dbPTM

EXOS4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EXOS4_HUMAN
UniProt AC	Q9NPD3
Protein Name	Exosome complex component RRP41
Gene Name	EXOSC4
Organism	Homo sapiens (Human).
Sequence Length	245
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. EXOSC4 binds to ARE-containing RNAs..
Protein Sequence	MAGLELLSDQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRARALPDRALVNCQYSSATFSTGERKRRPHGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFVDGTALADLSHVEEAAGGPQLALALLPASGQIALLEMDARLHEDHLERVLEAAAQAARDVHTLLDRVVRQHVREASILLGD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAGLELLSD ------CCCCCCCCC	31.14	22223895
12	Nitration	ELLSDQGYRVDGRRA CCCCCCCCEECCCCH	11.22	-
53	Phosphorylation	TKALAVVYGPHEIRG EEEEEEEECHHHHCC	20.52	23186163
61	Phosphorylation	GPHEIRGSRARALPD CHHHHCCCCCCCCCC	16.96	23312004
76	Phosphorylation	RALVNCQYSSATFST CEEEECEECCCEECC	13.54	28152594
77	Phosphorylation	ALVNCQYSSATFSTG EEEECEECCCEECCC	6.39	28152594
78	Phosphorylation	LVNCQYSSATFSTGE EEECEECCCEECCCC	26.79	28152594
80	Phosphorylation	NCQYSSATFSTGERK ECEECCCEECCCCCC	21.77	28152594
82	Phosphorylation	QYSSATFSTGERKRR EECCCEECCCCCCCC	31.02	27732954
83	Phosphorylation	YSSATFSTGERKRRP ECCCEECCCCCCCCC	38.58	27732954
95	Ubiquitination	RRPHGDRKSCEMGLQ CCCCCCHHHHHHHHH	65.28	23000965
95	Malonylation	RRPHGDRKSCEMGLQ CCCCCCHHHHHHHHH	65.28	26320211
96	Phosphorylation	RPHGDRKSCEMGLQL CCCCCHHHHHHHHHH	19.06	30108239
99	Sulfoxidation	GDRKSCEMGLQLRQT CCHHHHHHHHHHHHH	8.34	21406390
230	Methylation	DVHTLLDRVVRQHVR HHHHHHHHHHHHHHH	28.88	-
240	Phosphorylation	RQHVREASILLGD-- HHHHHHHHHHCCC--	14.71	28348404

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 EXOS4_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EXOS4_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 EXOS4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EF1A1_HUMAN	EEF1A1	physical	15231747
EXOS2_HUMAN	EXOSC2	physical	12419256
EXOS4_HUMAN	EXOSC4	physical	12419256
EXOS7_HUMAN	EXOSC7	physical	20531386
EXOS9_HUMAN	EXOSC9	physical	20531386
EXOS3_HUMAN	EXOSC3	physical	20531386
EXOS5_HUMAN	EXOSC5	physical	20531386
EXOS8_HUMAN	EXOSC8	physical	20531386
EXOS1_HUMAN	EXOSC1	physical	20531386
EXOS2_HUMAN	EXOSC2	physical	20531386
SK2L2_HUMAN	SKIV2L2	physical	20531386
EXOSX_HUMAN	EXOSC10	physical	20531386
EXOS6_HUMAN	EXOSC6	physical	20531386
DI3L1_HUMAN	DIS3L	physical	20531386
EXOS7_HUMAN	EXOSC7	physical	22939629
EXOS9_HUMAN	EXOSC9	physical	22939629
EXOSX_HUMAN	EXOSC10	physical	22939629
EXOS8_HUMAN	EXOSC8	physical	22939629
EXOS5_HUMAN	EXOSC5	physical	22939629
