RRP44_HUMAN - dbPTM
RRP44_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP44_HUMAN
UniProt AC Q9Y2L1
Protein Name Exosome complex exonuclease RRP44
Gene Name DIS3
Organism Homo sapiens (Human).
Sequence Length 958
Subcellular Localization Cytoplasm . Nucleus, nucleolus . Nucleus, nucleoplasm . Nucleus . Predominantly located in the nucleus (PubMed:20531386). According to PubMed:12429849, found in the nucleolus (PubMed:12429849). According to PubMed:20531386, excluded from nucleolus su
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. DIS3 has both 3'-5' exonuclease and endonuclease activities..
Protein Sequence MLKSKTFLKKTRAGGVMKIVREHYLRDDIGCGAPGCAACGGAHEGPALEPQPQDPASSVCPQPHYLLPDTNVLLHQIDVLEDPAIRNVIVLQTVLQEVRNRSAPVYKRIRDVTNNQEKHFYTFTNEHHRETYVEQEQGENANDRNDRAIRVAAKWYNEHLKKMSADNQLQVIFITNDRRNKEKAIEEGIPAFTCEEYVKSLTANPELIDRLACLSEEGNEIESGKIIFSEHLPLSKLQQGIKSGTYLQGTFRASRENYLEATVWIHGDNEENKEIILQGLKHLNRAVHEDIVAVELLPKSQWVAPSSVVLHDEGQNEEDVEKEEETERMLKTAVSEKMLKPTGRVVGIIKRNWRPYCGMLSKSDIKESRRHLFTPADKRIPRIRIETRQASTLEGRRIIVAIDGWPRNSRYPNGHFVRNLGDVGEKETETEVLLLEHDVPHQPFSQAVLSFLPKMPWSITEKDMKNREDLRHLCICSVDPPGCTDIDDALHCRELENGNLEVGVHIADVSHFIRPGNALDQESARRGTTVYLCEKRIDMVPELLSSNLCSLKCDVDRLAFSCIWEMNHNAEILKTKFTKSVINSKASLTYAEAQLRIDSANMNDDITTSLRGLNKLAKILKKRRIEKGALTLSSPEVRFHMDSETHDPIDLQTKELRETNSMVEEFMLLANISVAKKIHEEFSEHALLRKHPAPPPSNYEILVKAARSRNLEIKTDTAKSLAESLDQAESPTFPYLNTLLRILATRCMMQAVYFCSGMDNDFHHYGLASPIYTHFTSPIRRYADVIVHRLLAVAIGADCTYPELTDKHKLADICKNLNFRHKMAQYAQRASVAFHTQLFFKSKGIVSEEAYILFVRKNAIVVLIPKYGLEGTVFFEEKDKPNPQLIYDDEIPSLKIEDTVFHVFDKVKVKIMLDSSNLQHQKIRMSLVEPQIPGISIPTDTSNMDLNGPKKKKMKLGK
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
1Acetylation-------MLKSKTFL
-------CCCCCHHH		10.8322814378
4Phosphorylation----MLKSKTFLKKT
----CCCCCHHHHHH		32.7323312004
5Acetylation---MLKSKTFLKKTR
---CCCCCHHHHHHC		41.537298029
6Phosphorylation--MLKSKTFLKKTRA
--CCCCCHHHHHHCC		41.0923312004
11PhosphorylationSKTFLKKTRAGGVMK
CCHHHHHHCCCCHHH		24.9423312004
12MethylationKTFLKKTRAGGVMKI
CHHHHHHCCCCHHHH		39.86-
18AcetylationTRAGGVMKIVREHYL
HCCCCHHHHHHHHHC		35.3319608861
18UbiquitinationTRAGGVMKIVREHYL
HCCCCHHHHHHHHHC		35.3319608861
107UbiquitinationNRSAPVYKRIRDVTN
HCCCCCHHHHHHCCC		41.40-
113PhosphorylationYKRIRDVTNNQEKHF
HHHHHHCCCCCEEEE		32.5124719451
118UbiquitinationDVTNNQEKHFYTFTN
HCCCCCEEEEEEECC		29.2921890473
118 (in isoform 1)Ubiquitination-29.2921890473
124PhosphorylationEKHFYTFTNEHHRET
EEEEEEECCHHHHHH		31.7124719451
154AcetylationRAIRVAAKWYNEHLK
HHHHHHHHHHHHHHH		40.2425953088
154UbiquitinationRAIRVAAKWYNEHLK
HHHHHHHHHHHHHHH		40.24-
164PhosphorylationNEHLKKMSADNQLQV
HHHHHHCCCCCCEEE		41.15-
175PhosphorylationQLQVIFITNDRRNKE
