THO2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: THO2_SCHPO
• UniProt AC: Q09779
• Protein Name: THO complex subunit 2
• Gene Name: tho2
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 1628
• 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..
• Protein Sequence: MTSLPEKDQQGEVSVSENQKKLSEEWEPYIDKLVASNRTRDERVESIQELFQKCVIEEKLPVDIFFSIFSLAFERLEEKNTLASYVIDTLWLFDTEWIKNFHEGSHDKAEKRLVSIGKGLKEFLPEEWLLSRLDCKFLENINVVPNGDFLNRKIVRTNTSLLYRQKKFNLLREESEGFSHLMINFFDALTCLRNKSLNEDYLIVQVNKSIISTIGAFDLDPNKVLDLILLLFSENLLDSWRFFLSILRNSPWGPNKERKFWNQLPDREKETFLNNLSNANGIFNFDERFTNTKSIMSQVLGHNLQYMYKEDDENLESYFMMVALLIKYNFISIDNIWAHLSPSDEELGKELGKYKDKLDEQTFKAKGNALTMAAPLPDDEIEDGETMDGQKAEAVPEIKKAKPSQKLGLLKSLLSIGDLSSSLLILGRYPFLLRAYPELSNLYHKLLHISISSIYANYSPLKLLPNDVRERLKQPKFIPEDSRLREITLRPPKEKNLVFSLDPFADRFNKTESEVFYYFENYDEDIPILRNLTEFYNIAIPWLRLSGLALCHDPVIVTKLCRIGQKCVDNSSESRTLWLDIIRSLLLPLITLIDVNTGLSYELFELLSKFDSSTRYALYGEWSSTSMKKFPELKLQNSITEKETKGILRRLTKTNVKQFGRLLAKVCHSNPCTVFSIALNQIETYDNLVEVVVDSARFITALDFDALTFIILSSFSNEFKKRLKSDGTSIAHWLQGLASFCGRVFRRYSSLDCTSIVEYVIKQFKVNQMFDLVILKELLSQMTGLQPWTNLSDNQIQGAAGGPVLRQLSLSLIYENPDVVRKSSMRLFNTLQKNGLATQLLVLLSQKYSTCIYDVTDENSHLKLISSLQDECSDVLYLLMEFLNMVCSPKSYYKLIPSFEQLIQDFHIQPQVAFYLSRYKNLDHSLTGSNTEDAMDIDYENTSSPNTASNPVWSIDNSVITELLPKQIWDYFSPNFYLTFWKLSLYDVFVPLERYEFERSRAFDQIRQTDAANTFYSRHRHDRQKIMQLSNSLQNELKEHINSLESVRKVLQGDCVKWFIPNGVFPNGTRLEHARFNCARYLWTLCIAPRLKMSPHDALYCAKFVKLLHSLGTPNFSTMSFLEILFNSQLPSFIFSMTQREADNFGRFLYEVLYDITSWYRDKILYERECLANGALPGFRLYWSDEQNDPDLSAVLPYNKFVLLFSKWHKYLTSYFESCLLSTEYMHIYNSVIILEKILPCFPLIIESGSALKRAAERLKDEEKREDLKVLALGYFAKLSKKQPEWVSFNSFSGTVRPSNSEKLQRPQQLSVAATSAVDSKTASISEEQAKIDKQKVALNPSAPEFVPDSTPSDAVASETDNKNLVENKAVEKRVEARSSANERKQEERRRKTTPEGNRRALRTRTPTNEDIQRSDSKLREDQSRDRTPQSRSFTNENNDNLRSVSRHTRREPQQAQNLNARREHESQKSDRWRQNGNVNRNPRVSNNNSTNVSRERSSEANHRTSNDNKRDEVTEGKDKNKRQDISGESNSRQNNAISRAGRSNGSNRGNDSRDADGRRSTHYASNKRPRSSDSQSPSNLREEDERENSRRRARQDDRRDRDSRQQRDRPRDRTSRSAREEKRRKIQ

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
1353	Phosphorylation	FVPDSTPSDAVASET CCCCCCCCHHCCCCC		21712547
1404	Phosphorylation	GNRRALRTRTPTNED HHHHHHHCCCCCHHH		29996109
1406	Phosphorylation	RRALRTRTPTNEDIQ HHHHHCCCCCHHHHH		28889911
1408	Phosphorylation	ALRTRTPTNEDIQRS HHHCCCCCHHHHHHC		28889911
1575	Phosphorylation	KRPRSSDSQSPSNLR CCCCCCCCCCCCCHH		25720772
1577	Phosphorylation	PRSSDSQSPSNLREE CCCCCCCCCCCHHHH		28889911
1579	Phosphorylation	SSDSQSPSNLREEDE CCCCCCCCCHHHHHH		29996109

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

Oops, there are no upstream regulatory protein records of THO2_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of THO2_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 THO2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MTR4_SCHPO	mtr4	physical	22965128

Drug and Disease Associations

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