Q16630 (CPSF6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cleavage and polyadenylation specificity factor subunit 6

Alternative name(s):
Cleavage and polyadenylation specificity factor 68 kDa subunit
Short name=CFIm68
Short name=CPSF 68 kDa subunit
Pre-mRNA cleavage factor Im 68 kDa subunit
Protein HPBRII-4/7

Gene names

Name:	CPSF6
Synonyms:	CFIM68

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	551 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. Involved in association with NUDT21/CPSF5 in pre-MRNA 3'-end poly(A) site cleavage and poly(A) addition. CPSF6 binds to cleavage and polyadenylation RNA substrates and promotes RNA looping. Ref.1 Ref.7 Ref.8 Ref.14 Ref.16
Subunit structure	Component of the cleavage factor Im (CFIm) complex, composed at least of 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, SFRS3, SFRS7, SNRNP70 and TRA2B/SFRS10. Ref.1 Ref.7 Ref.9 Ref.10 Ref.14 Ref.16
Subcellular location	Nucleus. Note: In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles. Ref.1 Ref.9 Ref.14
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
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA polyadenylation Inferred from mutant phenotype Ref.14. Source: UniProtKB protein tetramerization Inferred from direct assay Ref.14. Source: UniProtKB
Cellular_component	mRNA cleavage factor complex Inferred from direct assay Ref.14Ref.1. Source: UniProtKB paraspeckles Inferred from direct assay Ref.1. Source: UniProtKB ribonucleoprotein complex Inferred from direct assay PubMed 18809582. Source: MGI
Molecular_function	mRNA binding Inferred from direct assay Ref.16. Source: UniProtKB nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PLSCR1	O15162	2	EBI-358410,EBI-740019
WWP1	Q9H0M0	3	EBI-358410,EBI-742157

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q16630-1)

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: Q16630-2)

The sequence of this isoform differs from the canonical sequence as follows:
     231-231: P → PGNLIKHLVKGTRPLFLETRIPWHMGHSIEEIPIFGLK

Isoform 3 (identifier: Q16630-3)

The sequence of this isoform differs from the canonical sequence as follows:
     188-260: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 551

551

Cleavage and polyadenylation specificity factor subunit 6

PRO_0000081521

Regions

Domain

81 – 161

81

RRM

Region

81 – 161

81

Necessary for interaction with NUDT21/CPSF5

Region

510 – 551

42

Sufficient for nuclear targeting

Compositional bias

208 – 398

191

Pro-rich

Compositional bias

490 – 551

62

Arg-rich

Amino acid modifications

Modified residue

404

1

Phosphothreonine Ref.11

Modified residue

407

1

Phosphothreonine Ref.13

Natural variations

Alternative sequence

188 – 260

73

Missing in isoform 3.

VSP_017191

Alternative sequence

231

1

P → PGNLIKHLVKGTRPLFLETR IPWHMGHSIEEIPIFGLK in isoform 2.

VSP_017192

Experimental info

Mutagenesis

84

1

Y → A: Reduces affinity for UGUA RNA by 40%; when associated with A-128. Ref.16

Mutagenesis

86

1

G → V: Abolishes interaction with NUDT21/CPSF5; when associated with V-87. Ref.9

Mutagenesis

87

1

N → V: Abolishes interaction with NUDT21/CPSF5; when associated with V-86. Ref.9

Mutagenesis

90 – 91

2

WW → AA: Reduces affinity for UGUA RNA by 70%. Strongly reduced affinity for UGUA RNA; when associated with A-94.

Mutagenesis

94

1

D → A: Strongly reduced affinity for UGUA RNA; when associated with 90-A-A-91. Ref.16

Mutagenesis

111

1

E → A: Reduces affinity for UGUA RNA by 85%. Ref.16

Mutagenesis

126

1

F → A: Increases affinity for UGUA RNA by 40%. Ref.16

Mutagenesis

128

1

L → A: Reduces affinity for UGUA RNA by 40%; when associated with A-84. Ref.16

Sequence conflict

9

1

D → N in CAA47751. Ref.2

Sequence conflict

9

1

D → N in CAA47752. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

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551

Helix Strand Turn

Details...