CEEEEEEECCCCCHH		21.9625278378
178MethylationVIFITNDRRNKEKAI
EEEEECCCCCHHHHH		46.25-
183UbiquitinationNDRRNKEKAIEEGIP
CCCCCHHHHHHCCCC		57.16-
194GlutathionylationEGIPAFTCEEYVKSL
CCCCCCCHHHHHHHH		2.7822555962
199UbiquitinationFTCEEYVKSLTANPE
CCHHHHHHHHCCCHH		38.55-
200PhosphorylationTCEEYVKSLTANPEL
CHHHHHHHHCCCHHH		22.4020860994
206 (in isoform 2)Ubiquitination-59.1521890473
210MethylationANPELIDRLACLSEE
CCHHHHHHHHHHCCC		19.72-
212 (in isoform 2)Ubiquitination-7.9721890473
215PhosphorylationIDRLACLSEEGNEIE
HHHHHHHCCCCCCCC		33.2225159151
223PhosphorylationEEGNEIESGKIIFSE
CCCCCCCCCCEEEEC		51.5623403867
225UbiquitinationGNEIESGKIIFSEHL
CCCCCCCCEEEECCC		41.74-
236AcetylationSEHLPLSKLQQGIKS
ECCCCHHHHHHHHHC		58.9825953088
236UbiquitinationSEHLPLSKLQQGIKS
ECCCCHHHHHHHHHC		58.9821890473
236 (in isoform 1)Ubiquitination-58.9821890473
242UbiquitinationSKLQQGIKSGTYLQG
HHHHHHHHCCCEEEE		50.0521890473
242 (in isoform 1)Ubiquitination-50.0521890473
246PhosphorylationQGIKSGTYLQGTFRA
HHHHCCCEEEEEEEC		10.6828152594
281UbiquitinationEIILQGLKHLNRAVH
HHHHHHHHHHHHHHH		53.52-
299UbiquitinationVAVELLPKSQWVAPS
EEEEECCCCCEECCC		56.07-
331SumoylationEETERMLKTAVSEKM
HHHHHHHHHHHHHHH		25.70-
3312-HydroxyisobutyrylationEETERMLKTAVSEKM
HHHHHHHHHHHHHHH		25.70-
331MethylationEETERMLKTAVSEKM
HHHHHHHHHHHHHHH		25.7024129315
331SumoylationEETERMLKTAVSEKM
HHHHHHHHHHHHHHH		25.70-
331UbiquitinationEETERMLKTAVSEKM
HHHHHHHHHHHHHHH		25.70-
337AcetylationLKTAVSEKMLKPTGR
HHHHHHHHHHCCCCC		41.8623749302
337UbiquitinationLKTAVSEKMLKPTGR
HHHHHHHHHHCCCCC		41.86-
340AcetylationAVSEKMLKPTGRVVG
HHHHHHHCCCCCEEE		36.7127452117
340UbiquitinationAVSEKMLKPTGRVVG
HHHHHHHCCCCCEEE		36.71-
3502-HydroxyisobutyrylationGRVVGIIKRNWRPYC
CCEEEEEECCCCCCC		37.45-
350AcetylationGRVVGIIKRNWRPYC
CCEEEEEECCCCCCC		37.4525953088
362UbiquitinationPYCGMLSKSDIKESR
CCCCCCCHHHHHHHH		48.46-
378AcetylationHLFTPADKRIPRIRI
HCCCCHHHCCCCEEE		55.0925953088
409PhosphorylationIDGWPRNSRYPNGHF
ECCCCCCCCCCCCCC		34.1823401153
462AcetylationMPWSITEKDMKNRED
CCCCCCHHHHCCHHH		55.2426822725
462UbiquitinationMPWSITEKDMKNRED
CCCCCCHHHHCCHHH		55.24-
477PhosphorylationLRHLCICSVDPPGCT
HHHEEEEECCCCCCC		15.0526074081
484PhosphorylationSVDPPGCTDIDDALH
ECCCCCCCCHHHHCC		41.7426074081
535AcetylationTTVYLCEKRIDMVPE
CEEEEECCHHCCHHH		54.3726051181
535UbiquitinationTTVYLCEKRIDMVPE
CEEEEECCHHCCHHH		54.37-
552AcetylationSSNLCSLKCDVDRLA
HCCCCCCCCCHHHHH		16.4626051181
578PhosphorylationEILKTKFTKSVINSK
HHHHHHCHHHHHCCH		24.7826434776
579UbiquitinationILKTKFTKSVINSKA
HHHHHCHHHHHCCHH		45.95-
580PhosphorylationLKTKFTKSVINSKAS
HHHHCHHHHHCCHHC		25.7726434776
584PhosphorylationFTKSVINSKASLTYA
CHHHHHCCHHCCEEE		20.6226434776
