UniProt ID | PIF1_YEAST | |
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UniProt AC | P07271 | |
Protein Name | ATP-dependent DNA helicase PIF1 {ECO:0000255|HAMAP-Rule:MF_03176} | |
Gene Name | PIF1 {ECO:0000255|HAMAP-Rule:MF_03176} | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 859 | |
Subcellular Localization |
Isoform Nuclear: Nucleus, nucleolus . Mainly concentrated in the nucleolus, and occasionally redistributes to single nuclear foci outside the nucleolus, probably sites of DNA repair. Isoform Mitochondrial: Mitochondrion inner membrane Peripheral m |
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Protein Description | DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule of ATP. Processes at an unwinding rate of about 75 bp/s. Resolves G4 structures, preventing replication pausing and double-strand breaks (DSBs) at G4 motifs. Involved in the maintenance of telomeric DNA. Inhibits telomere elongation, de novo telomere formation and telomere addition to DSBs via catalytic inhibition of telomerase. Reduces the processivity of telomerase by displacing active telomerase from DNA ends. Releases telomerase by unwinding the short telomerase RNA/telomeric DNA hybrid that is the intermediate in the telomerase reaction. Involved in the maintenance of ribosomal (rDNA). Required for efficient fork arrest at the replication fork barrier within rDNA. Involved in the maintenance of mitochondrial (mtDNA). Required to maintain mtDNA under conditions that introduce dsDNA breaks in mtDNA, either preventing or repairing dsDNA breaks. May inhibit replication progression to allow time for repair. May have a general role in chromosomal replication by affecting Okazaki fragment maturation. May have a role in conjunction with DNA2 helicase/nuclease in 5'-flap extension during Okazaki fragment processing.. | |
Protein Sequence | MPKWIRSTLNHIIPRRPFICSFNSFLLLKNVSHAKLSFSMSSRGFRSNNFIQAQLKHPSILSKEDLDLLSDSDDWEEPDCIQLETEKQEKKIITDIHKEDPVDKKPMRDKNVMNFINKDSPLSWNDMFKPSIIQPPQLISENSFDQSSQKKSRSTGFKNPLRPALKKESSFDELQNNSISQERSLEMINENEKKKMQFGEKIAVLTQRPSFTELQNDQDDSNLNPHNGVKVKIPICLSKEQESIIKLAENGHNIFYTGSAGTGKSILLREMIKVLKGIYGRENVAVTASTGLAACNIGGITIHSFAGIGLGKGDADKLYKKVRRSRKHLRRWENIGALVVDEISMLDAELLDKLDFIARKIRKNHQPFGGIQLIFCGDFFQLPPVSKDPNRPTKFAFESKAWKEGVKMTIMLQKVFRQRGDVKFIDMLNRMRLGNIDDETEREFKKLSRPLPDDEIIPAELYSTRMEVERANNSRLSKLPGQVHIFNAIDGGALEDEELKERLLQNFLAPKELHLKVGAQVMMVKNLDATLVNGSLGKVIEFMDPETYFCYEALTNDPSMPPEKLETWAENPSKLKAAMEREQSDGEESAVASRKSSVKEGFAKSDIGEPVSPLDSSVFDFMKRVKTDDEVVLENIKRKEQLMQTIHQNSAGKRRLPLVRFKASDMSTRMVLVEPEDWAIEDENEKPLVSRVQLPLMLAWSLSIHKSQGQTLPKVKVDLRRVFEKGQAYVALSRAVSREGLQVLNFDRTRIKAHQKVIDFYLTLSSAESAYKQLEADEQVKKRKLDYAPGPKYKAKSKSKSNSPAPISATTQSNNGIAAMLQRHSRKRFQLKKESNSNQVHSLVSDEPRGQDTEDHILE | |
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 |
---|---|---|---|---|---|
