EXOSX_HUMAN - dbPTM
EXOSX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EXOSX_HUMAN
UniProt AC Q01780
Protein Name Exosome component 10
Gene Name EXOSC10
Organism Homo sapiens (Human).
Sequence Length 885
Subcellular Localization Cytoplasm. Nucleus, nucleolus. Nucleus. Strongly enriched in the nucleolus and a small amount has been found in cytoplasm supporting the existence of a nucleolar RNA exosome complex form.
Protein Description Putative 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. EXOSC10 has 3'-5' exonuclease activity (By similarity). EXOSC10 is required for nucleolar localization of C1D and probably mediates the association of MTREX, C1D and MPP6 wth the RNA exosome involved in the maturation of 5.8S rRNA..
Protein Sequence MAPPSTREPRVLSATSATKSDGEMVLPGFPDADSFVKFALGSVVAVTKASGGLPQFGDEYDFYRSFPGFQAFCETQGDRLLQCMSRVMQYHGCRSNIKDRSKVTELEDKFDLLVDANDVILERVGILLDEASGVNKNQQPVLPAGLQVPKTVVSSWNRKAAEYGKKAKSETFRLLHAKNIIRPQLKFREKIDNSNTPFLPKIFIKPNAQKPLPQALSKERRERPQDRPEDLDVPPALADFIHQQRTQQVEQDMFAHPYQYELNHFTPADAVLQKPQPQLYRPIEETPCHFISSLDELVELNEKLLNCQEFAVDLEHHSYRSFLGLTCLMQISTRTEDFIIDTLELRSDMYILNESLTDPAIVKVFHGADSDIEWLQKDFGLYVVNMFDTHQAARLLNLGRHSLDHLLKLYCNVDSNKQYQLADWRIRPLPEEMLSYARDDTHYLLYIYDKMRLEMWERGNGQPVQLQVVWQRSRDICLKKFIKPIFTDESYLELYRKQKKHLNTQQLTAFQLLFAWRDKTARREDESYGYVLPNHMMLKIAEELPKEPQGIIACCNPVPPLVRQQINEMHLLIQQAREMPLLKSEVAAGVKKSGPLPSAERLENVLFGPHDCSHAPPDGYPIIPTSGSVPVQKQASLFPDEKEDNLLGTTCLIATAVITLFNEPSAEDSKKGPLTVAQKKAQNIMESFENPFRMFLPSLGHRAPVSQAAKFDPSTKIYEISNRWKLAQVQVQKDSKEAVKKKAAEQTAAREQAKEACKAAAEQAISVRQQVVLENAAKKRERATSDPRTTEQKQEKKRLKISKKPKDPEPPEKEFTPYDYSQSDFKAFAGNSKSKVSSQFDPNKQTPSGKKCIAAKKIKQSVGNKSMSFPTGKSDRGFRYNWPQR
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
13PhosphorylationTREPRVLSATSATKS
CCCCCEEECCCCCCC
27.0025159151
15PhosphorylationEPRVLSATSATKSDG
CCCEEECCCCCCCCC
18.6021406692
16PhosphorylationPRVLSATSATKSDGE
CCEEECCCCCCCCCC
33.3925159151
18PhosphorylationVLSATSATKSDGEMV
EEECCCCCCCCCCEE
30.7424719451
19UbiquitinationLSATSATKSDGEMVL
EECCCCCCCCCCEEC
46.39-
19SumoylationLSATSATKSDGEMVL
EECCCCCCCCCCEEC
46.3928112733
24SulfoxidationATKSDGEMVLPGFPD
CCCCCCCEECCCCCC
4.6021406390
37AcetylationPDADSFVKFALGSVV
CCHHHHHHHHHCCEE
23.9420167786
48UbiquitinationGSVVAVTKASGGLPQ
CCEEEEEECCCCCCC
33.68-
79MethylationFCETQGDRLLQCMSR
