EXOS3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EXOS3_HUMAN
• UniProt AC: Q9NQT5
• Protein Name: Exosome complex component RRP40
• Gene Name: EXOSC3
• Organism: Homo sapiens (Human).
• Sequence Length: 275
• Subcellular Localization: Cytoplasm . Nucleus, nucleolus . Nucleus .
• 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. EXOSC3 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC9 and EXOSC5..
• Protein Sequence: MAEPASVAAESLAGSRARAARTVLGQVVLPGEELLLPEQEDAEGPGGAVERPLSLNARACSRVRVVCGPGLRRCGDRLLVTKCGRLRHKEPGSGSGGGVYWVDSQQKRYVPVKGDHVIGIVTAKSGDIFKVDVGGSEPASLSYLSFEGATKRNRPNVQVGDLIYGQFVVANKDMEPEMVCIDSCGRANGMGVIGQDGLLFKVTLGLIRKLLAPDCEIIQEVGKLYPLEIVFGMNGRIWVKAKTIQQTLILANILEACEHMTSDQRKQIFSRLAES

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	------MAEPASVAA ------CCCCHHHHH	31.32	22223895
6	Phosphorylation	--MAEPASVAAESLA --CCCCHHHHHHHHH	24.01	23186163
11	Phosphorylation	PASVAAESLAGSRAR CHHHHHHHHHHHHHH	20.84	30108239
15	Phosphorylation	AAESLAGSRARAART HHHHHHHHHHHHHHH	19.70	23186163
82	Acetylation	GDRLLVTKCGRLRHK CCEEEEEECCEECCC	27.49	25953088
82	Ubiquitination	GDRLLVTKCGRLRHK CCEEEEEECCEECCC	27.49	-
82	2-Hydroxyisobutyrylation	GDRLLVTKCGRLRHK CCEEEEEECCEECCC	27.49	-
89	Ubiquitination	KCGRLRHKEPGSGSG ECCEECCCCCCCCCC	60.20	-
107	Ubiquitination	YWVDSQQKRYVPVKG EEECCCCCEEECCCC	37.75	-
109	Phosphorylation	VDSQQKRYVPVKGDH ECCCCCEEECCCCCE	19.01	29496907
113	Ubiquitination	QKRYVPVKGDHVIGI CCEEECCCCCEEEEE	53.18	21890473
113	Ubiquitination	QKRYVPVKGDHVIGI CCEEECCCCCEEEEE	53.18	21890473
113	Ubiquitination	QKRYVPVKGDHVIGI CCEEECCCCCEEEEE	53.18	21890473
124	Ubiquitination	VIGIVTAKSGDIFKV EEEEEEECCCCEEEE	45.68	-
124	Acetylation	VIGIVTAKSGDIFKV EEEEEEECCCCEEEE	45.68	25953088
130	Acetylation	AKSGDIFKVDVGGSE ECCCCEEEEEECCCC	37.55	26051181
151	Ubiquitination	LSFEGATKRNRPNVQ EEECCCCCCCCCCCE	47.33	21890473
151	Acetylation	LSFEGATKRNRPNVQ EEECCCCCCCCCCCE	47.33	25953088
151	Sumoylation	LSFEGATKRNRPNVQ EEECCCCCCCCCCCE	47.33	28112733
161 (in isoform 2)	Phosphorylation	-	30.91	-
161	Phosphorylation	RPNVQVGDLIYGQFV CCCCEECCEECCEEE	30.91	-
162 (in isoform 2)	Phosphorylation	-	2.40	-
162	Phosphorylation	PNVQVGDLIYGQFVV CCCEECCEECCEEEE	2.40	-
209	Ubiquitination	VTLGLIRKLLAPDCE HHHHHHHHHHCCCCH	40.64	-

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

Oops, there are no upstream regulatory protein records of EXOS3_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EXOS3_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 EXOS3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EXOS5_HUMAN	EXOSC5	physical	12419256
EXOS1_HUMAN	EXOSC1	physical	20531389
EXOS2_HUMAN	EXOSC2	physical	20531389
EXOS3_HUMAN	EXOSC3	physical	20531389
EXOS4_HUMAN	EXOSC4	physical	20531389
EXOS5_HUMAN	EXOSC5	physical	20531389
EXOS6_HUMAN	EXOSC6	physical	20531389
EXOS7_HUMAN	EXOSC7	physical	20531389
EXOS8_HUMAN	EXOSC8	physical	20531389
EXOS9_HUMAN	EXOSC9	physical	20531389
EXOSX_HUMAN	EXOSC10	physical	20531389
MPH6_HUMAN	MPHOSPH6	physical	20531389
DI3L1_HUMAN	DIS3L	physical	20531389
RRP44_HUMAN	DIS3	physical	20531389
A4_HUMAN	APP	physical	21832049
EXOS5_HUMAN	EXOSC5	physical	22939629
EXOS9_HUMAN	EXOSC9	physical	22939629
EXOS4_HUMAN	EXOSC4	physical	22939629
EXOSX_HUMAN	EXOSC10	physical	22939629
AICDA_HUMAN	AICDA	physical	21255825
EXOS5_HUMAN	EXOSC5	physical	15231747
CK5P1_HUMAN	CDK5RAP1	physical	15231747
ATPD_HUMAN	ATP5D	physical	15231747
EXOS8_HUMAN	EXOSC8	physical	15231747
EXOSX_HUMAN	EXOSC10	physical	26186194
SK2L2_HUMAN	SKIV2L2	physical	26186194
EXOS7_HUMAN	EXOSC7	physical	26186194
MPH6_HUMAN	MPHOSPH6	physical	26186194
EXOS8_HUMAN	EXOSC8	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
AF9_HUMAN	MLLT3	physical	26186194
ZCHC8_HUMAN	ZCCHC8	physical	26186194
EXOS2_HUMAN	EXOSC2	physical	26186194
EXOS1_HUMAN	EXOSC1	physical	26186194
C1D_HUMAN	C1D	physical	26186194
RBM7_HUMAN	RBM7	physical	26186194
EXOS6_HUMAN	EXOSC6	physical	26186194
C43BP_HUMAN	COL4A3BP	physical	26186194
EXOS1_HUMAN	EXOSC1	physical	26344197
EXOS6_HUMAN	EXOSC6	physical	26344197
DI3L1_HUMAN	DIS3L	physical	28514442
EXOS7_HUMAN	EXOSC7	physical	28514442
EXOS8_HUMAN	EXOSC8	physical	28514442
EXOSX_HUMAN	EXOSC10	physical	28514442
HBS1L_HUMAN	HBS1L	physical	28514442
MPH6_HUMAN	MPHOSPH6	physical	28514442
RBM7_HUMAN	RBM7	physical	28514442
EXOS5_HUMAN	EXOSC5	physical	28514442
EXOS2_HUMAN	EXOSC2	physical	28514442
AF9_HUMAN	MLLT3	physical	28514442
ZCHC8_HUMAN	ZCCHC8	physical	28514442
EXOS4_HUMAN	EXOSC4	physical	28514442
C43BP_HUMAN	COL4A3BP	physical	28514442
EXOS9_HUMAN	EXOSC9	physical	28514442
EXOS6_HUMAN	EXOSC6	physical	28514442
SK2L2_HUMAN	SKIV2L2	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• 614678: Pontocerebellar hypoplasia 1B (PCH1B)
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330