585UbiquitinationTKSVINSKASLTYAE
HHHHHCCHHCCEEEE		37.19-
587PhosphorylationSVINSKASLTYAEAQ
HHHCCHHCCEEEEHH		25.6126434776
589PhosphorylationINSKASLTYAEAQLR
HCCHHCCEEEEHHHH		20.4226434776
590PhosphorylationNSKASLTYAEAQLRI
CCHHCCEEEEHHHHC		14.0323025827
599PhosphorylationEAQLRIDSANMNDDI
EHHHHCCCCCCCCHH		21.12-
602SulfoxidationLRIDSANMNDDITTS
HHCCCCCCCCHHHHH		6.1021406390
607PhosphorylationANMNDDITTSLRGLN
CCCCCHHHHHHHHHH		19.8220860994
608PhosphorylationNMNDDITTSLRGLNK
CCCCHHHHHHHHHHH		26.54-
627UbiquitinationLKKRRIEKGALTLSS
HHHCCCCCCCCCCCC		47.30-
631PhosphorylationRIEKGALTLSSPEVR
CCCCCCCCCCCCCEE		24.8620873877
633PhosphorylationEKGALTLSSPEVRFH
CCCCCCCCCCCEEEE		38.3128450419
634PhosphorylationKGALTLSSPEVRFHM
CCCCCCCCCCEEEEC		28.3525159151
654AcetylationDPIDLQTKELRETNS
CCCCCCCHHHHHHCC		41.6225953088
654UbiquitinationDPIDLQTKELRETNS
CCCCCCCHHHHHHCC		41.62-
659PhosphorylationQTKELRETNSMVEEF
CCHHHHHHCCHHHHH		26.59-
673PhosphorylationFMLLANISVAKKIHE
HHHHHHHHHHHHHHH		18.81-
677UbiquitinationANISVAKKIHEEFSE
HHHHHHHHHHHHHHH		39.29-
684 (in isoform 2)Ubiquitination-38.20-
690UbiquitinationSEHALLRKHPAPPPS
HHHHHHHCCCCCCCC		54.64-
704UbiquitinationSNYEILVKAARSRNL
CCHHHHHHHHHHCCC		32.65-
714UbiquitinationRSRNLEIKTDTAKSL
HHCCCEECHHHHHHH		30.85-
719UbiquitinationEIKTDTAKSLAESLD
EECHHHHHHHHHHHH		48.36-
720PhosphorylationIKTDTAKSLAESLDQ
ECHHHHHHHHHHHHH		30.2827732954
724PhosphorylationTAKSLAESLDQAESP
HHHHHHHHHHHCCCC		31.4730624053
730PhosphorylationESLDQAESPTFPYLN
HHHHHCCCCCHHHHH		32.0530624053
732PhosphorylationLDQAESPTFPYLNTL
HHHCCCCCHHHHHHH		46.6630624053
735PhosphorylationAESPTFPYLNTLLRI
CCCCCHHHHHHHHHH		14.3727732954
785 (in isoform 2)Ubiquitination-3.6121890473
799GlutathionylationAVAIGADCTYPELTD
HHHHCCCCCCHHHCC		3.7822555962
807AcetylationTYPELTDKHKLADIC
CCHHHCCHHHHHHHH		37.0925953088
809UbiquitinationPELTDKHKLADICKN
HHHCCHHHHHHHHHH		51.62-
815AcetylationHKLADICKNLNFRHK
HHHHHHHHHCCHHHH		65.8825953088
815MalonylationHKLADICKNLNFRHK
HHHHHHHHHCCHHHH		65.8826320211
815UbiquitinationHKLADICKNLNFRHK
HHHHHHHHHCCHHHH		65.8821890473
815 (in isoform 1)Ubiquitination-65.8821890473
822AcetylationKNLNFRHKMAQYAQR
HHCCHHHHHHHHHHH		31.5125953088
822UbiquitinationKNLNFRHKMAQYAQR
HHCCHHHHHHHHHHH		31.51-
826PhosphorylationFRHKMAQYAQRASVA
HHHHHHHHHHHHHHH		8.6528152594
842PhosphorylationHTQLFFKSKGIVSEE
CHHHHHCCCCCCCCC		30.8422210691
847PhosphorylationFKSKGIVSEEAYILF
HCCCCCCCCCEEEEE		28.0022210691
851PhosphorylationGIVSEEAYILFVRKN
CCCCCCEEEEEEECC		11.0522210691
876 (in isoform 2)Ubiquitination-53.3121890473
880UbiquitinationVFFEEKDKPNPQLIY
EEEECCCCCCCCEEC		58.73-
892AcetylationLIYDDEIPSLKIEDT
EECCCCCCCCEEECC		31.4019608861
892UbiquitinationLIYDDEIPSLKIEDT