HHHHHHHHHHHHHHH
44.09-
90PhosphorylationCMSRVMQYHGCRSNI
HHHHHHHHHCCCCCC
5.10-
109AcetylationKVTELEDKFDLLVDA
HCCHHHHHHHEEECC
31.2530588635
136UbiquitinationDEASGVNKNQQPVLP
HCCCCCCCCCCCCCC
54.4422817900
136 (in isoform 1)Ubiquitination-54.4421906983
136 (in isoform 2)Ubiquitination-54.4421906983
150UbiquitinationPAGLQVPKTVVSSWN
CCCCCCCCHHHHHHH
55.9129967540
155PhosphorylationVPKTVVSSWNRKAAE
CCCHHHHHHHHHHHH
19.4325627689
168SumoylationAEYGKKAKSETFRLL
HHHHHHHHHHHHHHH
58.67-
168SumoylationAEYGKKAKSETFRLL
HHHHHHHHHHHHHHH
58.67-
178UbiquitinationTFRLLHAKNIIRPQL
HHHHHHHHHCCCCCH
37.6229967540
178AcetylationTFRLLHAKNIIRPQL
HHHHHHHHHCCCCCH
37.6225953088
186UbiquitinationNIIRPQLKFREKIDN
HCCCCCHHHHHHCCC
36.8129967540
190UbiquitinationPQLKFREKIDNSNTP
CCHHHHHHCCCCCCC
51.6233845483
194PhosphorylationFREKIDNSNTPFLPK
HHHHCCCCCCCCCCE
38.0329396449
196PhosphorylationEKIDNSNTPFLPKIF
HHCCCCCCCCCCEEC
18.4225159151
201SumoylationSNTPFLPKIFIKPNA
CCCCCCCEECCCCCC
53.01-
205SumoylationFLPKIFIKPNAQKPL
CCCEECCCCCCCCCC
22.82-
205SumoylationFLPKIFIKPNAQKPL
CCCEECCCCCCCCCC
22.82-
205UbiquitinationFLPKIFIKPNAQKPL
CCCEECCCCCCCCCC
22.8227667366
210UbiquitinationFIKPNAQKPLPQALS
CCCCCCCCCCCHHHC
46.22-
217PhosphorylationKPLPQALSKERRERP
CCCCHHHCHHHHHCC
35.1725159151
218UbiquitinationPLPQALSKERRERPQ
CCCHHHCHHHHHCCC
56.9733845483
218AcetylationPLPQALSKERRERPQ
CCCHHHCHHHHHCCC
56.9726051181
278UbiquitinationVLQKPQPQLYRPIEE
HCCCCCCCCCCCCCC
45.9721987572
294UbiquitinationPCHFISSLDELVELN
CCCHHCCHHHHHHHH
4.7821987572
347UbiquitinationIDTLELRSDMYILNE
EEEEHHCCCEEEECC
39.0824816145
352UbiquitinationLRSDMYILNESLTDP
HCCCEEEECCCCCCH
2.9924816145
363UbiquitinationLTDPAIVKVFHGADS
CCCHHHHHHHCCCCC
32.8224816145
365UbiquitinationDPAIVKVFHGADSDI
CHHHHHHHCCCCCCH
3.4924816145
368UbiquitinationIVKVFHGADSDIEWL
HHHHHCCCCCCHHHH
12.4524816145
370PhosphorylationKVFHGADSDIEWLQK
HHHCCCCCCHHHHHH
39.70-
370UbiquitinationKVFHGADSDIEWLQK
HHHCCCCCCHHHHHH
39.7024816145
381UbiquitinationWLQKDFGLYVVNMFD
HHHHHHCEEEEECCC
2.7124816145
386UbiquitinationFGLYVVNMFDTHQAA
HCEEEEECCCHHHHH
1.8624816145
408AcetylationHSLDHLLKLYCNVDS
CCHHHHHHHHCCCCC
43.7126051181
417UbiquitinationYCNVDSNKQYQLADW
HCCCCCCCCEEECCE
55.1021963094
417AcetylationYCNVDSNKQYQLADW
HCCCCCCCCEEECCE
55.1026051181
419PhosphorylationNVDSNKQYQLADWRI
CCCCCCCEEECCEEE
