dbPTM

EXOS2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EXOS2_HUMAN
UniProt AC	Q13868
Protein Name	Exosome complex component RRP4
Gene Name	EXOSC2
Organism	Homo sapiens (Human).
Sequence Length	293
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. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7..
Protein Sequence	MAMEMRLPVARKPLSERLGRDTKKHLVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVERVNKLICVKALKTRYIGEVGDIVVGRITEVQQKRWKVETNSRLDSVLLLSSMNLPGGELRRRSAEDELAMRGFLQEGDLISAEVQAVFSDGAVSLHTRSLKYGKLGQGVLVQVSPSLVKRQKTHFHDLPCGASVILGNNGFIWIYPTPEHKEEEAGGFIANLEPVSLADREVISRLRNCIISLVTQRMMLYDTSILYCYEASLPHQIKDILKPEIMEEIVMETRQRLLEQEG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
15	Phosphorylation	PVARKPLSERLGRDT CCCCCCHHHHHCCCC	29.24	20068231
24	Ubiquitination	RLGRDTKKHLVVPGD HHCCCCCCCEEECCC	44.24	-
32	Phosphorylation	HLVVPGDTITTDTGF CEEECCCEEECCCCC	26.58	22817900
37	Phosphorylation	GDTITTDTGFMRGHG CCEEECCCCCCCCCC	30.17	22817900
41	Methylation	TTDTGFMRGHGTYMG ECCCCCCCCCCCCCC	31.53	115492941
45	Phosphorylation	GFMRGHGTYMGEEKL CCCCCCCCCCCCHHH	12.50	22817900
46	Phosphorylation	FMRGHGTYMGEEKLI CCCCCCCCCCCHHHH	14.02	22817900
51	Ubiquitination	GTYMGEEKLIASVAG CCCCCCHHHHHHHHC	40.67	-
55	Phosphorylation	GEEKLIASVAGSVER CCHHHHHHHHCCHHH	12.90	23532336
59	Phosphorylation	LIASVAGSVERVNKL HHHHHHCCHHHHHHH	15.86	25003641
65	Acetylation	GSVERVNKLICVKAL CCHHHHHHHHHHHHC	36.05	25953088
65	Ubiquitination	GSVERVNKLICVKAL CCHHHHHHHHHHHHC	36.05	-
68	S-nitrosylation	ERVNKLICVKALKTR HHHHHHHHHHHCCCE	3.58	19483679
68	S-nitrosocysteine	ERVNKLICVKALKTR HHHHHHHHHHHCCCE	3.58	-
70	2-Hydroxyisobutyrylation	VNKLICVKALKTRYI HHHHHHHHHCCCEEC	43.52	-
70	Acetylation	VNKLICVKALKTRYI HHHHHHHHHCCCEEC	43.52	25953088
70	Ubiquitination	VNKLICVKALKTRYI HHHHHHHHHCCCEEC	43.52	-
94	2-Hydroxyisobutyrylation	RITEVQQKRWKVETN EHHHHHHHCCCCCCC	43.04	-
94 (in isoform 3)	Phosphorylation	-	43.04	28731282
94	Acetylation	RITEVQQKRWKVETN EHHHHHHHCCCCCCC	43.04	25953088
94	Ubiquitination	RITEVQQKRWKVETN EHHHHHHHCCCCCCC	43.04	-
97	Ubiquitination	EVQQKRWKVETNSRL HHHHHCCCCCCCCCH	33.94	-
97	Acetylation	EVQQKRWKVETNSRL HHHHHCCCCCCCCCH	33.94	26051181
106	Phosphorylation	ETNSRLDSVLLLSSM CCCCCHHHHHHHHHC	21.18	23612710
111	Phosphorylation	LDSVLLLSSMNLPGG HHHHHHHHHCCCCCC	27.75	22496350
112	Phosphorylation	DSVLLLSSMNLPGGE HHHHHHHHCCCCCCH	16.20	22496350
124	Phosphorylation	GGELRRRSAEDELAM CCHHCCCCHHHHHHH	33.91	29255136
131	Sulfoxidation	SAEDELAMRGFLQEG CHHHHHHHHHHCCCC	7.23	21406390
135	Ubiquitination	ELAMRGFLQEGDLIS HHHHHHHCCCCCEEE	5.16	-
150	Ubiquitination	AEVQAVFSDGAVSLH EEEEEHHCCCCEEEE	28.65	-
165	Ubiquitination	TRSLKYGKLGQGVLV ECEECCCCCCCCEEE	46.48	-
165	Acetylation	TRSLKYGKLGQGVLV ECEECCCCCCCCEEE	46.48	-
175	Phosphorylation	QGVLVQVSPSLVKRQ CCEEEEECHHHHHCC	7.53	25159151
177	Phosphorylation	VLVQVSPSLVKRQKT EEEEECHHHHHCCCC	37.98	19413330
180	Ubiquitination	QVSPSLVKRQKTHFH EECHHHHHCCCCCCC	55.17	21906983
243	Phosphorylation	RLRNCIISLVTQRMM HHHHHHHHHHHHHHH	9.25	21712546
258	Phosphorylation	LYDTSILYCYEASLP HHCCHHHHHHHCCCC	7.42	29496907
260	Phosphorylation	DTSILYCYEASLPHQ CCHHHHHHHCCCCHH	10.85	29496907
269	Ubiquitination	ASLPHQIKDILKPEI CCCCHHHHHHHCHHH	31.95	-
273	Ubiquitination	HQIKDILKPEIMEEI HHHHHHHCHHHHHHH	40.72	-

