HNRPD_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: HNRPD_RAT
• UniProt AC: Q9JJ54
• Protein Name: Heterogeneous nuclear ribonucleoprotein D0
• Gene Name: Hnrnpd
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 353
• 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: MSEEQFGGDGAAAAATAAVGGSAGEQEGAMVAAAQGAAAAAGSGSGGGSAPGGTEGGSTEAEGAKIDASKNEEDEGHSNSSPRHTEAATAQREEWKMFIGGLSWDTTKKDLKDYFSKFGDVVDCTLKLDPITGRSRGFGFVLFKESESVDKVMDQKEHKLNGKVIDPKRAKAMKTKEPVKKIFVGGLSPDTPEEKIREYFGGFGEVESIELPMDNKTNKRRGFCFITFKEEEPVKKIMEKKYHNVGLSKCEIKVAMSKEQYQQQQQWGSRGGFAGRARGRGGGPSQNWNQGYSNYWNQGYGSYGYNSQGYGGYGGYDYTGYNSYYGYGDYSNQQSGYGKVSRRGGHQNSYKPY

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
2	Acetylation	------MSEEQFGGD ------CCHHHCCCH	50.25	-
49	Ubiquitination	GSGSGGGSAPGGTEG CCCCCCCCCCCCCCC	20.44	-
69	Phosphorylation	EGAKIDASKNEEDEG CCCCCCCCCCCCCCC	32.06	25403869
70	Acetylation	GAKIDASKNEEDEGH CCCCCCCCCCCCCCC	70.83	22902405
78	Phosphorylation	NEEDEGHSNSSPRHT CCCCCCCCCCCHHHH	49.62	23712012
80	Phosphorylation	EDEGHSNSSPRHTEA CCCCCCCCCHHHHHH	44.74	23712012
81	Phosphorylation	DEGHSNSSPRHTEAA CCCCCCCCHHHHHHH	30.15	23712012
85	Phosphorylation	SNSSPRHTEAATAQR CCCCHHHHHHHHHCH	28.71	23984901
89	Phosphorylation	PRHTEAATAQREEWK HHHHHHHHHCHHHHH	30.30	23984901
108	Ubiquitination	GLSWDTTKKDLKDYF CCCCCCCHHHHHHHH	46.51	-
112	Acetylation	DTTKKDLKDYFSKFG CCCHHHHHHHHHHHC	61.59	22902405
117	Methylation	DLKDYFSKFGDVVDC HHHHHHHHHCCEEEE	43.39	-
125	Phosphorylation	FGDVVDCTLKLDPIT HCCEEEEEEEECCCC	23.59	23984901
132	Phosphorylation	TLKLDPITGRSRGFG EEEECCCCCCCCCEE	31.75	23984901
151	Acetylation	KESESVDKVMDQKEH ECCCCHHHHHHHHHH	36.99	22902405
163	Acetylation	KEHKLNGKVIDPKRA HHHHHCCEECCHHHH	34.64	22902405
168	Acetylation	NGKVIDPKRAKAMKT CCEECCHHHHHHCCC	62.33	22902405
188	Phosphorylation	KIFVGGLSPDTPEEK EEECCCCCCCCHHHH	24.81	27097102
191	Phosphorylation	VGGLSPDTPEEKIRE CCCCCCCCHHHHHHH	35.66	27097102
195	Acetylation	SPDTPEEKIREYFGG CCCCHHHHHHHHHCC	45.46	22902405
241	Acetylation	VKKIMEKKYHNVGLS HHHHHHHHHHCCCCC	38.13	22902405
249	Acetylation	YHNVGLSKCEIKVAM HHCCCCCHHEEEEEE	40.71	-
269	Phosphorylation	QQQQQWGSRGGFAGR HHHHHHHCCCCHHHC	25.45	27097102
270	Methylation	QQQQWGSRGGFAGRA HHHHHHCCCCHHHCC	45.36	-
273 (in isoform 4)	Phosphorylation	-	7.89	27097102
276	Methylation	SRGGFAGRARGRGGG CCCCHHHCCCCCCCC	20.06	-
278	Methylation	GGFAGRARGRGGGPS CCHHHCCCCCCCCCC	33.70	-
280	Methylation	FAGRARGRGGGPSQN HHHCCCCCCCCCCCC	34.72	-
292	Phosphorylation	SQNWNQGYSNYWNQG CCCCCCCCCCCCCCC	5.51	21373199
292 (in isoform 3)	Phosphorylation	-	5.51	27097102
343	Asymmetric dimethylarginine	GYGKVSRRGGHQNSY CCCCCCCCCCCCCCC	48.19	-
343	Methylation	GYGKVSRRGGHQNSY CCCCCCCCCCCCCCC	48.19	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of HNRPD_RAT !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
343	R	Methylation	Arg-343 is dimethylated, probably to asymmetric dimethylarginine.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of HNRPD_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of HNRPD_RAT !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.