PSIP1_HUMAN	PSIP1	physical	22939629
AICDA_HUMAN	AICDA	physical	21255825
EXOS9_HUMAN	EXOSC9	physical	15231747
NSMA3_HUMAN	SMPD4	physical	15231747
SEN15_HUMAN	TSEN15	physical	15231747
FAHD1_HUMAN	FAHD1	physical	15231747
NEK1_HUMAN	NEK1	physical	15231747
AK1A1_HUMAN	AKR1A1	physical	15231747
GT2D1_HUMAN	GTF2IRD1	physical	15231747
LRC8D_HUMAN	LRRC8D	physical	15231747
MPZL1_HUMAN	MPZL1	physical	15231747
G45IP_HUMAN	GADD45GIP1	physical	15231747
EXOS3_HUMAN	EXOSC3	physical	15231747
DXO_HUMAN	DXO	physical	15231747
SKIV2_HUMAN	SKIV2L	physical	15231747
EXOSX_HUMAN	EXOSC10	physical	15231747
NMI_HUMAN	NMI	physical	22863883
TOM1_HUMAN	TOM1	physical	22863883
EXOSX_HUMAN	EXOSC10	physical	26344197
EXOS2_HUMAN	EXOSC2	physical	26344197
EXOS3_HUMAN	EXOSC3	physical	26344197
EXOS5_HUMAN	EXOSC5	physical	26344197
EXOS6_HUMAN	EXOSC6	physical	26344197
EXOS7_HUMAN	EXOSC7	physical	26344197
TTC37_HUMAN	TTC37	physical	26344197
DSRAD_HUMAN	ADAR	physical	26496610
ETFA_HUMAN	ETFA	physical	26496610
ROA1_HUMAN	HNRNPA1	physical	26496610
HNRPU_HUMAN	HNRNPU	physical	26496610
DNLI3_HUMAN	LIG3	physical	26496610
MECP2_HUMAN	MECP2	physical	26496610
PHF1_HUMAN	PHF1	physical	26496610
EXOS9_HUMAN	EXOSC9	physical	26496610
EXOSX_HUMAN	EXOSC10	physical	26496610
RL13_HUMAN	RPL13	physical	26496610
RL18A_HUMAN	RPL18A	physical	26496610
RL37A_HUMAN	RPL37A	physical	26496610
RS3_HUMAN	RPS3	physical	26496610
RS4X_HUMAN	RPS4X	physical	26496610
RS10_HUMAN	RPS10	physical	26496610
RS29_HUMAN	RPS29	physical	26496610
EI2BD_HUMAN	EIF2B4	physical	26496610
IF2B_HUMAN	EIF2S2	physical	26496610
MED17_HUMAN	MED17	physical	26496610
MPH6_HUMAN	MPHOSPH6	physical	26496610
NS1BP_HUMAN	IVNS1ABP	physical	26496610
EXOS8_HUMAN	EXOSC8	physical	26496610
EXOS7_HUMAN	EXOSC7	physical	26496610
EXOS2_HUMAN	EXOSC2	physical	26496610
EXOS3_HUMAN	EXOSC3	physical	26496610
EXOS1_HUMAN	EXOSC1	physical	26496610
RM48_HUMAN	MRPL48	physical	26496610
GAR1_HUMAN	GAR1	physical	26496610
SHQ1_HUMAN	SHQ1	physical	26496610
LRC59_HUMAN	LRRC59	physical	26496610
EXOS5_HUMAN	EXOSC5	physical	26496610
SAS10_HUMAN	UTP3	physical	26496610
WDR18_HUMAN	WDR18	physical	26496610
TXD16_HUMAN	TXNDC16	physical	26496610
SPA5L_HUMAN	SPATA5L1	physical	26496610
LYRIC_HUMAN	MTDH	physical	26496610
DI3L1_HUMAN	DIS3L	physical	26496610
EXOS6_HUMAN	EXOSC6	physical	26496610
CHAP1_HUMAN	CHAMP1	physical	26496610
DHYS_HUMAN	DHPS	physical	27173435
LUM_HUMAN	LUM	physical	27173435
RSRC1_HUMAN	RSRC1	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 EXOS4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.	19413330 [Abstract]