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O43809

- CPSF5_HUMAN

UniProt

O43809 - CPSF5_HUMAN

Protein

Cleavage and polyadenylation specificity factor subunit 5

Gene

NUDT21

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    Functioni

    Component of the cleavage factor Im (CFIm) complex that plays a key role in pre-mRNA 3'-processing. Involved in association with CPSF6 or CPSF7 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. NUDT21/CPSF5 binds to cleavage and polyadenylation RNA substrates. The homodimer mediates simultaneous sequence-specific recognition of two 5'-UGUA-3' elements within the pre-mRNA. Binds to, but does not hydrolyze mono- and di-adenosine nucleotides. May have a role in mRNA export.6 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei55 – 551Interaction with RNA
    Sitei63 – 631Interaction with RNA
    Sitei208 – 2081Interaction with RNA

    GO - Molecular functioni

    1. AU-rich element binding Source: UniProtKB
    2. histone deacetylase binding Source: UniProtKB
    3. hydrolase activity Source: InterPro
    4. mRNA binding Source: UniProtKB
    5. poly(A) RNA binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA 3'-end processing Source: Reactome
    3. mRNA polyadenylation Source: UniProtKB
    4. mRNA processing Source: UniProtKB
    5. mRNA splicing, via spliceosome Source: Reactome
    6. protein tetramerization Source: UniProtKB
    7. RNA splicing Source: Reactome
    8. termination of RNA polymerase II transcription Source: Reactome
    9. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cleavage and polyadenylation specificity factor subunit 5
    Alternative name(s):
    Cleavage and polyadenylation specificity factor 25 kDa subunit
    Short name:
    CFIm25
    Short name:
    CPSF 25 kDa subunit
    Nucleoside diphosphate-linked moiety X motif 21
    Short name:
    Nudix motif 21
    Pre-mRNA cleavage factor Im 25 kDa subunit
    Gene namesi
    Name:NUDT21
    Synonyms:CFIM25, CPSF25, CPSF5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:13870. NUDT21.

    Subcellular locationi

    Nucleus 3 Publications
    Note: In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles.

    GO - Cellular componenti

    1. centrosome Source: LIFEdb
    2. mRNA cleavage factor complex Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. paraspeckles Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi23 – 231K → R: Abolishes acetylation. 1 Publication
    Mutagenesisi29 – 291K → R: No effect on acetylation. 1 Publication
    Mutagenesisi55 – 551E → A: Reduces affinity for UGUA RNA by 88%. 2 Publications
    Mutagenesisi63 – 631R → S: Reduces affinity for UGUA RNA by 99%. 2 Publications
    Mutagenesisi81 – 811E → A: Reduces affinity for UGUA RNA by 12%. 1 Publication
    Mutagenesisi103 – 1031F → A: Reduces affinity for UGUA RNA by 99%. 2 Publications
    Mutagenesisi103 – 1031F → W: Reduces affinity for UGUA RNA by over 90%. 2 Publications
    Mutagenesisi154 – 1541E → A: Reduces affinity for UGUA RNA by 50%.
    Mutagenesisi158 – 1581Y → A: Abolishes interaction with CPSF6; when associated with A-160. 1 Publication
    Mutagenesisi160 – 1601Y → A: Abolishes interaction with CPSF6; when associated with A-158. 1 Publication

    Organism-specific databases

    PharmGKBiPA26845.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 227226Cleavage and polyadenylation specificity factor subunit 5PRO_0000057150Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei23 – 231N6-acetyllysine2 Publications
    Modified residuei29 – 291N6-acetyllysine1 Publication
    Modified residuei40 – 401Phosphotyrosine1 Publication
    Modified residuei56 – 561N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylated mainly by p300/CBP, recruited to the complex by CPSF6. Acetylation decreases interaction with PAPAO. Deacetylated by the class I/II HDACs, HDAC1, HDAC3 and HDAC10, and by the class III HDACs, SIRT1 AND SIRT2.3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO43809.
    PaxDbiO43809.
    PeptideAtlasiO43809.
    PRIDEiO43809.

    2D gel databases

    UCD-2DPAGEO43809.

    PTM databases

    PhosphoSiteiO43809.