EECCCCCCCCEEECC		31.4019608861
892 (in isoform 2)Ubiquitination-31.4021890473
893PhosphorylationIYDDEIPSLKIEDTV
ECCCCCCCCEEECCE		48.2124719451
895UbiquitinationDDEIPSLKIEDTVFH
CCCCCCCEEECCEEE		48.68-
906AcetylationTVFHVFDKVKVKIML
CEEECCCEEEEEEEE		32.2725953088
906UbiquitinationTVFHVFDKVKVKIML
CEEECCCEEEEEEEE		32.2721890473
906 (in isoform 1)Ubiquitination-32.2721890473
908UbiquitinationFHVFDKVKVKIMLDS
EECCCEEEEEEEECC		43.48-
910AcetylationVFDKVKVKIMLDSSN
CCCEEEEEEEECCCC		19.3827452117
910UbiquitinationVFDKVKVKIMLDSSN
CCCEEEEEEEECCCC		19.38-
912SulfoxidationDKVKVKIMLDSSNLQ
CEEEEEEEECCCCCC		2.5621406390
922AcetylationSSNLQHQKIRMSLVE
CCCCCCCEEHHHHCC		30.1023954790
922MalonylationSSNLQHQKIRMSLVE
CCCCCCCEEHHHHCC		30.1030639696
922UbiquitinationSSNLQHQKIRMSLVE
CCCCCCCEEHHHHCC		30.1019608861
922 (in isoform 1)Ubiquitination-30.1021890473
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 RRP44_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP44_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 RRP44_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBT17_HUMANZBTB17physical
15231747
EXOS7_HUMANEXOSC7physical
20531386
EXOS4_HUMANEXOSC4physical
20531386
EXOS9_HUMANEXOSC9physical
20531386
EXOS5_HUMANEXOSC5physical
20531386
EXOS8_HUMANEXOSC8physical
20531386
EXOS1_HUMANEXOSC1physical
20531386
EXOS2_HUMANEXOSC2physical
20531386
SK2L2_HUMANSKIV2L2physical
20531386
EXOSX_HUMANEXOSC10physical
20531386
SPD2B_HUMANSH3PXD2Bphysical
22939629
WDR1_HUMANWDR1physical
22939629
STXB3_HUMANSTXBP3physical
22939629
AICDA_HUMANAICDAphysical
21255825
EXOS8_HUMANEXOSC8physical
15231747
EXOSX_HUMANEXOSC10physical
15231747
NTM1A_HUMANNTMT1physical
15231747
TWF1_HUMANTWF1physical
22863883
EXOSX_HUMANEXOSC10physical
26344197
EXOS4_HUMANEXOSC4physical
26344197
EXOS7_HUMANEXOSC7physical
26344197
EXOS9_HUMANEXOSC9physical
26344197
GNAS3_HUMANGNASphysical
26344197
GNAS2_HUMANGNASphysical
26344197
ALEX_HUMANGNASphysical
26344197
GNAS1_HUMANGNASphysical
26344197
IMB1_HUMANKPNB1physical
26344197
RAN_HUMANRANphysical
26344197
RAVR1_HUMANRAVER1physical
26344197
SPS1_HUMANSEPHS1physical
26344197
SARNP_HUMANSARNPphysical
27173435
SEPT7_HUMANSEPT7physical
27173435
COPZ1_HUMANCOPZ1physical
27173435
SCYL2_HUMANSCYL2physical
27173435
CDK5_HUMANCDK5physical
27173435
SHLB1_HUMANSH3GLB1physical
27173435
CHRD1_HUMANCHORDC1physical
27173435
PRCC_HUMANPRCCphysical
27173435
DRG1_HUMANDRG1physical
27173435
SEP11_HUMANSEPT11physical
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 RRP44_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-18 AND LYS-922, AND MASSSPECTROMETRY.

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