EXOS7_HUMAN - dbPTM
EXOS7_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOS7_HUMAN
UniProt AC Q15024
Protein Name Exosome complex component RRP42
Gene Name EXOSC7
Organism Homo sapiens (Human).
Sequence Length 291
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 MASVTLSEAEKVYIVHGVQEDLRVDGRGCEDYRCVEVETDVVSNTSGSARVKLGHTDILVGVKAEMGTPKLEKPNEGYLEFFVDCSASATPEFEGRGGDDLGTEIANTLYRIFNNKSSVDLKTLCISPREHCWVLYVDVLLLECGGNLFDAISIAVKAALFNTRIPRVRVLEDEEGSKDIELSDDPYDCIRLSVENVPCIVTLCKIGYRHVVDATLQEEACSLASLLVSVTSKGVVTCMRKVGKGSLDPESIFEMMETGKRVGKVLHASLQSVVHKEESLGPKRQKVGFLG
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
2Acetylation------MASVTLSEA
------CCCEECCCC		16.8322223895
3Phosphorylation-----MASVTLSEAE
-----CCCEECCCCE		17.8420068231
5Phosphorylation---MASVTLSEAEKV
---CCCEECCCCEEE		23.2820068231
7Phosphorylation-MASVTLSEAEKVYI
-CCCEECCCCEEEEE		25.9520068231
11UbiquitinationVTLSEAEKVYIVHGV
EECCCCEEEEEEECC		47.59-
52UbiquitinationTSGSARVKLGHTDIL
CCCCCEEEECCCCEE		43.10-
56PhosphorylationARVKLGHTDILVGVK
CEEEECCCCEEEEEE		23.9622210691
63UbiquitinationTDILVGVKAEMGTPK
CCEEEEEEECCCCCC		32.47-
68PhosphorylationGVKAEMGTPKLEKPN
EEEECCCCCCCCCCC		18.8829514088
1162-HydroxyisobutyrylationLYRIFNNKSSVDLKT
HHHHHCCCCCCCCEE		45.25-
116UbiquitinationLYRIFNNKSSVDLKT
HHHHHCCCCCCCCEE		45.2519608861
116AcetylationLYRIFNNKSSVDLKT
HHHHHCCCCCCCCEE		45.2519608861
117PhosphorylationYRIFNNKSSVDLKTL
HHHHCCCCCCCCEEE		37.4023403867
118PhosphorylationRIFNNKSSVDLKTLC
HHHCCCCCCCCEEEE		22.6623403867
122AcetylationNKSSVDLKTLCISPR
CCCCCCCEEEEECCC		34.6826051181
122UbiquitinationNKSSVDLKTLCISPR
CCCCCCCEEEEECCC		34.68-
177PhosphorylationVLEDEEGSKDIELSD
EEECCCCCCCEECCC		30.3630266825
178UbiquitinationLEDEEGSKDIELSDD
EECCCCCCCEECCCC		73.84-
178AcetylationLEDEEGSKDIELSDD
EECCCCCCCEECCCC		73.8426051181
183PhosphorylationGSKDIELSDDPYDCI
CCCCEECCCCHHCEE		27.4630266825
187PhosphorylationIELSDDPYDCIRLSV
EECCCCHHCEEEEEE		30.3727642862
193PhosphorylationPYDCIRLSVENVPCI
HHCEEEEEECCCCEE		19.96-
202PhosphorylationENVPCIVTLCKIGYR
CCCCEEEEEECCCHH		13.41-
205UbiquitinationPCIVTLCKIGYRHVV
CEEEEEECCCHHHHC		42.13-
205AcetylationPCIVTLCKIGYRHVV
CEEEEEECCCHHHHC		42.1326051181
244UbiquitinationTCMRKVGKGSLDPES
HEHHEECCCCCCHHH		48.60-
246PhosphorylationMRKVGKGSLDPESIF
HHEECCCCCCHHHHH		32.8420068231
251PhosphorylationKGSLDPESIFEMMET
CCCCCHHHHHHHHHH		37.6620068231
258PhosphorylationSIFEMMETGKRVGKV
HHHHHHHHCCCHHHH		30.0620068231
260UbiquitinationFEMMETGKRVGKVLH
HHHHHHCCCHHHHHH		51.86-
260AcetylationFEMMETGKRVGKVLH
