EXOS8_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EXOS8_HUMAN
• UniProt AC: Q96B26
• Protein Name: Exosome complex component RRP43
• Gene Name: EXOSC8
• Organism: Homo sapiens (Human).
• Sequence Length: 276
• Subcellular Localization: Cytoplasm . Nucleus . Nucleus, nucleolus.
• Protein Description: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC8 binds to ARE-containing RNAs..
• Protein Sequence: MAAGFKTVEPLEYYRRFLKENCRPDGRELGEFRTTTVNIGSISTADGSALVKLGNTTVICGVKAEFAAPSTDAPDKGYVVPNVDLPPLCSSRFRSGPPGEEAQVASQFIADVIENSQIIQKEDLCISPGKLVWVLYCDLICLDYDGNILDACTFALLAALKNVQLPEVTINEETALAEVNLKKKSYLNIRTHPVATSFAVFDDTLLIVDPTGEEEHLATGTLTIVMDEEGKLCCLHKPGGSGLTGAKLQDCMSRAVTRHKEVKKLMDEVIKSMKPK

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
2	Acetylation	------MAAGFKTVE ------CCCCCCCCC	19.11	22814378
6	Ubiquitination	--MAAGFKTVEPLEY --CCCCCCCCCCHHH	51.23	23000965
6	Acetylation	--MAAGFKTVEPLEY --CCCCCCCCCCHHH	51.23	25953088
7	Phosphorylation	-MAAGFKTVEPLEYY -CCCCCCCCCCHHHH	28.04	24719451
13	Phosphorylation	KTVEPLEYYRRFLKE CCCCCHHHHHHHHHH	15.23	24114839
19	Acetylation	EYYRRFLKENCRPDG HHHHHHHHHHCCCCC	44.14	26822725
19	Ubiquitination	EYYRRFLKENCRPDG HHHHHHHHHHCCCCC	44.14	24816145
36	Phosphorylation	LGEFRTTTVNIGSIS CCEEEEEEEEECCCC	15.79	28985074
48	Phosphorylation	SISTADGSALVKLGN CCCCCCCCEEEEECC	20.98	28985074
127	Phosphorylation	QKEDLCISPGKLVWV EHHHCEECCCCEEEE	26.97	24719451
182	Ubiquitination	ALAEVNLKKKSYLNI EEEECCCCCCCCEEC	53.61	32015554
183	Ubiquitination	LAEVNLKKKSYLNIR EEECCCCCCCCEECC	50.55	-
184	Ubiquitination	AEVNLKKKSYLNIRT EECCCCCCCCEECCC	42.62	-
186	Phosphorylation	VNLKKKSYLNIRTHP CCCCCCCCEECCCCC	16.79	-
237	Ubiquitination	GKLCCLHKPGGSGLT CCEEEEECCCCCCCC	32.20	29967540
247	Ubiquitination	GSGLTGAKLQDCMSR CCCCCCHHHHHHHHH	48.29	29967540
271	Ubiquitination	KLMDEVIKSMKPK-- HHHHHHHHHCCCC--	50.07	32015554

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

Oops, there are no upstream regulatory protein records of EXOS8_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EXOS8_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 EXOS8_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EXOS5_HUMAN	EXOSC5	physical	12419256
EXOS6_HUMAN	EXOSC6	physical	12419256
AICDA_HUMAN	AICDA	physical	21255825
FHOD1_HUMAN	FHOD1	physical	15231747
RASF1_HUMAN	RASSF1	physical	15231747
MKRN1_HUMAN	MKRN1	physical	15231747
CWC22_HUMAN	CWC22	physical	15231747
FOXN3_HUMAN	FOXN3	physical	15231747
EXOS1_HUMAN	EXOSC1	physical	15231747
EXOS6_HUMAN	EXOSC6	physical	15231747
EXOS3_HUMAN	EXOSC3	physical	15231747
EXOS5_HUMAN	EXOSC5	physical	15231747
EXOSX_HUMAN	EXOSC10	physical	15231747
EXOS8_HUMAN	EXOSC8	physical	15231747
TTP_HUMAN	ZFP36	physical	15231747
EXOS8_HUMAN	EXOSC8	physical	25416956
OTUD4_HUMAN	OTUD4	physical	25416956
DUS23_HUMAN	DUSP23	physical	25416956
F90A1_HUMAN	FAM90A1	physical	25416956
EXOS5_HUMAN	EXOSC5	physical	25416956
AEN_HUMAN	AEN	physical	25416956
TXD17_HUMAN	TXNDC17	physical	25416956
CONA1_HUMAN	COL23A1	physical	25416956
MORN4_HUMAN	MORN4	physical	25416956
EXOSX_HUMAN	EXOSC10	physical	26186194
MPH6_HUMAN	MPHOSPH6	physical	26186194
SK2L2_HUMAN	SKIV2L2	physical	26186194
EXOS4_HUMAN	EXOSC4	physical	26186194
HBS1L_HUMAN	HBS1L	physical	26186194
EXOS9_HUMAN	EXOSC9	physical	26186194
DI3L1_HUMAN	DIS3L	physical	26186194
EXOS5_HUMAN	EXOSC5	physical	26186194
ZCHC8_HUMAN	ZCCHC8	physical	26186194
EXOS2_HUMAN	EXOSC2	physical	26186194
EXOS1_HUMAN	EXOSC1	physical	26186194
C1D_HUMAN	C1D	physical	26186194
PAXI_HUMAN	PXN	physical	26186194
RBM7_HUMAN	RBM7	physical	26186194
EXOS1_HUMAN	EXOSC1	physical	26344197
EXOSX_HUMAN	EXOSC10	physical	26344197
EXOS2_HUMAN	EXOSC2	physical	26344197
MPH6_HUMAN	MPHOSPH6	physical	26344197
EXOS5_HUMAN	EXOSC5	physical	21516116
RSMB_HUMAN	SNRPB	physical	21516116
DI3L1_HUMAN	DIS3L	physical	28514442
MPH6_HUMAN	MPHOSPH6	physical	28514442
EXOSX_HUMAN	EXOSC10	physical	28514442
PAXI_HUMAN	PXN	physical	28514442
RBM7_HUMAN	RBM7	physical	28514442
EXOS2_HUMAN	EXOSC2	physical	28514442
HBS1L_HUMAN	HBS1L	physical	28514442
EXOS5_HUMAN	EXOSC5	physical	28514442
ZCHC8_HUMAN	ZCCHC8	physical	28514442
EXOS4_HUMAN	EXOSC4	physical	28514442
EXOS9_HUMAN	EXOSC9	physical	28514442

Drug and Disease Associations

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