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Protein Page:
PARN (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: EC 3.1.13.4; Ribonuclease; RNA binding protein
Cellular Component: cytoplasm; nucleolus; nucleus; cytosol
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® Total Proteins
Select Structure to View Below

PARN

Protein Structure Not Found.


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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
 

Show Multiple Sequence Alignment


 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 22 S163-p AGALSyVsPNtsKCP
0 1 T166-p LSyVsPNtsKCPVTI
0 2 S167-p SyVsPNtsKCPVTIP
0 1 K220-a IYQTLSWkYPKGIHV
0 1 K243-a ERYIVISkVDEEERk
0 1 K250-a kVDEEERkRREQQKH
0 2 K326-u FPRLLDTkLMAsTQP
0 1 S330-p LDTkLMAsTQPFKDI
0 1 K499-a KIAVNTSkYAESYRI
0 3 E518 EYMGRKQEEKQIKRK
0 2 K523 KQEEKQIKRKWTEDs
0 1 S530-p KRKWTEDsWKEADSK
1 63 S557-p NHYYRNNsFTAPSTV
0 23 K566-a TAPSTVGkRNLsPsQ
0 1 N568 PSTVGkRNLsPsQEE
0 9 S570-p TVGkRNLsPsQEEAG
0 3 S572-p GkRNLsPsQEEAGLE
0 8 S583-p AGLEDGVsGEIsDtE
0 8 S587-p DGVsGEIsDtELEQT
0 4 T589-p VsGEIsDtELEQTDS
0 15 S619-p KRMKKELsPAGsISK
0 3 S623-p KELsPAGsISKNsPA
0 3 S628-p AGsISKNsPAtLFEV
0 3 T631-p ISKNsPAtLFEVPDT
  mouse

 
S151 EQFDEKRSQANGAGA
- gap
- gap
- gap
A160 ANGAGALAKCPVTIP
K213 IYQTLSWKYPKGIHV
K236 ERHIVISKVDEEERK
K243 KVDEEERKRREQEKY
K319 FPRLLDTKLMASTQP
S323 LDTKLMASTQPFKDI
K492 QIAVNTSKYAESYRI
K511-a EYVGKKQkGKQVkRK
K516-a KQkGKQVkRKWTEDS
S523 kRKWTEDSWKEVDRK
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
K213 IYQTLSWKYPKGIHV
K236 ERHIVISKVDEEERK
K243 KVDEEERKRREQEKY
K319 FPRLLDTKLMASTQP
S323 LDTKLMASTQPFKDI
K492 QIAVNTSKYAESYRI
E511 EYVGKKQESKQVKRK
K516 KQESKQVKRKWTEDS
S523 KRKWTEDSWKEVDRK
S543 GPCYHTNSFTAAGIV
K552 TAAGIVGKRTLsPDP
T554 AGIVGKRTLsPDPRE
S556-p IVGKRTLsPDPREAG
D558 GKRTLsPDPREAGVV
S569-p AGVVDREsEGIsDPE
S573-p DREsEGIsDPELEQT
P575 EsEGIsDPELEQTDY
S605 KRMKKEFSLAGSASD
S609 KEFSLAGSASDSPAV
S613 LAGSASDSPAVLFEV
V616 SASDSPAVLFEVPDT
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