| UniProt ID | SAC3_YEAST | |
|---|---|---|
| UniProt AC | P46674 | |
| Protein Name | Nuclear mRNA export protein SAC3 | |
| Gene Name | SAC3 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1301 | |
| Subcellular Localization | Nucleus envelope . Localizes to the nuclear pores. | |
| Protein Description | Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket.. | |
| Protein Sequence | MNTSFGSVVPSTNFNFFKGHGNNDNTSANSTVNNSNFFLNSNETKPSKNVFMVHSTSQKKSQQPLQNLSHSPSYTENKPDKKKKYMINDAKTIQLVGPLISSPDNLGFQKRSHKARELPRFLINQEPQLEKRAFVQDPWDKANQEKMISLEESIDDLNELYETLKKMRNTERSIMEEKGLVDKADSAKDLYDAIVFQGTCLDMCPTFERSRRNVEYTVYSYEKNQPNDKKASRTKALKVFARPAAAAAPPLPSDVRPPHILVKTLDYIVDNLLTTLPESEGFLWDRMRSIRQDFTYQNYSGPEAVDCNERIVRIHLLILHIMVKSNVEFSLQQELEQLHKSLITLSEIYDDVRSSGGTCPNEAEFRAYALLSKIRDPQYDENIQRLPKHIFQDKLVQMALCFRRVISNSAYTERGFVKTENCLNFYARFFQLMQSPSLPLLMGFFLQMHLTDIRFYALRALSHTLNKKHKPIPFIYLENMLLFNNRQEIIEFCNYYSIEIINGDAADLKTLQHYSHKLSETQPLKKTYLTCLERRLQKTTYKGLINGGEDNLASSVYVKDPKKDRIPSIADQSFLMENFQNNYNEKLNQNSSVKPQINTSPKRVATRPNHFPFSQESKQLPQISQSHTLSTNPLLTPQVHGDLSEQKQQQIKTVTDGGSPFVFDQSAQNSTVEASKAHMISTTSNGAYDEKLSSEQEEMRKKEEQRIEEEKTQLKKKQENADKQVITEQIANDLVKEVVNSSVISIVKREFSEANYRKDFIDTMTRELYDAFLHERLYLIYMDSRAELKRNSTLKKKFFEKWQASYSQAKKNRILEEKKREEIKLVSHQLGVPGFKKSTCLFRTPYKGNVNSSFMLSSSDKNLIFSPVNDEFNKFATHLTKISKLWRPLEMQSIYYDNLTKKFPSNSLTPANLFIYAKDWTSLSNRWILSKFNLQTAQDSKKFSNNIISSRIICIDDEYEPSDFSDLQLLIFNTGVTNPDIFDLEMKLKDDGEELIKLITGISLNTNICFSLLIIYWESAENTLSESTIKHLLKLNRISKNYSSVIERIDLMNLTEESPHKCLEDKLSEISHSYVYKLTERGKYDKTLRQKRSLAGIHSRSTQLQTTKDIDQKMKKMLEKEKNKYQQQIGERNTYAHLESHIDASPRSKKRKLPILLSTSHSSQFKTPLASRLNTSGSSTSPPLPSHLAMKFRKNSRVTSLHTVLPVSTPSHSNNIPAASFSGNNTTDIQSQQLIENQKSTSVYLNNVSERILGNQEICQTPINPVTPVLDGADQGKEDIPDSILELKILIDSVKKKVNND | |
| 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 |
|---|---|---|---|---|---|
| 3 | Phosphorylation | -----MNTSFGSVVP -----CCCCCCCCCC | 36.97 | 30377154 | |
| 4 | Phosphorylation | ----MNTSFGSVVPS ----CCCCCCCCCCC | 38.92 | 30377154 | |
| 7 | Phosphorylation | -MNTSFGSVVPSTNF -CCCCCCCCCCCCCC | 20.24 | 30377154 | |
| 26 | Phosphorylation | GHGNNDNTSANSTVN CCCCCCCCCCCCCCC | 31.89 | 23749301 | |
| 55 | Phosphorylation | KNVFMVHSTSQKKSQ CCEEEEEECCCCCCC | 20.53 | 30377154 | |
| 69 | Phosphorylation | QQPLQNLSHSPSYTE CCCCCCCCCCCCCCC | 29.48 | 21440633 | |
| 568 | Phosphorylation | PKKDRIPSIADQSFL CCCCCCCCHHCHHHH | 28.21 | 20377248 | |
| 573 | Phosphorylation | IPSIADQSFLMENFQ CCCHHCHHHHHHHHH | 22.39 | 21551504 | |
| 591 | Phosphorylation | NEKLNQNSSVKPQIN HHHHCCCCCCCCCCC | 27.09 | 26447709 | |
| 592 | Phosphorylation | EKLNQNSSVKPQINT HHHCCCCCCCCCCCC | 41.53 | 26447709 | |
| 599 | Phosphorylation | SVKPQINTSPKRVAT CCCCCCCCCCCCCCC | 48.30 | 22369663 | |
