| UniProt ID | FHL1_YEAST | |
|---|---|---|
| UniProt AC | P39521 | |
| Protein Name | Pre-rRNA-processing protein FHL1 | |
| Gene Name | FHL1 | |
| Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
| Sequence Length | 936 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | Controls the pre-rRNA processing machinery in conjunction with IFH1. Presumably acts as a transcriptional regulator of genes specifically involved in that process. IFH1 convert FHL1 from a repressor to an activator.. | |
| Protein Sequence | MDGEMAIIESSNHVGTSSPTTETQFTIDSSALKDQETKESITNSPTSEVPIETKLPKSSDIVTEEKHPQNTTTDIENEVENPVTDDNGNLKLELPDNLDNADFSKLLEFDAKNDEALFNSNELLSHTMDPVNNIDLTHDHSREVSSKEDINIEPVNPDEDEREKTQDNTAAVKTEGIRNSEDTSIQKDEPTADAIYTDVHKLSVNKDTETLPTLVDEKNNMLHMRNNSITPIMFQQHELVGQPPQNTVTENNSTDAETTQRKLSEPIDASLPLPNEQPTIFAYARLDFQSFTFYVQTLHAIIGRRSENDFSHKVDVNLGPSKSISRRHAQIFYNFGTGRFELSIIGKNGAFVDDIFVEKGNTVPLRNKTKIQIGQIPFQFILPEQERNDDSKSPENADIAESEINTRNLKKNEPKSKKKITTGAKPKKAQTKPAVKKEKKPPKIPKKVYTLEEIPVEYRTKPTVSYSAMLTTCIRKYSTAKGMSLSEIYAGIRELFPYYKYCPDGWQSSVRHNLSLNKSFRKVSKEGKGWLWGLDEEYIAERERQKKKQSEIAVAKAQAAQLKLEQQQHKLQQVPQRGKKDIVSQRSNVNARKQNISQTLAANRAASNRKNTASDNQRTMKYLQEQLVILTRDRKGLSKQVIAAILTQALAMTINQVTQAAKNKGITGNPLTALMDKNPQHLNLILAAAVNAATAKVTKGEVKQLVNPETTAAAALAAKAQHSKPIRQPIVQTPHVPDRPPSQLSASASSHPNNYLHDKQPGSFDPSSLSRFFQPRQNARATSSVAATSVPAAASQNVDAQPKPKPAQDNDLESESGTSSSSSSSSESGSESDSGSDDGSASGSGDNSSTSSESESESDSGSEVDEKNNKNEKIDSESIKNNESKDDIPSKDENSSNDNREISKTDEEGHDSKRRKVSEDINEGITEVNVSLEEKL | |
| 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 |
|---|---|---|---|---|---|
| 37 | Phosphorylation | SALKDQETKESITNS HHHCCHHHHHHHHCC | 34.18 | 22369663 | |
| 40 | Phosphorylation | KDQETKESITNSPTS CCHHHHHHHHCCCCC | 35.95 | 22369663 | |
| 42 | Phosphorylation | QETKESITNSPTSEV HHHHHHHHCCCCCCC | 38.63 | 22890988 | |
| 44 | Phosphorylation | TKESITNSPTSEVPI HHHHHHCCCCCCCCC | 22.39 | 22369663 | |
| 46 | Phosphorylation | ESITNSPTSEVPIET HHHHCCCCCCCCCCC | 37.02 | 22369663 | |
| 47 | Phosphorylation | SITNSPTSEVPIETK HHHCCCCCCCCCCCC | 39.73 | 22369663 | |
| 53 | Phosphorylation | TSEVPIETKLPKSSD CCCCCCCCCCCCCCC | 38.30 | 22890988 | |
| 57 | Acetylation | PIETKLPKSSDIVTE CCCCCCCCCCCCCCC | 73.38 | 25381059 | |
| 71 | Phosphorylation | EEKHPQNTTTDIENE CCCCCCCCCCCCHHH | 26.31 | 20377248 | |
| 72 | Phosphorylation | EKHPQNTTTDIENEV CCCCCCCCCCCHHHC | 29.98 | 22369663 | |
| 73 | Phosphorylation | KHPQNTTTDIENEVE CCCCCCCCCCHHHCC | 32.70 | 22369663 | |
| 84 | Phosphorylation | NEVENPVTDDNGNLK HHCCCCCCCCCCCEE | 38.60 | 22369663 | |
| 104 | Phosphorylation | NLDNADFSKLLEFDA CCCCCCHHHHHHHHC | 23.96 | 21551504 | |
| 165 | Phosphorylation | DEDEREKTQDNTAAV CHHHHHHHCCCCHHH | 36.08 | 22369663 | |
| 169 | Phosphorylation | REKTQDNTAAVKTEG HHHHCCCCHHHHHHC | 25.04 | 20377248 | |
| 180 | Phosphorylation | KTEGIRNSEDTSIQK HHHCCCCCCCCCCCC | 27.31 | 28889911 | |
| 183 | Phosphorylation | GIRNSEDTSIQKDEP CCCCCCCCCCCCCCC | 24.55 | 21440633 | |
| 184 | Phosphorylation | IRNSEDTSIQKDEPT CCCCCCCCCCCCCCC | 35.03 | 25752575 | |
| 187 | Acetylation | SEDTSIQKDEPTADA CCCCCCCCCCCCCCC | 63.49 | 24489116 | |
| 208 | Phosphorylation | KLSVNKDTETLPTLV HCCCCCCCCCCCCHH | 32.26 | 23749301 | |
| 213 | Phosphorylation | KDTETLPTLVDEKNN CCCCCCCCHHCCCCC | 42.39 | 23749301 | |
