| UniProt ID | SIZ2_YEAST | |
|---|---|---|
| UniProt AC | Q12216 | |
| Protein Name | E3 SUMO-protein ligase SIZ2 | |
| Gene Name | NFI1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 726 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | May act as an E3 ligase mediating SUMO/Smt3 attachment to septins. May be involved in chromosome maintenance.. | |
| Protein Sequence | MASVMSNNNNNNNNNNASYMFTNPLSNTGGGLINEIKDAINEMEQLKVLELKQICKSLDLSITGKKAVLQDRIKQFLRKSCDIGHIDPWRPKAIKILIAKVRINSSLPKYSTLWETLKTGAFKHPVASGQLPVTALQSTALPPYSQQQALAYSFTSPFYKPIVQIPDANKKLKQSAGRGCTKMKFKVSKSNHDLLKSNKSYKLYLFSGFSIPFIYETVGHEAIDFPYPCELVFNGTKLEDNVKGLKKQNGTGNPANLTPYLKVPTEMNHLDLHYLNIDKEYSISCFIVEVFSPEALLGKILKRPKIIKQATTAYIKRTLNEQDDDDIITTSTVLSLQCPISCTRMKYPAKTDQCKHIQCFDALWFLHSQSQVPTWQCPICQHPIKFDQLKISEFVDNIIQNCNEDVEQVEISVDGSWKPIHNSSAVITDTVNQNHSVKNENQGTVKQEQDYDSRNAFDTNLRNGSNHNEPEIISLDSSDDEAFIPASKSFPTHVNPRNDQLRADIFPSESEGSSDYNPNHTSTPKGSPTMDQDNYQDAFQMRSFLNQGATTNINDTPTNNSSINSFVTATNGDSRIFYNRGPSTPLLPAVLQNLTNQTEAQRNPYGPNYNTTAQDRNLLGIEGDLPPIPPVDPNSEAETELPTRTTSAAHLPPYIHVSTSGHGDDGKIRKRRHSNVSIYIPKNPYATLMKRRPQANHAIMNKTLAQTNDFNTSAQDNSEVVDLTSD | |
| 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 |
|---|---|---|---|---|---|
| 428 | Phosphorylation | HNSSAVITDTVNQNH CCCCEEEEECCCCCC | 21.01 | 27017623 | |
| 436 | Phosphorylation | DTVNQNHSVKNENQG ECCCCCCCCCCCCCC | 42.19 | 27017623 | |
| 438 | Sumoylation | VNQNHSVKNENQGTV CCCCCCCCCCCCCCC | 62.65 | - | |
| 446 | Sumoylation | NENQGTVKQEQDYDS CCCCCCCEEECCCCC | 48.21 | - | |
| 474 | Phosphorylation | HNEPEIISLDSSDDE CCCCCEEECCCCCCC | 31.61 | 19795423 | |
| 477 | Phosphorylation | PEIISLDSSDDEAFI CCEEECCCCCCCCCC | 40.74 | 21440633 | |
| 478 | Phosphorylation | EIISLDSSDDEAFIP CEEECCCCCCCCCCC | 49.07 | 21440633 | |
| 487 | Phosphorylation | DEAFIPASKSFPTHV CCCCCCCCCCCCCCC | 24.39 | 19795423 | |
| 489 | Phosphorylation | AFIPASKSFPTHVNP CCCCCCCCCCCCCCC | 33.68 | 23749301 | |
| 516 | Phosphorylation | ESEGSSDYNPNHTST CCCCCCCCCCCCCCC | 34.17 | 22369663 | |
| 521 | Phosphorylation | SDYNPNHTSTPKGSP CCCCCCCCCCCCCCC | 40.72 | 22369663 | |
| 522 | Phosphorylation | DYNPNHTSTPKGSPT CCCCCCCCCCCCCCC | 34.85 | 22369663 | |
| 523 | Phosphorylation | YNPNHTSTPKGSPTM CCCCCCCCCCCCCCC | 30.12 | 22369663 | |
| 527 | Phosphorylation | HTSTPKGSPTMDQDN CCCCCCCCCCCCCCC | 24.27 | 28889911 | |
| 529 | Phosphorylation | STPKGSPTMDQDNYQ CCCCCCCCCCCCCHH | 34.77 | 19779198 | |
| 584 | Phosphorylation | FYNRGPSTPLLPAVL EEECCCCCCCHHHHH | 22.53 | 28889911 | |
| 674 | Phosphorylation | KIRKRRHSNVSIYIP CEEECCCCCEEEEEC | 36.80 | 28889911 | |
| 677 | Phosphorylation | KRRHSNVSIYIPKNP ECCCCCEEEEECCCH | 17.58 | 24961812 | |
| 724 | Phosphorylation | NSEVVDLTSD----- CCCEEECCCC----- | 26.78 | 29734811 | |
| 725 | Phosphorylation | SEVVDLTSD------ CCEEECCCC------ | 48.93 | 27017623 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SIZ2_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 SIZ2_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-527, AND MASSSPECTROMETRY. | |
