EXOS9_HUMAN - dbPTM
EXOS9_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOS9_HUMAN
UniProt AC Q06265
Protein Name Exosome complex component RRP45
Gene Name EXOSC9
Organism Homo sapiens (Human).
Sequence Length 439
Subcellular Localization Cytoplasm. Nucleus . Nucleus, nucleolus . Nucleus, nucleoplasm . Colocalizes with SETX in nuclear foci upon induction of transcription-related DNA damage at the S phase (PubMed:24105744).
Isoform 1: Nucleus, nucleolus.
Isoform 2: Nucleus, nucleolus
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. EXOSC9 binds to ARE-containing RNAs..
Protein Sequence MKETPLSNCERRFLLRAIEEKKRLDGRQTYDYRNIRISFGTDYGCCIVELGKTRVLGQVSCELVSPKLNRATEGILFFNLELSQMAAPAFEPGRQSDLLVKLNRLMERCLRNSKCIDTESLCVVAGEKVWQIRVDLHLLNHDGNIIDAASIAAIVALCHFRRPDVSVQGDEVTLYTPEERDPVPLSIHHMPICVSFAFFQQGTYLLVDPNEREERVMDGLLVIAMNKHREICTIQSSGGIMLLKDQVLRCSKIAGVKVAEITELILKALENDQKVRKEGGKFGFAESIANQRITAFKMEKAPIDTSDVEEKAEEIIAEAEPPSEVVSTPVLWTPGTAQIGEGVENSWGDLEDSEKEDDEGGGDQAIILDGIKMDTGVEVSDIGSQDAPIILSDSEEEEMIILEPDKNPKKIRTQTTSAKQEKAPSKKPVKRRKKKRAAN
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
2 (in isoform 2)Ubiquitination-71.00-
2Ubiquitination------MKETPLSNC
------CCCCCCCHH		71.00-
4Phosphorylation----MKETPLSNCER
----CCCCCCCHHHH		24.8221815630
7Phosphorylation-MKETPLSNCERRFL
-CCCCCCCHHHHHHH		40.4123312004
41PhosphorylationNIRISFGTDYGCCIV
CEEEEECCCCCEEEE		24.8428152594
43PhosphorylationRISFGTDYGCCIVEL
EEEECCCCCEEEEEE		16.3528152594
52UbiquitinationCCIVELGKTRVLGQV
EEEEEECCCEEEEEE		45.87-
52 (in isoform 2)Ubiquitination-45.87-
60PhosphorylationTRVLGQVSCELVSPK
CEEEEEEEEEEECCC		8.2530624053
65PhosphorylationQVSCELVSPKLNRAT
EEEEEEECCCCCCCC		29.0130266825
65 (in isoform 2)Phosphorylation-29.0127251275
67UbiquitinationSCELVSPKLNRATEG
EEEEECCCCCCCCCE		51.38-
67 (in isoform 2)Ubiquitination-51.38-
67AcetylationSCELVSPKLNRATEG
EEEEECCCCCCCCCE		51.3825953088
67MalonylationSCELVSPKLNRATEG
EEEEECCCCCCCCCE		51.3826320211
101UbiquitinationRQSDLLVKLNRLMER
CHHHHHHHHHHHHHH		39.76-
101AcetylationRQSDLLVKLNRLMER
CHHHHHHHHHHHHHH		39.7625953088
101 (in isoform 2)Ubiquitination-39.76-
114AcetylationERCLRNSKCIDTESL
HHHHHCCCCCCCHHE		38.4726051181
114UbiquitinationERCLRNSKCIDTESL
HHHHHCCCCCCCHHE		38.47-
114 (in isoform 2)Ubiquitination-38.47-
176PhosphorylationGDEVTLYTPEERDPV
CCEEEEECCCCCCCC		27.6028985074
183 (in isoform 3)Ubiquitination-9.7421906983
183 (in isoform 4)Ubiquitination-9.7421906983
186PhosphorylationERDPVPLSIHHMPIC
CCCCCCCEECCCCEE		17.51-
197 (in isoform 3)Ubiquitination-9.2421906983
197 (in isoform 4)Ubiquitination-9.2421906983
216 (in isoform 3)Ubiquitination-4.6621906983
216 (in isoform 4)Ubiquitination-4.6621906983
227AcetylationLLVIAMNKHREICTI
EEEEEECCCCCEEEE		30.8425953088
252UbiquitinationDQVLRCSKIAGVKVA
HHHHHHHHCCCCCHH		39.95-
257UbiquitinationCSKIAGVKVAEITEL
HHHCCCCCHHHHHHH		34.51-
257 (in isoform 2)Ubiquitination-34.51-
267UbiquitinationEITELILKALENDQK
HHHHHHHHHHHCCHH		43.8821906983
267 (in isoform 1)Ubiquitination-43.8821906983
267 (in isoform 2)Ubiquitination-43.8821906983
274 (in isoform 2)Ubiquitination-47.04-
274UbiquitinationKALENDQKVRKEGGK
HHHHCCHHHHHCCCC		47.04-
277 (in isoform 2)Ubiquitination-64.79-
277AcetylationENDQKVRKEGGKFGF
HCCHHHHHCCCCCCH		64.7925953088
281AcetylationKVRKEGGKFGFAESI
HHHHCCCCCCHHHHH		53.8523749302
281 (in isoform 2)Ubiquitination-53.8521906983
281 (in isoform 1)Ubiquitination-53.8521906983
281UbiquitinationKVRKEGGKFGFAESI
HHHHCCCCCCHHHHH		53.8521906983
287PhosphorylationGKFGFAESIANQRIT
CCCCHHHHHHHCCCE		24.4628555341
294PhosphorylationSIANQRITAFKMEKA
HHHHCCCEEEECEEC		28.3828555341
297 (in isoform 2)Acetylation-43.62-
297SumoylationNQRITAFKMEKAPID
HCCCEEEECEECCCC		43.62-
297AcetylationNQRITAFKMEKAPID
HCCCEEEECEECCCC		43.6219608861
297SumoylationNQRITAFKMEKAPID
HCCCEEEECEECCCC		43.6225114211
