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PARN (human)

Overview PARN 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. Homodimer. Interacts with KHSRP and CELF1/CUGBP1. Found in a mRNA decay complex with RENT1, RENT2 and RENT3B. Ubiquitous. Belongs to the CAF1 family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB. Protein type: RNA binding protein; Ribonuclease; EC 3.1.13.4 Cellular Component: cytoplasm; nucleolus; cytosol; nucleus Molecular Function: protein binding; nuclease activity; poly(A)-specific ribonuclease activity; mRNA 3'-UTR binding; metal ion binding; nucleotide binding; protein kinase binding Biological Process: poly(A) tail shortening; RNA metabolic process; RNA modification; mRNA catabolic process, nonsense-mediated decay; female gamete generation; gene expression; mRNA metabolic process; mRNA catabolic process, deadenylation-dependent decay Reference #:  O95453 (UniProtKB) Alt. Names/Synonyms: DAN; Deadenylating nuclease; Deadenylation nuclease; PARN; poly(A)-specific ribonuclease (deadenylation nuclease); Poly(A)-specific ribonuclease PARN; Polyadenylate-specific ribonuclease Gene Symbols: PARN Molecular weight: 73,451 Da Basal Isoelectric point: 5.86  Predict pI for various phosphorylation states Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below PARN 2A1R - A/B=1-430 (human) 2A1S - A/B/C/D=1-430 (human) 3CTR - A=445-540 (human) 1UG8 - A=169-242 (mouse) 1WHV - A=430-516 (mouse) 3D45 - A/B=1-505 (mouse)

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	Sites Implicated In
cell cycle regulation: S557‑p

	Modification Sites and Domains	Show Modification Legend
Click here to view phosphorylation modifications only

	Modification Sites in Parent Protein, Orthologs, and Isoforms	Show Modification Legend

SS  SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.	MS  MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.			human
0	1		S151-p	EQYDEKRsQANGAGA
0	2		Y161-p	NGAGALSyVsPNtsK
0	21		S163-p	AGALSyVsPNtsKCP
0	1		T166-p	LSyVsPNtsKCPVtI
0	1		S167-p	SyVsPNtsKCPVtIP
0	1		T172-p	NtsKCPVtIPEDQKK
0	1		K220-a	IYQTLSWkYPKGIHV
0	1		K243-a	ERYIVISkVDEEERk
0	1		K250-a	kVDEEERkRREQQKH
0	2		K326-u	FPRLLDTkLMASTQP
0	1		T341-p	FKDIINNtSLAELEK
0	1		K499-a	KIAVNTSkYAESYRI
0	1		Y500	IAVNTSkYAESYRIQ
0	1		Y509	ESYRIQTYAEYMGRK
0	1		Y512	RIQTYAEYMGRKQEE
0	3		E518	EYMGRKQEEKQIKRK
0	1		K520	MGRKQEEKQIKRKWT
0	2		K523	KQEEKQIKRKWTEDS
0	1		Y552-p	PYTLQNHyYRNNsFT
1	60		S557-p	NHyYRNNsFTAPSTV
0	23		K566-a	TAPSTVGkRNLsPsQ
0	1		N568	PSTVGkRNLsPsQEE
0	6		S570-p	TVGkRNLsPsQEEAG
0	2		S572-p	GkRNLsPsQEEAGLE
0	5		S583-p	AGLEDGVsGEIsDtE
0	4		S587-p	DGVsGEIsDtELEQT
0	4		T589-p	VsGEIsDtELEQTDS
0	14		S619-p	KRMKKELsPAGsISK
0	2		S623-p	KELsPAGsISKNsPA
0	3		S628-p	AGsISKNsPAtLFEV
0	3		T631-p	ISKNsPAtLFEVPDT

	mouse
S151	EQFDEKRSQANGAGA
-	gap
-	gap
-	gap
A160	ANGAGALAKCPVTIP
T165	ALAKCPVTIPEDQKK
K213	IYQTLSWKYPKGIHV
K236	ERHIVISKVDEEERK
K243	KVDEEERKRREQEKY
K319	FPRLLDTKLMASTQP
T334	FKDIINNTSLAELEK
K492	QIAVNTSKYAESYRI
Y493	IAVNTSKYAESYRIQ
Y502	ESYRIQTYAEYVGKK
Y505	RIQTYAEYVGKKQkG
K511-a	EYVGKKQkGkQVkRK
K513-a	VGKKQkGkQVkRKWT
K516-a	KQkGkQVkRKWTEDS
C538	RPHMQGPCYHSNSFT
S543	GPCYHSNSFTAAGML
K552	TAAGMLGKRtLsPDP
T554-p	AGMLGKRtLsPDPRE
S556-p	MLGKRtLsPDPREAA
D558	GKRtLsPDPREAALE
S569-p	AALEDREsEEVsDsE
S573-p	DREsEEVsDsELEQT
S575-p	EsEEVsDsELEQTDS
S605	KRMKKELSLAGSVSD
S609	KELSLAGSVSDSPAV
S613	LAGSVSDSPAVLFEV
V616	SVSDSPAVLFEVPDT

	rat
S151	EQFDEKRSQANGAGA
-	gap
-	gap
-	gap
T160	ANGAGALTKCPVTIP
T165	ALTKCPVTIPEDQKK
K213	IYQTLSWKYPKGIHV
K236	ERHIVISKVDEEERK
K243	KVDEEERKRREQEKY
K319	FPRLLDTKLMASTQP
T334	FKDIINNTSLAELEK
K492	QIAVNTSKyAESYRI
Y493-p	IAVNTSKyAESYRIQ
Y502-p	ESYRIQTyAEyVGKK
Y505-p	RIQTyAEyVGKKQES
E511	EyVGKKQESKQVKRK
K513	VGKKQESKQVKRKWT
K516	KQESKQVKRKWTEDS
C538	RPHVPGPCYHTNSFT
S543	GPCYHTNSFTAAGIV
K552	TAAGIVGKRTLSPDP
T554	AGIVGKRTLSPDPRE
S556	IVGKRTLSPDPREAG
D558	GKRTLSPDPREAGVV
S569	AGVVDRESEGISDPE
S573	DRESEGISDPELEQT
P575	ESEGISDPELEQTDY
S605	KRMKKEFSLAGSASD
S609	KEFSLAGSASDSPAV
S613	LAGSASDSPAVLFEV
V616	SASDSPAVLFEVPDT

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