PARN_HUMAN - dbPTM
PARN_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PARN_HUMAN
UniProt AC O95453
Protein Name Poly(A)-specific ribonuclease PARN
Gene Name PARN
Organism Homo sapiens (Human).
Sequence Length 639
Subcellular Localization Nucleus . Cytoplasm . Nucleus, nucleolus . Some nuclear fraction is nucleolar.
Protein Description 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization..
Protein Sequence MEIIRSNFKSNLHKVYQAIEEADFFAIDGEFSGISDGPSVSALTNGFDTPEERYQKLKKHSMDFLLFQFGLCTFKYDYTDSKYITKSFNFYVFPKPFNRSSPDVKFVCQSSSIDFLASQGFDFNKVFRNGIPYLNQEEERQLREQYDEKRSQANGAGALSYVSPNTSKCPVTIPEDQKKFIDQVVEKIEDLLQSEENKNLDLEPCTGFQRKLIYQTLSWKYPKGIHVETLETEKKERYIVISKVDEEERKRREQQKHAKEQEELNDAVGFSRVIHAIANSGKLVIGHNMLLDVMHTVHQFYCPLPADLSEFKEMTTCVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFNPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSFLSPPKIHVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVKIAVNTSKYAESYRIQTYAEYMGRKQEEKQIKRKWTEDSWKEADSKRLNPQCIPYTLQNHYYRNNSFTAPSTVGKRNLSPSQEEAGLEDGVSGEISDTELEQTDSCAEPLSEGRKKAKKLKRMKKELSPAGSISKNSPATLFEVPDTW
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
9UbiquitinationEIIRSNFKSNLHKVY
CHHHHHHHHHHHHHH		42.56-
61PhosphorylationYQKLKKHSMDFLLFQ
HHHHHHHCHHHHHHH		29.0024719451
72UbiquitinationLLFQFGLCTFKYDYT
HHHHHCCCEEECCCC		4.2621890473
76PhosphorylationFGLCTFKYDYTDSKY
HCCCEEECCCCCCEE		15.2524719451
78PhosphorylationLCTFKYDYTDSKYIT
CCEEECCCCCCEEEE		14.9028102081
79PhosphorylationCTFKYDYTDSKYITK
CEEECCCCCCEEEEE		30.7928102081
81PhosphorylationFKYDYTDSKYITKSF
EECCCCCCEEEEEEE		21.4024719451
82UbiquitinationKYDYTDSKYITKSFN
ECCCCCCEEEEEEEE		43.40-
84UbiquitinationDYTDSKYITKSFNFY
CCCCCEEEEEEEEEE		4.49-
100PhosphorylationFPKPFNRSSPDVKFV
ECCCCCCCCCCCEEE		47.5325159151
101PhosphorylationPKPFNRSSPDVKFVC
CCCCCCCCCCCEEEE		23.1425627689
146PhosphorylationERQLREQYDEKRSQA
HHHHHHHHHHHHHHH		22.7122817901
151UbiquitinationEQYDEKRSQANGAGA
HHHHHHHHHHCCCCC		44.7221890473
151PhosphorylationEQYDEKRSQANGAGA
HHHHHHHHHHCCCCC		44.7223927012
160PhosphorylationANGAGALSYVSPNTS
HCCCCCCCEECCCCC		23.9730266825
161PhosphorylationNGAGALSYVSPNTSK
CCCCCCCEECCCCCC		13.0523927012
163PhosphorylationAGALSYVSPNTSKCP
CCCCCEECCCCCCCC		12.2825159151
166PhosphorylationLSYVSPNTSKCPVTI
CCEECCCCCCCCCCC		32.7130266825
167PhosphorylationSYVSPNTSKCPVTIP
CEECCCCCCCCCCCC		38.6130266825
168UbiquitinationYVSPNTSKCPVTIPE
EECCCCCCCCCCCCH		40.28-
172PhosphorylationNTSKCPVTIPEDQKK
CCCCCCCCCCHHHHH		18.8926074081
179UbiquitinationTIPEDQKKFIDQVVE
CCCHHHHHHHHHHHH		41.75-
198UbiquitinationLLQSEENKNLDLEPC
HHHCHHHCCCCCCCC		63.27-
211MalonylationPCTGFQRKLIYQTLS
CCCHHHHHHHHHHHC		28.5826320211
220AcetylationIYQTLSWKYPKGIHV
HHHHHCCCCCCCEEE		48.5819608861
223UbiquitinationTLSWKYPKGIHVETL
HHCCCCCCCEEEEEE		68.36-
229PhosphorylationPKGIHVETLETEKKE
