| UniProt ID | SPT16_YEAST | |
|---|---|---|
| UniProt AC | P32558 | |
| Protein Name | FACT complex subunit SPT16 | |
| Gene Name | SPT16 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 1035 | |
| Subcellular Localization | Nucleus. Chromosome. Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. | |
| Protein Description | Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.. | |
| Protein Sequence | MEELNIDFDVFKKRIELLYSKYNEFEGSPNSLLFVLGSSNAENPYQKTTILHNWLLSYEFPATLIALVPGKVIIITSSAKAKHLQKAIDLFKDPESKITLELWQRNNKEPELNKKLFDDVIALINSAGKTVGIPEKDSYQGKFMTEWNPVWEAAVKENEFNVIDISLGLSKVWEVKDVNEQAFLSVSSKGSDKFMDLLSNEMVRAVDEELKITNAKLSDKIENKIDDVKFLKQLSPDLSALCPPNYKFNFDLLDWTYSPIIQSGKKFDLRVSARSTNDQLYGNGCILASCGIRYNNYCSNITRTFLIDPSEEMANNYDFLLTLQKEIVTNILKPGRTPKEVYESVIEYIEKTKPELVPNFTKNIGSLIGLEFRDSNFILNVKNDYRKIQRGDCFNISFGFNNLKDSQSANNYALQLADTVQIPLDETEPPRFLTNYTKAKSQISFYFNNEEEDNNKKKSSPATKVPSKPDRNSKILRTKLRGEARGGAEDAQKEQIRKENQKKLHEKLEKNGLLRFSAADANGPDSEPRQYFKKYESYVRDSQLPTNIRDLRIHVDWKSQTIILPIYGRPVPFHINSYKNGSKNEEGEYTYLRLNFNSPGSSGGISKKVEELPYEESADNQFVRSITLRSKDGDRMSETFKQIADLKKEATKREQERKALADVVQQDKLIENKTGRTKRLDQIFVRPNPDTKRVPSTVFIHENGIRFQSPLRTDSRIDILFSNIKNLIFQSCKGELIVVIHIHLKNPILMGKKKIQDVQFYREASDMSVDETGGGRRGQSRFRRYGDEDELEQEQEERRKRAALDKEFKYFADAIAEASNGLLTVENTFRDLGFQGVPNRSAVFCMPTTDCLVQLIEPPFLVINLEEVEICILERVQFGLKNFDMVFVYKDFNKPVTHINTVPIESLDFLKQWLTDMDIPYTVSTINLNWATIMKSLQDDPYQFFLDGGWNFLATGSDDEASDESEEEVSEYEASEDDVSDESAFSEDEEGSEVDDDISGDESEDYTGDESEEGEDWDELEKKAARADRGANFRD | |
| 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 |
|---|---|---|---|---|---|
| 92 | Acetylation | QKAIDLFKDPESKIT HHHHHHHCCHHHCHH | 78.61 | 24489116 | |
| 136 | Acetylation | KTVGIPEKDSYQGKF CCCCCCCCCCCCCEE | 46.77 | 24489116 | |
| 166 | Phosphorylation | EFNVIDISLGLSKVW CCEEEEEECCCCCEE | 16.79 | 28889911 | |
| 211 | Acetylation | RAVDEELKITNAKLS HHHCHHHHHCCHHHH | 51.25 | 24489116 | |
| 213 | Phosphorylation | VDEELKITNAKLSDK HCHHHHHCCHHHHHH | 27.77 | 21126336 | |
| 218 | Phosphorylation | KITNAKLSDKIENKI HHCCHHHHHHHHHCH | 35.83 | 21126336 | |
| 220 | Acetylation | TNAKLSDKIENKIDD CCHHHHHHHHHCHHH | 48.85 | 24489116 | |
| 224 | Acetylation | LSDKIENKIDDVKFL HHHHHHHCHHHHHHH | 34.42 | 24489116 | |
| 229 | Acetylation | ENKIDDVKFLKQLSP HHCHHHHHHHHHHCC | 52.56 | 24489116 | |
| 235 | Phosphorylation | VKFLKQLSPDLSALC HHHHHHHCCCHHHHC | 17.55 | 28152593 | |
| 382 | Acetylation | SNFILNVKNDYRKIQ CCEEEEECCCCHHCC | 42.92 | 24489116 | |
| 434 | Phosphorylation | TEPPRFLTNYTKAKS CCCCCCCCCCCCCCC | 24.38 | 28889911 | |
| 459 | Phosphorylation | EDNNKKKSSPATKVP CCCCCCCCCCCCCCC | 50.89 | 29136822 | |
| 460 | Phosphorylation | DNNKKKSSPATKVPS CCCCCCCCCCCCCCC | 27.68 | 17563356 | |
