Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9UKF6

- CPSF3_HUMAN

UniProt

Q9UKF6 - CPSF3_HUMAN

Protein

Cleavage and polyadenylation specificity factor subunit 3

Gene

CPSF3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 118 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner.4 Publications

    Cofactori

    Binds 2 zinc ions per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi71 – 711Zinc 1
    Metal bindingi73 – 731Zinc 1
    Metal bindingi75 – 751Zinc 2
    Metal bindingi76 – 761Zinc 2
    Metal bindingi158 – 1581Zinc 1
    Metal bindingi179 – 1791Zinc 1
    Metal bindingi179 – 1791Zinc 2
    Active sitei396 – 3961Proton donorSequence Analysis
    Metal bindingi418 – 4181Zinc 2

    GO - Molecular functioni

    1. 5'-3' exonuclease activity Source: UniProtKB
    2. endoribonuclease activity Source: UniProtKB
    3. metal ion binding Source: UniProtKB-KW
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. histone mRNA 3'-end processing Source: UniProtKB
    3. mRNA 3'-end processing Source: Reactome
    4. mRNA cleavage Source: ProtInc
    5. mRNA export from nucleus Source: Reactome
    6. mRNA polyadenylation Source: ProtInc
    7. mRNA splicing, via spliceosome Source: Reactome
    8. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    9. RNA splicing Source: Reactome
    10. termination of RNA polymerase II transcription Source: Reactome
    11. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease, Ribonucleoprotein

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    Metal-binding, RNA-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cleavage and polyadenylation specificity factor subunit 3 (EC:3.1.27.-)
    Alternative name(s):
    Cleavage and polyadenylation specificity factor 73 kDa subunit
    Short name:
    CPSF 73 kDa subunit
    mRNA 3'-end-processing endonuclease CPSF-73
    Gene namesi
    Name:CPSF3
    Synonyms:CPSF73
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:2326. CPSF3.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. mRNA cleavage and polyadenylation specificity factor complex Source: UniProtKB
    2. nucleoplasm Source: Reactome
    3. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi73 – 731H → A: Inhibits histone 3'-end processing. 2 Publications
    Mutagenesisi75 – 762DH → KA: Loss of histone 3'-end processing. 2 Publications
    Mutagenesisi75 – 751D → A: Inhibits histone 3'-end processing. 2 Publications
    Mutagenesisi76 – 761H → A: Inhibits histone 3'-end processing. 2 Publications
    Mutagenesisi334 – 3341S → A: Does not inhibit histone 3'-end processing. 2 Publications
    Mutagenesisi396 – 3961H → A: Inhibits histone 3'-end processing. 2 Publications
    Mutagenesisi462 – 4621K → R: Reduced sumoylation; when associated with R-465 and R-545. 2 Publications
    Mutagenesisi465 – 4651K → R: Reduced sumoylation; when associated with R-462 and R-545. 2 Publications
    Mutagenesisi545 – 5451K → R: Reduced sumoylation; when associated with R-462 and R-465. 2 Publications

    Organism-specific databases

    PharmGKBiPA26843.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 684683Cleavage and polyadenylation specificity factor subunit 3PRO_0000074400Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine2 Publications
    Cross-linki462 – 462Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki465 – 465Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki545 – 545Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei681 – 6811Phosphothreonine1 Publication

    Post-translational modificationi

    Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3.1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UKF6.
    PaxDbiQ9UKF6.
    PeptideAtlasiQ9UKF6.
    PRIDEiQ9UKF6.

    PTM databases

    PhosphoSiteiQ9UKF6.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9UKF6.
    BgeeiQ9UKF6.
    CleanExiHS_CPSF3.
    GenevestigatoriQ9UKF6.

    Organism-specific databases

    HPAiHPA034657.

    Interactioni

    Subunit structurei

    Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF2, CSTF2 and SYMPK. Interacts with TUT1; the interaction is direct and mediates the recruitment of the CPSF complex on the 3'UTR of pre-mRNAs. Interacts with WDR33.5 Publications

    Protein-protein interaction databases

    BioGridi119680. 23 interactions.
    DIPiDIP-42501N.
    IntActiQ9UKF6. 8 interactions.
    MINTiMINT-1742891.
    STRINGi9606.ENSP00000238112.

    Structurei

    Secondary structure

    1
    684
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi10 – 2516
    Beta strandi27 – 326
    Beta strandi35 – 395
    Helixi49 – 524
    Helixi56 – 583
    Helixi61 – 633
    Beta strandi66 – 683
    Helixi74 – 774
    Helixi80 – 867
    Beta strandi91 – 966
    Helixi97 – 11014
    Helixi125 – 1317
    Helixi132 – 1343
    Beta strandi135 – 1384
    Beta strandi144 – 1463
    Beta strandi149 – 1557
    Beta strandi163 – 1697
    Beta strandi172 – 1765
    Beta strandi186 – 1883
    Beta strandi199 – 2046
    Turni206 – 2094
    Helixi215 – 23117
    Beta strandi235 – 2395
    Beta strandi242 – 2454
    Helixi246 – 25914
    Helixi261 – 2633
    Beta strandi268 – 2714
    Helixi275 – 28410
    Turni285 – 2873
    Beta strandi307 – 3104
    Helixi314 – 3163
    Beta strandi321 – 3288
    Helixi335 – 34410
    Beta strandi351 – 3544
    Helixi363 – 3675
    Beta strandi372 – 3754
    Beta strandi381 – 3833
    Beta strandi386 – 3905
    Helixi399 – 40911
    Beta strandi412 – 4198
    Helixi421 – 43515
    Beta strandi444 – 4463
    Beta strandi454 – 4585

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2I7TX-ray2.10A1-459[»]
    2I7VX-ray2.10A1-459[»]
    ProteinModelPortaliQ9UKF6.
    SMRiQ9UKF6. Positions 7-459.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UKF6.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1236.
    HOGENOMiHOG000203394.
    HOVERGENiHBG051107.
    InParanoidiQ9UKF6.
    KOiK14403.
    OMAiEISFSAH.
    OrthoDBiEOG7BW0HT.
    PhylomeDBiQ9UKF6.
    TreeFamiTF105643.

    Family and domain databases

    Gene3Di3.60.15.10. 1 hit.
    InterProiIPR001279. Beta-lactamas-like.
    IPR022712. Beta_Casp.
    IPR021718. CPSF73-100_C.
    IPR011108. RMMBL.
    [Graphical view]
    PfamiPF10996. Beta-Casp. 1 hit.
    PF11718. CPSF73-100_C. 1 hit.
    PF00753. Lactamase_B. 1 hit.
    PF07521. RMMBL. 1 hit.
    [Graphical view]
    SMARTiSM01027. Beta-Casp. 1 hit.
    SM01098. CPSF73-100_C. 1 hit.
    SM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9UKF6-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAIPAEESD QLLIRPLGAG QEVGRSCIIL EFKGRKIMLD CGIHPGLEGM    50
    DALPYIDLID PAEIDLLLIS HFHLDHCGAL PWFLQKTSFK GRTFMTHATK 100
    AIYRWLLSDY VKVSNISADD MLYTETDLEE SMDKIETINF HEVKEVAGIK 150
    FWCYHAGHVL GAAMFMIEIA GVKLLYTGDF SRQEDRHLMA AEIPNIKPDI 200
    LIIESTYGTH IHEKREEREA RFCNTVHDIV NRGGRGLIPV FALGRAQELL 250
    LILDEYWQNH PELHDIPIYY ASSLAKKCMA VYQTYVNAMN DKIRKQININ 300
    NPFVFKHISN LKSMDHFDDI GPSVVMASPG MMQSGLSREL FESWCTDKRN 350
    GVIIAGYCVE GTLAKHIMSE PEEITTMSGQ KLPLKMSVDY ISFSAHTDYQ 400
    QTSEFIRALK PPHVILVHGE QNEMARLKAA LIREYEDNDE VHIEVHNPRN 450
    TEAVTLNFRG EKLAKVMGFL ADKKPEQGQR VSGILVKRNF NYHILSPCDL 500
    SNYTDLAMST VKQTQAIPYT GPFNLLCYQL QKLTGDVEEL EIQEKPALKV 550
    FKNITVIQEP GMVVLEWLAN PSNDMYADTV TTVILEVQSN PKIRKGAVQK 600
    VSKKLEMHVY SKRLEIMLQD IFGEDCVSVK DDSILSVTVD GKTANLNLET 650
    RTVECEEGSE DDESLREMVE LAAQRLYEAL TPVH 684
    Length:684
    Mass (Da):77,486
    Last modified:May 1, 2000 - v1
    Checksum:iF8AA24EA6FB78377
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti142 – 1421E → G.1 Publication
    Corresponds to variant rs17850770 [ dbSNP | Ensembl ].
    VAR_037646
    Natural varianti578 – 5781D → N in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035873

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171877 mRNA. Translation: AAF00224.1.
    AC080162 Genomic DNA. Translation: AAY14858.1.
    CH471053 Genomic DNA. Translation: EAX00989.1.
    BC011654 mRNA. Translation: AAH11654.1.
    BC020211 mRNA. Translation: AAH20211.1.
    AF017269 mRNA. Translation: AAB70268.1.
    CCDSiCCDS1664.1.
    RefSeqiNP_057291.1. NM_016207.3.
    UniGeneiHs.515972.

    Genome annotation databases

    EnsembliENST00000238112; ENSP00000238112; ENSG00000119203.
    GeneIDi51692.
    KEGGihsa:51692.
    UCSCiuc002qzo.2. human.

    Polymorphism databases

    DMDMi18203503.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF171877 mRNA. Translation: AAF00224.1 .
    AC080162 Genomic DNA. Translation: AAY14858.1 .
    CH471053 Genomic DNA. Translation: EAX00989.1 .
    BC011654 mRNA. Translation: AAH11654.1 .
    BC020211 mRNA. Translation: AAH20211.1 .
    AF017269 mRNA. Translation: AAB70268.1 .
    CCDSi CCDS1664.1.
    RefSeqi NP_057291.1. NM_016207.3.
    UniGenei Hs.515972.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2I7T X-ray 2.10 A 1-459 [» ]
    2I7V X-ray 2.10 A 1-459 [» ]
    ProteinModelPortali Q9UKF6.
    SMRi Q9UKF6. Positions 7-459.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119680. 23 interactions.
    DIPi DIP-42501N.
    IntActi Q9UKF6. 8 interactions.
    MINTi MINT-1742891.
    STRINGi 9606.ENSP00000238112.

    PTM databases

    PhosphoSitei Q9UKF6.

    Polymorphism databases

    DMDMi 18203503.

    Proteomic databases

    MaxQBi Q9UKF6.
    PaxDbi Q9UKF6.
    PeptideAtlasi Q9UKF6.
    PRIDEi Q9UKF6.

    Protocols and materials databases

    DNASUi 51692.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000238112 ; ENSP00000238112 ; ENSG00000119203 .
    GeneIDi 51692.
    KEGGi hsa:51692.
    UCSCi uc002qzo.2. human.

    Organism-specific databases

    CTDi 51692.
    GeneCardsi GC02P009514.
    HGNCi HGNC:2326. CPSF3.
    HPAi HPA034657.
    MIMi 606029. gene.
    neXtProti NX_Q9UKF6.
    PharmGKBi PA26843.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1236.
    HOGENOMi HOG000203394.
    HOVERGENi HBG051107.
    InParanoidi Q9UKF6.
    KOi K14403.
    OMAi EISFSAH.
    OrthoDBi EOG7BW0HT.
    PhylomeDBi Q9UKF6.
    TreeFami TF105643.

    Enzyme and pathway databases

    Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_1835. Transport of Mature mRNA Derived from an Intronless Transcript.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    ChiTaRSi CPSF3. human.
    EvolutionaryTracei Q9UKF6.
    GeneWikii CPSF3.
    GenomeRNAii 51692.
    NextBioi 55702.
    PROi Q9UKF6.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UKF6.
    Bgeei Q9UKF6.
    CleanExi HS_CPSF3.
    Genevestigatori Q9UKF6.

    Family and domain databases

    Gene3Di 3.60.15.10. 1 hit.
    InterProi IPR001279. Beta-lactamas-like.
    IPR022712. Beta_Casp.
    IPR021718. CPSF73-100_C.
    IPR011108. RMMBL.
    [Graphical view ]
    Pfami PF10996. Beta-Casp. 1 hit.
    PF11718. CPSF73-100_C. 1 hit.
    PF00753. Lactamase_B. 1 hit.
    PF07521. RMMBL. 1 hit.
    [Graphical view ]
    SMARTi SM01027. Beta-Casp. 1 hit.
    SM01098. CPSF73-100_C. 1 hit.
    SM00849. Lactamase_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56281. SSF56281. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Homo sapiens mRNA for CPSF (cleavage and polyadenylation specificity factor) 73 kDa subunit."
      Yu S., Chen W., Pang X., Dong X., Wang H.
      Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Hepatoma.
    2. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANT GLY-142.
      Tissue: Brain and Uterus.
    5. "H. sapiens mRNA for the 73 kDa subunit of CPSF (cleavage and polyadenylation specificity factor, partial cds)."
      Pusch W.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 120-498.
    6. "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and stimulates poly(A) polymerase."
      Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.
      EMBO J. 23:616-626(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PRE-MRNA 3'-END PROCESSING, IDENTIFICATION IN THE CPSF COMPLEX.
    7. "Evidence that polyadenylation factor CPSF-73 is the mRNA 3' processing endonuclease."
      Ryan K., Calvo O., Manley J.L.
      RNA 10:565-573(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Sumoylation modulates the assembly and activity of the pre-mRNA 3' processing complex."
      Vethantham V., Rao N., Manley J.L.
      Mol. Cell. Biol. 27:8848-8858(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-462; LYS-465 AND LYS-545, MUTAGENESIS OF LYS-462; LYS-465 AND LYS-545.
    9. "Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation."
      Kolev N.G., Yario T.A., Benson E., Steitz J.A.
      EMBO Rep. 9:1013-1018(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CPSF2; CSTF2 AND SYMPK, MUTAGENESIS OF HIS-73; ASP-75; HIS-76; SER-334 AND HIS-396.
    10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    11. "Molecular architecture of the human pre-mRNA 3' processing complex."
      Shi Y., Di Giammartino D.C., Taylor D., Sarkeshik A., Rice W.J., Yates J.R. III, Frank J., Manley J.L.
      Mol. Cell 33:365-376(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WDR33.
    12. "The poly A polymerase Star-PAP controls 3'-end cleavage by promoting CPSF interaction and specificity toward the pre-mRNA."
      Laishram R.S., Anderson R.A.
      EMBO J. 29:4132-4145(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE CPSF COMPLEX, INTERACTION WITH TUT1.
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-681, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease."
      Mandel C.R., Kaneko S., Zhang H., Gebauer D., Vethantham V., Manley J.L., Tong L.
      Nature 444:953-956(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-459 IN COMPLEX WITH ZINC IONS, FUNCTION, MUTAGENESIS OF 75-ASP-HIS-76.
    17. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-578.

    Entry informationi

    Entry nameiCPSF3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UKF6
    Secondary accession number(s): O14769, Q53RS2, Q96F36
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 118 of the entry and version 1 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, Reference proteome

    Documents

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

    External Data

    Dasty 3