HNRPD_MOUSE - dbPTM
HNRPD_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HNRPD_MOUSE
UniProt AC Q60668
Protein Name Heterogeneous nuclear ribonucleoprotein D0
Gene Name Hnrnpd
Organism Mus musculus (Mouse).
Sequence Length 355
Subcellular Localization Nucleus . Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Component of ribonucleosomes. Cytoplasmic localization oscillates diurnally.
Protein Description Binds with high affinity to RNA molecules that contain AU-rich elements (AREs) found within the 3'-UTR of many proto-oncogenes and cytokine mRNAs. Also binds to double- and single-stranded DNA sequences in a specific manner and functions a transcription factor. Each of the RNA-binding domains specifically can bind solely to a single-stranded non-monotonous 5'-UUAG-3' sequence and also weaker to the single-stranded 5'-TTAGGG-3' telomeric DNA repeat. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats. Binding of RRM1 to DNA inhibits the formation of DNA quadruplex structure which may play a role in telomere elongation. May be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. May play a role in the regulation of the rhythmic expression of circadian clock core genes. Directly binds to the 3'UTR of CRY1 mRNA and induces CRY1 rhythmic translation. May also be involved in the regulation of PER2 translation..
Protein Sequence MSEEQFGGDGAAAAATAAVGGSAGEQEGAMVAAAAQGPAAAAGSGSGGGGSAAGGTEGGSAEAEGAKIDASKNEEDEGHSNSSPRHTEAAAAQREEWKMFIGGLSWDTTKKDLKDYFSKFGEVVDCTLKLDPITGRSRGFGFVLFKESESVDKVMDQKEHKLNGKVIDPKRAKAMKTKEPVKKIFVGGLSPDTPEEKIREYFGGFGEVESIELPMDNKTNKRRGFCFITFKEEEPVKKIMEKKYHNVGLSKCEIKVAMSKEQYQQQQQWGSRGGFAGRARGRGGGPSQNWNQGYSNYWNQGYGNYGYNSQGYGGYGGYDYTGYNNYYGYGDYSNQQSGYGKVSRRGGHQNSYKPY
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
2Phosphorylation------MSEEQFGGD
------CCHHHCCCH		50.2525338131
2Acetylation------MSEEQFGGD
------CCHHHCCCH		50.25-
16PhosphorylationDGAAAAATAAVGGSA
HHHHHHHHHHHCCCH		15.4925338131
22PhosphorylationATAAVGGSAGEQEGA
HHHHHCCCHHHHHHH		27.4625338131
60PhosphorylationAGGTEGGSAEAEGAK
CCCCCCCCCCCCCCC		33.52-
71PhosphorylationEGAKIDASKNEEDEG
CCCCCCCCCCCCCCC		32.0623684622
80PhosphorylationNEEDEGHSNSSPRHT
CCCCCCCCCCCHHHH		49.6227087446
82PhosphorylationEDEGHSNSSPRHTEA
CCCCCCCCCHHHHHH		44.7427087446
83 (in isoform 3)Phosphorylation-30.1519144319
83PhosphorylationDEGHSNSSPRHTEAA
CCCCCCCCHHHHHHH		30.1527087446
87PhosphorylationSNSSPRHTEAAAAQR
CCCCHHHHHHHHHHH		28.7126643407
110UbiquitinationGLSWDTTKKDLKDYF
CCCCCCCHHHHHHHH		46.5122790023
114AcetylationDTTKKDLKDYFSKFG
CCCHHHHHHHHHHHC		61.5923236377
114UbiquitinationDTTKKDLKDYFSKFG
CCCHHHHHHHHHHHC		61.5922790023
119MethylationDLKDYFSKFGEVVDC
HHHHHHHHHCCEEEE		47.71-
119UbiquitinationDLKDYFSKFGEVVDC
HHHHHHHHHCCEEEE		47.7122790023
119AcetylationDLKDYFSKFGEVVDC
HHHHHHHHHCCEEEE		47.7123806337
126S-nitrosylationKFGEVVDCTLKLDPI
HHCCEEEEEEEECCC		3.0320925432
126S-nitrosocysteineKFGEVVDCTLKLDPI
HHCCEEEEEEEECCC		3.03-
127PhosphorylationFGEVVDCTLKLDPIT