| 600 | Phosphorylation | VKPQINTSPKRVATR CCCCCCCCCCCCCCC | 24.76 | 22369663 | |
| 683 | Phosphorylation | KAHMISTTSNGAYDE HCEEEECCCCCHHCC | 17.26 | 30377154 | |
| 748 | Acetylation | SSVISIVKREFSEAN CHHHHHHHHHHHHHH | 44.53 | 14718168 | |
| 844 | Phosphorylation | KSTCLFRTPYKGNVN CCEEEEECCCCCCCC | 24.52 | 21440633 | |
| 853 | Phosphorylation | YKGNVNSSFMLSSSD CCCCCCCCEECCCCC | 14.96 | 19779198 | |
| 866 | Phosphorylation | SDKNLIFSPVNDEFN CCCCCEEECCCHHHH | 22.42 | 17330950 | |
| 877 | Phosphorylation | DEFNKFATHLTKISK HHHHHHHHHHHHHHH | 22.13 | 28889911 | |
| 880 | Phosphorylation | NKFATHLTKISKLWR HHHHHHHHHHHHHHC | 20.80 | 28889911 | |
| 1145 | Phosphorylation | LESHIDASPRSKKRK HHHHHCCCCCCCCCC | 19.66 | 19779198 | |
| 1159 | Phosphorylation | KLPILLSTSHSSQFK CCCEEEECCCCCCCC | 30.35 | 21440633 | |
| 1167 | Phosphorylation | SHSSQFKTPLASRLN CCCCCCCCCCHHHCC | 25.48 | 20377248 | |
| 1171 | Phosphorylation | QFKTPLASRLNTSGS CCCCCCHHHCCCCCC | 45.01 | 21440633 | |
| 1175 | Phosphorylation | PLASRLNTSGSSTSP CCHHHCCCCCCCCCC | 38.77 | 29136822 | |
| 1176 | Phosphorylation | LASRLNTSGSSTSPP CHHHCCCCCCCCCCC | 35.29 | 29136822 | |
| 1178 | Phosphorylation | SRLNTSGSSTSPPLP HHCCCCCCCCCCCCC | 30.15 | 20377248 | |
| 1179 | Phosphorylation | RLNTSGSSTSPPLPS HCCCCCCCCCCCCCC | 36.11 | 29136822 | |
| 1180 | Phosphorylation | LNTSGSSTSPPLPSH CCCCCCCCCCCCCCH | 47.12 | 20377248 | |
| 1181 | Phosphorylation | NTSGSSTSPPLPSHL CCCCCCCCCCCCCHH | 26.86 | 21082442 | |
| 1186 | Phosphorylation | STSPPLPSHLAMKFR CCCCCCCCHHHHHCC | 38.52 | 29136822 | |
| 1240 | Phosphorylation | QLIENQKSTSVYLNN HHHHCCCCCCEEECC | 19.02 | 30377154 | |
| 1241 | Phosphorylation | LIENQKSTSVYLNNV HHHCCCCCCEEECCH | 29.28 | 30377154 | |
| 1242 | Phosphorylation | IENQKSTSVYLNNVS HHCCCCCCEEECCHH | 18.82 | 30377154 | |
| 1293 | Phosphorylation | ELKILIDSVKKKVNN HHHHHHHHHHHHHCC | 28.92 | 21440633 |
| 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 SAC3_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SAC3_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 SAC3_YEAST !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "Sus1, a functional component of the SAGA histone acetylase complexand the nuclear pore-associated mRNA export machinery."; Rodriguez-Navarro S., Fischer T., Luo M.-J., Antunez O.,Brettschneider S., Lechner J., Perez-Ortin J.E., Reed R., Hurt E.C.; Cell 116:75-86(2004). Cited for: INTERACTION WITH SUS1, AND ACETYLATION AT LYS-748. | |
| 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-600; SER-866; THR-1180AND SER-1181, AND MASS SPECTROMETRY. | |
| "Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-866, AND MASSSPECTROMETRY. | |
