822 | Phosphorylation | IDISGTMSGGGNHVA EEECCCCCCCCCHHH | 33.84 | 29136822 | |
| 869 | Phosphorylation | ENNFRVASDTVHEME HCCCCCCHHHHHHHH | 30.84 | 27017623 | |
| 871 | Phosphorylation | NFRVASDTVHEMEEE CCCCCHHHHHHHHHH | 22.67 | 27017623 | |
| 905 | Phosphorylation | MEADSLASELTLAEQ HHHHHHHHHHHHHHH | 38.13 | 27017623 | |
| 1095 | Acetylation | EMKNKLEKLNSLLTY HHHHHHHHHHHHHHH | 64.50 | 24489116 | |
| 1160 | Phosphorylation | SCETQDESEIKDAET HCCCCCHHHHCCCHH | 53.57 | 21440633 | |
| 1167 | Phosphorylation | SEIKDAETSCDNYHP HHHCCCHHCCCCCCC | 36.05 | 19779198 | |
| 1168 | Phosphorylation | EIKDAETSCDNYHPM HHCCCHHCCCCCCCC | 15.81 | 19779198 |
| 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 SMC4_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMC4_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 SMC4_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-40; THR-43; SER-113 ANDTHR-809, AND MASS SPECTROMETRY. | |