Reviewed, UniProtKB/Swiss-Prot Q8N684 (CPSF7_HUMAN)

Names 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=CPSF 59 kDa subunit
    Pre-mRNA cleavage factor Im 59 kDa subunit

Gene names

Name:

CPSF7

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.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Subunit structure	Probable component of the cleavage factor Im (CFIm) complex, composed at least of NUDT21/CPSF5 and CPSF6 or CPSF7.
Subcellular location	NucleusProbable.
Sequence similarities	Belongs to the RRM CPSF6/7 family. Contains 1 RRM (RNA recognition motif) domain.

Ontologies

Keywords
Biological process	mRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Ligand	RNA-binding
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	nuclear mRNA splicing, via spliceosome Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ATXN1	P54253	1	EBI-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 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	72	1	Phosphotyrosine
	Modified residue	73	1	Phosphothreonine
	Modified residue	197	1	Phosphoserine
	Modified residue	203	1	Phosphothreonine By similarity
	Modified residue	413	1	Phosphoserine
	Modified residue	423	1	Phosphoserine
	Modified residue	429	1	Phosphoserine
Natural variations
	Alternative sequence	176 – 184	9	Missing in isoform 2.		VSP_017194
Experimental info
	Sequence conflict	335	1	A → V in CAD97884. Ref.2
	Sequence conflict	353	1	S → F in CAD97884. Ref.2
	Sequence conflict	387	1	E → D Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 69529E441D742CF9	FASTA	471	52,050
	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
	Isoform 2 [UniParc]. Checksum: A3E41F7CB8340247		462	51,096
	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 QARKRIPPRA 190 200 210 220 230 240 HSRDSSDSAD GRATPSENLV PSSARVDKPP SVLPYFNRPP SALPLMGLPP PPIPPPPPLS 250 260 270 280 290 300 SSFGVPPPPP GIHYQHLMPP PPRLPPHLAV PPPGAIPPAL HLNPAFFPPP NATVGPPPDT 310 320 330 340 350 360 YMKASAPYNH HGSRDSGPPP STVSEAEFED IMKRNRAISS SAISKAVSGA SAGDYSDAIE 370 380 390 400 410 420 TLLTAIAVIK QSRVANDERC RVLISSLKDC LHGIEAKSYS VGASGSSSRK RHRSRERSPS 430 440 450 460 RSRESSRRHR DLLHNEDRHD DYFQERNREH ERHRDRERDR HH

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 German cDNA consortium Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases 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. , 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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
RefSeq	NP_079087.2.
UniGene	Hs.444552 Hs.702348
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8N684.
PTM databases
PhosphoSite	Q8N684.
Genome annotation databases
Ensembl	ENSG00000149532. Homo sapiens. [Contig view]
GeneID	79869.
KEGG	hsa:79869.
Organism-specific databases
H-InvDB	HIX0009690.
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q8N684.
HOVERGEN	Q8N684.
Enzyme and pathway databases
Reactome	REACT_1675. mRNA Processing. REACT_1788. Transcription. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q8N684.
GermOnline	ENSG00000149532. Homo sapiens.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR000504. RRM_RNP1. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
Pfam	PF00076. RRM_1. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. [Graphical view]
BLOCKS	Search...
ProtoNet	Search...
Other Resources
NextBio	69628.

Entry information

Entry name

CPSF7_HUMAN

Accession

Primary (citable) accession number: Q8N684
Secondary accession number(s): Q7Z3H9, Q9H025, Q9H9V1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	October 1, 2002
Last modified:	November 4, 2008
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)