PARN_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PARN_MOUSE
• UniProt AC: Q8VDG3
• Protein Name: Poly(A)-specific ribonuclease PARN
• Gene Name: Parn
• Organism: Mus musculus (Mouse).
• Sequence Length: 624
• 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 (By similarity)..
• Protein Sequence: MEIIRSNFKINLHKVYQAIEEADFFAIDGEFSGISDGPSVTALTSGFDTPEERYQKLKKHSMDFLLFQFGLCAFKYDHTDSKHVTKSFNFYVFPKPFSRSSPDVKFVCQSSSIDFLASQGFDFNKVFCSGIPYLNQEEERQLREQFDEKRSQANGAGALAKCPVTIPEDQKKFIDQVIEKIEDFLQSEEKRSLELDPCTGFQRKLIYQTLSWKYPKGIHVETLETDKKERHIVISKVDEEERKRREQEKYTKEQEELNDAVGFSRVIHAIANSGKLVVGHNMLLDVMHTIHQFYCPLPADLNEFKEMAICVFPRLLDTKLMASTQPFKDIINNTSLAELEKRLKETPFDPPKVESAEGFPSYDTASEQLHEAGYDAYITGLCFISMANYLGSLLSPPKMCVSARSKLIEPFFNKLFLMRVMDIPYLNLEGPDLQPKRDHVLHVTFPKEWKTSDLYQLFSAFGNIQISWIDDTSAFVSLSQPEQVQIAVNTSKYAESYRIQTYAEYVGKKQEGKQVKRKWTEDSWKEVDRKRPHMQGPCYHSNSFTAAGVLGKRTLSPDPREAALEDRESEEVSDSELEQTDSCTDPLPEGRKKSKKLKRMKKELSLAGSVSDSPAVLFEVPDTW

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
100	Phosphorylation	FPKPFSRSSPDVKFV ECCCCCCCCCCCEEE	45.05	25338131
101	Phosphorylation	PKPFSRSSPDVKFVC CCCCCCCCCCCEEEE	24.82	25338131
213	Acetylation	IYQTLSWKYPKGIHV HHHHHCCCCCCCEEE	48.58	-
335	Phosphorylation	KDIINNTSLAELEKR HHHHCCCCHHHHHHH	27.92	25338131
492	Acetylation	QIAVNTSKYAESYRI EEEEECHHHHHHHCH	46.58	-
508	Acetylation	TYAEYVGKKQEGKQV HHHHHHCCCCCCCCC	41.04	23806337
513	Acetylation	VGKKQEGKQVKRKWT HCCCCCCCCCCCCCC	51.68	15306213
516	Acetylation	KQEGKQVKRKWTEDS CCCCCCCCCCCCCCH	45.85	15306217
523	Phosphorylation	KRKWTEDSWKEVDRK CCCCCCCHHHHHHHC	33.54	-
543	Phosphorylation	GPCYHSNSFTAAGVL CCCCCCCCCCCCEEE	27.30	-
554	Phosphorylation	AGVLGKRTLSPDPRE CEEECCCCCCCCHHH	34.76	25159016
556	Phosphorylation	VLGKRTLSPDPREAA EECCCCCCCCHHHHH	27.00	26824392
569	Phosphorylation	AALEDRESEEVSDSE HHHCHHHCCCCCHHH	39.69	25521595
573	Phosphorylation	DRESEEVSDSELEQT HHHCCCCCHHHHHCC	38.40	25521595
575	Phosphorylation	ESEEVSDSELEQTDS HCCCCCHHHHHCCCC	36.25	27087446
580	Phosphorylation	SDSELEQTDSCTDPL CHHHHHCCCCCCCCC	22.09	25619855
582	Phosphorylation	SELEQTDSCTDPLPE HHHHCCCCCCCCCCC	23.46	25619855
584	Phosphorylation	LEQTDSCTDPLPEGR HHCCCCCCCCCCCCH	44.60	25619855
605	Phosphorylation	KRMKKELSLAGSVSD HHHHHHHHHCCCCCC	19.77	26643407
609	Phosphorylation	KELSLAGSVSDSPAV HHHHHCCCCCCCCEE	16.91	26643407
611	Phosphorylation	LSLAGSVSDSPAVLF HHHCCCCCCCCEEEE	33.78	26643407
613	Phosphorylation	LAGSVSDSPAVLFEV HCCCCCCCCEEEEEC	13.78	26643407

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
543	S	Phosphorylation	Kinase	MAPKAPK2	P49138	Uniprot

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of PARN_MOUSE !!

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Oops, there are no PPI records of PARN_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573 AND SER-575, ANDMASS SPECTROMETRY.
PubMed: 17242355