Beta strand

84 – 87

4

Helix

94 – 102

9

Turn

103 – 105

3

Beta strand

112 – 116

5

Turn

118 – 120

3

Beta strand

123 – 129

7

Helix

134 – 143

10

Helix

144 – 146

3

Beta strand

149 – 151

3

Beta strand

155 – 158

4

Helix

161 – 170

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified February 7, 2006. Version 2. Checksum: 721A5DA1B456AA79	FASTA	551	59,210
	10 20 30 40 50 60 MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR DYMDTLPPTV 70 80 90 100 110 120 GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA VHSLGVNDIL EIKFFENRAN 130 140 150 160 170 180 GQSKGFALVG VGSEASSKKL MDLLPKRELH GQNPVVTPCN KQFLSQFEMQ SRKTTQSGQM 190 200 210 220 230 240 SGEGKAGPPG GSSRAAFPQG GRGRGRFPGA VPGGDRFPGP AGPGGPPPPF PAGQTPPRPP 250 260 270 280 290 300 LGPPGPPGPP GPPPPGQVLP PPLAGPPNRG DRPPPPVLFP GQPFGQPPLG PLPPGPPPPV 310 320 330 340 350 360 PGYGPPPGPP PPQQGPPPPP GPFPPRPPGP LGPPLTLAPP PHLPGPPPGA PPPAPHVNPA 370 380 390 400 410 420 FFPPPTNSGM PTSDSRGPPP TDPYGRPPPY DRGDYGPPGR EMDTARTPLS EAEFEEIMNR 430 440 450 460 470 480 NRAISSSAIS RAVSDASAGD YGSAIETLVT AISLIKQSKV SADDRCKVLI SSLQDCLHGI 490 500 510 520 530 540 ESKSYGSGSR RERSRERDHS RSREKSRRHK SRSRDRHDDY YRERSRERER HRDRDRDRDR 550 ERDREREYRH R
	Isoform 2 [UniParc]. Checksum: 1F2B7051251A7E52	FASTA	588	63,471
	10 20 30 40 50 60 MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR DYMDTLPPTV 70 80 90 100 110 120 GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA VHSLGVNDIL EIKFFENRAN 130 140 150 160 170 180 GQSKGFALVG VGSEASSKKL MDLLPKRELH GQNPVVTPCN KQFLSQFEMQ SRKTTQSGQM 190 200 210 220 230 240 SGEGKAGPPG GSSRAAFPQG GRGRGRFPGA VPGGDRFPGP AGPGGPPPPF PGNLIKHLVK 250 260 270 280 290 300 GTRPLFLETR IPWHMGHSIE EIPIFGLKAG QTPPRPPLGP PGPPGPPGPP PPGQVLPPPL 310 320 330 340 350 360 AGPPNRGDRP PPPVLFPGQP FGQPPLGPLP PGPPPPVPGY GPPPGPPPPQ QGPPPPPGPF 370 380 390 400 410 420 PPRPPGPLGP PLTLAPPPHL PGPPPGAPPP APHVNPAFFP PPTNSGMPTS DSRGPPPTDP 430 440 450 460 470 480 YGRPPPYDRG DYGPPGREMD TARTPLSEAE FEEIMNRNRA ISSSAISRAV SDASAGDYGS 490 500 510 520 530 540 AIETLVTAIS LIKQSKVSAD DRCKVLISSL QDCLHGIESK SYGSGSRRER SRERDHSRSR 550 560 570 580 EKSRRHKSRS RDRHDDYYRE RSRERERHRD RDRDRDRERD REREYRHR
	Isoform 3 [UniParc]. Checksum: 464F41AA4386F880	FASTA	478	52,326
	10 20 30 40 50 60 MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR DYMDTLPPTV 70 80 90 100 110 120 GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA VHSLGVNDIL EIKFFENRAN 130 140 150 160 170 180 GQSKGFALVG VGSEASSKKL MDLLPKRELH GQNPVVTPCN KQFLSQFEMQ SRKTTQSGQM 190 200 210 220 230 240 SGEGKAGPPL AGPPNRGDRP PPPVLFPGQP FGQPPLGPLP PGPPPPVPGY GPPPGPPPPQ 250 260 270 280 290 300 QGPPPPPGPF PPRPPGPLGP PLTLAPPPHL PGPPPGAPPP APHVNPAFFP PPTNSGMPTS 310 320 330 340 350 360 DSRGPPPTDP YGRPPPYDRG DYGPPGREMD TARTPLSEAE FEEIMNRNRA ISSSAISRAV 370 380 390 400 410 420 SDASAGDYGS AIETLVTAIS LIKQSKVSAD DRCKVLISSL QDCLHGIESK SYGSGSRRER 430 440 450 460 470 SRERDHSRSR EKSRRHKSRS RDRHDDYYRE RSRERERHRD RDRDRDRERD REREYRHR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human pre-mRNA cleavage factor Im is related to spliceosomal SR proteins and can be reconstituted in vitro from recombinant subunits." Rueegsegger U., Blank D., Keller W. Mol. Cell 1:243-253(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 125-138 AND 162-168, FUNCTION, IDENTIFICATION IN THE CLEAVAGE FACTOR IM COMPLEX, SUBCELLULAR LOCATION. Tissue: Leukemia.
[2]	Fleischhauer K.L. Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). Tissue: Leukemia.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Spleen.
[4]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Heart.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). Tissue: Kidney.
[7]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX.
[8]	"A mechanism for the regulation of pre-mRNA 3' processing by human cleavage factor Im." Brown K.M., Gilmartin G.M. Mol. Cell 12:1467-1476(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"Distinct sequence motifs within the 68-kDa subunit of cleavage factor Im mediate RNA binding, protein-protein interactions, and subcellular localization." Dettwiler S., Aringhieri C., Cardinale S., Keller W., Barabino S.M. J. Biol. Chem. 279:35788-35797(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH NUDT21/CPSF5; SFRS3; SFRS7 AND TRA2B, RNA-BINDING, MUTAGENESIS OF GLY-86 AND ASN-87, SUBCELLULAR LOCATION.
[10]	"Association of polyadenylation cleavage factor I with U1 snRNP." Awasthi S., Alwine J.C. RNA 9:1400-1409(2003) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN A CLEAVAGE FACTOR IM COMPLEX, INTERACTION WITH NUDT21/CPSF5 AND SNRNP70.
[11]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[14]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[15]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"Crystal structure of a human cleavage factor CFI(m)25/CFI(m)68/RNA complex provides an insight into poly(A) site recognition and RNA looping." Yang Q., Coseno M., Gilmartin G.M., Doublie S. Structure 19:368-377(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 13-235 IN COMPLEX WITH NUDT21/CPSF5 AND RNA, FUNCTION, SUBUNIT, MUTAGENESIS OF TYR-84; 90-TRP-TRP-91; ASP-94; GLU-111; PHE-126 AND LEU-128.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X67336 Genomic DNA. Translation: CAA47751.1.
X67337 mRNA. Translation: CAA47752.1.
AK223568 mRNA. Translation: BAD97288.1.
AK292024 mRNA. Translation: BAF84713.1.
CH471054 Genomic DNA. Translation: EAW97215.1.
BC000714 mRNA. Translation: AAH00714.1.
BC005000 mRNA. Translation: AAH05000.1.

