Q8N684 (CPSF7_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 91.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Cleavage and polyadenylation specificity factor subunit 7 Alternative name(s): Cleavage and polyadenylation specificity factor 59 kDa subunit Short name=CFIm59 Short name=CPSF 59 kDa subunit Pre-mRNA cleavage factor Im 59 kDa subunit | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 471 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Component of the cleavage factor Im complex (CFIm) that plays a key role in pre-mRNA 3' processing. Binds to cleavage and polyadenylation RNA substrates. Ref.6 |
| Subunit structure | 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 NUDT21/CPSF5. Ref.13 Ref.15 |
| Subcellular location | |
| Sequence similarities | Belongs to the RRM CPSF6/7 family. Contains 1 RRM (RNA recognition motif) domain. |
| Sequence caution | The sequence AAH18135.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB14118.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence CAD97884.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. |
Ontologies
| Keywords | |
|---|---|
| Biological process | mRNA processing |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Ligand | RNA-binding |
| PTM | Phosphoprotein |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | mRNA 3'-end processing Traceable author statement. Source: Reactome nuclear mRNA splicing, via spliceosomeTraceable author statement. Source: Reactome protein tetramerizationInferred from direct assay Ref.13. Source: UniProtKB termination of RNA polymerase II transcriptionTraceable author statement. Source: Reactome |
| Cellular component | mRNA cleavage factor complex Inferred from direct assay Ref.13. Source: UniProtKB |
| Molecular function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide bindingInferred from electronic annotation. Source: InterPro protein bindingInferred from physical interaction Ref.13. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| ATXN1 | P54253 | 2 | EBI-746909,EBI-930964 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q8N684-1) 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. | ||||||
| Isoform 2 (identifier: Q8N684-2) The sequence of this isoform differs from the canonical sequence as follows: 176-184: Missing. | ||||||
| Isoform 3 (identifier: Q8N684-3) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → MGRPESAGGGSRGPFEGGGRARRAGGIFLTLSILRTRDLPSGAM |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||
Molecule processing | |||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 471 | 471 | Cleavage and polyadenylation specificity factor subunit 7 | PRO_0000081527 | |||||||||||||||||
Regions | |||||||||||||||||||||
| Domain | 82 – 162 | 81 | RRM | ||||||||||||||||||
| Compositional bias | 51 – 54 | 4 | Poly-Pro | ||||||||||||||||||
| Compositional bias | 218 – 329 | 112 | Pro-rich | ||||||||||||||||||
| Compositional bias | 418 – 469 | 52 | Arg-rich | ||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||
| Modified residue | 48 | 1 | Phosphoserine Ref.12 | ||||||||||||||||||
| Modified residue | 72 | 1 | Phosphotyrosine Ref.7 | ||||||||||||||||||
| Modified residue | 73 | 1 | Phosphothreonine Ref.7 | ||||||||||||||||||
| Modified residue | 197 | 1 | Phosphoserine Ref.10 | ||||||||||||||||||
| Modified residue | 203 | 1 | Phosphothreonine Ref.11 Ref.12 | ||||||||||||||||||
| Modified residue | 413 | 1 | Phosphoserine Ref.9 Ref.11 | ||||||||||||||||||
| Modified residue | 423 | 1 | Phosphoserine Ref.8 | ||||||||||||||||||
| Modified residue | 429 | 1 | Phosphoserine Ref.8 | ||||||||||||||||||
Natural variations | |||||||||||||||||||||
| Alternative sequence | 1 | 1 | M → MGRPESAGGGSRGPFEGGGR ARRAGGIFLTLSILRTRDLP SGAM in isoform 3. | VSP_038975 | |||||||||||||||||
| Alternative sequence | 176 – 184 | 9 | Missing in isoform 2. | VSP_017194 | |||||||||||||||||
Experimental info | |||||||||||||||||||||
| Sequence conflict | 335 | 1 | A → V in CAD97884. Ref.3 | ||||||||||||||||||
| Sequence conflict | 353 | 1 | S → F in CAD97884. Ref.3 | ||||||||||||||||||
| Sequence conflict | 387 | 1 | E → D in BAB14118. Ref.2 | ||||||||||||||||||
Secondary structure | |||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||
| Beta strand | 83 – 86 | 4 | |||||||||||||||||||
| Helix | 95 – 104 | 10 | |||||||||||||||||||
| Beta strand | 110 – 117 | 8 | |||||||||||||||||||
| Beta strand | 127 – 133 | 7 | |||||||||||||||||||
| Helix | 135 – 144 | 10 | |||||||||||||||||||
| Helix | 162 – 176 | 15 | |||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning of a second SR protein related subunit of human pre-mRNA cleavage factor I." Rueegsegger U., Blank D., Dettwiler S., Keller W. Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Cervix carcinoma. |
| [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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Teratocarcinoma. |
