XRN2_MOUSE - dbPTM
XRN2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XRN2_MOUSE
UniProt AC Q9DBR1
Protein Name 5'-3' exoribonuclease 2
Gene Name Xrn2
Organism Mus musculus (Mouse).
Sequence Length 951
Subcellular Localization Nucleus, nucleolus .
Protein Description Possesses 5'->3' exoribonuclease activity. May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5' fragment which is subsequently processed to form the mature mRNA and a 3' fragment which remains attached to the elongating polymerase. The processive degradation of this 3' fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (By similarity)..
Protein Sequence MGVPAFFRWLSRKYPSIIVNCVEEKPKECNGVKIPVDASKPNPNDVEFDNLYLDMNGIIHPCTHPEDKPAPKNEDEMMVAIFEYIDRLFNIVRPRRLLYMAIDGVAPRAKMNQQRSRRFRASKEGMEAAVEKQRVREEILAKGGFLPPEEIKERFDSNCITPGTEFMDNLAKCLRYYIADRLNNDPGWKNLTVILSDASAPGEGEHKIMDYIRRQRAQPNHDPNTHHCLCGADADLIMLGLATHEPNFTIIREEFKPNKPKPCALCNQFGHEVKDCEGLPREKKGKHDELADSLPCAEGEFIFLRLNVLREYLERELTMASLPFPFDVERSIDDWVFMCFFVGNDFLPHLPSLEIREGAIDRLVNIYKNVVHKTGGYLTESGYVNLQRVQMIMLAVGEVEDSIFKKRKDDEDSFRRRQKEKRKRMKRDQPAFTPSGILTPHALGSRNSPGCQVASNPRQAAYEMRMQRNSSPSISPNTSFASDGSPSPLGGIKRKAEDSDSEPEPEDNVRLWEAGWKQRYYKNKFDVDAADEKFRRKVVQSYVEGLCWVLRYYYQGCASWKWYYPFHYAPFASDFEGIADMSSEFEKGTKPFKPLEQLMGVFPAASGNFLPPTWRKLMSDPDSSIIDFYPEDFAIDLNGKKYAWQGVALLPFVDERRLRAALEEVYPDLTPEENRRNSLGGDVLFVGKLHPLRDFILELYQTGSTEPVDVPPELCHGIQGTFSLDEEAILPDQTVCSPVPMLRDLTQNTAVSINFKDPQFAEDYVFKAAMLPGARKPATVLKPGDWEKSSNGRQWKPQLGFNRDRRPVHLDQAAFRTLGHVTPRGSGTSVYTNTALPPANYQGNNYRPLLRGQAQIPKLMSNMRPQDSWRGPPPLFQQHRFERSVGAEPLLPWNRMIQNQNAAFQPNQYQMLGGPGGYPPRRDDHRGGRQGYPREGRKYPLPPPSGRYSWN
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
286AcetylationLPREKKGKHDELADS
CCCCCCCCCCHHHHH		57.6823806337
406AcetylationVEDSIFKKRKDDEDS
CCHHHHHHCCCCHHH		54.6630988531
433PhosphorylationKRDQPAFTPSGILTP
CCCCCCCCCCCCCCH		20.7426160508
435PhosphorylationDQPAFTPSGILTPHA
CCCCCCCCCCCCHHH		35.0925266776
439PhosphorylationFTPSGILTPHALGSR
CCCCCCCCHHHCCCC		15.8826745281
445PhosphorylationLTPHALGSRNSPGCQ
CCHHHCCCCCCCCCC		29.1926160508
448PhosphorylationHALGSRNSPGCQVAS
HHCCCCCCCCCCCCC		22.8925521595
455PhosphorylationSPGCQVASNPRQAAY
CCCCCCCCCHHHHHH		48.8125266776
470PhosphorylationEMRMQRNSSPSISPN
HHHHHHCCCCCCCCC		45.9025521595
471PhosphorylationMRMQRNSSPSISPNT
HHHHHCCCCCCCCCC		26.6427087446
473PhosphorylationMQRNSSPSISPNTSF
HHHCCCCCCCCCCCC		37.3325521595
475PhosphorylationRNSSPSISPNTSFAS
HCCCCCCCCCCCCCC		19.2125521595
478PhosphorylationSPSISPNTSFASDGS
CCCCCCCCCCCCCCC		28.7127087446
479PhosphorylationPSISPNTSFASDGSP
CCCCCCCCCCCCCCC		26.0027087446
482PhosphorylationSPNTSFASDGSPSPL
CCCCCCCCCCCCCCC		40.2627087446
485PhosphorylationTSFASDGSPSPLGGI
CCCCCCCCCCCCCCC		27.4825521595
487PhosphorylationFASDGSPSPLGGIKR
CCCCCCCCCCCCCCC		34.1625521595
493UbiquitinationPSPLGGIKRKAEDSD
CCCCCCCCCCCCCCC		51.63-
499 (in isoform 2)Phosphorylation-34.2419144319
499PhosphorylationIKRKAEDSDSEPEPE
CCCCCCCCCCCCCCH		34.2427087446
501 (in isoform 2)Phosphorylation-60.0319144319
501PhosphorylationRKAEDSDSEPEPEDN
CCCCCCCCCCCCHHH		60.0327087446
533UbiquitinationDVDAADEKFRRKVVQ
