O95453 (PARN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Protein existence	Evidence 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.23 Ref.25
Subcellular location	Nucleus. Cytoplasm. Nucleus › nucleolus. 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 process	Nonsense-mediated mRNA decay
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	Magnesium Metal-binding RNA-binding
Molecular function	Exonuclease Hydrolase Nuclease
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA modification Traceable author statement Ref.1. Source: ProtInc female gamete generation Traceable author statement Ref.1. Source: ProtInc 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
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	mRNA 3'-UTR binding Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro poly(A)-specific ribonuclease activity Traceable author statement. Source: Reactome
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 639

639

Poly(A)-specific ribonuclease PARN

PRO_0000212851

Regions

Domain

178 – 245

68

R3H

Sites

Metal binding

28

1

Divalent metal cation; catalytic Probable

Metal binding

30

1

Divalent metal cation; catalytic Probable

Metal binding

292

1

Divalent metal cation; catalytic Probable

Metal binding

382

1

Divalent metal cation; catalytic Probable

Site

326

1

Interaction with poly(A)

Amino acid modifications

Modified residue

163

1

Phosphoserine Ref.16 Ref.19

Modified residue

220

1

N6-acetyllysine Ref.20

Modified residue

499

1

N6-acetyllysine Ref.20

Modified residue

557

1

Phosphoserine; by MAPKAPK2 Ref.16 Ref.18 Ref.21 Ref.24 Ref.26

Modified residue

587

1

Phosphoserine By similarity

Modified residue

619

1

Phosphoserine Ref.21 Ref.24

Modified residue

623

1

Phosphoserine Ref.24

Modified residue

628

1

Phosphoserine Ref.21

Modified residue

631

1

Phosphothreonine Ref.21

Natural variations

Alternative sequence

1 – 61

61

Missing in isoform 2.

VSP_042846

Alternative sequence

53 – 98

46

Missing in isoform 3.

VSP_042847

Experimental info

Mutagenesis

28

1

D → 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

Mutagenesis

28

1

D → 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

Mutagenesis

30

1

E → 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

Mutagenesis

30

1

E → 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

Mutagenesis

31

1

F → A: Reduced affinity for poly(A). Loss of activity. Ref.25

Mutagenesis

34

1

I → A: Reduced affinity for poly(A). Strongly reduced activity. Ref.25

Mutagenesis

113

1

I → A: Loss of dimerization. Loss of activity. Ref.25

Mutagenesis

115

1

F → A: Reduced affinity for poly(A). Little effect on activity.

Mutagenesis

123

1

F → A: Loss of dimerization. Loss of activity. Ref.25

Mutagenesis

292

1

D → A: Loss of function but does not abolish ability to bind RNA. Ref.10 Ref.15

Mutagenesis

292

1

D → 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

Mutagenesis

326

1

K → A: Reduced affinity for poly(A). Little effect on activity.

Mutagenesis

377

1

H → A: Loss of activity. Ref.25

Mutagenesis

382

1

D → 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

Mutagenesis

382

1

D → 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

Mutagenesis

557

1

S → A: Strong reduction of phosphorylation by MAPKAPK2.

Secondary structure

1

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639

Helix Strand Turn

Details...

