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Protein

Cleavage and polyadenylation specificity factor subunit 6

Gene

CPSF6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.5 Publications

GO - Molecular functioni

  1. mRNA binding Source: UniProtKB
  2. nucleotide binding Source: InterPro
  3. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. mRNA polyadenylation Source: UniProtKB
  2. mRNA processing Source: UniProtKB
  3. protein tetramerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiREACT_121141. Signaling by FGFR1 fusion mutants.

Names & Taxonomyi

Protein namesi
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 namesi
Name:CPSF6
Synonyms:CFIM68
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:13871. CPSF6.

Subcellular locationi

  1. Nucleus 3 Publications

  2. Note: In punctate subnuclear structures localized adjacent to nuclear speckles, called paraspeckles.

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. mRNA cleavage factor complex Source: UniProtKB
  3. nucleoplasm Source: HPA
  4. nucleus Source: UniProtKB
  5. paraspeckles Source: UniProtKB
  6. ribonucleoprotein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi84 – 841Y → A: Reduces affinity for UGUA RNA by 40%; when associated with A-128. 1 Publication
Mutagenesisi86 – 861G → V: Abolishes interaction with NUDT21/CPSF5; when associated with V-87. 1 Publication
Mutagenesisi87 – 871N → V: Abolishes interaction with NUDT21/CPSF5; when associated with V-86. 1 Publication
Mutagenesisi90 – 912WW → AA: Reduces affinity for UGUA RNA by 70%. Strongly reduced affinity for UGUA RNA; when associated with A-94. 1 Publication
Mutagenesisi94 – 941D → A: Strongly reduced affinity for UGUA RNA; when associated with 90-A-A-91. 1 Publication
Mutagenesisi111 – 1111E → A: Reduces affinity for UGUA RNA by 85%. 1 Publication
Mutagenesisi126 – 1261F → A: Increases affinity for UGUA RNA by 40%. 1 Publication
Mutagenesisi128 – 1281L → A: Reduces affinity for UGUA RNA by 40%; when associated with A-84. 1 Publication

Organism-specific databases

PharmGKBiPA26846.

Polymorphism and mutation databases

BioMutaiCPSF6.
DMDMi88909266.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Cleavage and polyadenylation specificity factor subunit 6PRO_0000081521Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei404 – 4041Phosphothreonine1 Publication
Modified residuei407 – 4071Phosphothreonine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ16630.
PaxDbiQ16630.
PeptideAtlasiQ16630.
PRIDEiQ16630.

PTM databases

PhosphoSiteiQ16630.

Expressioni

Gene expression databases

BgeeiQ16630.
CleanExiHS_CPSF6.
ExpressionAtlasiQ16630. baseline and differential.
GenevestigatoriQ16630.

Organism-specific databases

HPAiHPA039973.

Interactioni

Subunit structurei

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/SFRS10.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARMC7Q9H6L44EBI-358410,EBI-742909
NUDT21O438095EBI-358410,EBI-355720
OTUB2Q96DC93EBI-358410,EBI-746259
PLSCR1O151622EBI-358410,EBI-740019
PPIL1Q9Y3C63EBI-358410,EBI-2557649
TOLLIPQ6FIE93EBI-358410,EBI-10249783
WWP1Q9H0M03EBI-358410,EBI-742157

Protein-protein interaction databases

BioGridi116238. 74 interactions.
DIPiDIP-34501N.
IntActiQ16630. 31 interactions.
MINTiMINT-1153789.
STRINGi9606.ENSP00000391774.