13.7027642862
441PhosphorylationLSYARDDTHYLLYIY
HHHCCCCCEEEEEEE
19.4021406692
443PhosphorylationYARDDTHYLLYIYDK
HCCCCCEEEEEEEHH
10.6521406692
446PhosphorylationDDTHYLLYIYDKMRL
CCCEEEEEEEHHHHH
8.5421406692
448PhosphorylationTHYLLYIYDKMRLEM
CEEEEEEEHHHHHHH
8.9221406692
450AcetylationYLLYIYDKMRLEMWE
EEEEEEHHHHHHHHH
14.6726051181
480AcetylationSRDICLKKFIKPIFT
CHHHHHHHHHHCCCC
39.1026051181
483SumoylationICLKKFIKPIFTDES
HHHHHHHHCCCCCHH
34.88-
483SumoylationICLKKFIKPIFTDES
HHHHHHHHCCCCCHH
34.88-
490PhosphorylationKPIFTDESYLELYRK
HCCCCCHHHHHHHHH
37.5218452278
490 (in isoform 2)Phosphorylation-37.52-
491PhosphorylationPIFTDESYLELYRKQ
CCCCCHHHHHHHHHH
11.3618452278
491 (in isoform 2)Phosphorylation-11.36-
530PhosphorylationREDESYGYVLPNHMM
CCCCCCCCCCCCCHH
7.20-
583SumoylationAREMPLLKSEVAAGV
HHHCCCHHHHHHHCC
52.86-
583SumoylationAREMPLLKSEVAAGV
HHHCCCHHHHHHHCC
52.8625114211
583UbiquitinationAREMPLLKSEVAAGV
HHHCCCHHHHHHHCC
52.8629967540
591UbiquitinationSEVAAGVKKSGPLPS
HHHHHCCCCCCCCCC
40.0633845483
592UbiquitinationEVAAGVKKSGPLPSA
HHHHCCCCCCCCCCH
59.2329967540
593PhosphorylationVAAGVKKSGPLPSAE
HHHCCCCCCCCCCHH
39.6725159151
598PhosphorylationKKSGPLPSAERLENV
CCCCCCCCHHHHHCC
50.9030177828
633UbiquitinationSGSVPVQKQASLFPD
CCCCCCCCCHHCCCC
48.3329967540
636PhosphorylationVPVQKQASLFPDEKE
CCCCCCHHCCCCCCC
28.2221815630
642SumoylationASLFPDEKEDNLLGT
HHCCCCCCCCCCCHH
77.18-
649PhosphorylationKEDNLLGTTCLIATA
CCCCCCHHHHHHHHH
17.8226074081
650PhosphorylationEDNLLGTTCLIATAV
CCCCCHHHHHHHHHH
11.9726074081
655PhosphorylationGTTCLIATAVITLFN
HHHHHHHHHHHHHHC
17.9226074081
659PhosphorylationLIATAVITLFNEPSA
HHHHHHHHHHCCCCC
20.7826074081
671UbiquitinationPSAEDSKKGPLTVAQ
CCCCHHCCCCCCHHH
70.4829967540
679UbiquitinationGPLTVAQKKAQNIME
CCCCHHHHHHHHHHH
40.1029967540
680UbiquitinationPLTVAQKKAQNIMES
CCCHHHHHHHHHHHH
43.03-
698PhosphorylationPFRMFLPSLGHRAPV
HHHHHHHHHCCCCCH
49.4821406692
710SumoylationAPVSQAAKFDPSTKI
CCHHHHCCCCCCCCE
54.00-
710UbiquitinationAPVSQAAKFDPSTKI
CCHHHHCCCCCCCCE
54.0027667366
710SumoylationAPVSQAAKFDPSTKI
CCHHHHCCCCCCCCE
54.0028112733
710AcetylationAPVSQAAKFDPSTKI
CCHHHHCCCCCCCCE
54.0025953088
716UbiquitinationAKFDPSTKIYEISNR
CCCCCCCCEEEECCC
47.8629967540
718PhosphorylationFDPSTKIYEISNRWK
CCCCCCEEEECCCEE
14.5728442448
725UbiquitinationYEISNRWKLAQVQVQ
