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UniProtKB/Swiss-Prot entry Q8N684


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CPSF7_HUMAN
Primary accession number Q8N684
Secondary accession numbers Q7Z3H9 Q9H025 Q9H9V1
Integrated into Swiss-Prot on February 7, 2006
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 56)
Name and origin of the protein
Protein name Cleavage and polyadenylation specificity factor subunit 7
Synonyms Cleavage and polyadenylation specificity factor 59 kDa subunit
CPSF 59 kDa subunit
Pre-mRNA cleavage factor Im 59 kDa subunit
Gene name
Name: CPSF7
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cervix carcinoma;
Rueegsegger U., Blank D., Dettwiler S., Keller W.;
"Cloning of a second SR protein related subunit of human pre-mRNA cleavage factor I.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-471 (ISOFORMS 1/2).
TISSUE=Bone marrow, and Embryonic brain;
The German cDNA consortium;
Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-471 (ISOFORMS 1/2).
TISSUE=Teratocarcinoma;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, AND RNA-BINDING.
DOI=10.1074/jbc.271.11.6107; PubMed=8626397 [NCBI, ExPASy, EBI, Israel, Japan]
Rueegsegger U., Beyer K., Keller W.;
"Purification and characterization of human cleavage factor Im involved in the 3' end processing of messenger RNA precursors.";
J. Biol. Chem. 271:6107-6113(1996).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-72 AND THR-73, AND MASS SPECTROMETRY.
TISSUE=T-cell;
DOI=10.1021/ac035352d; PubMed=15144186 [NCBI, ExPASy, EBI, Israel, Japan]
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423 AND SER-429, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-203 AND SER-413, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ275970; CAC81661.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BX537888; CAD97884.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL512759; CAC21678.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018135; AAH18135.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK022591; BAB14118.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_079087.2; -.
UniGene Hs.444552
3D structure databases
ModBase Q8N684.
Protein-protein interaction databases
IntAct Q8N684; -.
PTM databases
PhosphoSite Q8N684; -.
Enzyme and pathway databases
Reactome REACT_1675; mRNA Processing.
REACT_1788; Transcription.
REACT_71; Gene Expression.
Organism-specific databases
H-InvDB HIX0009690; -.
GeneCards Q8N684.
Gene expression databases
ArrayExpress Q8N684; -.
GermOnline ENSG00000149532; Homo sapiens.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from UniProtKB-KW).
GO:0000166; Molecular function: nucleotide binding (inferred from electronic annotation from InterPro).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0003723; Molecular function: RNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0000398; Biological process: nuclear mRNA splicing, via spliceosome (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
Pfam PF00076; RRM_1; 1.
Pfam graphical view of domain structure.
SMART SM00360; RRM; 1.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q8N684.
Genome annotation databases
Ensembl ENSG00000149532; Homo sapiens. [Contig view]
GeneID 79869; -.
KEGG hsa:79869; -.
Phylogenomic databases
HOGENOM Q8N684; -.
HOVERGEN Q8N684; -.
Other
NextBio 69628; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; mRNA processing; Nucleus; Phosphoprotein; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   471  471     Cleavage and polyadenylation specificity factor subunit 7. PRO_0000081527
DOMAIN   82   162  81     RRM. 
COMPBIAS   51    54  4     Poly-Pro. 
COMPBIAS   218   329  112     Pro-rich. 
COMPBIAS   418   469  52     Arg-rich. 
MOD_RES   72    72        Phosphotyrosine. 
MOD_RES   73    73        Phosphothreonine. 
MOD_RES   197   197        Phosphoserine. 
MOD_RES   203   203        Phosphothreonine. 
MOD_RES   413   413        Phosphoserine. 
MOD_RES   423   423        Phosphoserine. 
MOD_RES   429   429        Phosphoserine. 
VAR_SEQ   176   184        Missing (in isoform 2). VSP_017194
CONFLICT   335   335        A -> V (in Ref. 2; CAD97884). 
CONFLICT   353   353        S -> F (in Ref. 2; CAD97884). 
CONFLICT   387   387        E -> D (in Ref. 4). 
Sequence information
Length: 471 AA [This is the length of the unprocessed precursor] Molecular weight: 52050 Da [This is the MW of the unprocessed precursor] CRC64: 69529E441D742CF9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSEGVDLIDI YADEEFNQDP EFNNTDQIDL YDDVLTATSQ PSDDRSSSTE PPPPVRQEPS 

        70         80         90        100        110        120 
PKPNNKTPAI LYTYSGLRNR RAAVYVGSFS WWTTDQQLIQ VIRSIGVYDV VELKFAENRA 

       130        140        150        160        170        180 
NGQSKGYAEV VVASENSVHK LLELLPGKVL NGEKVDVRPA TRQNLSQFEA QARKRECVRV 

       190        200        210        220        230        240 
PRGGIPPRAH SRDSSDSADG RATPSENLVP SSARVDKPPS VLPYFNRPPS ALPLMGLPPP 

       250        260        270        280        290        300 
PIPPPPPLSS SFGVPPPPPG IHYQHLMPPP PRLPPHLAVP PPGAIPPALH LNPAFFPPPN 

       310        320        330        340        350        360 
ATVGPPPDTY MKASAPYNHH GSRDSGPPPS TVSEAEFEDI MKRNRAISSS AISKAVSGAS 

       370        380        390        400        410        420 
AGDYSDAIET LLTAIAVIKQ SRVANDERCR VLISSLKDCL HGIEAKSYSV GASGSSSRKR 

       430        440        450        460        470 
HRSRERSPSR SRESSRRHRD LLHNEDRHDD YFQERNREHE RHRDRERDRH H 

Q8N684 in FASTA format

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Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
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