Structurei

Secondary structure

1
551
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi84 – 874Combined sources
Helixi94 – 1029Combined sources
Turni103 – 1053Combined sources
Beta strandi112 – 1165Combined sources
Turni118 – 1203Combined sources
Beta strandi123 – 1297Combined sources
Helixi134 – 14310Combined sources
Helixi144 – 1463Combined sources
Beta strandi149 – 1513Combined sources
Beta strandi155 – 1584Combined sources
Helixi161 – 17010Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P5TX-ray2.70L/M/N/O/P/Q80-161[»]
3P6YX-ray2.90C/D/G/H/K/L/O/P80-161[»]
3Q2SX-ray2.90C/D13-235[»]
3Q2TX-ray3.06C/D13-235[»]
4B4NX-ray1.81B276-290[»]
4U0AX-ray2.05B276-290[»]
4U0BX-ray2.80M/N/O/P/Q/R/S/T/U/V/W/X276-290[»]
4WYMX-ray2.60M/N/O/P/Q/R/S/T/U/V/W276-290[»]
SMRiQ16630. Positions 80-158.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini81 – 16181RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 16181Necessary for interaction with NUDT21/CPSF5Add
BLAST
Regioni510 – 55142Sufficient for nuclear targetingAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi208 – 398191Pro-richAdd
BLAST
Compositional biasi490 – 55162Arg-richAdd
BLAST

Sequence similaritiesi

Belongs to the RRM CPSF6/7 family.Curated
Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG313287.
GeneTreeiENSGT00730000110905.
HOGENOMiHOG000111137.
InParanoidiQ16630.
KOiK14398.
OMAiSAPNVVY.
OrthoDBiEOG74TX09.
PhylomeDBiQ16630.
TreeFamiTF316430.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q16630-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR
60 70 80 90 100
DYMDTLPPTV GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA
110 120 130 140 150
VHSLGVNDIL EIKFFENRAN GQSKGFALVG VGSEASSKKL MDLLPKRELH
160 170 180 190 200
GQNPVVTPCN KQFLSQFEMQ SRKTTQSGQM SGEGKAGPPG GSSRAAFPQG
210 220 230 240 250
GRGRGRFPGA VPGGDRFPGP AGPGGPPPPF PAGQTPPRPP LGPPGPPGPP
260 270 280 290 300
GPPPPGQVLP PPLAGPPNRG DRPPPPVLFP GQPFGQPPLG PLPPGPPPPV
310 320 330 340 350
PGYGPPPGPP PPQQGPPPPP GPFPPRPPGP LGPPLTLAPP PHLPGPPPGA
360 370 380 390 400
PPPAPHVNPA FFPPPTNSGM PTSDSRGPPP TDPYGRPPPY DRGDYGPPGR
410 420 430 440 450
EMDTARTPLS EAEFEEIMNR NRAISSSAIS RAVSDASAGD YGSAIETLVT
460 470 480 490 500
AISLIKQSKV SADDRCKVLI SSLQDCLHGI ESKSYGSGSR RERSRERDHS
510 520 530 540 550
RSREKSRRHK SRSRDRHDDY YRERSRERER HRDRDRDRDR ERDREREYRH

R
Length:551
Mass (Da):59,210
Last modified:February 7, 2006 - v2
Checksum:i721A5DA1B456AA79
GO
Isoform 2 (identifier: Q16630-2) [UniParc]FASTAAdd to basket

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

Show »
Length:588
Mass (Da):63,471
Checksum:i1F2B7051251A7E52
GO
Isoform 3 (identifier: Q16630-3) [UniParc]FASTAAdd to basket

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

Show »
Length:478
Mass (Da):52,326
Checksum:i464F41AA4386F880
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti9 – 91D → N in CAA47751 (Ref. 2) Curated
Sequence conflicti9 – 91D → N in CAA47752 (Ref. 2) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei188 – 26073Missing in isoform 3. 1 PublicationVSP_017191Add
BLAST
Alternative sequencei231 – 2311P → PGNLIKHLVKGTRPLFLETR IPWHMGHSIEEIPIFGLK in isoform 2. 1 PublicationVSP_017192

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS73494.1. [Q16630-2]
CCDS8988.1. [Q16630-1]
PIRiS57447.
RefSeqiNP_001287876.1. NM_001300947.1. [Q16630-2]
NP_008938.2. NM_007007.2. [Q16630-1]
UniGeneiHs.369606.