297UbiquitinationNQRITAFKMEKAPID
HCCCEEEECEECCCC		43.62-
297 (in isoform 2)Ubiquitination-43.62-
300UbiquitinationITAFKMEKAPIDTSD
CEEEECEECCCCCCH		56.832190698
300 (in isoform 1)Ubiquitination-56.8321906983
300 (in isoform 2)Ubiquitination-56.8321906983
305PhosphorylationMEKAPIDTSDVEEKA
CEECCCCCCHHHHHH		27.7829255136
305 (in isoform 2)Phosphorylation-27.7824719451
306 (in isoform 2)Phosphorylation-35.59-
306PhosphorylationEKAPIDTSDVEEKAE
EECCCCCCHHHHHHH		35.5929255136
325 (in isoform 4)Phosphorylation-4.9017081983
327 (in isoform 4)Phosphorylation-31.9724275569
346PhosphorylationIGEGVENSWGDLEDS
CCCCCCCCCCCCHHC		20.9424275569
353PhosphorylationSWGDLEDSEKEDDEG
CCCCCHHCCCCCCCC		40.9922468782
375PhosphorylationLDGIKMDTGVEVSDI
ECCEEECCCCEEHHC		39.3629523821
380PhosphorylationMDTGVEVSDIGSQDA
ECCCCEEHHCCCCCC		15.2524275569
384PhosphorylationVEVSDIGSQDAPIIL
CEEHHCCCCCCCEEE		25.8125219547
392PhosphorylationQDAPIILSDSEEEEM
CCCCEEECCCCCCEE		28.7825159151
394PhosphorylationAPIILSDSEEEEMII
CCEEECCCCCCEEEE		43.4625159151
409 (in isoform 2)Phosphorylation-70.9417081983
411 (in isoform 2)Phosphorylation-7.8124275569
413PhosphorylationKNPKKIRTQTTSAKQ
CCCCCCCCCCCCHHH		33.4726074081
415PhosphorylationPKKIRTQTTSAKQEK
CCCCCCCCCCHHHHC		23.3126074081
416PhosphorylationKKIRTQTTSAKQEKA
CCCCCCCCCHHHHCC		19.5026074081
417PhosphorylationKIRTQTTSAKQEKAP
CCCCCCCCHHHHCCC		36.5430622161
419SumoylationRTQTTSAKQEKAPSK
CCCCCCHHHHCCCCC		59.77-
419AcetylationRTQTTSAKQEKAPSK
CCCCCCHHHHCCCCC		59.7730588641
419SumoylationRTQTTSAKQEKAPSK
CCCCCCHHHHCCCCC		59.7728112733
425PhosphorylationAKQEKAPSKKPVKRR
HHHHCCCCCCCCCHH		59.1626074081
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
392SPhosphorylationKinaseCSNK2A1P68400
GPS
394SPhosphorylationKinaseCSNK2A1P68400
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOS9_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 EXOS9_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EXOSX_HUMANEXOSC10physical
22939629
AICDA_HUMANAICDAphysical
21255825
EXOS4_HUMANEXOSC4physical
15231747
EXOS1_HUMANEXOSC1physical
26344197
EXOSX_HUMANEXOSC10physical
26344197
EXOS2_HUMANEXOSC2physical
26344197
EXOS3_HUMANEXOSC3physical
26344197
EXOS4_HUMANEXOSC4physical
26344197
EXOS5_HUMANEXOSC5physical
26344197
EXOS6_HUMANEXOSC6physical
26344197
EXOS7_HUMANEXOSC7physical
26344197
MPH6_HUMANMPHOSPH6physical
26344197
PSA5_HUMANPSMA5physical
26344197
EF1G_HUMANEEF1Gphysical
26496610
HPT_HUMANHPphysical
26496610
EXOSX_HUMANEXOSC10physical
26496610
TKT_HUMANTKTphysical
26496610
TRIPC_HUMANTRIP12physical
26496610
MPH6_HUMANMPHOSPH6physical
26496610
C1D_HUMANC1Dphysical
26496610
HBS1L_HUMANHBS1Lphysical
26496610
EXOS8_HUMANEXOSC8physical
26496610
EXOS7_HUMANEXOSC7physical
26496610
EXOS2_HUMANEXOSC2physical
26496610
EXOS3_HUMANEXOSC3physical
26496610
EXOS1_HUMANEXOSC1physical
26496610
EXOS4_HUMANEXOSC4physical
26496610
EXOS5_HUMANEXOSC5physical
26496610
ZN106_HUMANZNF106physical
26496610
S35E1_HUMANSLC35E1physical
26496610
M3K21_HUMANKIAA1804physical
26496610
DI3L1_HUMANDIS3Lphysical
26496610
EXOS6_HUMANEXOSC6physical
26496610
DAB2P_HUMANDAB2IPphysical
26496610
F111B_HUMANFAM111Bphysical
26496610
EXOS4_HUMANEXOSC4physical
27173435
EXOS2_HUMANEXOSC2physical
27173435
EXOS7_HUMANEXOSC7physical
27173435
LUM_HUMANLUMphysical
27173435
RSRC1_HUMANRSRC1physical
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 EXOS9_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-297, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306; SER-392 ANDSER-394, AND MASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-306, AND MASSSPECTROMETRY.
"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-392 AND SER-394, ANDMASS SPECTROMETRY.
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-305, AND MASSSPECTROMETRY.

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