| UniProt ID | HPR1_YEAST | |
|---|---|---|
| UniProt AC | P17629 | |
| Protein Name | THO complex subunit HPR1 | |
| Gene Name | HPR1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 752 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA.. | |
| Protein Sequence | MSNTEELIQNSIGFLQKTFKALPVSFDSIRHEPLPSSMLHASVLNFEWEPLEKNISAIHDRDSLIDIILKRFIIDSMTNAIEDEEENNLEKGLLNSCIGLDFVYNSRFNRSNPASWGNTFFELFSTIIDLLNSPSTFLKFWPYAESRIEWFKMNTSVEPVSLGESNLISYKQPLYEKLRHWNDILAKLENNDILNTVKHYNMKYKLENFLSELLPINEESNFNRSASISALQESDNEWNRSARERESNRSSDVIFAADYNFVFYHLIICPIEFAFSDLEYKNDVDRSLSPLLDAILEIEENFYSKIKMNNRTRYSLEEALNTEYYANYDVMTPKLPVYMKHSNAMKMDRNEFWANLQNIKESDDYTLRPTIMDISLSNTTCLYKQLTQEDDDYYRKQFILQLCFTTNLIRNLISSDETRNFYKSCYLRENPLSDIDFENLDEVNKKRGLNLCSYICDNRVLKFYKIKDPDFYRVIRKLMSSDEKFTTAKIDGFKEFQNFRISKEKIPPPAFDETFKKFTFIKMGNKLINNVWKIPTGLDKIEQEVKKPEGVYEAAQAKWESKISSETSGGEAKDEIIRQWQTLRFLRSRYLFDFDKVNEKTGVDGLFEEPRKVEALDDSFKEKLLYKINQEHRKKLQDAREYKIGKERKKRALEEEASFPEREQKIKSQRINSASQTEGDELKSEQTQPKGEISEENTKIKSSEVSSQDPDSGVAGEFAPQNTTAQLENPKTEDNNAATSNISNGSSTQDMK | |
| 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 |
|---|---|---|---|---|---|
| 76 | Phosphorylation | LKRFIIDSMTNAIED HHHHHHHHHHHCCCH | 19.66 | 30377154 | |
| 78 | Phosphorylation | RFIIDSMTNAIEDEE HHHHHHHHHCCCHHH | 26.00 | 30377154 | |
| 155 | Phosphorylation | IEWFKMNTSVEPVSL EEEEECCCCCCCCCC | 30.56 | 29734811 | |
| 161 | Phosphorylation | NTSVEPVSLGESNLI CCCCCCCCCCCCCCC | 41.18 | 29734811 | |
| 165 | Phosphorylation | EPVSLGESNLISYKQ CCCCCCCCCCCCCCC | 34.83 | 29734811 | |
| 170 | Phosphorylation | GESNLISYKQPLYEK CCCCCCCCCCHHHHH | 13.47 | 25521595 | |
| 171 | Acetylation | ESNLISYKQPLYEKL CCCCCCCCCHHHHHH | 38.35 | 24489116 | |
| 225 | Phosphorylation | EESNFNRSASISALQ CCCCCCCCCCHHHHH | 27.72 | 19779198 | |
| 227 | Phosphorylation | SNFNRSASISALQES CCCCCCCCHHHHHHC | 20.51 | 25752575 | |
| 229 | Phosphorylation | FNRSASISALQESDN CCCCCCHHHHHHCCC | 22.04 | 28889911 | |
| 234 | Phosphorylation | SISALQESDNEWNRS CHHHHHHCCCHHHHH | 32.54 | 22369663 | |
| 375 | Phosphorylation | RPTIMDISLSNTTCL CCEEEEEECCCCEEE | 22.83 | 21551504 | |
| 377 | Phosphorylation | TIMDISLSNTTCLYK EEEEEECCCCEEEEH | 25.91 | 21551504 | |
| 379 | Phosphorylation | MDISLSNTTCLYKQL EEEECCCCEEEEHHC | 18.60 | 21551504 | |
| 380 | Phosphorylation | DISLSNTTCLYKQLT EEECCCCEEEEHHCC | 12.55 | 21551504 | |
| 445 | Ubiquitination | ENLDEVNKKRGLNLC CCHHHHHHHCCCCHH | 49.36 | 17644757 | |
| 446 | Ubiquitination | NLDEVNKKRGLNLCS CHHHHHHHCCCCHHH | 46.63 | 17644757 | |