    Expressioni

    Gene expression databases

    ArrayExpressiO43809.
    BgeeiO43809.
    CleanExiHS_NUDT21.
    GenevestigatoriO43809.

    Organism-specific databases

    HPAiHPA019863.

    Interactioni

    Subunit structurei

    Homodimer. Component of the cleavage factor Im (CFIm) complex, composed of, at least, NUDT21/CPSF5 and CPSF6 or CPSF7. Within the cleavage factor Im complex, the NUDT21/CPSF5 homodimer is at the core of a heterotetramer, and is clasped by two additional subunits (CPSF6 or CPSF7). Interacts with CPSF6, CPSF7, PABPN1 and SNRNP70. Interacts with PAPOLA; the interaction is diminished by acetylation.11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ATXN1P542532EBI-355720,EBI-930964
    CARM1Q86X552EBI-355720,EBI-2339854
    CPSF6Q166305EBI-355720,EBI-358410

    Protein-protein interaction databases

    BioGridi116237. 92 interactions.
    DIPiDIP-42502N.
    IntActiO43809. 55 interactions.
    MINTiMINT-5002263.
    STRINGi9606.ENSP00000300291.

    Structurei

    Secondary structure

    1
    227
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni31 – 333
    Beta strandi36 – 394
    Helixi42 – 443
    Beta strandi45 – 506
    Helixi60 – 7415
    Beta strandi76 – 8813
    Beta strandi91 – 10010
    Beta strandi103 – 1053
    Beta strandi107 – 1104
    Helixi117 – 12913
    Beta strandi132 – 1343
    Beta strandi140 – 15011
    Beta strandi152 – 1554
    Beta strandi158 – 1603
    Beta strandi169 – 17810
    Beta strandi181 – 1888
    Beta strandi192 – 1976
    Helixi198 – 2014
    Helixi205 – 2128
    Helixi215 – 2195
    Beta strandi223 – 2264

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CL3X-ray1.90A21-227[»]
    2J8QX-ray2.30A/B24-227[»]
    3BAPX-ray1.85A1-227[»]
    3BHOX-ray1.80A20-227[»]
    3MDGX-ray2.22A/B1-227[»]
    3MDIX-ray2.07A/B1-227[»]
    3N9UX-ray1.92A/B21-227[»]
    3P5TX-ray2.70A/B/C/D/E/F34-227[»]
    3P6YX-ray2.90A/B/E/F/I/J/M/N34-227[»]
    3Q2SX-ray2.90A/B21-227[»]
    3Q2TX-ray3.06A/B21-227[»]
    ProteinModelPortaliO43809.
    SMRiO43809. Positions 22-227.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43809.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini76 – 201126Nudix hydrolasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 147146Necessary for RNA-bindingAdd
    BLAST
    Regioni81 – 16080Necessary for interactions with PAPOLA and PABPN1Add
    BLAST
    Regioni102 – 1043Interaction with RNA

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi109 – 13022Nudix boxAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Nudix hydrolase family. CPSF5 subfamily.Curated
    Contains 1 nudix hydrolase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG294795.
    HOGENOMiHOG000161320.
    HOVERGENiHBG052968.
    InParanoidiO43809.
    KOiK14397.
    OMAiCLAQWWR.
    OrthoDBiEOG7KSX9M.
    PhylomeDBiO43809.
    TreeFamiTF106356.

    Family and domain databases

    Gene3Di3.90.79.10. 1 hit.
    InterProiIPR016706. Cleav_polyA_spec_factor_su5.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view]
    PANTHERiPTHR13047. PTHR13047. 1 hit.
    PfamiPF13869. NUDIX_2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF017888. CPSF-25. 1 hit.
    SUPFAMiSSF55811. SSF55811. 1 hit.
    PROSITEiPS51462. NUDIX. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O43809-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVVPPNRSQ TGWPRGVTQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK    50
    EPLYEKDSSV AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG 100
    TTFFKLPGGE LNPGEDEVEG LKRLMTEILG RQDGVLQDWV IDDCIGNWWR 150
    PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ EKALFAVPKN YKLVAAPLFE 200
    LYDNAPGYGP IISSLPQLLS RFNFIYN 227
    Length:227
    Mass (Da):26,227
    Last modified:June 1, 1998 - v1
    Checksum:iD204243E57F1CCC5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti57 – 571D → G in CAG33200. 1 PublicationCurated
    Sequence conflicti112 – 1121N → D in CAD97606. (PubMed:17974005)Curated
    Sequence conflicti218 – 2181L → P in CAD97606. (PubMed:17974005)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001810 mRNA. Translation: CAA05026.1.
    CR456919 mRNA. Translation: CAG33200.1.
    BX537360 mRNA. Translation: CAD97606.1.
    AC092140 Genomic DNA. No translation available.
    BC001403 mRNA. Translation: AAH01403.1.
    CCDSiCCDS10760.1.
    RefSeqiNP_008937.1. NM_007006.2.
    UniGeneiHs.528834.