HHHHHHCCCHHHHHH		51.8626051181
264UbiquitinationETGKRVGKVLHASLQ
HHCCCHHHHHHHHHH		38.47-
276UbiquitinationSLQSVVHKEESLGPK
HHHHHHHCHHHCCCC		52.1221890473
283UbiquitinationKEESLGPKRQKVGFL
CHHHCCCCCCCCCCC		66.71-
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 EXOS7_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOS7_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 EXOS7_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOS1_HUMANEXOSC1physical
11812149
EXOS2_HUMANEXOSC2physical
12419256
EXOS4_HUMANEXOSC4physical
12419256
EXOS1_HUMANEXOSC1physical
12419256
EXOS6_HUMANEXOSC6physical
12419256
A4_HUMANAPPphysical
21832049
AICDA_HUMANAICDAphysical
21255825
EXOS2_HUMANEXOSC2physical
15231747
EXOSX_HUMANEXOSC10physical
15231747
DXO_HUMANDXOphysical
15231747
EXOSX_HUMANEXOSC10physical
26186194
MPH6_HUMANMPHOSPH6physical
26186194
EXOS8_HUMANEXOSC8physical
26186194
SK2L2_HUMANSKIV2L2physical
26186194
EXOS4_HUMANEXOSC4physical
26186194
HBS1L_HUMANHBS1Lphysical
26186194
EXOS9_HUMANEXOSC9physical
26186194
DI3L1_HUMANDIS3Lphysical
26186194
EXOS5_HUMANEXOSC5physical
26186194
ZCHC8_HUMANZCCHC8physical
26186194
EXOS2_HUMANEXOSC2physical
26186194
EXOS1_HUMANEXOSC1physical
26186194
ZC3H1_HUMANZFC3H1physical
26186194
C1D_HUMANC1Dphysical
26186194
EXOS6_HUMANEXOSC6physical
26186194
UBP30_HUMANUSP30physical
26186194
GGYF2_HUMANGIGYF2physical
26186194
EXOS1_HUMANEXOSC1physical
26344197
EXOSX_HUMANEXOSC10physical
26344197
EXOS2_HUMANEXOSC2physical
26344197
EXOS3_HUMANEXOSC3physical
26344197
EXOS5_HUMANEXOSC5physical
26344197
MPH6_HUMANMPHOSPH6physical
26344197
DI3L1_HUMANDIS3Lphysical
28514442
EXOSX_HUMANEXOSC10physical
28514442
ZC3H1_HUMANZFC3H1physical
28514442
EXOS8_HUMANEXOSC8physical
28514442
HBS1L_HUMANHBS1Lphysical
28514442
MPH6_HUMANMPHOSPH6physical
28514442
EXOS2_HUMANEXOSC2physical
28514442
EXOS5_HUMANEXOSC5physical
28514442
UBP30_HUMANUSP30physical
28514442
EXOS4_HUMANEXOSC4physical
28514442
EXOS9_HUMANEXOSC9physical
28514442
EXOS6_HUMANEXOSC6physical
28514442
ZCHC8_HUMANZCCHC8physical
28514442
SK2L2_HUMANSKIV2L2physical
28514442
EXOS4_HUMANEXOSC4physical
27173435
LUM_HUMANLUMphysical
27173435
RSRC1_HUMANRSRC1physical
27173435
DHYS_HUMANDHPSphysical
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 EXOS7_HUMAN

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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.
"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-116, AND MASS SPECTROMETRY.

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