41 | Phosphorylation | AKLSFSMSSRGFRSN CEEEEECCCCCCCCC | 18.71 | 28889911 | |
47 | Phosphorylation | MSSRGFRSNNFIQAQ CCCCCCCCCCCHHHH | 33.59 | 28889911 | |
70 | Phosphorylation | KEDLDLLSDSDDWEE HHHHHCCCCCCCCCC | 42.22 | 21440633 | |
72 | Phosphorylation | DLDLLSDSDDWEEPD HHHCCCCCCCCCCCC | 33.81 | 21440633 | |
140 | Phosphorylation | IQPPQLISENSFDQS CCCCCHHCCCCCCHH | 39.04 | 21440633 | |
143 | Phosphorylation | PQLISENSFDQSSQK CCHHCCCCCCHHHHH | 26.58 | 21551504 | |
169 | Phosphorylation | RPALKKESSFDELQN HHHHHCCCCHHHHHH | 45.22 | 22369663 | |
170 | Phosphorylation | PALKKESSFDELQNN HHHHCCCCHHHHHHC | 37.50 | 22369663 | |
178 | Phosphorylation | FDELQNNSISQERSL HHHHHHCCCCHHHHH | 31.03 | 22369663 | |
180 | Phosphorylation | ELQNNSISQERSLEM HHHHCCCCHHHHHHH | 26.30 | 23749301 | |
184 | Phosphorylation | NSISQERSLEMINEN CCCCHHHHHHHHCHH | 28.12 | 28889911 | |
210 | Phosphorylation | AVLTQRPSFTELQND EEHHCCCCCHHHCCC | 47.17 | 25521595 | |
212 | Phosphorylation | LTQRPSFTELQNDQD HHCCCCCHHHCCCCC | 39.87 | 25521595 | |
584 | Phosphorylation | AAMEREQSDGEESAV HHHHHHHCCCCHHHH | 42.71 | 21551504 | |
589 | Phosphorylation | EQSDGEESAVASRKS HHCCCCHHHHHHCHH | 24.60 | 21551504 | |
593 | Phosphorylation | GEESAVASRKSSVKE CCHHHHHHCHHHHHH | 33.37 | 30377154 | |
612 | Phosphorylation | SDIGEPVSPLDSSVF CCCCCCCCCCCHHHH | 30.38 | 21440633 | |
616 | Phosphorylation | EPVSPLDSSVFDFMK CCCCCCCHHHHHHHH | 35.76 | 30377154 | |
627 | Phosphorylation | DFMKRVKTDDEVVLE HHHHHCCCCCHHHHH | 45.91 | 30377154 | |
737 | Phosphorylation | VALSRAVSREGLQVL HHHHHHHHHCCCEEE | 24.51 | 23749301 | |
766 | Phosphorylation | DFYLTLSSAESAYKQ HHHHHHCCHHHHHHH | 38.89 | 28889911 | |
769 | Phosphorylation | LTLSSAESAYKQLEA HHHCCHHHHHHHHHH | 36.29 | 28889911 | |
797 | Phosphorylation | GPKYKAKSKSKSNSP CHHHCCCCCCCCCCC | 47.20 | 24961812 | |
799 | Phosphorylation | KYKAKSKSKSNSPAP HHCCCCCCCCCCCCC | 48.70 | 24961812 | |
801 | Phosphorylation | KAKSKSKSNSPAPIS CCCCCCCCCCCCCCC | 50.02 | 21440633 | |
803 | Phosphorylation | KSKSKSNSPAPISAT CCCCCCCCCCCCCEE | 29.54 | 23749301 | |
808 | Phosphorylation | SNSPAPISATTQSNN CCCCCCCCEECCCCC | 20.64 | 24961812 | |
810 | Phosphorylation | SPAPISATTQSNNGI CCCCCCEECCCCCHH | 20.69 | 24961812 | |
811 | Phosphorylation | PAPISATTQSNNGIA CCCCCEECCCCCHHH | 29.71 | 24961812 | |
813 | Phosphorylation | PISATTQSNNGIAAM CCCEECCCCCHHHHH | 30.12 | 24961812 | |
825 | Phosphorylation | AAMLQRHSRKRFQLK HHHHHHHHHHHHEEC | 41.51 | 24961812 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of PIF1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of PIF1_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of PIF1_YEAST !! |
Kegg Drug | ||||||
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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-47; SER-169; SER-170 ANDSER-584, 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-169 AND SER-210, ANDMASS SPECTROMETRY. |