RTF1_SCHPO - dbPTM
RTF1_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTF1_SCHPO
UniProt AC O94667
Protein Name RNA polymerase-associated protein C651.09c
Gene Name SPBC651.09c
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 560
Subcellular Localization Nucleus, nucleoplasm .
Protein Description The PAF1 complex is a multifunctional complex. Involved in transcription initiation via genetic interactions with TATA-binding proteins. Involved in elongation. Also has a role in transcription-coupled histone modification. Important for TATA site selection by TBP. Directly or indirectly regulates the DNA-binding properties of the TATA box-binding protein, and the relative activities of different TATA elements (By similarity)..
Protein Sequence MADFQDELLALAGIDDSDVASNRKRAHDDLDDVLSSSSDEDNNENVGQDYAEESGGEGNEKSEDEFEEKFKNPYRLEGKFKDEADRAKIMAMTEIERESILFEREEEISKLMERRELAIRLHQQNAQYMAQSTRRSTRDKPLTSAAAGKRDKLTELKKRRQERSARSVSERTRKRSPVSDYEEQNESEKSEEEEGYSPSYAEEKVEQVSKDNASANLYDLNAIRLGRKHVAEYMYHPIFESTVTGCFVRVKIGERDGQGVYRLCQVKGILESRKPYRVDGVLTKVSLECFHGRSKRVFDVNVLSNEPFSDHDFQRWHHQMMEDKLSMPSKNFVQRKLNDLRDMSKYVLSEKEVSDIINRKKELSRVPSNIAAEKTRLRQRRQAAYVAGNAELVKEIDDQLNTLEELSMGSNQNSNSAMDQLAKVNERNRRRNHTEIRLAEQRMNEERRRLSAAATATPMSAPTSVLTGTSPQPSPSLSTSIMSTPKLNPSESVVVASEKASSPDLSPKLLPSESQIFDEGIAVTQTPNTLEDKDFKLHEKAVHGIDDIIATVDFGIDINI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
17PhosphorylationALAGIDDSDVASNRK
HHHCCCHHHHHHCCH		30.1821712547
21PhosphorylationIDDSDVASNRKRAHD
CCHHHHHHCCHHCCC		36.7021712547
62PhosphorylationGGEGNEKSEDEFEEK
CCCCCCCCHHHHHHH		44.0724763107
176PhosphorylationSERTRKRSPVSDYEE
HHHHHCCCCCCCHHH		32.4629996109
179PhosphorylationTRKRSPVSDYEEQNE
HHCCCCCCCHHHHCH		37.5529996109
181PhosphorylationKRSPVSDYEEQNESE
CCCCCCCHHHHCHHH		17.5429996109
187PhosphorylationDYEEQNESEKSEEEE
CHHHHCHHHHCHHHC		58.8524763107
190PhosphorylationEQNESEKSEEEEGYS
HHCHHHHCHHHCCCC		46.3021712547
196PhosphorylationKSEEEEGYSPSYAEE
HCHHHCCCCCHHHHH		22.2329996109
197PhosphorylationSEEEEGYSPSYAEEK
CHHHCCCCCHHHHHH		20.4428889911
199PhosphorylationEEEGYSPSYAEEKVE
HHCCCCCHHHHHHHH		30.9129996109
469PhosphorylationPTSVLTGTSPQPSPS
CCCHHCCCCCCCCCC		31.8127738172
470PhosphorylationTSVLTGTSPQPSPSL
CCHHCCCCCCCCCCC		23.9225720772
474PhosphorylationTGTSPQPSPSLSTSI
CCCCCCCCCCCCCCC		23.1327738172
476PhosphorylationTSPQPSPSLSTSIMS
CCCCCCCCCCCCCCC		39.0125720772
484PhosphorylationLSTSIMSTPKLNPSE
CCCCCCCCCCCCCCC		13.6827738172
497PhosphorylationSESVVVASEKASSPD
CCCEEEEECCCCCCC		28.2024763107
501PhosphorylationVVASEKASSPDLSPK
EEEECCCCCCCCCCC		54.1729996109
502PhosphorylationVASEKASSPDLSPKL
EEECCCCCCCCCCCC		27.5628889911
506PhosphorylationKASSPDLSPKLLPSE
CCCCCCCCCCCCCCH		27.6328889911
512PhosphorylationLSPKLLPSESQIFDE
CCCCCCCCHHHHCCC		50.2621712547
514PhosphorylationPKLLPSESQIFDEGI
CCCCCCHHHHCCCCE		32.6824763107
524PhosphorylationFDEGIAVTQTPNTLE
CCCCEEEECCCCCCC		20.0829996109
526PhosphorylationEGIAVTQTPNTLEDK
CCEEEECCCCCCCCC		14.7824763107
529PhosphorylationAVTQTPNTLEDKDFK
EEECCCCCCCCCCCH		32.5027738172
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
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 RTF1_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTF1_SCHPO !!
Disease-associated PTM Sites based on SAP

* 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 RTF1_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CDK9_SCHPOcdk9genetic
24385927
CDC73_SCHPOcdc73genetic
24385927
SIB1_SCHPOsib1physical
24385927
YLW5_SCHPOski7physical
24385927
RAD54_SCHPOrad54physical
24385927
YD72_SCHPOSPAC32A11.02cphysical
24385927
YEJJ_SCHPOabo1physical
24385927
KLF1_SCHPOklf1physical
24385927
SDHB_SCHPOsdh2physical
24385927
MU178_SCHPOmug178physical
24385927
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTF1_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; SER-502 ANDSER-506, AND MASS SPECTROMETRY.

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