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O95453

- PARN_HUMAN

UniProt

O95453 - PARN_HUMAN

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Protein

Poly(A)-specific ribonuclease PARN

Gene
PARN, DAN
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.5 Publications

Catalytic activityi

Exonucleolytic cleavage of poly(A) to 5'-AMP.2 Publications

Cofactori

Divalent metal cations. Mg2+ is the most probable.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi28 – 281Divalent metal cation; catalytic Inferred
Metal bindingi30 – 301Divalent metal cation; catalytic Inferred
Metal bindingi292 – 2921Divalent metal cation; catalytic Inferred
Sitei326 – 3261Interaction with poly(A)
Metal bindingi382 – 3821Divalent metal cation; catalytic Inferred

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. mRNA 3'-UTR binding Source: ProtInc
  3. nuclease activity Source: ProtInc
  4. nucleotide binding Source: InterPro
  5. poly(A) RNA binding Source: UniProtKB
  6. poly(A)-specific ribonuclease activity Source: Reactome
  7. protein binding Source: UniProtKB
  8. protein kinase binding Source: UniProtKB

GO - Biological processi

  1. female gamete generation Source: ProtInc
  2. gene expression Source: Reactome
  3. mRNA metabolic process Source: Reactome
  4. nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: Reactome
  5. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
  6. nuclear-transcribed mRNA poly(A) tail shortening Source: Reactome
  7. nucleic acid phosphodiester bond hydrolysis Source: GOC
  8. RNA metabolic process Source: Reactome
  9. RNA modification Source: ProtInc
  10. RNA phosphodiester bond hydrolysis, exonucleolytic Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

Nonsense-mediated mRNA decay

Keywords - Ligandi

Magnesium, Metal-binding, RNA-binding

Enzyme and pathway databases

BRENDAi3.1.13.4. 2681.
ReactomeiREACT_18355. ATF4 activates genes.
REACT_20514. Deadenylation of mRNA.
REACT_25042. KSRP destabilizes mRNA.

Names & Taxonomyi

Protein namesi
Recommended name:
Poly(A)-specific ribonuclease PARN (EC:3.1.13.4)
Alternative name(s):
Deadenylating nuclease
Deadenylation nuclease
Polyadenylate-specific ribonuclease
Gene namesi
Name:PARN
Synonyms:DAN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:8609. PARN.

Subcellular locationi

Nucleus. Cytoplasm. Nucleusnucleolus
Note: Some nuclear fraction is nucleolar.2 Publications

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. nucleolus Source: UniProtKB-SubCell
  4. nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi28 – 281D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications
Mutagenesisi28 – 281D → 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+). 3 Publications
Mutagenesisi30 – 301E → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications
Mutagenesisi30 – 301E → C: Loss of function in the presence of Mg(2+), Mn(2+), Zn(2+), Co(2+) or Cd(2+). 3 Publications
Mutagenesisi31 – 311F → A: Reduced affinity for poly(A). Loss of activity. 1 Publication
Mutagenesisi34 – 341I → A: Reduced affinity for poly(A). Strongly reduced activity. 1 Publication
Mutagenesisi113 – 1131I → A: Loss of dimerization. Loss of activity. 1 Publication
Mutagenesisi115 – 1151F → A: Reduced affinity for poly(A). Little effect on activity.
Mutagenesisi123 – 1231F → A: Loss of dimerization. Loss of activity. 1 Publication
Mutagenesisi292 – 2921D → A: Loss of function but does not abolish ability to bind RNA. 2 Publications
Mutagenesisi292 – 2921D → 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+). 2 Publications
Mutagenesisi326 – 3261K → A: Reduced affinity for poly(A). Little effect on activity.
Mutagenesisi377 – 3771H → A: Loss of activity. 1 Publication
Mutagenesisi382 – 3821D → A: Loss of function but does not abolish ability to bind RNA. Induces a decrease in degradation of mRNAs containing AREs. 3 Publications
Mutagenesisi382 – 3821D → 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+). 3 Publications
Mutagenesisi557 – 5571S → A: Strong reduction of phosphorylation by MAPKAPK2.

Organism-specific databases

PharmGKBiPA29072.
PA32949.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 639639Poly(A)-specific ribonuclease PARNPRO_0000212851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei163 – 1631Phosphoserine2 Publications
Modified residuei220 – 2201N6-acetyllysine1 Publication
Modified residuei499 – 4991N6-acetyllysine1 Publication
Modified residuei557 – 5571Phosphoserine; by MAPKAPK25 Publications
Modified residuei619 – 6191Phosphoserine2 Publications
Modified residuei623 – 6231Phosphoserine1 Publication
Modified residuei628 – 6281Phosphoserine1 Publication
Modified residuei631 – 6311Phosphothreonine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95453.
PaxDbiO95453.
PRIDEiO95453.

2D gel databases

SWISS-2DPAGEO95453.

PTM databases

PhosphoSiteiO95453.