| 546 | Ubiquitination | DKIEQEVKKPEGVYE HHHHHHHHCCCCHHH | 62.95 | 17644757 | |
| 547 | Ubiquitination | KIEQEVKKPEGVYEA HHHHHHHCCCCHHHH | 54.18 | 17644757 | |
| 558 | Ubiquitination | VYEAAQAKWESKISS HHHHHHHHHHHHCCC | 39.14 | 17644757 | |
| 558 | Acetylation | VYEAAQAKWESKISS HHHHHHHHHHHHCCC | 39.14 | 22865919 | |
| 562 | Ubiquitination | AQAKWESKISSETSG HHHHHHHHCCCCCCC | 34.78 | 17644757 | |
| 573 | Acetylation | ETSGGEAKDEIIRQW CCCCCHHHHHHHHHH | 52.14 | 24489116 | |
| 573 | Ubiquitination | ETSGGEAKDEIIRQW CCCCCHHHHHHHHHH | 52.14 | 17644757 | |
| 596 | Acetylation | RYLFDFDKVNEKTGV HHCCCHHHCCCCCCC | 47.13 | 24489116 | |
| 619 | Phosphorylation | KVEALDDSFKEKLLY HHHHCCHHHHHHHHH | 37.57 | 28889911 | |
| 623 | Ubiquitination | LDDSFKEKLLYKINQ CCHHHHHHHHHHHCH | 44.37 | 17644757 | |
| 627 | Ubiquitination | FKEKLLYKINQEHRK HHHHHHHHHCHHHHH | 34.84 | 17644757 | |
| 634 | Ubiquitination | KINQEHRKKLQDARE HHCHHHHHHHHHHHH | 60.80 | 17644757 | |
| 635 | Ubiquitination | INQEHRKKLQDAREY HCHHHHHHHHHHHHH | 51.87 | 17644757 | |
| 643 | Ubiquitination | LQDAREYKIGKERKK HHHHHHHHCCHHHHH | 39.98 | 17644757 | |
| 646 | Ubiquitination | AREYKIGKERKKRAL HHHHHCCHHHHHHHH | 58.79 | 17644757 | |
| 649 | Ubiquitination | YKIGKERKKRALEEE HHCCHHHHHHHHHHH | 47.94 | 17644757 | |
| 668 | Phosphorylation | EREQKIKSQRINSAS HHHHHHHHHHHCCCC | 28.32 | 21440633 | |
| 673 | Phosphorylation | IKSQRINSASQTEGD HHHHHHCCCCCCCHH | 27.25 | 22369663 | |
| 675 | Phosphorylation | SQRINSASQTEGDEL HHHHCCCCCCCHHHH | 37.14 | 22369663 | |
| 677 | Phosphorylation | RINSASQTEGDELKS HHCCCCCCCHHHHHC | 39.17 | 21440633 | |
| 683 | Ubiquitination | QTEGDELKSEQTQPK CCCHHHHHCCCCCCC | 50.31 | 23749301 | |
| 694 | Phosphorylation | TQPKGEISEENTKIK CCCCCCCCCCCCCCC | 34.26 | 23749301 | |
| 702 | Phosphorylation | EENTKIKSSEVSSQD CCCCCCCCCCCCCCC | 34.89 | 21551504 | |
| 703 | Phosphorylation | ENTKIKSSEVSSQDP CCCCCCCCCCCCCCC | 36.69 | 19779198 | |
| 706 | Phosphorylation | KIKSSEVSSQDPDSG CCCCCCCCCCCCCCC | 20.45 | 21551504 | |
| 707 | Phosphorylation | IKSSEVSSQDPDSGV CCCCCCCCCCCCCCC | 43.72 | 25752575 | |
| 712 | Phosphorylation | VSSQDPDSGVAGEFA CCCCCCCCCCCCCCC | 40.32 | 30377154 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HPR1_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 HPR1_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-227; SER-234; SER-619;SER-673; SER-675 AND SER-707, 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-675, AND MASSSPECTROMETRY. | |
| "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-234, AND MASSSPECTROMETRY. | |