EEECCCEEEEEEEEC
30.61-
747PhosphorylationKKKAAEQTAAREQAK
HHHHHHHHHHHHHHH
17.50-
754TrimethylationTAAREQAKEACKAAA
HHHHHHHHHHHHHHH
45.60-
754UbiquitinationTAAREQAKEACKAAA
HHHHHHHHHHHHHHH
45.6024816145
754MethylationTAAREQAKEACKAAA
HHHHHHHHHHHHHHH
45.60-
766PhosphorylationAAAEQAISVRQQVVL
HHHHHHHHHHHHHHH
17.7929978859
772UbiquitinationISVRQQVVLENAAKK
HHHHHHHHHHHHHHH
4.8924816145
778AcetylationVVLENAAKKRERATS
HHHHHHHHHHHHHCC
50.3725953088
779UbiquitinationVLENAAKKRERATSD
HHHHHHHHHHHHCCC
55.5624816145
784PhosphorylationAKKRERATSDPRTTE
HHHHHHHCCCCCCHH
39.6223312004
784UbiquitinationAKKRERATSDPRTTE
HHHHHHHCCCCCCHH
39.6224816145
785PhosphorylationKKRERATSDPRTTEQ
HHHHHHCCCCCCHHH
44.6325849741
788UbiquitinationERATSDPRTTEQKQE
HHHCCCCCCHHHHHH
60.3133845483
789PhosphorylationRATSDPRTTEQKQEK
HHCCCCCCHHHHHHH
39.8223312004
790PhosphorylationATSDPRTTEQKQEKK
HCCCCCCHHHHHHHH
37.3823312004
797UbiquitinationTEQKQEKKRLKISKK
HHHHHHHHHHCCCCC
63.3124816145
801UbiquitinationQEKKRLKISKKPKDP
HHHHHHCCCCCCCCC
9.6332015554
802UbiquitinationEKKRLKISKKPKDPE
HHHHHCCCCCCCCCC
32.8024816145
813UbiquitinationKDPEPPEKEFTPYDY
CCCCCCCCCCCCCCC
64.9933845483
816PhosphorylationEPPEKEFTPYDYSQS
CCCCCCCCCCCCCHH
23.2528796482
818PhosphorylationPEKEFTPYDYSQSDF
CCCCCCCCCCCHHHH
25.1823663014
820PhosphorylationKEFTPYDYSQSDFKA
CCCCCCCCCHHHHHH
11.6323663014
821PhosphorylationEFTPYDYSQSDFKAF
CCCCCCCCHHHHHHH
21.9525159151
823PhosphorylationTPYDYSQSDFKAFAG
CCCCCCHHHHHHHCC
38.7923663014
826SumoylationDYSQSDFKAFAGNSK
CCCHHHHHHHCCCCC
47.81-
826SumoylationDYSQSDFKAFAGNSK
CCCHHHHHHHCCCCC
47.8128112733
826UbiquitinationDYSQSDFKAFAGNSK
CCCHHHHHHHCCCCC
47.8132015554
833SumoylationKAFAGNSKSKVSSQF
HHHCCCCCCCCHHCC
59.2928112733
835MethylationFAGNSKSKVSSQFDP
HCCCCCCCCHHCCCC
50.2823644510
835SumoylationFAGNSKSKVSSQFDP
HCCCCCCCCHHCCCC
50.28-
835SumoylationFAGNSKSKVSSQFDP
HCCCCCCCCHHCCCC
50.28-
837PhosphorylationGNSKSKVSSQFDPNK
CCCCCCCHHCCCCCC
23.3524732914
838PhosphorylationNSKSKVSSQFDPNKQ
CCCCCCHHCCCCCCC
37.5424732914
844AcetylationSSQFDPNKQTPSGKK
HHCCCCCCCCCCCCC
62.0226051181
846PhosphorylationQFDPNKQTPSGKKCI
CCCCCCCCCCCCCEE
22.4925159151
848PhosphorylationDPNKQTPSGKKCIAA
CCCCCCCCCCCEEEH
67.6324732914
850AcetylationNKQTPSGKKCIAAKK
CCCCCCCCCEEEHHH
49.1326051181
851AcetylationKQTPSGKKCIAAKKI
CCCCCCCCEEEHHHH