    Genome annotation databases

    EnsembliENST00000300291; ENSP00000300291; ENSG00000167005.
    GeneIDi11051.
    KEGGihsa:11051.
    UCSCiuc002eja.3. human.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001810 mRNA. Translation: CAA05026.1 .
    CR456919 mRNA. Translation: CAG33200.1 .
    BX537360 mRNA. Translation: CAD97606.1 .
    AC092140 Genomic DNA. No translation available.
    BC001403 mRNA. Translation: AAH01403.1 .
    CCDSi CCDS10760.1.
    RefSeqi NP_008937.1. NM_007006.2.
    UniGenei Hs.528834.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CL3 X-ray 1.90 A 21-227 [» ]
    2J8Q X-ray 2.30 A/B 24-227 [» ]
    3BAP X-ray 1.85 A 1-227 [» ]
    3BHO X-ray 1.80 A 20-227 [» ]
    3MDG X-ray 2.22 A/B 1-227 [» ]
    3MDI X-ray 2.07 A/B 1-227 [» ]
    3N9U X-ray 1.92 A/B 21-227 [» ]
    3P5T X-ray 2.70 A/B/C/D/E/F 34-227 [» ]
    3P6Y X-ray 2.90 A/B/E/F/I/J/M/N 34-227 [» ]
    3Q2S X-ray 2.90 A/B 21-227 [» ]
    3Q2T X-ray 3.06 A/B 21-227 [» ]
    ProteinModelPortali O43809.
    SMRi O43809. Positions 22-227.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116237. 92 interactions.
    DIPi DIP-42502N.
    IntActi O43809. 55 interactions.
    MINTi MINT-5002263.
    STRINGi 9606.ENSP00000300291.

    PTM databases

    PhosphoSitei O43809.

    2D gel databases

    UCD-2DPAGE O43809.

    Proteomic databases

    MaxQBi O43809.
    PaxDbi O43809.
    PeptideAtlasi O43809.
    PRIDEi O43809.

    Protocols and materials databases

    DNASUi 11051.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000300291 ; ENSP00000300291 ; ENSG00000167005 .
    GeneIDi 11051.
    KEGGi hsa:11051.
    UCSCi uc002eja.3. human.

    Organism-specific databases

    CTDi 11051.
    GeneCardsi GC16M056463.
    HGNCi HGNC:13870. NUDT21.
    HPAi HPA019863.
    MIMi 604978. gene.
    neXtProti NX_O43809.
    PharmGKBi PA26845.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG294795.
    HOGENOMi HOG000161320.
    HOVERGENi HBG052968.
    InParanoidi O43809.
    KOi K14397.
    OMAi CLAQWWR.
    OrthoDBi EOG7KSX9M.
    PhylomeDBi O43809.
    TreeFami TF106356.

    Enzyme and pathway databases

    Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi NUDT21. human.
    EvolutionaryTracei O43809.
    GeneWikii NUDT21.
    GenomeRNAii 11051.
    NextBioi 41991.
    PROi O43809.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O43809.
    Bgeei O43809.
    CleanExi HS_NUDT21.
    Genevestigatori O43809.