| 228 | Phosphorylation | MLHMRNNSITPIMFQ EEEECCCCCCCEEEE | 31.24 | 24909858 | |
| 230 | Phosphorylation | HMRNNSITPIMFQQH EECCCCCCCEEEEHH | 13.44 | 21440633 | |
| 247 | Phosphorylation | VGQPPQNTVTENNST CCCCCCCCCCCCCCC | 24.45 | 28889911 | |
| 253 | Phosphorylation | NTVTENNSTDAETTQ CCCCCCCCCCHHHHH | 38.97 | 23749301 | |
| 254 | Phosphorylation | TVTENNSTDAETTQR CCCCCCCCCHHHHHH | 41.15 | 23749301 | |
| 264 | Phosphorylation | ETTQRKLSEPIDASL HHHHHHHCCCCCCCC | 44.34 | 22369663 | |
| 270 | Phosphorylation | LSEPIDASLPLPNEQ HCCCCCCCCCCCCCC | 27.11 | 28132839 | |
| 391 | Phosphorylation | EQERNDDSKSPENAD HHHCCCCCCCHHHHH | 37.59 | 22369663 | |
| 393 | Phosphorylation | ERNDDSKSPENADIA HCCCCCCCHHHHHHH | 41.20 | 22369663 | |
| 471 | Phosphorylation | VSYSAMLTTCIRKYS CCHHHHHHHHHHHHH | 13.41 | 19684113 | |
| 472 | Phosphorylation | SYSAMLTTCIRKYST CHHHHHHHHHHHHHC | 11.28 | 19684113 | |
| 570 | Acetylation | KLEQQQHKLQQVPQR HHHHHHHHHHHCCCC | 43.59 | 25381059 | |
| 579 | Acetylation | QQVPQRGKKDIVSQR HHCCCCCHHHHHHHH | 49.84 | 25381059 | |
| 580 | Acetylation | QVPQRGKKDIVSQRS HCCCCCHHHHHHHHH | 56.35 | 25381059 | |
| 593 | Acetylation | RSNVNARKQNISQTL HHHHHHHHHCHHHHH | 45.33 | 25381059 | |
| 647 | Phosphorylation | QVIAAILTQALAMTI HHHHHHHHHHHHHHH | 12.99 | 19823750 | |
| 653 | Phosphorylation | LTQALAMTINQVTQA HHHHHHHHHHHHHHH | 15.92 | 19823750 | |
| 658 | Phosphorylation | AMTINQVTQAAKNKG HHHHHHHHHHHHHCC | 11.61 | 19823750 | |
| 667 | Phosphorylation | AAKNKGITGNPLTAL HHHHCCCCCCHHHHH | 39.31 | 21126336 | |
| 755 | Phosphorylation | ASSHPNNYLHDKQPG CCCCCCCCCCCCCCC | 16.44 | 28889911 | |
| 763 | Phosphorylation | LHDKQPGSFDPSSLS CCCCCCCCCCHHHHH | 32.91 | 30377154 | |
| 876 | Phosphorylation | NKNEKIDSESIKNNE CCCCCCCHHHHCCCC | 36.39 | 28889911 | |
| 878 | Phosphorylation | NEKIDSESIKNNESK CCCCCHHHHCCCCCC | 42.70 | 28889911 | |
| 884 | Phosphorylation | ESIKNNESKDDIPSK HHHCCCCCCCCCCCC | 43.43 | 29136822 | |
| 890 | Phosphorylation | ESKDDIPSKDENSSN CCCCCCCCCCCCCCC | 53.74 | 21551504 | |
| 895 | Phosphorylation | IPSKDENSSNDNREI CCCCCCCCCCCCCCC | 28.59 | 21551504 | |
| 896 | Phosphorylation | PSKDENSSNDNREIS CCCCCCCCCCCCCCC | 60.84 | 21551504 | |
| 903 | Phosphorylation | SNDNREISKTDEEGH CCCCCCCCCCCCCCC | 25.42 | 21551504 | |
| 905 | Phosphorylation | DNREISKTDEEGHDS CCCCCCCCCCCCCHH | 41.68 | 21551504 | |
| 912 | Phosphorylation | TDEEGHDSKRRKVSE CCCCCCHHHCHHHHH | 23.53 | 21551504 | |
| 913 | Acetylation | DEEGHDSKRRKVSED CCCCCHHHCHHHHHH | 63.38 | 25381059 | |
| 918 | Phosphorylation | DSKRRKVSEDINEGI HHHCHHHHHHHHCCC | 32.36 | 29734811 |
| 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 FHL1_YEAST !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of FHL1_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 FHL1_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-44; THR-46; SER-47;SER-264; SER-391 AND SER-393, 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-391 AND SER-393, ANDMASS 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-44, AND MASSSPECTROMETRY. | |
| "Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway."; Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.; Mol. Cell. Proteomics 4:310-327(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, AND MASSSPECTROMETRY. | |