HCCEEEEEEEECCCC		23.5925159016
129MalonylationEVVDCTLKLDPITGR
CEEEEEEEECCCCCC		32.4626073543
129UbiquitinationEVVDCTLKLDPITGR
CEEEEEEEECCCCCC		32.46-
153UbiquitinationKESESVDKVMDQKEH
ECCCCHHHHHHHHHH		36.9922790023
165AcetylationKEHKLNGKVIDPKRA
HHHHHCCEECCHHHH		34.6423954790
177PhosphorylationKRAKAMKTKEPVKKI
HHHHHCCCCCCCCEE		27.7921659604
183MalonylationKTKEPVKKIFVGGLS
CCCCCCCEEECCCCC		41.4326320211
190PhosphorylationKIFVGGLSPDTPEEK
EEECCCCCCCCHHHH		24.8125521595
193PhosphorylationVGGLSPDTPEEKIRE
CCCCCCCCHHHHHHH		35.6624925903
197UbiquitinationSPDTPEEKIREYFGG
CCCCHHHHHHHHHCC		45.46-
197MalonylationSPDTPEEKIREYFGG
CCCCHHHHHHHHHCC		45.4626320211
197AcetylationSPDTPEEKIREYFGG
CCCCHHHHHHHHHCC		45.4622826441
210PhosphorylationGGFGEVESIELPMDN
CCCCCEEEEEECCCC		26.9129514104
218UbiquitinationIELPMDNKTNKRRGF
EEECCCCCCCCCCCE		49.5722790023
226S-nitrosylationTNKRRGFCFITFKEE
CCCCCCEEEEEECCC		2.4120925432
226S-palmitoylationTNKRRGFCFITFKEE
CCCCCCEEEEEECCC		2.4128526873
226S-nitrosocysteineTNKRRGFCFITFKEE
CCCCCCEEEEEECCC		2.41-
231AcetylationGFCFITFKEEEPVKK
CEEEEEECCCCHHHH		56.4122826441
237UbiquitinationFKEEEPVKKIMEKKY
ECCCCHHHHHHHHHH		47.5022790023
243MalonylationVKKIMEKKYHNVGLS
HHHHHHHHHHCCCCC		38.1326320211
243AcetylationVKKIMEKKYHNVGLS
HHHHHHHHHHCCCCC		38.1323806337
244PhosphorylationKKIMEKKYHNVGLSK
HHHHHHHHHCCCCCH		15.0829514104
250PhosphorylationKYHNVGLSKCEIKVA
HHHCCCCCHHEEEEE		29.3629514104
251AcetylationYHNVGLSKCEIKVAM
HHCCCCCHHEEEEEE		40.7122826441
251UbiquitinationYHNVGLSKCEIKVAM
HHCCCCCHHEEEEEE		40.71-
251MalonylationYHNVGLSKCEIKVAM
HHCCCCCHHEEEEEE		40.7126320211
252 (in isoform 4)Phosphorylation-6.1725890499
261 (in isoform 4)Methylation-47.4124129315
263 (in isoform 4)Methylation-14.9124129315
271PhosphorylationQQQQQWGSRGGFAGR
HHHHHHHCCCCHHHC		25.45-
271 (in isoform 3)Phosphorylation-25.4525890499
272DimethylationQQQQWGSRGGFAGRA
HHHHHHCCCCHHHCC		45.36-
272MethylationQQQQWGSRGGFAGRA
HHHHHHCCCCHHHCC		45.3624129315
278MethylationSRGGFAGRARGRGGG
CCCCHHHCCCCCCCC		20.0624129315
280 (in isoform 3)Methylation-33.7024129315
280MethylationGGFAGRARGRGGGPS
CCHHHCCCCCCCCCC		33.7012019173
282 (in isoform 3)Methylation-34.7224129315
282MethylationFAGRARGRGGGPSQN
HHHCCCCCCCCCCCC		34.7224129315
344MethylationSGYGKVSRRGGHQNS
CCCCCCCCCCCCCCC		44.2218962907
344DimethylationSGYGKVSRRGGHQNS
CCCCCCCCCCCCCCC		44.22-
345MethylationGYGKVSRRGGHQNSY
CCCCCCCCCCCCCCC		48.1924129315
345Asymmetric dimethylarginineGYGKVSRRGGHQNSY
CCCCCCCCCCCCCCC		48.19-
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 HNRPD_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
345RMethylation

24129315
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 HNRPD_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CITE4_MOUSECited4physical
20211142
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HNRPD_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-80 AND SER-83, AND MASSSPECTROMETRY.

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