| 463 | Phosphorylation | KKKSSPATKVPSKPD CCCCCCCCCCCCCCC | 35.64 | 29136822 | |
| 467 | Phosphorylation | SPATKVPSKPDRNSK CCCCCCCCCCCCCCH | 60.86 | 30377154 | |
| 473 | Phosphorylation | PSKPDRNSKILRTKL CCCCCCCCHHHHHHH | 23.20 | 30377154 | |
| 510 | Acetylation | KLHEKLEKNGLLRFS HHHHHHHHCCCEEEE | 67.75 | 24489116 | |
| 526 | Phosphorylation | ADANGPDSEPRQYFK CCCCCCCCCHHHHHH | 53.27 | 25752575 | |
| 534 | Acetylation | EPRQYFKKYESYVRD CHHHHHHHHHHHHCC | 44.33 | 25381059 | |
| 537 | Phosphorylation | QYFKKYESYVRDSQL HHHHHHHHHHCCCCC | 26.32 | 30377154 | |
| 542 | Phosphorylation | YESYVRDSQLPTNIR HHHHHCCCCCCCCCC | 24.05 | 28889911 | |
| 577 | Phosphorylation | PVPFHINSYKNGSKN CCCEEEEECCCCCCC | 36.56 | 30377154 | |
| 582 | Phosphorylation | INSYKNGSKNEEGEY EEECCCCCCCCCCEE | 41.52 | 27017623 | |
| 583 | Ubiquitination | NSYKNGSKNEEGEYT EECCCCCCCCCCEEE | 70.54 | 23749301 | |
| 590 | Phosphorylation | KNEEGEYTYLRLNFN CCCCCEEEEEEEECC | 16.27 | 27017623 | |
| 598 | Phosphorylation | YLRLNFNSPGSSGGI EEEEECCCCCCCCCC | 26.88 | 22369663 | |
| 601 | Phosphorylation | LNFNSPGSSGGISKK EECCCCCCCCCCCCC | 29.24 | 22369663 | |
| 602 | Phosphorylation | NFNSPGSSGGISKKV ECCCCCCCCCCCCCC | 47.13 | 22369663 | |
| 606 | Phosphorylation | PGSSGGISKKVEELP CCCCCCCCCCCEECC | 29.69 | 19779198 | |
| 607 | Acetylation | GSSGGISKKVEELPY CCCCCCCCCCEECCC | 59.94 | 24489116 | |
| 608 | Ubiquitination | SSGGISKKVEELPYE CCCCCCCCCEECCCC | 48.35 | 23749301 | |
| 637 | Phosphorylation | SKDGDRMSETFKQIA CCCCCHHHHHHHHHH | 34.09 | 27717283 | |
| 639 | Phosphorylation | DGDRMSETFKQIADL CCCHHHHHHHHHHHH | 28.91 | 27717283 | |
| 641 | Acetylation | DRMSETFKQIADLKK CHHHHHHHHHHHHHH | 48.49 | 24489116 | |
| 668 | Acetylation | ADVVQQDKLIENKTG HHHHHHHHHHHCCCC | 47.21 | 24489116 | |
| 713 | Phosphorylation | RFQSPLRTDSRIDIL EECCCCCCCCCHHHH | 46.11 | 30377154 | |
| 715 | Phosphorylation | QSPLRTDSRIDILFS CCCCCCCCCHHHHHH | 30.44 | 30377154 | |
| 765 | Phosphorylation | VQFYREASDMSVDET CEEHHHHHCCCCCCC | 29.15 | 9832518 | |
| 768 | Phosphorylation | YREASDMSVDETGGG HHHHHCCCCCCCCCC | 31.26 | 27214570 | |
| 800 | Ubiquitination | QEQEERRKRAALDKE HHHHHHHHHHHHHHH | 53.24 | 19722269 | |
| 806 | Ubiquitination | RKRAALDKEFKYFAD HHHHHHHHHHHHHHH | 66.94 | 19722269 | |
| 1011 | Phosphorylation | EDYTGDESEEGEDWD CCCCCCCCCCCCCHH | 45.76 | 28889911 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SPT16_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 SPT16_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-235; SER-460; SER-526;SER-542; SER-598; SER-601; SER-602; SER-765 AND SER-1011, AND MASSSPECTROMETRY. | |
| "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-460, AND MASSSPECTROMETRY. | |
