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O43809

- CPSF5_HUMAN

UniProt

O43809 - CPSF5_HUMAN

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Protein

Cleavage and polyadenylation specificity factor subunit 5

Gene
NUDT21, CFIM25, CPSF25, CPSF5
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

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
Complete GO annotation...

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 SIRT2.2 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.10 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.

Miscellaneous databases

EvolutionaryTraceiO43809.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini76 – 201126Nudix hydrolaseAdd
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

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

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 128 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.

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

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