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Reviewed, UniProtKB/Swiss-Prot Q8N684 (CPSF7_HUMAN)

Last modified February 9, 2010. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cleavage and polyadenylation specificity factor subunit 7
Alternative name(s):
    Cleavage and polyadenylation specificity factor 59 kDa subunit
      Short name=CPSF 59 kDa subunit
    Pre-mRNA cleavage factor Im 59 kDa subunit
Gene names
Name: CPSF7
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length471 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Probable 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.5

Subunit structure

Probable component of the cleavage factor Im (CFIm) complex, composed at least of NUDT21/CPSF5 and CPSF6 or CPSF7.

Subcellular location

Nucleus Probable.

Sequence similarities

Belongs to the RRM CPSF6/7 family.

Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
   Biological processmRNA processing
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   LigandRNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processRNA splicing

Inferred from Experiment. Source: Reactome

mRNA processing

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ATXN1P542531EBI-746909,EBI-930964

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 471471Cleavage and polyadenylation specificity factor subunit 7
PRO_0000081527

Regions

Domain82 – 16281RRM
Compositional bias51 – 544Poly-Pro
Compositional bias218 – 329112Pro-rich
Compositional bias418 – 46952Arg-rich

Amino acid modifications

Modified residue481Phosphoserine Ref.12
Modified residue721Phosphotyrosine Ref.6
Modified residue731Phosphothreonine Ref.6
Modified residue1971Phosphoserine Ref.9
Modified residue2031Phosphothreonine Ref.12 Ref.10
Modified residue4131Phosphoserine Ref.10 Ref.8
Modified residue4231Phosphoserine Ref.7
Modified residue4291Phosphoserine Ref.7

Natural variations

Alternative sequence176 – 1849Missing in isoform 2.
VSP_017194

Experimental info

Sequence conflict3351A → V in CAD97884. Ref.2
Sequence conflict3531S → F in CAD97884. Ref.2
Sequence conflict3871E → D Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 69529E441D742CF9

FASTA47152,050
        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 

« Hide

Isoform 2.

Checksum: A3E41F7CB8340247
Show »

FASTA46251,096

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]"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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 338-471 (ISOFORMS 1/2).
Tissue: Bone marrow and Embryonic brain.
[3]"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: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Uterus.
[4]"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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-471 (ISOFORMS 1/2).
Tissue: Teratocarcinoma.
[5]"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.
[6]"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: T-cell.
[7]"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: Epithelium.
[8]"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: Epithelium.
[9]"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.
[10]"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.
[11]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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: T-cell.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ275970 mRNA. Translation: CAC81661.1.
BX537888 mRNA. Translation: CAD97884.1. Different initiation.
AL512759 mRNA. Translation: CAC21678.1.
BC018135 mRNA. Translation: AAH18135.1.
AK022591 mRNA. Translation: BAB14118.1. Different initiation.
AK096343 mRNA. Translation: BAG53266.1.
IPIIPI00550821.
IPI00719106.
RefSeqNP_001129512.1.
NP_001136037.1.
NP_079087.3.
UniGeneHs.444552
Hs.718984

3D structure databases

SMRQ8N684. Positions 80-164.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8N684. 8 interactions.
STRINGQ8N684.

PTM databases

PhosphoSiteQ8N684.

Proteomic databases

PRIDEQ8N684.

Genome annotation databases

EnsemblENST00000340437; ENSP00000345412; ENSG00000149532; Homo sapiens. [Genome view]
ENST00000394888; ENSP00000378352; ENSG00000149532; Homo sapiens. [Genome view]
GeneID79869.
KEGGhsa:79869.
UCSCuc001nro.1. human.
uc001nrp.1. human.

Organism-specific databases

CTD79869.
GeneCardsGC11M060926.
H-InvDBHIX0009690.
HGNCHGNC:30098. CPSF7.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09513.
HOGENOMHBG505348.
HOVERGENQ8N684.
InParanoidQ8N684.
OrthoDBEOG92RGSS.
PhylomeDBQ8N684.

Enzyme and pathway databases

ReactomeREACT_125. Processing of Capped Intron-Containing Pre-mRNA.
REACT_1788. Transcription.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ8N684.
BgeeQ8N684.
GenevestigatorQ8N684.
GermOnlineENSG00000149532. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
PfamPF00076. RRM_1. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio69628.
PMAP-CutDBQ8N684.

Entry information

Entry nameCPSF7_HUMAN
AccessionPrimary (citable) accession number: Q8N684
Secondary accession number(s): B3KU04 expand/collapse secondary AC list , Q7Z3H9, Q9H025, Q9H9V1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: October 1, 2002
Last modified: February 9, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents