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Q16630

- CPSF6_HUMAN

UniProt

Q16630 - CPSF6_HUMAN

Protein

Cleavage and polyadenylation specificity factor subunit 6

Gene

CPSF6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 2 (07 Feb 2006)
      Previous versions | rss
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    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
    4. protein binding Source: UniProtKB

    GO - Biological processi

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

    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: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:13871. CPSF6.

    Subcellular locationi

    Nucleus 3 Publications
    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. nucleus Source: UniProtKB
    4. paraspeckles Source: UniProtKB
    5. ribonucleoprotein complex Source: MGI

    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.
    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.

    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

    ArrayExpressiQ16630.
    BgeeiQ16630.
    CleanExiHS_CPSF6.
    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
    NUDT21O438095EBI-358410,EBI-355720
    PLSCR1O151622EBI-358410,EBI-740019
    WWP1Q9H0M03EBI-358410,EBI-742157

    Protein-protein interaction databases

    BioGridi116238. 62 interactions.
    DIPiDIP-34501N.
    IntActiQ16630. 28 interactions.
    MINTiMINT-1153789.
    STRINGi9606.ENSP00000391774.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    ProteinModelPortaliQ16630.
    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.
    HOGENOMiHOG000111137.
    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. Align

    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

    MADGVDHIDI YADVGEEFNQ EAEYGGHDQI DLYDDVISPS ANNGDAPEDR    50
    DYMDTLPPTV GDDVGKGAAP NVVYTYTGKR IALYIGNLTW WTTDEDLTEA 100
    VHSLGVNDIL EIKFFENRAN GQSKGFALVG VGSEASSKKL MDLLPKRELH 150
    GQNPVVTPCN KQFLSQFEMQ SRKTTQSGQM SGEGKAGPPG GSSRAAFPQG 200
    GRGRGRFPGA VPGGDRFPGP AGPGGPPPPF PAGQTPPRPP LGPPGPPGPP 250
    GPPPPGQVLP PPLAGPPNRG DRPPPPVLFP GQPFGQPPLG PLPPGPPPPV 300
    PGYGPPPGPP PPQQGPPPPP GPFPPRPPGP LGPPLTLAPP PHLPGPPPGA 350
    PPPAPHVNPA FFPPPTNSGM PTSDSRGPPP TDPYGRPPPY DRGDYGPPGR 400
    EMDTARTPLS EAEFEEIMNR NRAISSSAIS RAVSDASAGD YGSAIETLVT 450
    AISLIKQSKV SADDRCKVLI SSLQDCLHGI ESKSYGSGSR RERSRERDHS 500
    RSREKSRRHK SRSRDRHDDY YRERSRERER HRDRDRDRDR ERDREREYRH 550
    R 551
    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. 1 PublicationCurated
    Sequence conflicti9 – 91D → N in CAA47752. 1 PublicationCurated

    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:
    EMBL
    GenBank
    DDBJ
    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.
    CCDSiCCDS8988.1. [Q16630-1]
    PIRiS57447.
    RefSeqiNP_008938.2. NM_007007.2. [Q16630-1]
    XP_005268646.1. XM_005268589.1. [Q16630-2]
    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 databases

    DMDMi88909266.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS8988.1. [Q16630-1 ]
    PIRi S57447.
    RefSeqi NP_008938.2. NM_007007.2. [Q16630-1 ]
    XP_005268646.1. XM_005268589.1. [Q16630-2 ]
    UniGenei Hs.369606.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali Q16630.
    SMRi Q16630. Positions 80-158.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116238. 62 interactions.
    DIPi DIP-34501N.
    IntActi Q16630. 28 interactions.
    MINTi MINT-1153789.
    STRINGi 9606.ENSP00000391774.

    PTM databases

    PhosphoSitei Q16630.

    Polymorphism databases

    DMDMi 88909266.

    Proteomic databases

    MaxQBi Q16630.
    PaxDbi Q16630.
    PeptideAtlasi Q16630.
    PRIDEi Q16630.

    Protocols and materials databases

    DNASUi 11052.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000266679 ; ENSP00000266679 ; ENSG00000111605 . [Q16630-2 ]
    ENST00000435070 ; ENSP00000391774 ; ENSG00000111605 . [Q16630-1 ]
    GeneIDi 11052.
    KEGGi hsa:11052.
    UCSCi uc001sut.4. human. [Q16630-1 ]
    uc001suu.4. human. [Q16630-2 ]

    Organism-specific databases

    CTDi 11052.
    GeneCardsi GC12P069633.
    HGNCi HGNC:13871. CPSF6.
    HPAi HPA039973.
    MIMi 604979. gene.
    neXtProti NX_Q16630.
    PharmGKBi PA26846.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313287.
    HOGENOMi HOG000111137.
    KOi K14398.
    OMAi SAPNVVY.
    OrthoDBi EOG74TX09.
    PhylomeDBi Q16630.
    TreeFami TF316430.

    Enzyme and pathway databases

    Reactomei REACT_121141. Signaling by FGFR1 fusion mutants.

    Miscellaneous databases

    GeneWikii CPSF6.
    GenomeRNAii 11052.
    NextBioi 41995.
    PROi Q16630.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q16630.
    Bgeei Q16630.
    CleanExi HS_CPSF6.
    Genevestigatori Q16630.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 129 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