CCCEEEEEECCCCCE		28.8929083192
232PhosphorylationIHVETLETEKKERYI
EEEEEECCCCCEEEE		57.1029083192
2342-HydroxyisobutyrylationVETLETEKKERYIVI
EEEECCCCCEEEEEE		68.31-
238UbiquitinationETEKKERYIVISKVD
CCCCCEEEEEEEECC		10.71-
238PhosphorylationETEKKERYIVISKVD
CCCCCEEEEEEEECC		10.7123312004
242PhosphorylationKERYIVISKVDEEER
CEEEEEEEECCHHHH		18.7423312004
243AcetylationERYIVISKVDEEERK
EEEEEEEECCHHHHH		42.4520167786
246UbiquitinationIVISKVDEEERKRRE
EEEEECCHHHHHHHH		65.82-
250AcetylationKVDEEERKRREQQKH
ECCHHHHHHHHHHHH		60.1220167786
259UbiquitinationREQQKHAKEQEELND
HHHHHHHHHHHHHHH		60.70-
259AcetylationREQQKHAKEQEELND
HHHHHHHHHHHHHHH		60.7026051181
265UbiquitinationAKEQEELNDAVGFSR
HHHHHHHHHHHCHHH		38.1721890473
280UbiquitinationVIHAIANSGKLVIGH
HHHHHHHCCCEEECH		28.4321890473
324AcetylationCVFPRLLDTKLMAST
HHHHHHHCHHHHCCC		46.52-
324UbiquitinationCVFPRLLDTKLMAST
HHHHHHHCHHHHCCC		46.52-
3262-HydroxyisobutyrylationFPRLLDTKLMASTQP
HHHHHCHHHHCCCCC		35.61-
326AcetylationFPRLLDTKLMASTQP
HHHHHCHHHHCCCCC		35.6125953088
326UbiquitinationFPRLLDTKLMASTQP
HHHHHCHHHHCCCCC		35.6121890473
326MalonylationFPRLLDTKLMASTQP
HHHHHCHHHHCCCCC		35.6126320211
330PhosphorylationLDTKLMASTQPFKDI
HCHHHHCCCCCHHHH		17.3823186163
331PhosphorylationDTKLMASTQPFKDII
CHHHHCCCCCHHHHH		30.6223186163
341PhosphorylationFKDIINNTSLAELEK
HHHHHCCCCHHHHHH		22.1920873877
342PhosphorylationKDIINNTSLAELEKR
HHHHCCCCHHHHHHH		27.9230576142
348UbiquitinationTSLAELEKRLKETPF
CCHHHHHHHHHCCCC		75.54-
402PhosphorylationNYLGSFLSPPKIHVS
HHHHHHCCCCEEECC		36.8324719451
409PhosphorylationSPPKIHVSARSKLIE
CCCEEECCCCHHHHH		12.1024719451
413UbiquitinationIHVSARSKLIEPFFN
EECCCCHHHHHHHHH		48.18-
413MalonylationIHVSARSKLIEPFFN
EECCCCHHHHHHHHH		48.1826320211
413AcetylationIHVSARSKLIEPFFN
EECCCCHHHHHHHHH		48.1825953088
421UbiquitinationLIEPFFNKLFLMRVM
HHHHHHHHHHHHHHH		35.14-
451PhosphorylationRDHVLHVTFPKEWKT
CCEEEEEECCCCCCH		24.3824719451
499UbiquitinationKIAVNTSKYAESYRI
EEEEECHHHHHHHHH		46.5819608861
499AcetylationKIAVNTSKYAESYRI
EEEEECHHHHHHHHH		46.5819608861
508PhosphorylationAESYRIQTYAEYMGR
HHHHHHHHHHHHCCH		23.4822210691
512PhosphorylationRIQTYAEYMGRKQEE
HHHHHHHHCCHHHHH		9.1922210691
527PhosphorylationKQIKRKWTEDSWKEA
HHHHHHCCHHHHHHH		32.7120873877
530PhosphorylationKRKWTEDSWKEADSK
HHHCCHHHHHHHHHH		33.5420873877
532UbiquitinationKWTEDSWKEADSKRL
HCCHHHHHHHHHHCC		47.15-
536PhosphorylationDSWKEADSKRLNPQC
HHHHHHHHHCCCCCC		27.0726074081
546PhosphorylationLNPQCIPYTLQNHYY
CCCCCHHHHHHCCCC		10.5226074081
547PhosphorylationNPQCIPYTLQNHYYR
CCCCHHHHHHCCCCC		19.2626074081
552PhosphorylationPYTLQNHYYRNNSFT
HHHHHCCCCCCCCCC		16.2126074081
553PhosphorylationYTLQNHYYRNNSFTA
HHHHCCCCCCCCCCC		10.1826074081
557PhosphorylationNHYYRNNSFTAPSTV
CCCCCCCCCCCCCCC		27.7629255136
559PhosphorylationYYRNNSFTAPSTVGK
CCCCCCCCCCCCCCC		37.1630266825
