Q8N684 (CPSF7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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=CFIm59
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.
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	Nucleus Probable Ref.13.
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 spliceosome Traceable author statement. Source: Reactome protein tetramerization Inferred from direct assay Ref.13. Source: UniProtKB termination of RNA polymerase II transcription Traceable 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 binding Inferred from electronic annotation. Source: InterPro protein binding Inferred 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

1

.

.

.

.

.

.

.

.

.

.

.

.

.

471

Helix Strand Turn

Details...

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

	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	FASTA	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
	Isoform 3 [UniParc]. Checksum: 37D5BE0605F7A0FB	FASTA	514	56,375
	10 20 30 40 50 60 MGRPESAGGG SRGPFEGGGR ARRAGGIFLT LSILRTRDLP SGAMSEGVDL IDIYADEEFN 70 80 90 100 110 120 QDPEFNNTDQ IDLYDDVLTA TSQPSDDRSS STEPPPPVRQ EPSPKPNNKT PAILYTYSGL 130 140 150 160 170 180 RNRRAAVYVG SFSWWTTDQQ LIQVIRSIGV YDVVELKFAE NRANGQSKGY AEVVVASENS 190 200 210 220 230 240 VHKLLELLPG KVLNGEKVDV RPATRQNLSQ FEAQARKREC VRVPRGGIPP RAHSRDSSDS 250 260 270 280 290 300 ADGRATPSEN LVPSSARVDK PPSVLPYFNR PPSALPLMGL PPPPIPPPPP LSSSFGVPPP 310 320 330 340 350 360 PPGIHYQHLM PPPPRLPPHL AVPPPGAIPP ALHLNPAFFP PPNATVGPPP DTYMKASAPY 370 380 390 400 410 420 NHHGSRDSGP PPSTVSEAEF EDIMKRNRAI SSSAISKAVS GASAGDYSDA IETLLTAIAV 430 440 450 460 470 480 IKQSRVANDE RCRVLISSLK DCLHGIEAKS YSVGASGSSS RKRHRSRERS PSRSRESSRR 490 500 510 HRDLLHNEDR HDDYFQERNR EHERHRDRER DRHH

References

	« Hide 'large scale' referencesShow '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. , 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] (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. , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., 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

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3N9U	X-ray	1.92	C/I	50-182	[»]

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 , C9K0Q4, Q7Z3H9, Q9H025, Q9H9V1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete 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.