EXOS5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EXOS5_HUMAN
• UniProt AC: Q9NQT4
• Protein Name: Exosome complex component RRP46
• Gene Name: EXOSC5
• Organism: Homo sapiens (Human).
• Sequence Length: 235
• Subcellular Localization: Nucleus, nucleolus . Cytoplasm . 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..
• Protein Sequence: MEEETHTDAKIRAENGTGSSPRGPGCSLRHFACEQNLLSRPDGSASFLQGDTSVLAGVYGPAEVKVSKEIFNKATLEVILRPKIGLPGVAEKSRERLIRNTCEAVVLGTLHPRTSITVVLQVVSDAGSLLACCLNAACMALVDAGVPMRALFCGVACALDSDGTLVLDPTSKQEKEARAVLTFALDSVERKLLMSSTKGLYSDTELQQCLAAAQAASQHVFRFYRESLQRRYSKS

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
5	Phosphorylation	---MEEETHTDAKIR ---CCCCCCCCCCHH	33.10	26074081
7	Phosphorylation	-MEEETHTDAKIRAE -CCCCCCCCCCHHCC	45.10	26074081
10	Acetylation	EETHTDAKIRAENGT CCCCCCCCHHCCCCC	35.22	25953088
10	Ubiquitination	EETHTDAKIRAENGT CCCCCCCCHHCCCCC	35.22	24816145
17	Phosphorylation	KIRAENGTGSSPRGP CHHCCCCCCCCCCCC	45.53	30266825
19	Phosphorylation	RAENGTGSSPRGPGC HCCCCCCCCCCCCCC	36.69	23401153
20	Phosphorylation	AENGTGSSPRGPGCS CCCCCCCCCCCCCCC	21.69	30266825
27	Phosphorylation	SPRGPGCSLRHFACE CCCCCCCCHHHHHHH	34.06	24732914
52	Phosphorylation	ASFLQGDTSVLAGVY CHHHCCCCEEEEECC	27.79	23607784
53	Phosphorylation	SFLQGDTSVLAGVYG HHHCCCCEEEEECCC	21.63	23607784
59	Phosphorylation	TSVLAGVYGPAEVKV CEEEEECCCCCEEEE	19.24	23607784
65	Ubiquitination	VYGPAEVKVSKEIFN CCCCCEEEECHHHHC	32.09	32015554
68	Ubiquitination	PAEVKVSKEIFNKAT CCEEEECHHHHCCCC	58.79	33845483
68	Acetylation	PAEVKVSKEIFNKAT CCEEEECHHHHCCCC	58.79	23749302
92	Acetylation	GLPGVAEKSRERLIR CCCCCHHHHHHHHHH	45.11	25953088
92	Ubiquitination	GLPGVAEKSRERLIR CCCCCHHHHHHHHHH	45.11	27667366
102	Glutathionylation	ERLIRNTCEAVVLGT HHHHHHHHEEEEECC	3.45	22555962
187	Phosphorylation	VLTFALDSVERKLLM HHHHHHHHHHHHHHH	27.08	22210691
191	2-Hydroxyisobutyrylation	ALDSVERKLLMSSTK HHHHHHHHHHHHCCC	32.25	-
191	Ubiquitination	ALDSVERKLLMSSTK HHHHHHHHHHHHCCC	32.25	29967540
196	Phosphorylation	ERKLLMSSTKGLYSD HHHHHHHCCCCCCCH	21.85	22210691
197	Phosphorylation	RKLLMSSTKGLYSDT HHHHHHCCCCCCCHH	23.09	22210691

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

Oops, there are no upstream regulatory protein records of EXOS5_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EXOS5_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 EXOS5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SFPQ_HUMAN	SFPQ	physical	15231747
EXOS1_HUMAN	EXOSC1	physical	11812149
EXOS1_HUMAN	EXOSC1	physical	12419256
EXOS8_HUMAN	EXOSC8	physical	12419256
EXOSX_HUMAN	EXOSC10	physical	22939629
EXOS9_HUMAN	EXOSC9	physical	22939629
PSIP1_HUMAN	PSIP1	physical	22939629
AICDA_HUMAN	AICDA	physical	21255825
EXOS1_HUMAN	EXOSC1	physical	15231747
EXOS3_HUMAN	EXOSC3	physical	15231747
EXOSX_HUMAN	EXOSC10	physical	15231747
EXOS8_HUMAN	EXOSC8	physical	15231747
LSM5_HUMAN	LSM5	physical	15231747
LIPE_HUMAN	LIPG	physical	15231747
PA2G4_HUMAN	PA2G4	physical	15231747
PO210_HUMAN	NUP210	physical	15231747
KPYM_HUMAN	PKM	physical	15231747
ZN558_HUMAN	ZNF558	physical	15231747
CK5P1_HUMAN	CDK5RAP1	physical	15231747
RPAB5_HUMAN	POLR2L	physical	15231747
TRI54_HUMAN	TRIM54	physical	25416956
DOCK8_HUMAN	DOCK8	physical	25416956
EXOS1_HUMAN	EXOSC1	physical	26344197
EXOSX_HUMAN	EXOSC10	physical	26344197
EXOS3_HUMAN	EXOSC3	physical	26344197
EXOS6_HUMAN	EXOSC6	physical	26344197
EXOS8_HUMAN	EXOSC8	physical	26344197
MPH6_HUMAN	MPHOSPH6	physical	26344197
PSA1_HUMAN	PSMA1	physical	26344197
PSA2_HUMAN	PSMA2	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSA5_HUMAN	PSMA5	physical	26344197
PSA6_HUMAN	PSMA6	physical	26344197
TPIS_HUMAN	TPI1	physical	26344197
DECR_HUMAN	DECR1	physical	26496610
LRP4_HUMAN	LRP4	physical	26496610
ODO1_HUMAN	OGDH	physical	26496610
EXOS9_HUMAN	EXOSC9	physical	26496610
EXOSX_HUMAN	EXOSC10	physical	26496610
RS7_HUMAN	RPS7	physical	26496610
RS16_HUMAN	RPS16	physical	26496610
ZO2_HUMAN	TJP2	physical	26496610
MPH6_HUMAN	MPHOSPH6	physical	26496610
C1D_HUMAN	C1D	physical	26496610
TBL3_HUMAN	TBL3	physical	26496610
WDR3_HUMAN	WDR3	physical	26496610
EXOS8_HUMAN	EXOSC8	physical	26496610
EXOS7_HUMAN	EXOSC7	physical	26496610
EXOS2_HUMAN	EXOSC2	physical	26496610
SK2L2_HUMAN	SKIV2L2	physical	26496610
RL36_HUMAN	RPL36	physical	26496610
EXOS3_HUMAN	EXOSC3	physical	26496610
EXOS1_HUMAN	EXOSC1	physical	26496610
SCLY_HUMAN	SCLY	physical	26496610
EXOS4_HUMAN	EXOSC4	physical	26496610
GNL3L_HUMAN	GNL3L	physical	26496610
PAPD5_HUMAN	PAPD5	physical	26496610
RM41_HUMAN	MRPL41	physical	26496610
WDR75_HUMAN	WDR75	physical	26496610
DI3L1_HUMAN	DIS3L	physical	26496610
EXOS6_HUMAN	EXOSC6	physical	26496610

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.

Related Literatures of Post-Translational Modification

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20, AND MASSSPECTROMETRY.
PubMed: 17081983