EXOS6_HUMAN - dbPTM
EXOS6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOS6_HUMAN
UniProt AC Q5RKV6
Protein Name Exosome complex component MTR3
Gene Name EXOSC6
Organism Homo sapiens (Human).
Sequence Length 272
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..
Protein Sequence MPGDHRRIRGPEESQPPQLYAADEEEAPGTRDPTRLRPVYARAGLLSQAKGSAYLEAGGTKVLCAVSGPRQAEGGERGGGPAGAGGEAPAALRGRLLCDFRRAPFAGRRRRAPPGGCEERELALALQEALEPAVRLGRYPRAQLEVSALLLEDGGSALAAALTAAALALADAGVEMYDLVVGCGLSLAPGPAPTWLLDPTRLEEERAAAGLTVALMPVLNQVAGLLGSGEGGLTESWAEAVRLGLEGCQRLYPVLQQSLVRAARRRGAAAQP
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 Orthologous
Protein Cluster
20PhosphorylationESQPPQLYAADEEEA
CCCCCCCEECCCCCC
8.4227642862
40PhosphorylationPTRLRPVYARAGLLS
CCCCHHHHHHHCHHH
7.9528152594
50UbiquitinationAGLLSQAKGSAYLEA
HCHHHHHCCCEEEEE
45.8421906983
61UbiquitinationYLEAGGTKVLCAVSG
EEEECCEEEEEEECC
36.16-
77MethylationRQAEGGERGGGPAGA
CCCCCCCCCCCCCCC
52.94-
93MethylationGEAPAALRGRLLCDF
CCCCHHHCCCCHHCC
24.37-
252PhosphorylationLEGCQRLYPVLQQSL
HHHHHHHHHHHHHHH
8.0925599653
258PhosphorylationLYPVLQQSLVRAARR
HHHHHHHHHHHHHHH
18.8325599653

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 EXOS6_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOS6_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 EXOS6_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSB1_HUMANPSMB1physical
15231747
EXOS8_HUMANEXOSC8physical
12419256
EXOS7_HUMANEXOSC7physical
12419256
DJC30_HUMANDNAJC30physical
15231747
EXOS1_HUMANEXOSC1physical
12419256
EXOS7_HUMANEXOSC7physical
22939629
AICDA_HUMANAICDAphysical
21255825
EIF3I_HUMANEIF3Iphysical
15231747
EXOS7_HUMANEXOSC7physical
15231747
NDUAD_HUMANNDUFA13physical
15231747
GSE1_HUMANGSE1physical
15231747
C1QBP_HUMANC1QBPphysical
15231747
CPSF5_HUMANNUDT21physical
15231747
RBGPR_HUMANRAB3GAP2physical
15231747
SRSF3_HUMANSRSF3physical
15231747
ERR1_HUMANESRRAphysical
15231747
MI4GD_HUMANMIF4GDphysical
15231747
MOCS3_HUMANMOCS3physical
15231747
CHSS2_HUMANCHPFphysical
15231747
EFTU_HUMANTUFMphysical
15231747
RM04_HUMANMRPL4physical
15231747
MA2C1_HUMANMAN2C1physical
15231747
RT18B_HUMANMRPS18Bphysical
15231747
EXOS1_HUMANEXOSC1physical
15231747
EXOSX_HUMANEXOSC10physical
15231747
EXOS8_HUMANEXOSC8physical
15231747
EXOS6_HUMANEXOSC6physical
15231747
DCP1B_HUMANDCP1Bphysical
15231747
TTP_HUMANZFP36physical
15231747
SK2L2_HUMANSKIV2L2physical
15231747

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 EXOS6_HUMAN

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Related Literatures of Post-Translational Modification

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