Helix

5 – 21

17

Beta strand

23 – 32

10

Beta strand

36 – 38

3

Helix

50 – 60

11

Turn

61 – 63

3

Beta strand

66 – 77

12

Turn

78 – 81

4

Beta strand

82 – 92

11

Beta strand

97 – 101

5

Beta strand

105 – 109

5

Helix

110 – 118

9

Helix

123 – 127

5

Helix

136 – 141

6

Helix

175 – 177

3

Helix

178 – 192

15

Helix

207 – 217

11

Turn

222 – 224

3

Beta strand

228 – 231

4

Beta strand

237 – 240

4

Beta strand

245 – 248

4

Turn

249 – 252

4

Helix

260 – 265

6

Helix

271 – 280

10

Beta strand

283 – 288

6

Helix

290 – 300

11

Helix

308 – 318

11

Beta strand

320 – 324

5

Helix

325 – 329

5

Turn

332 – 337

6

Helix

343 – 349

7

Beta strand

360 – 362

3

Helix

379 – 397

19

Helix

398 – 400

3

Beta strand

401 – 403

3

Turn

413 – 415

3

Helix

416 – 418

3

Beta strand

419 – 429

11

Beta strand

445 – 451

7

Helix

458 – 464

7

Turn

465 – 467

3

Beta strand

468 – 477

10

Beta strand

480 – 488

9

Helix

490 – 498

9

Helix

509 – 513

5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 6994BE39384DF7AC	FASTA	639	73,451
	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
	Isoform 2 [UniParc]. Checksum: 5E62F237DB650802	FASTA	578	66,574
	10 20 30 40 50 60 MDFLLFQFGL CTFKYDYTDS KYITKSFNFY VFPKPFNRSS PDVKFVCQSS SIDFLASQGF 70 80 90 100 110 120 DFNKVFRNGI PYLNQEEERQ LREQYDEKRS QANGAGALSY VSPNTSKCPV TIPEDQKKFI 130 140 150 160 170 180 DQVVEKIEDL LQSEENKNLD LEPCTGFQRK LIYQTLSWKY PKGIHVETLE TEKKERYIVI 190 200 210 220 230 240 SKVDEEERKR REQQKHAKEQ EELNDAVGFS RVIHAIANSG KLVIGHNMLL DVMHTVHQFY 250 260 270 280 290 300 CPLPADLSEF KEMTTCVFPR LLDTKLMAST QPFKDIINNT SLAELEKRLK ETPFNPPKVE 310 320 330 340 350 360 SAEGFPSYDT ASEQLHEAGY DAYITGLCFI SMANYLGSFL SPPKIHVSAR SKLIEPFFNK 370 380 390 400 410 420 LFLMRVMDIP YLNLEGPDLQ PKRDHVLHVT FPKEWKTSDL YQLFSAFGNI QISWIDDTSA 430 440 450 460 470 480 FVSLSQPEQV KIAVNTSKYA ESYRIQTYAE YMGRKQEEKQ IKRKWTEDSW KEADSKRLNP 490 500 510 520 530 540 QCIPYTLQNH YYRNNSFTAP STVGKRNLSP SQEEAGLEDG VSGEISDTEL EQTDSCAEPL 550 560 570 SEGRKKAKKL KRMKKELSPA GSISKNSPAT LFEVPDTW
	Isoform 3 [UniParc]. Checksum: 2908EEB765F91D80	FASTA	593	67,722
	10 20 30 40 50 60 MEIIRSNFKS NLHKVYQAIE EADFFAIDGE FSGISDGPSV SALTNGFDTP EERSSPDVKF 70 80 90 100 110 120 VCQSSSIDFL ASQGFDFNKV FRNGIPYLNQ EEERQLREQY DEKRSQANGA GALSYVSPNT 130 140 150 160 170 180 SKCPVTIPED QKKFIDQVVE KIEDLLQSEE NKNLDLEPCT GFQRKLIYQT LSWKYPKGIH 190 200 210 220 230 240 VETLETEKKE RYIVISKVDE EERKRREQQK HAKEQEELND AVGFSRVIHA IANSGKLVIG 250 260 270 280 290 300 HNMLLDVMHT VHQFYCPLPA DLSEFKEMTT CVFPRLLDTK LMASTQPFKD IINNTSLAEL 310 320 330 340 350 360 EKRLKETPFN PPKVESAEGF PSYDTASEQL HEAGYDAYIT GLCFISMANY LGSFLSPPKI 370 380 390 400 410 420 HVSARSKLIE PFFNKLFLMR VMDIPYLNLE GPDLQPKRDH VLHVTFPKEW KTSDLYQLFS 430 440 450 460 470 480 AFGNIQISWI DDTSAFVSLS QPEQVKIAVN TSKYAESYRI QTYAEYMGRK QEEKQIKRKW 490 500 510 520 530 540 TEDSWKEADS KRLNPQCIPY TLQNHYYRNN SFTAPSTVGK RNLSPSQEEA GLEDGVSGEI 550 560 570 580 590 SDTELEQTDS CAEPLSEGRK KAKKLKRMKK ELSPAGSISK NSPATLFEVP DTW

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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], MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[20]	"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, MASS SPECTROMETRY.
[21]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[22]	"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].
[23]	"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.
[24]	"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, MASS SPECTROMETRY.
[25]	"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.
[26]	"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.

IPI

IPI00294744.

RefSeq

NP_001127949.1. NM_001134477.2.
NP_001229921.1. NM_001242992.1.
NP_002573.1. NM_002582.3.

UniGene

Hs.253197.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2A1R	X-ray	2.60	A/B	1-430	[»]
2A1S	X-ray	2.60	A/B/C/D	1-430	[»]
3CTR	X-ray	2.10	A	445-540	[»]

ProteinModelPortal

O95453.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31124N.

IntAct

O95453. 2 interactions.

STRING

9606.ENSP00000387911.

PTM databases

PhosphoSite

O95453.

2D gel databases

SWISS-2DPAGE

O95453.

Proteomic databases

PaxDb

O95453.

PRIDE

O95453.

Protocols and materials databases

DNASU

2987.
5073.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000341484; ENSP00000345456; ENSG00000140694.
ENST00000420015; ENSP00000410525; ENSG00000140694.
ENST00000437198; ENSP00000387911; ENSG00000140694.

GeneID

5073.

KEGG

hsa:5073.

UCSC

uc010uzc.2. human.

Organism-specific databases

CTD

5073.

GeneCards

GC16M014529.

HGNC

HGNC:8609. PARN.

HPA

CAB011673.
HPA006314.
HPA012010.

MIM

604212. gene.

neXtProt

NX_O95453.

PharmGKB

PA29072.
PA32949.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG145331.

HOGENOM

HOG000007285.

HOVERGEN

HBG053512.

InParanoid

O95453.

KO

K01148.

OMA

LEQTDSC.

Enzyme and pathway databases

BRENDA

3.1.13.4. 2681.

Reactome

REACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpress

O95453.

Bgee

O95453.

CleanEx

HS_PARN.

Genevestigator

O95453.

GermOnline

ENSG00000140694. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR014789. PolyA-riboNase_RNA_binding.
IPR001374. R3H_ss-bd.
IPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view]

Pfam

PF04857. CAF1. 1 hit.
PF01424. R3H. 1 hit.
PF08675. RNA_bind. 1 hit.
[Graphical view]

SUPFAM

SSF53098. RNaseH_fold. 1 hit.

PROSITE

PS51061. R3H. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PARN. human.

EvolutionaryTrace

O95453.

GenomeRNAi

5073.

NextBio

11844.

SOURCE

Search...

Entry information

Entry name

PARN_HUMAN

Accession

Primary (citable) accession number: O95453
Secondary accession number(s): B2RCB3 , B4DDG8, B4DWR4, B4E1H6

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 1, 2005
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 112 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.