IPI

IPI00012998.
IPI00030654.
IPI01025254.

PIR

S57447.

RefSeq

NP_008938.2. NM_007007.2.

UniGene

Hs.369606.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3P5T	X-ray	2.70	L/M/N/O/P/Q	80-161	[»]
3P6Y	X-ray	2.90	C/D/G/H/K/L/O/P	80-161	[»]
3Q2S	X-ray	2.90	C/D	13-235	[»]
3Q2T	X-ray	3.06	C/D	13-235	[»]
4B4N	X-ray	1.81	B	276-290	[»]

ProteinModelPortal

Q16630.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34501N.

IntAct

Q16630. 25 interactions.

MINT

MINT-1153789.

STRING

9606.ENSP00000391774.

PTM databases

PhosphoSite

Q16630.

Polymorphism databases

DMDM

88909266.

Proteomic databases

PaxDb

Q16630.

PeptideAtlas

Q16630.

PRIDE

Q16630.

Protocols and materials databases

DNASU

11052.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000266679; ENSP00000266679; ENSG00000111605.
ENST00000435070; ENSP00000391774; ENSG00000111605.

GeneID

11052.

KEGG

hsa:11052.

UCSC

uc001sut.4. human.
uc001suu.4. human.

Organism-specific databases

CTD

11052.

GeneCards

GC12P069633.

HGNC

HGNC:13871. CPSF6.

HPA

HPA039973.

MIM

604979. gene.

neXtProt

NX_Q16630.

PharmGKB

PA26846.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG313287.

HOGENOM

HOG000111137.

KO

K14398.

OMA

GKGSAPN.

OrthoDB

EOG432101.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q16630.

Bgee

Q16630.

CleanEx

HS_CPSF6.

Genevestigator

Q16630.

GermOnline

ENSG00000111605. Homo sapiens.

Family and domain databases

Gene3D

3.30.70.330. 1 hit.

InterPro

IPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]

SMART

SM00360. RRM. 1 hit.
[Graphical view]

PROSITE

PS50102. RRM. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

GenomeRNAi

11052.

NextBio

41995.

SOURCE

Search...

Entry information

Entry name

CPSF6_HUMAN

Accession

Primary (citable) accession number: Q16630
Secondary accession number(s): A8K7K9 , Q53ES1, Q9BSJ7, Q9BW18

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	February 7, 2006
Last modified:	May 1, 2013
This is version 116 of the entry and version 2 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.