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
Oops, there are no upstream regulatory protein records of EXOS2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EXOS2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of EXOS2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EXOS4_HUMAN	EXOSC4	physical	12419256
EXOS7_HUMAN	EXOSC7	physical	12419256
EXOS4_HUMAN	EXOSC4	physical	22939629
EXOS5_HUMAN	EXOSC5	physical	22939629
EXOS9_HUMAN	EXOSC9	physical	22939629
EXOS3_HUMAN	EXOSC3	physical	22939629
RAN_HUMAN	RAN	physical	22939629
AICDA_HUMAN	AICDA	physical	21255825
EXOS7_HUMAN	EXOSC7	physical	15231747
ZN408_HUMAN	ZNF408	physical	15231747
RNF8_HUMAN	RNF8	physical	15231747
GLT13_HUMAN	GALNT13	physical	15231747
SIA7A_HUMAN	ST6GALNAC1	physical	15231747
RM48_HUMAN	MRPL48	physical	15231747
RRP44_HUMAN	DIS3	physical	26344197
EXOSX_HUMAN	EXOSC10	physical	26344197
EXOS3_HUMAN	EXOSC3	physical	26344197
EXOS5_HUMAN	EXOSC5	physical	26344197
EXOS6_HUMAN	EXOSC6	physical	26344197
NUCL_HUMAN	NCL	physical	26496610
PEX1_HUMAN	PEX1	physical	26496610
EXOS9_HUMAN	EXOSC9	physical	26496610
EXOSX_HUMAN	EXOSC10	physical	26496610
PRC2A_HUMAN	PRRC2A	physical	26496610
PRC1_HUMAN	PRC1	physical	26496610
WDR46_HUMAN	WDR46	physical	26496610
MPH6_HUMAN	MPHOSPH6	physical	26496610
EXOS8_HUMAN	EXOSC8	physical	26496610
EXOS7_HUMAN	EXOSC7	physical	26496610
FBXL4_HUMAN	FBXL4	physical	26496610
EXOS3_HUMAN	EXOSC3	physical	26496610
EXOS1_HUMAN	EXOSC1	physical	26496610
NT5D3_HUMAN	NT5DC3	physical	26496610
EXOS4_HUMAN	EXOSC4	physical	26496610
ASXL2_HUMAN	ASXL2	physical	26496610
PLXA3_HUMAN	PLXNA3	physical	26496610
EXOS5_HUMAN	EXOSC5	physical	26496610
MASU1_HUMAN	MALSU1	physical	26496610
DI3L1_HUMAN	DIS3L	physical	26496610
EXOS6_HUMAN	EXOSC6	physical	26496610
PTGR2_HUMAN	PTGR2	physical	26496610
EXOS4_HUMAN	EXOSC4	physical	27173435
EXOS7_HUMAN	EXOSC7	physical	27173435
LUM_HUMAN	LUM	physical	27173435
RSRC1_HUMAN	RSRC1	physical	27173435
DHYS_HUMAN	DHPS	physical	27173435

Drug and Disease Associations

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

Regulatory Network of EXOS2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-165, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175 AND SER-177, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32; THR-37; THR-45 ANDTYR-46, AND MASS SPECTROMETRY.	18187866 [Abstract]