| [3] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Bone marrow and Embryonic brain. |
| [4] | "Human chromosome 11 DNA sequence and analysis including novel gene identification." Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. Sakaki Y.Nature 440:497-500(2006) [PubMed: 16554811] [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: 15489334] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Uterus. |
| [6] | "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: 8626397] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, RNA-BINDING. |
| [7] | "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry." Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C. Anal. Chem. 76:2763-2772(2004) [PubMed: 15144186] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-72 AND THR-73, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [8] | "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND SER-429, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [11] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND SER-413, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-48 AND THR-203, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [13] | "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: 20695905] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION. |
| [14] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [15] | "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 50-182 IN COMPLEX WITH NUDT21/CPSF5, SUBUNIT. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AJ275970 mRNA. Translation: CAC81661.1. AK022591 mRNA. Translation: BAB14118.1. Different initiation. AK096343 mRNA. Translation: BAG53266.1. AL512759 mRNA. Translation: CAC21678.1. BX537888 mRNA. Translation: CAD97884.1. Different initiation. AP003108 Genomic DNA. No translation available. BC018135 mRNA. Translation: AAH18135.1. Different initiation. | ||||||||||||
| IPI | IPI00550821. IPI00719106. IPI00915356. | ||||||||||||
| RefSeq | NP_001129512.1. NM_001136040.2. NP_001136037.1. NM_001142565.1. NP_079087.3. NM_024811.3. | ||||||||||||
| UniGene | Hs.718984. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q8N684. | ||||||||||||
| SMR | Q8N684. Positions 82-177. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q8N684. 9 interactions. | ||||||||||||
| MINT | MINT-1469392. | ||||||||||||
| STRING | Q8N684. | ||||||||||||
PTM databases | |||||||||||||
| PhosphoSite | Q8N684. | ||||||||||||
Polymorphism databases | |||||||||||||
| DMDM | 74759932. | ||||||||||||
Proteomic databases | |||||||||||||
| PRIDE | Q8N684. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| Ensembl | ENST00000340437; ENSP00000345412; ENSG00000149532. ENST00000394888; ENSP00000378352; ENSG00000149532. ENST00000413232; ENSP00000393828; ENSG00000149532. | ||||||||||||
| GeneID | 79869. | ||||||||||||
| KEGG | hsa:79869. | ||||||||||||
| UCSC | uc001nro.1. human. uc001nrp.1. human. | ||||||||||||
Organism-specific databases | |||||||||||||
| CTD | 79869. | ||||||||||||
| GeneCards | GC11M061170. | ||||||||||||
| H-InvDB | HIX0009690. | ||||||||||||
| HGNC | HGNC:30098. CPSF7. | ||||||||||||
| HPA | HPA041094. | ||||||||||||
| neXtProt | NX_Q8N684. | ||||||||||||
| GenAtlas | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | prNOG09513. | ||||||||||||
| GeneTree | ENSGT00600000084083. | ||||||||||||
| HOGENOM | HBG505348. | ||||||||||||
| HOVERGEN | HBG056699. | ||||||||||||
| InParanoid | Q8N684. | ||||||||||||
| OMA | MKASTPY. | ||||||||||||
| OrthoDB | EOG44BB2Q. | ||||||||||||
| PhylomeDB | Q8N684. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| Reactome | REACT_1675. mRNA Processing. REACT_1788. Transcription. REACT_71. Gene Expression. REACT_78. Post-Elongation Processing of the Transcript. | ||||||||||||
Gene expression databases | |||||||||||||
| ArrayExpress | Q8N684. | ||||||||||||
| Bgee | Q8N684. | ||||||||||||
| Genevestigator | Q8N684. | ||||||||||||
| GermOnline | ENSG00000149532. Homo sapiens. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. [Graphical view] | ||||||||||||
| Gene3D | G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit. | ||||||||||||
| KO | K14398. | ||||||||||||
| Pfam | PF00076. RRM_1. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00360. RRM. 1 hit. [Graphical view] | ||||||||||||
| PROSITE | PS50102. RRM. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Other | |||||||||||||
| NextBio | 69628. | ||||||||||||
| PMAP-CutDB | Q8N684. | ||||||||||||
Entry information
| Entry name | CPSF7_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q8N684 Secondary accession number(s): B3KU04 Q9H9V1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 11 Human chromosome 11: entries, gene names and cross-references to MIM |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with