CCHHHCHHHHHHHHH		44.72-
640AcetylationFAIDLNGKKYAWQGV
EEEECCCCEEEEEEE		41.3522361613
641AcetylationAIDLNGKKYAWQGVA
EEECCCCEEEEEEEE		41.4122826441
666PhosphorylationRAALEEVYPDLTPEE
HHHHHHHCCCCCHHH		8.3627717184
670PhosphorylationEEVYPDLTPEENRRN
HHHCCCCCHHHHHCC		35.7129514104
678PhosphorylationPEENRRNSLGGDVLF
HHHHHCCCCCCCEEE		26.9526824392
688UbiquitinationGDVLFVGKLHPLRDF
CCEEEEECCCCHHHH		38.02-
796UbiquitinationSSNGRQWKPQLGFNR
CCCCCCCCCCCCCCC		17.97-
817PhosphorylationLDQAAFRTLGHVTPR
HHHHHHHHHCCCCCC		30.5529176673
824MethylationTLGHVTPRGSGTSVY
HHCCCCCCCCCCEEE		42.4126542391
824Asymmetric dimethylarginineTLGHVTPRGSGTSVY
HHCCCCCCCCCCEEE		42.41-
826PhosphorylationGHVTPRGSGTSVYTN
CCCCCCCCCCEEEEC		39.9325293948
828PhosphorylationVTPRGSGTSVYTNTA
CCCCCCCCEEEECCC		19.4025293948
829PhosphorylationTPRGSGTSVYTNTAL
CCCCCCCEEEECCCC		19.3625293948
831PhosphorylationRGSGTSVYTNTALPP
CCCCCEEEECCCCCC		8.2725293948
832PhosphorylationGSGTSVYTNTALPPA
CCCCEEEECCCCCCC		24.7625293948
834PhosphorylationGTSVYTNTALPPANY
CCEEEECCCCCCCCC		23.0525293948
841PhosphorylationTALPPANYQGNNYRP
CCCCCCCCCCCCCHH		21.6525293948
846PhosphorylationANYQGNNYRPLLRGQ
CCCCCCCCHHHHCCC		20.0125293948
847Asymmetric dimethylarginineNYQGNNYRPLLRGQA
CCCCCCCHHHHCCCC		19.95-
847MethylationNYQGNNYRPLLRGQA
CCCCCCCHHHHCCCC		19.9524129315
851Asymmetric dimethylarginineNNYRPLLRGQAQIPK
CCCHHHHCCCCHHHH		42.75-
851MethylationNNYRPLLRGQAQIPK
CCCHHHHCCCCHHHH		42.7554560683
864DimethylationPKLMSNMRPQDSWRG
HHHHHCCCCCCCCCC		29.94-
864MethylationPKLMSNMRPQDSWRG
HHHHHCCCCCCCCCC		29.9454560643
870DimethylationMRPQDSWRGPPPLFQ
CCCCCCCCCCCCHHH		52.25-
870MethylationMRPQDSWRGPPPLFQ
CCCCCCCCCCCCHHH		52.2554560659
880Asymmetric dimethylargininePPLFQQHRFERSVGA
CCHHHHHCHHCCCCC		30.68-
880MethylationPPLFQQHRFERSVGA
CCHHHHHCHHCCCCC		30.6824129315
883Asymmetric dimethylarginineFQQHRFERSVGAEPL
HHHHCHHCCCCCCCC		33.65-
883MethylationFQQHRFERSVGAEPL
HHHHCHHCCCCCCCC		33.6524129315
895MethylationEPLLPWNRMIQNQNA
CCCCCHHHHHCCCCC		21.5124129315
945PhosphorylationKYPLPPPSGRYSWN-
CCCCCCCCCCCCCC-		41.5026643407
947Asymmetric dimethylargininePLPPPSGRYSWN---
CCCCCCCCCCCC---		27.01-
947MethylationPLPPPSGRYSWN---
CCCCCCCCCCCC---		27.0124129315
948PhosphorylationLPPPSGRYSWN----
CCCCCCCCCCC----		22.8926643407
949PhosphorylationPPPSGRYSWN-----
CCCCCCCCCC-----		20.8426643407
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
439TPhosphorylationKinaseMAPK1P63085
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XRN2_MOUSE !!
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 XRN2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of XRN2_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of XRN2_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, ANDMASS SPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448; SER-499 ANDSER-501, AND MASS SPECTROMETRY.
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, ANDMASS SPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-499 AND SER-501, ANDMASS SPECTROMETRY.

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