34.1111924287
859SumoylationCIAAKKIKQSVGNKS
EEEHHHHHHHHCCCC
45.4628112733
861PhosphorylationAAKKIKQSVGNKSMS
EHHHHHHHHCCCCCC
27.3024719451
865AcetylationIKQSVGNKSMSFPTG
HHHHHCCCCCCCCCC
41.4230588629
866PhosphorylationKQSVGNKSMSFPTGK
HHHHCCCCCCCCCCC
24.5325159151
868PhosphorylationSVGNKSMSFPTGKSD
HHCCCCCCCCCCCCC
34.8525159151
871PhosphorylationNKSMSFPTGKSDRGF
CCCCCCCCCCCCCCC
56.0523312004
873SumoylationSMSFPTGKSDRGFRY
CCCCCCCCCCCCCCC
52.22-
873SumoylationSMSFPTGKSDRGFRY
CCCCCCCCCCCCCCC
52.2228112733
873AcetylationSMSFPTGKSDRGFRY
CCCCCCCCCCCCCCC
52.2225953088
874PhosphorylationMSFPTGKSDRGFRYN
CCCCCCCCCCCCCCC
33.6128555341
880PhosphorylationKSDRGFRYNWPQR--
CCCCCCCCCCCCC--
21.2227642862

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 EXOSX_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EXOSX_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 EXOSX_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AICDA_HUMANAICDAphysical
21255825
EXOS4_HUMANEXOSC4physical
15231747
SKIV2_HUMANSKIV2Lphysical
15231747
CIB1_HUMANCIB1physical
15231747
TOX4_HUMANTOX4physical
15231747
SCRIB_HUMANSCRIBphysical
15231747
PGES2_HUMANPTGES2physical
15231747
RUVB2_HUMANRUVBL2physical
15231747
NOMO1_HUMANNOMO1physical
15231747
NOMO2_HUMANNOMO2physical
15231747
SSRP1_HUMANSSRP1physical
15231747
UBP21_HUMANUSP21physical
15231747
B9D1_HUMANB9D1physical
15231747
FXRD1_HUMANFOXRED1physical
15231747
CHSS2_HUMANCHPFphysical
15231747
MIC60_HUMANIMMTphysical
15231747
RPE_HUMANRPEphysical
15231747
URP2_HUMANFERMT3physical
15231747
LCAT_HUMANLCATphysical
15231747
AL1B1_HUMANALDH1B1physical
15231747
EXOS6_HUMANEXOSC6physical
15231747
EXOS8_HUMANEXOSC8physical
15231747
DXO_HUMANDXOphysical
15231747
RRP44_HUMANDIS3physical
15231747
EIF3M_HUMANEIF3Mphysical
15231747
TADBP_HUMANTARDBPphysical
15231747
UBP16_HUMANUSP16physical
15231747
EXOS3_HUMANEXOSC3physical
26344197
HNRPR_HUMANHNRNPRphysical
26344197
SK2L2_HUMANSKIV2L2physical
26344197
LA_HUMANSSBphysical
26344197
SPT6H_HUMANSUPT6Hphysical
26344197
UT14A_HUMANUTP14Aphysical
26344197

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 EXOSX_HUMAN

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Related Literatures of Post-Translational Modification

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