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O95453

- PARN_HUMAN

UniProt

O95453 - PARN_HUMAN

Protein

Poly(A)-specific ribonuclease PARN

Gene

PARN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    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; catalyticCurated
    Metal bindingi30 – 301Divalent metal cation; catalyticCurated
    Metal bindingi292 – 2921Divalent metal cation; catalyticCurated
    Sitei326 – 3261Interaction with poly(A)
    Metal bindingi382 – 3821Divalent metal cation; catalyticCurated

    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

    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.

    GO - Cellular componenti

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

    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.6 Publications

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95453.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini178 – 24568R3HPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the CAF1 family.Curated
    Contains 1 R3H domain.PROSITE-ProRule annotation

    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. 1 PublicationVSP_042846Add
    BLAST
    Alternative sequencei53 – 9846Missing in isoform 3. 1 PublicationVSP_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

    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: October 1, 2014
    This is version 126 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