    Family and domain databases

    Gene3Di 3.90.79.10. 1 hit.
    InterProi IPR016706. Cleav_polyA_spec_factor_su5.
    IPR000086. NUDIX_hydrolase_dom.
    IPR015797. NUDIX_hydrolase_dom-like.
    [Graphical view ]
    PANTHERi PTHR13047. PTHR13047. 1 hit.
    Pfami PF13869. NUDIX_2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017888. CPSF-25. 1 hit.
    SUPFAMi SSF55811. SSF55811. 1 hit.
    PROSITEi PS51462. NUDIX. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits."
      Rueegsegger U., Blank D., Keller W.
      Mol. Cell 1:243-253(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-73 AND 183-189, FUNCTION, IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX, SUBCELLULAR LOCATION.
      Tissue: Brain.
    2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Retina.
    4. "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].
    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].
      Tissue: Placenta.
    6. Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-15; 24-50 AND 79-131, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors."
      Rueegsegger U., Beyer K., Keller W.
      J. Biol. Chem. 271:6107-6113(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, RNA-BINDING.
    8. "A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im."
      Brown K.M., Gilmartin G.M.
      Mol. Cell 12:1467-1476(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, RNA-BINDING.
    9. "Association of polyadenylation cleavage factor I with U1 snRNP."
      Awasthi S., Alwine J.C.
      RNA 9:1400-1409(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH CPSF6 AND SNRNP70, IDENTIFICATION BY MASS SPECTROMETRY.
    10. "Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization."
      Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M.
      J. Biol. Chem. 279:35788-35797(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH CPSF6; PAPOLA AND PABPN1, RNA-BINDING, SUBCELLULAR LOCATION.
    11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-40, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "Multiple histone deacetylases and the CREB-binding protein regulate pre-mRNA 3'-end processing."
      Shimazu T., Horinouchi S., Yoshida M.
      J. Biol. Chem. 282:4470-4478(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-23, INTERACTION WITH PAPOLA AND CPSF6, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF LYS-23 AND LYS-29.
    13. "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-23; LYS-29 AND LYS-56, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Evidence that cleavage factor Im is a heterotetrameric protein complex controlling alternative polyadenylation."
      Kim S., Yamamoto J., Chen Y., Aida M., Wada T., Handa H., Yamaguchi Y.
      Genes Cells 15:1003-1013(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Crystal structure of the 25 kDa subunit of human cleavage factor Im."
      Coseno M., Martin G., Berger C., Gilmartin G., Keller W., Doublie S.
      Nucleic Acids Res. 36:3474-3483(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH BETA DIADENOSINE TETRAPHOSPHATE, LACK OF METAL-BINDING, HOMODIMERIZATION.
    17. "The crystal structure of human cleavage and polyadenylation specific factor-5 reveals a dimeric Nudix protein with a conserved catalytic site."
      Tresaugues L., Stenmark P., Schaeler H., Flodin S., Welin M., Nyman T., Hammarstroem M., Moche M., Graeslund S., Nordlund P.
      Proteins 73:1047-1052(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF APO FORM AND IN COMPLEX WITH SULFATE.
    18. "Structural basis of UGUA recognition by the Nudix protein CFI(m)25 and implications for a regulatory role in mRNA 3' processing."
      Yang Q., Gilmartin G.M., Doublie S.
      Proc. Natl. Acad. Sci. U.S.A. 107:10062-10067(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) IN COMPLEXES WITH RNA UGUAAA AND UUGUAU, FUNCTION, SUBUNIT, MUTAGENESIS OF GLU-55; ARG-63; GLU-81 AND PHE-103.
    19. "Crystal structure of the complex between the 25 kDA subunit and the 59 kDA subunit (RRM domain) of human cleavage factor Im."
      Structural genomics consortium (SGC)
      Submitted (JUL-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.92 ANGSTROMS) OF 21-227 IN COMPLEX WITH CPSF7, SUBUNIT.
    20. "Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping."
      Yang Q., Coseno M., Gilmartin G.M., Doublie S.
      Structure 19:368-377(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 21-227 IN COMPLEX WITH CPSF6 AND RNA, FUNCTION, SUBUNIT, MUTAGENESIS OF GLU-55; ARG-63; PHE-103; TYR-158 AND TYR-160.

    Entry informationi

    Entry nameiCPSF5_HUMAN
    AccessioniPrimary (citable) accession number: O43809
    Secondary accession number(s): Q6IB85, Q6NE84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: June 1, 1998
    Last modified: October 1, 2014
    This is version 129 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

    Caution

    Lacks the conserved metal-binding residues in the NUDIX motif and does not have hydrolase activity.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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