562PhosphorylationNNSFTAPSTVGKRNL
CCCCCCCCCCCCCCC		33.0122167270
563PhosphorylationNSFTAPSTVGKRNLS
CCCCCCCCCCCCCCC		32.0226329039
566AcetylationTAPSTVGKRNLSPSQ
CCCCCCCCCCCCHHH		33.5025953088
566UbiquitinationTAPSTVGKRNLSPSQ
CCCCCCCCCCCCHHH		33.50-
570PhosphorylationTVGKRNLSPSQEEAG
CCCCCCCCHHHHHHC		26.5026503892
572PhosphorylationGKRNLSPSQEEAGLE
CCCCCCHHHHHHCCC		47.0130278072
583PhosphorylationAGLEDGVSGEISDTE
HCCCCCCCCCCCCCH		35.9230278072
587PhosphorylationDGVSGEISDTELEQT
CCCCCCCCCCHHHCC		33.8926503892
589PhosphorylationVSGEISDTELEQTDS
CCCCCCCCHHHCCCC		35.3630278072
594PhosphorylationSDTELEQTDSCAEPL
CCCHHHCCCCCCCCC		22.0930278072
596PhosphorylationTELEQTDSCAEPLSE
CHHHCCCCCCCCCCH		20.7228102081
602PhosphorylationDSCAEPLSEGRKKAK
CCCCCCCCHHHHHHH		49.0428450419
619PhosphorylationKRMKKELSPAGSISK
HHHHHHHCCCCCCCC		17.5029255136
623PhosphorylationKELSPAGSISKNSPA
HHHCCCCCCCCCCCC		26.2929255136
625PhosphorylationLSPAGSISKNSPATL
HCCCCCCCCCCCCCE		27.7323401153
628PhosphorylationAGSISKNSPATLFEV
CCCCCCCCCCCEEEC		21.4625159151
631PhosphorylationISKNSPATLFEVPDT
CCCCCCCCEEECCCC		35.0511742007
638PhosphorylationTLFEVPDTW------
CEEECCCCC------		27.3120873877
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
557SPhosphorylationKinaseMAPKAPK2P49137
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PARN_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 PARN_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPC1L_HUMANSPATC1Lphysical
15231747
PARN_HUMANPARNphysical
20379136
CSTF2_HUMANCSTF2physical
20379136
BARD1_HUMANBARD1physical
20379136
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616353Dyskeratosis congenita, autosomal recessive, 6 (DKCB6)
616371Pulmonary fibrosis, and/or bone marrow failure, telomere-related, 4 (PFBMFT4)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PARN_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-220 AND LYS-499, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"DNA damage activates a spatially distinct late cytoplasmic cell-cyclecheckpoint network controlled by MK2-mediated RNA stabilization.";
Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S.,van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A.,Yaffe M.B.;
Mol. Cell 40:34-49(2010).
Cited for: PHOSPHORYLATION AT SER-557 BY MAPKAPK2, AND PHOSPHORYLATION ATSER-557.
"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-163 AND SER-557, 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 SER-163; SER-587; SER-619;SER-623 AND SER-628, AND MASS SPECTROMETRY.
"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-557, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-557, ANDMASS SPECTROMETRY.
"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-619, AND MASSSPECTROMETRY.

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