RCQ1_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RCQ1_SCHPO
• UniProt AC: O13796
• Protein Name: Ribosome quality control complex subunit 1 {ECO:0000250|UniProtKB:Q05468}
• Gene Name: rqc1 {ECO:0000250|UniProtKB:Q05468}
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 656
• Subcellular Localization: Cytoplasm .
• Protein Description: Component of the ribosome quality control complex (RQC), a ribosome-associated complex that mediates ubiquitination and extraction of incompletely synthesized nascent chains for proteasomal degradation. Rqc1 is essential for the recruitment of cdc48 to ribosomal subunits..
• Protein Sequence: MSSRALRKLQRQRQTELLEEALDSESDEDDEFSSTSGKKVVNVFEILEKENNAINSEAEKSVSEEEQDEPLVEGESPIVSTNKKAKNKKKKKKQQKKKKVTGKRDLDNQSSDNEKLEGLESSKNIDDDIDEIEKAAAELKLKYREQDQVEHVAGVEESATIPLDKELDEKLNKLLGVNISMLNPDLEIRKIFGRIVEKRSVNARHDNLRRKRHVLVQPQEGWPPLVRSGLGMKLTGQSQDLECFFEITQSRAYQEVQETFEYYVQTYDPNNLLMLLRSHPFHIDTLLQVSEIIDQQGDHELSAELVARGLYAFDSILHPRFNLATGATRLPFAIPSNRRLFLCIWRYLQSLQSRGCWRTVFEFCKALLQFDMSDPYAIGTCIDIYALRRREFAWIIDFANYLENSNKISDTPNMLYSSALAMFYVHGDTTDTRASMLAAFERAPYMLSELLDTLNISFTKSSIPSPQDPVQELHSAMYALYAKDSWSDPTVLAFINSILEKETVTLHDVEGQFAELTENLSRRVILLNEQSLRKFLPQRILQGTILSFDPLPPDTYLSESQVFGRDISRRIASFLSDYLSRAREVNENEEEPPAHEFDLPPAEQLLQQIESEVGEESEDGTPVMTRLRSFFGSLFTSTNSETEPAEESTEEMGQGD

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
15	Phosphorylation	KLQRQRQTELLEEAL HHHHHHHHHHHHHHH		21712547
24	Phosphorylation	LLEEALDSESDEDDE HHHHHHCCCCCCCCC		24763107
26	Phosphorylation	EEALDSESDEDDEFS HHHHCCCCCCCCCCC		24763107
33	Phosphorylation	SDEDDEFSSTSGKKV CCCCCCCCCCCCCEE		21712547
34	Phosphorylation	DEDDEFSSTSGKKVV CCCCCCCCCCCCEEE		21712547
56	Phosphorylation	KENNAINSEAEKSVS HHCCCCCHHHHHCCC		28889911
61	Phosphorylation	INSEAEKSVSEEEQD CCHHHHHCCCHHHCC		28889911
63	Phosphorylation	SEAEKSVSEEEQDEP HHHHHCCCHHHCCCC		28889911
101	Phosphorylation	QQKKKKVTGKRDLDN HHHHHHCCCCCCCCC		21712547
110	Phosphorylation	KRDLDNQSSDNEKLE CCCCCCCCCCCHHHH		28889911
111	Phosphorylation	RDLDNQSSDNEKLEG CCCCCCCCCCHHHHH		28889911
121	Phosphorylation	EKLEGLESSKNIDDD HHHHHHHHCCCCCCC		28889911
122	Phosphorylation	KLEGLESSKNIDDDI HHHHHHHCCCCCCCH		21712547
573	Phosphorylation	DISRRIASFLSDYLS HHHHHHHHHHHHHHH		25720772
576	Phosphorylation	RRIASFLSDYLSRAR HHHHHHHHHHHHHHH		25720772
617	Phosphorylation	ESEVGEESEDGTPVM HHHHCCCCCCCCCHH		29996109
637	Phosphorylation	FFGSLFTSTNSETEP HHHHHHCCCCCCCCC		25720772
640	Phosphorylation	SLFTSTNSETEPAEE HHHCCCCCCCCCCHH		25720772
642	Phosphorylation	FTSTNSETEPAEEST HCCCCCCCCCCHHHH		25720772
648	Phosphorylation	ETEPAEESTEEMGQG CCCCCHHHHHHCCCC		25720772
649	Phosphorylation	TEPAEESTEEMGQGD CCCCHHHHHHCCCCC		25720772

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of RCQ1_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RCQ1_SCHPO !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RCQ1_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RCQ1_SCHPO	rqc1	physical	26771498

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.