Genome annotation databases

EnsembliENST00000266679; ENSP00000266679; ENSG00000111605. [Q16630-2]
ENST00000435070; ENSP00000391774; ENSG00000111605. [Q16630-1]
GeneIDi11052.
KEGGihsa:11052.
UCSCiuc001sut.4. human. [Q16630-1]
uc001suu.4. human. [Q16630-2]

Polymorphism and mutation databases

BioMutaiCPSF6.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS73494.1. [Q16630-2]
CCDS8988.1. [Q16630-1]
PIRiS57447.
RefSeqiNP_001287876.1. NM_001300947.1. [Q16630-2]
NP_008938.2. NM_007007.2. [Q16630-1]
UniGeneiHs.369606.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3P5TX-ray2.70L/M/N/O/P/Q80-161[»]
3P6YX-ray2.90C/D/G/H/K/L/O/P80-161[»]
3Q2SX-ray2.90C/D13-235[»]
3Q2TX-ray3.06C/D13-235[»]
4B4NX-ray1.81B276-290[»]
4U0AX-ray2.05B276-290[»]
4U0BX-ray2.80M/N/O/P/Q/R/S/T/U/V/W/X276-290[»]
4WYMX-ray2.60M/N/O/P/Q/R/S/T/U/V/W276-290[»]
SMRiQ16630. Positions 80-158.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116238. 74 interactions.
DIPiDIP-34501N.
IntActiQ16630. 31 interactions.
MINTiMINT-1153789.
STRINGi9606.ENSP00000391774.

PTM databases

PhosphoSiteiQ16630.

Polymorphism and mutation databases

BioMutaiCPSF6.
DMDMi88909266.

Proteomic databases

MaxQBiQ16630.
PaxDbiQ16630.
PeptideAtlasiQ16630.
PRIDEiQ16630.

Protocols and materials databases

DNASUi11052.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000266679; ENSP00000266679; ENSG00000111605. [Q16630-2]
ENST00000435070; ENSP00000391774; ENSG00000111605. [Q16630-1]
GeneIDi11052.
KEGGihsa:11052.
UCSCiuc001sut.4. human. [Q16630-1]
uc001suu.4. human. [Q16630-2]

Organism-specific databases

CTDi11052.
GeneCardsiGC12P069633.
HGNCiHGNC:13871. CPSF6.
HPAiHPA039973.
MIMi604979. gene.
neXtProtiNX_Q16630.
PharmGKBiPA26846.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG313287.
GeneTreeiENSGT00730000110905.
HOGENOMiHOG000111137.
InParanoidiQ16630.
KOiK14398.
OMAiSAPNVVY.
OrthoDBiEOG74TX09.
PhylomeDBiQ16630.
TreeFamiTF316430.

Enzyme and pathway databases

ReactomeiREACT_121141. Signaling by FGFR1 fusion mutants.

Miscellaneous databases

ChiTaRSiCPSF6. human.
GeneWikiiCPSF6.
GenomeRNAii11052.
NextBioi41995.
PROiQ16630.
SOURCEiSearch...

Gene expression databases

BgeeiQ16630.
CleanExiHS_CPSF6.
ExpressionAtlasiQ16630. baseline and differential.
GenevestigatoriQ16630.

Family and domain databases

Gene3Di3.30.70.330. 1 hit.
InterProiIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
[Graphical view]
SMARTiSM00360. RRM. 1 hit.
[Graphical view]
PROSITEiPS50102. RRM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  17. "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.

Entry informationi

Entry nameiCPSF6_HUMAN
AccessioniPrimary (citable) accession number: Q16630
Secondary accession number(s): A8K7K9
, Q53ES1, Q9BSJ7, Q9BW18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 7, 2006
Last sequence update: February 7, 2006
Last modified: April 29, 2015
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.