Expressioni

Tissue specificityi

Ubiquitous.2 Publications

Gene expression databases

ArrayExpressiO95453.
BgeeiO95453.
CleanExiHS_PARN.
GenevestigatoriO95453.

Organism-specific databases

HPAiCAB011673.
HPA006314.
HPA012010.

Interactioni

Subunit structurei

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.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BARD1Q997284EBI-372832,EBI-473181
CSTF2P332405EBI-372832,EBI-711360
NCBP1Q091612EBI-372832,EBI-464743

Protein-protein interaction databases

BioGridi111107. 15 interactions.
DIPiDIP-31124N.
IntActiO95453. 6 interactions.
MINTiMINT-3002980.
STRINGi9606.ENSP00000387911.

Structurei

Secondary structure

1
639
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 2117
Beta strandi23 – 3210
Beta strandi36 – 383
Helixi50 – 6011
Turni61 – 633
Beta strandi66 – 7712
Turni78 – 814
Beta strandi82 – 9211
Beta strandi97 – 1015
Beta strandi105 – 1095
Helixi110 – 1189
Helixi123 – 1275
Helixi136 – 1416
Helixi175 – 1773
Helixi178 – 19215
Helixi207 – 21711
Turni222 – 2243
Beta strandi228 – 2314
Beta strandi237 – 2404
Beta strandi245 – 2484
Turni249 – 2524
Helixi260 – 2656
Helixi271 – 28010
Beta strandi283 – 2886
Helixi290 – 30011
Helixi308 – 31811
Beta strandi320 – 3245
Helixi325 – 3295
Turni332 – 3376
Helixi343 – 3497
Beta strandi360 – 3623
Helixi379 – 39719
Helixi398 – 4003
Beta strandi401 – 4033
Turni413 – 4153
Helixi416 – 4183
Beta strandi419 – 42911
Beta strandi445 – 4517
Helixi458 – 4647
Turni465 – 4673
Beta strandi468 – 47710
Beta strandi480 – 4889
Helixi490 – 4989
Helixi509 – 5135

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A1RX-ray2.60A/B1-430[»]
2A1SX-ray2.60A/B/C/D1-430[»]
3CTRX-ray2.10A445-540[»]
ProteinModelPortaliO95453.
SMRiO95453. Positions 1-514.

Miscellaneous databases

EvolutionaryTraceiO95453.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini178 – 24568R3HAdd
BLAST

Sequence similaritiesi

Belongs to the CAF1 family.
Contains 1 R3H domain.

Phylogenomic databases

eggNOGiNOG145331.
HOGENOMiHOG000007285.
HOVERGENiHBG053512.
InParanoidiO95453.
KOiK01148.
OMAiLEQTDSC.
OrthoDBiEOG7GN2MD.
PhylomeDBiO95453.
TreeFamiTF314502.

Family and domain databases

Gene3Di3.30.1370.50. 1 hit.
3.30.420.10. 2 hits.
3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR014789. PolyA-riboNase_RNA_binding.
IPR001374. R3H_ss-bd.
IPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF04857. CAF1. 1 hit.
PF08675. RNA_bind. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 2 hits.
SSF82708. SSF82708. 1 hit.
PROSITEiPS51061. R3H. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O95453-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MEIIRSNFKS NLHKVYQAIE EADFFAIDGE FSGISDGPSV SALTNGFDTP    50
EERYQKLKKH SMDFLLFQFG LCTFKYDYTD SKYITKSFNF YVFPKPFNRS 100
SPDVKFVCQS SSIDFLASQG FDFNKVFRNG IPYLNQEEER QLREQYDEKR 150
SQANGAGALS YVSPNTSKCP VTIPEDQKKF IDQVVEKIED LLQSEENKNL 200
DLEPCTGFQR KLIYQTLSWK YPKGIHVETL ETEKKERYIV ISKVDEEERK 250
RREQQKHAKE QEELNDAVGF SRVIHAIANS GKLVIGHNML LDVMHTVHQF 300
YCPLPADLSE FKEMTTCVFP RLLDTKLMAS TQPFKDIINN TSLAELEKRL 350
KETPFNPPKV ESAEGFPSYD TASEQLHEAG YDAYITGLCF ISMANYLGSF 400
LSPPKIHVSA RSKLIEPFFN KLFLMRVMDI PYLNLEGPDL QPKRDHVLHV 450
TFPKEWKTSD LYQLFSAFGN IQISWIDDTS AFVSLSQPEQ VKIAVNTSKY 500
AESYRIQTYA EYMGRKQEEK QIKRKWTEDS WKEADSKRLN PQCIPYTLQN 550
HYYRNNSFTA PSTVGKRNLS PSQEEAGLED GVSGEISDTE LEQTDSCAEP 600
LSEGRKKAKK LKRMKKELSP AGSISKNSPA TLFEVPDTW 639
Length:639
Mass (Da):73,451
Last modified:May 1, 1999 - v1
Checksum:i6994BE39384DF7AC
GO
Isoform 2 (identifier: O95453-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-61: Missing.

