Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Exosome complex component RRP41  

UniProtKB / Swiss-Prot ID :  EXOS4_HUMAN

Gene Name (Synonyms) : 
EXOSC4, RRP41, SKI6  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus, nucleolus. Nucleus. 

Protein Function :  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 MAGLELLSDQGYRVDGRRAGELRKIQARMGVFAQADGSAYIEQGNTKALAVVYGPHEIRGSRARALPDRA...
Predicted Secondary Structure CCCCEEEECCCCCCCCCCCCCEEEEEEEECCCCCCCCEEEEEECCEEEEEEEEECCCCCCCCCCCCCCEE...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MAGLEL
---CCCCEE
31.14UniProtKB
Link-
240PhosphoserineVREASILLG
HHCCCHHHC
14.71Phosphositeplus
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
EXOS2_HUMANphysical interaction
physical interaction
EBI-371832
EBI-371837
intact12419256
12419256
EXOSX_HUMANphysical interactionEBI-374271
intact15231747
EXOS3_HUMANphysical interactionEBI-374274
intact15231747
DOM3Z_HUMANphysical interactionEBI-374277
intact15231747
SKIV2_HUMANphysical interactionEBI-374280
intact15231747
NSMA3_HUMANphysical interactionEBI-373650
intact15231747
EXOS9_HUMANphysical interactionEBI-373647
intact15231747
SEN15_HUMANphysical interactionEBI-373653
intact15231747
FAHD1_HUMANphysical interactionEBI-373656
intact15231747
NEK1_HUMANphysical interactionEBI-373659
intact15231747
AK1A1_HUMANphysical interactionEBI-373662
intact15231747
GT2D1_HUMANphysical interactionEBI-373665
intact15231747
LRC8D_HUMANphysical interactionEBI-373668
intact15231747
Q8WUP4_HUMANphysical interactionEBI-373671
intact15231747
G45IP_HUMANphysical interactionEBI-373674
intact15231747
EF1A1_HUMANphysical interactionEBI-373677
intact15231747
AK1A1_HUMANyeast 2-hybridHPRD:16221HPRD15231747
EF1A1_HUMANyeast 2-hybridHPRD:16221HPRD15231747
REN3B_HUMANin vitro
in vivo
HPRD:16221HPRD14527413
SKIV2_HUMANyeast 2-hybridHPRD:16221HPRD15231747
RENT1_HUMANin vitro
in vivo
HPRD:16221HPRD14527413
MPZL1_HUMANyeast 2-hybridHPRD:16221HPRD15231747
EXOS2_HUMANin vitro
in vivo
yeast 2-hybrid
HPRD:16221HPRD12419256
11719186
EXOS4_HUMANyeast 2-hybridHPRD:16221HPRD12419256
GT2D1_HUMANyeast 2-hybridHPRD:16221HPRD15231747
RENT2_HUMANin vitro
in vivo
HPRD:16221HPRD14527413
LRC8D_HUMANyeast 2-hybridHPRD:16221HPRD15231747
G45IP_HUMANyeast 2-hybridHPRD:16221HPRD15231747
NEK1_HUMANyeast 2-hybridHPRD:16221HPRD15231747
NSMA3_HUMANyeast 2-hybridHPRD:16221HPRD15231747
EXOSX_HUMANyeast 2-hybridHPRD:16221HPRD15231747
DOM3Z_HUMANyeast 2-hybridHPRD:16221HPRD15231747
HNRPD_HUMANyeast 2-hybridHPRD:16221HPRD15231747
EXOS8_HUMANENSP00000315476STRING
EXOS9_HUMANENSP00000315476STRING
EXOS7_HUMANENSP00000315476STRING
GT2D1_HUMANENSP00000315476STRING
EXOS3_HUMANENSP00000315476STRING
DOM3Z_HUMANENSP00000315476STRING
MPZL1_HUMANENSP00000315476STRING
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures