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O95453 (PARN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Poly(A)-specific ribonuclease PARN

EC=3.1.13.4
Alternative name(s):
Deadenylating nuclease
Deadenylation nuclease
Polyadenylate-specific ribonuclease
Gene names
Name:PARN
Synonyms:DAN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length639 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.9 Ref.13 Ref.14

Catalytic activity

Exonucleolytic cleavage of poly(A) to 5'-AMP. Ref.1 Ref.7

Cofactor

Divalent metal cations. Mg2+ is the most probable. Ref.9 Ref.15

Subunit structure

Homodimer. Interacts with KHSRP and CELF1/CUGBP1. Found in a mRNA decay complex with RENT1, RENT2 and RENT3B. Interacts with ZC3HAV1 in an RNA-independent manner. Ref.7 Ref.12 Ref.14 Ref.17 Ref.24 Ref.26

Subcellular location

Nucleus. Cytoplasm. Nucleusnucleolus. Note: Some nuclear fraction is nucleolar. Ref.1 Ref.11

Tissue specificity

Ubiquitous. Ref.1 Ref.6

Post-translational modification

Phosphorylation by MAPKAPK2, preventing GADD45A mRNA degradation after genotoxic stress.

Sequence similarities

Belongs to the CAF1 family.

Contains 1 R3H domain.

Ontologies

Keywords
   Biological processNonsense-mediated mRNA decay
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   LigandMagnesium
Metal-binding
RNA-binding
   Molecular functionExonuclease
Hydrolase
Nuclease
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA modification

Traceable author statement Ref.1. Source: ProtInc

RNA phosphodiester bond hydrolysis, exonucleolytic

Traceable author statement. Source: GOC

female gamete generation

Traceable author statement Ref.1. Source: ProtInc

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype PubMed 22890540. Source: UniProtKB

nuclear-transcribed mRNA poly(A) tail shortening

Traceable author statement. Source: Reactome

nucleic acid phosphodiester bond hydrolysis

Traceable author statement Ref.1. Source: GOC

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionmRNA 3'-UTR binding

Traceable author statement Ref.1. Source: ProtInc

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nuclease activity

Traceable author statement Ref.1. Source: ProtInc

nucleotide binding

Inferred from electronic annotation. Source: InterPro

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

poly(A)-specific ribonuclease activity

Traceable author statement. Source: Reactome

protein binding

Inferred from physical interaction Ref.24. Source: UniProtKB

protein kinase binding

Inferred from physical interaction Ref.27. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95453-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O95453-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.
Note: No experimental confirmation available. Non canonical splice junctions.
Isoform 3 (identifier: O95453-3)

The sequence of this isoform differs from the canonical sequence as follows:
     53-98: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 639639Poly(A)-specific ribonuclease PARN
PRO_0000212851

Regions

Domain178 – 24568R3H

Sites

Metal binding281Divalent metal cation; catalytic Probable
Metal binding301Divalent metal cation; catalytic Probable
Metal binding2921Divalent metal cation; catalytic Probable
Metal binding3821Divalent metal cation; catalytic Probable
Site3261Interaction with poly(A)

Amino acid modifications

Modified residue1631Phosphoserine Ref.16 Ref.20
Modified residue2201N6-acetyllysine Ref.21
Modified residue4991N6-acetyllysine Ref.21
Modified residue5571Phosphoserine; by MAPKAPK2 Ref.16 Ref.18 Ref.22 Ref.25 Ref.27
Modified residue6191Phosphoserine Ref.22 Ref.25
Modified residue6231Phosphoserine Ref.25
Modified residue6281Phosphoserine Ref.22
Modified residue6311Phosphothreonine Ref.22

Natural variations

Alternative sequence1 – 6161Missing in isoform 2.
VSP_042846
Alternative sequence53 – 9846Missing in isoform 3.
VSP_042847

Experimental info

Mutagenesis281D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. Ref.10 Ref.13 Ref.15
Mutagenesis281D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). Ref.10 Ref.13 Ref.15
Mutagenesis301E → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. Ref.10 Ref.13 Ref.15
Mutagenesis301E → C: Loss of function in the presence of Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+). Ref.10 Ref.13 Ref.15
Mutagenesis311F → A: Reduced affinity for poly(A). Loss of activity. Ref.26
Mutagenesis341I → A: Reduced affinity for poly(A). Strongly reduced activity. Ref.26
Mutagenesis1131I → A: Loss of dimerization. Loss of activity. Ref.26
Mutagenesis1151F → A: Reduced affinity for poly(A). Little effect on activity.
Mutagenesis1231F → A: Loss of dimerization. Loss of activity. Ref.26
Mutagenesis2921D → A: Loss of function but does not abolish ability to bind RNA. Ref.10 Ref.15
Mutagenesis2921D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). Ref.10 Ref.15
Mutagenesis3261K → A: Reduced affinity for poly(A). Little effect on activity.
Mutagenesis3771H → A: Loss of activity. Ref.26
Mutagenesis3821D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. Ref.10 Ref.13 Ref.15
Mutagenesis3821D → C: Loss of function in the presence of Mg(2+) but not in the presence of Mn(2+), Zn(2+), Co(2+) or Cd(2+). Ref.10 Ref.13 Ref.15
Mutagenesis5571S → A: Strong reduction of phosphorylation by MAPKAPK2.

Secondary structure

............................................................................ 639
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 6994BE39384DF7AC

FASTA63973,451
        10         20         30         40         50         60 
MEIIRSNFKS NLHKVYQAIE EADFFAIDGE FSGISDGPSV SALTNGFDTP EERYQKLKKH 

        70         80         90        100        110        120 
SMDFLLFQFG LCTFKYDYTD SKYITKSFNF YVFPKPFNRS SPDVKFVCQS SSIDFLASQG 

       130        140        150        160        170        180 
FDFNKVFRNG IPYLNQEEER QLREQYDEKR SQANGAGALS YVSPNTSKCP VTIPEDQKKF 

       190        200        210        220        230        240 
IDQVVEKIED LLQSEENKNL DLEPCTGFQR KLIYQTLSWK YPKGIHVETL ETEKKERYIV 

       250        260        270        280        290        300 
ISKVDEEERK RREQQKHAKE QEELNDAVGF SRVIHAIANS GKLVIGHNML LDVMHTVHQF 

       310        320        330        340        350        360 
YCPLPADLSE FKEMTTCVFP RLLDTKLMAS TQPFKDIINN TSLAELEKRL KETPFNPPKV 

       370        380        390        400        410        420 
ESAEGFPSYD TASEQLHEAG YDAYITGLCF ISMANYLGSF LSPPKIHVSA RSKLIEPFFN 

       430        440        450        460        470        480 
KLFLMRVMDI PYLNLEGPDL QPKRDHVLHV TFPKEWKTSD LYQLFSAFGN IQISWIDDTS 

       490        500        510        520        530        540 
AFVSLSQPEQ VKIAVNTSKY AESYRIQTYA EYMGRKQEEK QIKRKWTEDS WKEADSKRLN 

       550        560        570        580        590        600 
PQCIPYTLQN HYYRNNSFTA PSTVGKRNLS PSQEEAGLED GVSGEISDTE LEQTDSCAEP 

       610        620        630 
LSEGRKKAKK LKRMKKELSP AGSISKNSPA TLFEVPDTW 

« Hide

Isoform 2 [UniParc].

Checksum: 5E62F237DB650802
Show »

FASTA57866,574
Isoform 3 [UniParc].

Checksum: 2908EEB765F91D80
Show »

FASTA59367,722

References

« Hide 'large scale' references
[1]"The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes."
Koerner C.G., Wormington M., Muckenthaler M., Schneider S., Dehlin E., Wahle E.
EMBO J. 17:5427-5437(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Adrenal gland, Esophagus and Placenta.
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Testis.
[6]"The human gene for the poly(A)-specific ribonuclease (PARN) maps to 16p13 and has a truncated copy in the Prader-Willi/Angelman syndrome region on 15q11-->q13."
Buiting K., Koerner C., Ulrich B., Wahle E., Horsthemke B.
Cytogenet. Cell Genet. 87:125-131(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"A 54-kDa fragment of the Poly(A)-specific ribonuclease is an oligomeric, processive, and cap-interacting Poly(A)-specific 3' exonuclease."
Martinez J., Ren Y.-G., Thuresson A.-C., Hellman U., Aastroem J., Virtanen A.
J. Biol. Chem. 275:24222-24230(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME ACTIVITY, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY.
[8]"Interaction between a poly(A)-specific ribonuclease and the 5' cap influences mRNA deadenylation rates in vitro."
Gao M., Fritz D.T., Ford L.P., Wilusz J.
Mol. Cell 5:479-488(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation."
Martinez J., Ren Y.-G., Nilsson P., Ehrenberg M., Virtanen A.
J. Biol. Chem. 276:27923-27929(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, COFACTOR.
[10]"Identification of the active site of poly(A)-specific ribonuclease by site-directed mutagenesis and Fe(2+)-mediated cleavage."
Ren Y.-G., Martinez J., Virtanen A.
J. Biol. Chem. 277:5982-5987(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ASP-28; GLU-30; ASP-292 AND ASP-382.
[11]"Functional proteomic analysis of human nucleolus."
Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J.
Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"Nonsense-mediated mRNA decay in mammalian cells involves decapping, deadenylating, and exonucleolytic activities."
Lejeune F., Li X., Maquat L.E.
Mol. Cell 12:675-687(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNA DECAY COMPLEX WITH RENT1; RENT2 AND RENT3B.
[13]"Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease."
Lai W.S., Kennington E.A., Blackshear P.J.
Mol. Cell. Biol. 23:3798-3812(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ASP-28; GLU-30 AND ASP-382.
[14]"A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery."
Gherzi R., Lee K.-Y., Briata P., Wegmueller D., Moroni C., Karin M., Chen C.-Y.
Mol. Cell 14:571-583(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH KHSRP.
[15]"Coordination of divalent metal ions in the active site of poly(A)-specific ribonuclease."
Ren Y.-G., Kirsebom L.A., Virtanen A.
J. Biol. Chem. 279:48702-48706(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: COFACTOR, MUTAGENESIS OF ASP-28; GLU-30; ASP-292 AND ASP-382.
[16]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163 AND SER-557, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"CUG-BP binds to RNA substrates and recruits PARN deadenylase."
Moraes K.C., Wilusz C.J., Wilusz J.
RNA 12:1084-1091(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CELF1.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-220 AND LYS-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557; SER-619; SER-628 AND THR-631, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[23]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"Zinc-finger antiviral protein inhibits HIV-1 infection by selectively targeting multiply spliced viral mRNAs for degradation."
Zhu Y., Chen G., Lv F., Wang X., Ji X., Xu Y., Sun J., Wu L., Zheng Y.T., Gao G.
Proc. Natl. Acad. Sci. U.S.A. 108:15834-15839(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ZC3HAV1.
[25]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-557; SER-619 AND SER-623, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"Structural insight into poly(A) binding and catalytic mechanism of human PARN."
Wu M., Reuter M., Lilie H., Liu Y., Wahle E., Song H.
EMBO J. 24:4082-4093(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-430 IN COMPLEX WITH DNA, MUTAGENESIS OF PHE-31; ILE-34; ILE-113; PHE-123 AND HIS-377, SUBUNIT.
[27]"DNA damage activates a spatially distinct late cytoplasmic cell-cycle checkpoint network controlled by MK2-mediated RNA stabilization."
Reinhardt H.C., Hasskamp P., Schmedding I., Morandell S., van Vugt M.A., Wang X., Linding R., Ong S.E., Weaver D., Carr S.A., Yaffe M.B.
Mol. Cell 40:34-49(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-557 BY MAPKAPK2, PHOSPHORYLATION AT SER-557.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ005698 mRNA. Translation: CAA06683.1.
AK293189 mRNA. Translation: BAG56729.1.
AK301648 mRNA. Translation: BAG63126.1.
AK315020 mRNA. Translation: BAG37510.1.
AC009167 Genomic DNA. No translation available.
AC092291 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85110.1.
BC050029 mRNA. Translation: AAH50029.1.
CCDSCCDS45419.1. [O95453-1]
CCDS45420.1. [O95453-2]
CCDS58425.1. [O95453-3]
RefSeqNP_001127949.1. NM_001134477.2. [O95453-2]
NP_001229921.1. NM_001242992.1. [O95453-3]
NP_002573.1. NM_002582.3. [O95453-1]
UniGeneHs.253197.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A1RX-ray2.60A/B1-430[»]
2A1SX-ray2.60A/B/C/D1-430[»]
3CTRX-ray2.10A445-540[»]
ProteinModelPortalO95453.
SMRO95453. Positions 1-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111107. 15 interactions.
DIPDIP-31124N.
IntActO95453. 6 interactions.
MINTMINT-3002980.
STRING9606.ENSP00000387911.

PTM databases

PhosphoSiteO95453.

2D gel databases

SWISS-2DPAGEO95453.

Proteomic databases

MaxQBO95453.
PaxDbO95453.
PRIDEO95453.

Protocols and materials databases

DNASU2987.
5073.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341484; ENSP00000345456; ENSG00000140694. [O95453-2]
ENST00000420015; ENSP00000410525; ENSG00000140694. [O95453-3]
ENST00000437198; ENSP00000387911; ENSG00000140694. [O95453-1]
GeneID5073.
KEGGhsa:5073.
UCSCuc010uzc.2. human. [O95453-1]
uc010uze.2. human. [O95453-3]

Organism-specific databases

CTD5073.
GeneCardsGC16M014529.
HGNCHGNC:8609. PARN.
HPACAB011673.
HPA006314.
HPA012010.
MIM604212. gene.
neXtProtNX_O95453.
PharmGKBPA29072.
PA32949.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG145331.
HOGENOMHOG000007285.
HOVERGENHBG053512.
InParanoidO95453.
KOK01148.
OMALEQTDSC.
OrthoDBEOG7GN2MD.
PhylomeDBO95453.
TreeFamTF314502.

Enzyme and pathway databases

BRENDA3.1.13.4. 2681.
ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO95453.
BgeeO95453.
CleanExHS_PARN.
GenevestigatorO95453.

Family and domain databases

Gene3D3.30.1370.50. 1 hit.
3.30.420.10. 2 hits.
3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR014789. PolyA-riboNase_RNA_binding.
IPR001374. R3H_ss-bd.
IPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF04857. CAF1. 1 hit.
PF08675. RNA_bind. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 2 hits.
SSF82708. SSF82708. 1 hit.
PROSITEPS51061. R3H. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPARN. human.
EvolutionaryTraceO95453.
GeneWikiPARN.
Poly(A)-specific_ribonuclease.
GenomeRNAi5073.
NextBio11844.
PROO95453.
SOURCESearch...

Entry information

Entry namePARN_HUMAN
AccessionPrimary (citable) accession number: O95453
Secondary accession number(s): B2RCB3 expand/collapse secondary AC list , B4DDG8, B4DWR4, B4E1H6
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM