DXO_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DXO_HUMAN
• UniProt AC: O77932
• Protein Name: Decapping and exoribonuclease protein
• Gene Name: DXO
• Organism: Homo sapiens (Human).
• Sequence Length: 396
• Subcellular Localization: Nucleus .
• Protein Description: Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping, pyrophosphohydrolase and 5'-3' exonuclease activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. The 5' end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates (By similarity)..
• Protein Sequence: MDPRGTKRGAEKTEVAEPRNKLPRPAPSLPTDPALYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPTNGPGPNFDLRDGYPDRYQPRDEEVQERLDHLLCWLLEHRGRLEGGPGWLAEAIVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPNARAQRLARPPLLRELMYMGYKFEQYMCADKPGSSPDPSGEVNTNVAFCSVLRSRLGSHPLLFSGEVDCTDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPNVVAGFRNPDGFVSSLKTFPTMKMFEYVRNDRDGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHQDAPYAFLPIWYVEAMTQDLPSPPKTPSPK

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
47	Phosphorylation	FPFYRRPSELGCFSL CCCCCCHHHCCCEEH		28348404
68	Methylation	HGDARALRYYSPPPT CCCCCEEEECCCCCC		-
71	Phosphorylation	ARALRYYSPPPTNGP CCEEEECCCCCCCCC		28555341
75	Phosphorylation	RYYSPPPTNGPGPNF EECCCCCCCCCCCCC		28555341
91	Methylation	LRDGYPDRYQPRDEE CCCCCCCCCCCCCHH		-
130	Phosphorylation	WLAEAIVTWRGHLTK HHHHHHHHCHHHHHH		22210691
143	Phosphorylation	TKLLTTPYERQEGWQ HHHHCCCHHHCHHHH		22210691
154	Phosphorylation	EGWQLAASRFQGTLY HHHHHHHHHHCCEEE		22210691
186	Phosphorylation	PLLRELMYMGYKFEQ HHHHHHHHCCHHHHE		25690035
202	Phosphorylation	MCADKPGSSPDPSGE ECCCCCCCCCCCCCC		28348404
203	Phosphorylation	CADKPGSSPDPSGEV CCCCCCCCCCCCCCC		28348404
212	Phosphorylation	DPSGEVNTNVAFCSV CCCCCCCCCHHHHHH		-
262	Phosphorylation	KTSKEMHSPGQWRSF EECCCCCCCCCCHHH		26091039
270	Phosphorylation	PGQWRSFYRHKLLKW CCCCHHHHHHHHHHH		-
305	Phosphorylation	GFVSSLKTFPTMKMF CCHHHHCCCCCCHHH		24719451
314	Phosphorylation	PTMKMFEYVRNDRDG CCCHHHHHHHCCCCC		24719451
392	Phosphorylation	DLPSPPKTPSPK--- CCCCCCCCCCCC---		24719451
394	Phosphorylation	PSPPKTPSPK----- CCCCCCCCCC-----		-

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

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

Functions of PTM Sites

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

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
XRN2_HUMAN	XRN2	physical	15231747
DXO_HUMAN	DXO	physical	15231747
EXOSX_HUMAN	EXOSC10	physical	15231747
ANM6_HUMAN	PRMT6	physical	23455924
RECQ5_HUMAN	RECQL5	physical	26186194
RPAP2_HUMAN	RPAP2	physical	26186194
ARMC5_HUMAN	ARMC5	physical	26186194
RECQ5_HUMAN	RECQL5	physical	28514442
ARMC5_HUMAN	ARMC5	physical	28514442
MYZAP_HUMAN	POLR2M	physical	28514442
GRL1A_HUMAN	POLR2M	physical	28514442
GL1AD_HUMAN	POLR2M	physical	28514442
RPAP2_HUMAN	RPAP2	physical	28514442

Drug and Disease Associations

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