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Protein

Cleavage and polyadenylation specificity factor subunit 5

Gene

NUDT21

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • AU-rich element binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • hydrolase activity Source: InterPro
  • mRNA binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • gene expression Source: Reactome
  • mRNA 3'-end processing Source: Reactome
  • mRNA polyadenylation Source: UniProtKB
  • mRNA processing Source: UniProtKB
  • mRNA splicing, via spliceosome Source: Reactome
  • protein tetramerization Source: UniProtKB
  • RNA splicing Source: Reactome
  • termination of RNA polymerase II transcription Source: Reactome
  • 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_387. Cleavage of Growing Transcript in the Termination Region.
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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:13870. NUDT21.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: LIFEdb
  • mRNA cleavage factor complex Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • 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.

Polymorphism and mutation databases

BioMutaiNUDT21.

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

BgeeiO43809.
CleanExiHS_NUDT21.
ExpressionAtlasiO43809. baseline and differential.
GenevisibleiO43809. HS.

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
CPSF7Q8N6844EBI-355720,EBI-746909
GOLGA2Q083793EBI-355720,EBI-618309
TRIM27P143733EBI-355720,EBI-719493

Protein-protein interaction databases

BioGridi116237. 100 interactions.
DIPiDIP-42502N.
IntActiO43809. 57 interactions.
MINTiMINT-5002263.
STRINGi9606.ENSP00000300291.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000015814.
HOGENOMiHOG000161320.
HOVERGENiHBG052968.
InParanoidiO43809.
KOiK14397.
OMAiGDCLAQW.
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

        10         20         30         40         50
MSVVPPNRSQ TGWPRGVTQF GNKYIQQTKP LTLERTINLY PLTNYTFGTK
60 70 80 90 100
EPLYEKDSSV AARFQRMREE FDKIGMRRTV EGVLIVHEHR LPHVLLLQLG
110 120 130 140 150
TTFFKLPGGE LNPGEDEVEG LKRLMTEILG RQDGVLQDWV IDDCIGNWWR
160 170 180 190 200
PNFEPPQYPY IPAHITKPKE HKKLFLVQLQ EKALFAVPKN YKLVAAPLFE
210 220
LYDNAPGYGP IISSLPQLLS RFNFIYN
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 (Ref. 2) Curated
Sequence conflicti112 – 1121N → D in CAD97606 (PubMed:17974005).Curated
Sequence conflicti218 – 2181L → P in CAD97606 (PubMed:17974005).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi116237. 100 interactions.
DIPiDIP-42502N.
IntActiO43809. 57 interactions.
MINTiMINT-5002263.
STRINGi9606.ENSP00000300291.

PTM databases

PhosphoSiteiO43809.

Polymorphism and mutation databases

BioMutaiNUDT21.

2D gel databases

UCD-2DPAGEO43809.

Proteomic databases

MaxQBiO43809.
PaxDbiO43809.
PeptideAtlasiO43809.
PRIDEiO43809.

Protocols and materials databases

DNASUi11051.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11051.
GeneCardsiGC16M056463.
HGNCiHGNC:13870. NUDT21.
HPAiHPA019863.
MIMi604978. gene.
neXtProtiNX_O43809.
PharmGKBiPA26845.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG294795.
GeneTreeiENSGT00390000015814.
HOGENOMiHOG000161320.
HOVERGENiHBG052968.
InParanoidiO43809.
KOiK14397.
OMAiGDCLAQW.
OrthoDBiEOG7KSX9M.
PhylomeDBiO43809.
TreeFamiTF106356.

Enzyme and pathway databases

ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
REACT_1849. mRNA 3'-end processing.
REACT_387. Cleavage of Growing Transcript in the Termination Region.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

ChiTaRSiNUDT21. human.
EvolutionaryTraceiO43809.
GeneWikiiNUDT21.
GenomeRNAii11051.
NextBioi41991.
PROiO43809.
SOURCEiSearch...

Gene expression databases

BgeeiO43809.
CleanExiHS_NUDT21.
ExpressionAtlasiO43809. baseline and differential.
GenevisibleiO43809. HS.

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]
ProtoNetiSearch...

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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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: July 22, 2015
This is version 139 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.