Note: No experimental confirmation available. Non canonical splice junctions.

Show »
Length:578
Mass (Da):66,574
Checksum:i5E62F237DB650802
GO
Isoform 3 (identifier: O95453-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:593
Mass (Da):67,722
Checksum:i2908EEB765F91D80
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6161Missing in isoform 2. VSP_042846Add
BLAST
Alternative sequencei53 – 9846Missing in isoform 3. VSP_042847Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS45419.1. [O95453-1]
CCDS45420.1. [O95453-2]
CCDS58425.1. [O95453-3]
RefSeqiNP_001127949.1. NM_001134477.2. [O95453-2]
NP_001229921.1. NM_001242992.1. [O95453-3]
NP_002573.1. NM_002582.3. [O95453-1]
UniGeneiHs.253197.

Genome annotation databases

EnsembliENST00000341484; ENSP00000345456; ENSG00000140694. [O95453-2]
ENST00000420015; ENSP00000410525; ENSG00000140694. [O95453-3]
ENST00000437198; ENSP00000387911; ENSG00000140694. [O95453-1]
GeneIDi5073.
KEGGihsa:5073.
UCSCiuc010uzc.2. human. [O95453-1]
uc010uze.2. human. [O95453-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS45419.1. [O95453-1 ]
CCDS45420.1. [O95453-2 ]
CCDS58425.1. [O95453-3 ]
RefSeqi NP_001127949.1. NM_001134477.2. [O95453-2 ]
NP_001229921.1. NM_001242992.1. [O95453-3 ]
NP_002573.1. NM_002582.3. [O95453-1 ]
UniGenei Hs.253197.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali O95453.
SMRi O95453. Positions 1-514.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111107. 15 interactions.
DIPi DIP-31124N.
IntActi O95453. 6 interactions.
MINTi MINT-3002980.
STRINGi 9606.ENSP00000387911.

PTM databases

PhosphoSitei O95453.

2D gel databases

SWISS-2DPAGE O95453.

Proteomic databases

MaxQBi O95453.
PaxDbi O95453.
PRIDEi O95453.

Protocols and materials databases

DNASUi 2987.
5073.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341484 ; ENSP00000345456 ; ENSG00000140694 . [O95453-2 ]
ENST00000420015 ; ENSP00000410525 ; ENSG00000140694 . [O95453-3 ]
ENST00000437198 ; ENSP00000387911 ; ENSG00000140694 . [O95453-1 ]
GeneIDi 5073.
KEGGi hsa:5073.
UCSCi uc010uzc.2. human. [O95453-1 ]
uc010uze.2. human. [O95453-3 ]

Organism-specific databases

CTDi 5073.
GeneCardsi GC16M014529.
HGNCi HGNC:8609. PARN.
HPAi CAB011673.
HPA006314.
HPA012010.
MIMi 604212. gene.
neXtProti NX_O95453.
PharmGKBi PA29072.
PA32949.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG145331.
HOGENOMi HOG000007285.
HOVERGENi HBG053512.
InParanoidi O95453.
KOi K01148.
OMAi LEQTDSC.
OrthoDBi EOG7GN2MD.
PhylomeDBi O95453.
TreeFami TF314502.

Enzyme and pathway databases

BRENDAi 3.1.13.4. 2681.
Reactomei REACT_18355. ATF4 activates genes.
REACT_20514. Deadenylation of mRNA.
REACT_25042. KSRP destabilizes mRNA.

Miscellaneous databases

ChiTaRSi PARN. human.
EvolutionaryTracei O95453.
GeneWikii PARN.
Poly(A)-specific_ribonuclease.
GenomeRNAii 5073.
NextBioi 11844.
PROi O95453.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95453.
Bgeei O95453.
CleanExi HS_PARN.
Genevestigatori O95453.

Family and domain databases

Gene3Di 3.30.1370.50. 1 hit.
3.30.420.10. 2 hits.
3.30.70.330. 1 hit.
InterProi IPR012677. Nucleotide-bd_a/b_plait.
IPR014789. PolyA-riboNase_RNA_binding.
IPR001374. R3H_ss-bd.
IPR006941. RNase_CAF1.
IPR012337. RNaseH-like_dom.
[Graphical view ]
Pfami PF04857. CAF1. 1 hit.
PF08675. RNA_bind. 1 hit.
[Graphical view ]
SUPFAMi SSF53098. SSF53098. 2 hits.
SSF82708. SSF82708. 1 hit.
PROSITEi PS51061. R3H. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. 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.

Entry informationi

Entry nameiPARN_HUMAN
AccessioniPrimary (citable) accession number: O95453
Secondary accession number(s): B2RCB3
, B4DDG8, B4DWR4, B4E1H6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: May 1, 1999
Last modified: September 3, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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