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P33240

- CSTF2_HUMAN

UniProt

P33240 - CSTF2_HUMAN

Protein

Cleavage stimulation factor subunit 2

Gene

CSTF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      Previous versions | rss
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    Functioni

    One of the multiple factors required for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. This subunit is directly involved in the binding to pre-mRNAs By similarity.By similarity

    GO - Molecular functioni

    1. nucleotide binding Source: InterPro
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: IntAct
    4. RNA binding Source: ProtInc

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA 3'-end processing Source: Reactome
    3. mRNA cleavage Source: ProtInc
    4. mRNA polyadenylation Source: ProtInc
    5. mRNA splicing, via spliceosome Source: Reactome
    6. RNA splicing Source: Reactome
    7. termination of RNA polymerase II transcription Source: Reactome
    8. transcription from RNA polymerase II promoter Source: Reactome

    Keywords - Biological processi

    mRNA processing

    Keywords - Ligandi

    RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cleavage stimulation factor subunit 2
    Alternative name(s):
    CF-1 64 kDa subunit
    Cleavage stimulation factor 64 kDa subunit
    Short name:
    CSTF 64 kDa subunit
    Short name:
    CstF-64
    Gene namesi
    Name:CSTF2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:2484. CSTF2.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Localized with DDX1 in cleavage bodies.

    GO - Cellular componenti

    1. cleavage body Source: UniProtKB
    2. mRNA cleavage and polyadenylation specificity factor complex Source: UniProtKB
    3. nucleoplasm Source: Reactome
    4. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26986.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 577577Cleavage stimulation factor subunit 2PRO_0000081531Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei518 – 5181Phosphoserine2 Publications
    Modified residuei524 – 5241Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP33240.
    PaxDbiP33240.
    PRIDEiP33240.

    PTM databases

    PhosphoSiteiP33240.

    Expressioni

    Inductioni

    Up-regulated during the G0 to S phase transition.1 Publication

    Gene expression databases

    ArrayExpressiP33240.
    BgeeiP33240.
    CleanExiHS_CSTF2.
    GenevestigatoriP33240.

    Organism-specific databases

    HPAiCAB004680.
    HPA000427.

    Interactioni

    Subunit structurei

    The CSTF complex is composed of CSTF1 (50 kDa subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF2 directly interacts with CSTF3, SYMPK and RPO2TC1. Interacts with HSF1 in heat-stressed cells. Interacts with CPSF2, CPSF3 and FIP1L1. Interacts with DDX1.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BARD1Q997288EBI-711360,EBI-473181
    CPSF2Q9P2I02EBI-711360,EBI-1043224
    PARNO954535EBI-711360,EBI-372832
    SUB1P539993EBI-711374,EBI-998260

    Protein-protein interaction databases

    BioGridi107860. 42 interactions.
    DIPiDIP-36129N.
    IntActiP33240. 19 interactions.
    MINTiMINT-1375144.
    STRINGi9606.ENSP00000362063.

    Structurei

    Secondary structure

    1
    577
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi12 – 154
    Beta strandi18 – 225
    Helixi29 – 379
    Beta strandi43 – 508
    Turni51 – 544
    Beta strandi55 – 639
    Helixi67 – 7610
    Beta strandi77 – 815
    Beta strandi83 – 853
    Beta strandi87 – 915
    Helixi97 – 1048
    Helixi532 – 5354
    Helixi537 – 5459
    Helixi549 – 5535
    Helixi557 – 5604
    Helixi562 – 57110

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P1TNMR-A8-111[»]
    2J8PNMR-A531-577[»]
    ProteinModelPortaliP33240.
    SMRiP33240. Positions 8-111, 529-577.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33240.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 9479RRMPROSITE-ProRule annotationAdd
    BLAST
    Repeati410 – 41451; approximate
    Repeati415 – 41952
    Repeati420 – 42453
    Repeati425 – 42954; approximate
    Repeati430 – 43455; approximate
    Repeati435 – 43956
    Repeati440 – 44457
    Repeati445 – 44958
    Repeati450 – 45459
    Repeati455 – 459510; approximate
    Repeati460 – 464511
    Repeati465 – 469512; approximate

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni108 – 248141Interactions with CSTF3 and SYMPKAdd
    BLAST
    Regioni410 – 4696012 X 5 AA tandem repeats of M-E-A-R-[AG]Add
    BLAST
    Regioni514 – 57764Interaction with RPO2TC1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi198 – 409212Gly/Pro-richAdd
    BLAST
    Compositional biasi470 – 52657Gly/Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOGENOMiHOG000214373.
    HOVERGENiHBG051145.
    InParanoidiP33240.
    KOiK14407.
    OrthoDBiEOG7N63NZ.
    PhylomeDBiP33240.
    TreeFamiTF314948.

    Family and domain databases

    Gene3Di3.30.70.330. 1 hit.
    InterProiIPR025742. CSTF2_hinge.
    IPR026896. CSTF_C.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view]
    PfamiPF14327. CSTF2_hinge. 1 hit.
    PF14304. CSTF_C. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P33240-1) [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

    MAGLTVRDPA VDRSLRSVFV GNIPYEATEE QLKDIFSEVG PVVSFRLVYD    50
    RETGKPKGYG FCEYQDQETA LSAMRNLNGR EFSGRALRVD NAASEKNKEE 100
    LKSLGTGAPV IESPYGETIS PEDAPESISK AVASLPPEQM FELMKQMKLC 150
    VQNSPQEARN MLLQNPQLAY ALLQAQVVMR IVDPEIALKI LHRQTNIPTL 200
    IAGNPQPVHG AGPGSGSNVS MNQQNPQAPQ AQSLGGMHVN GAPPLMQASM 250
    QGGVPAPGQM PAAVTGPGPG SLAPGGGMQA QVGMPGSGPV SMERGQVPMQ 300
    DPRAAMQRGS LPANVPTPRG LLGDAPNDPR GGTLLSVTGE VEPRGYLGPP 350
    HQGPPMHHVP GHESRGPPPH ELRGGPLPEP RPLMAEPRGP MLDQRGPPLD 400
    GRGGRDPRGI DARGMEARAM EARGLDARGL EARAMEARAM EARAMEARAM 450
    EARAMEVRGM EARGMDTRGP VPGPRGPIPS GMQGPSPINM GAVVPQGSRQ 500
    VPVMQGTGMQ GASIQGGSQP GGFSPGQNQV TPQDHEKAAL IMQVLQLTAD 550
    QIAMLPPEQR QSILILKEQI QKSTGAP 577
    Length:577
    Mass (Da):60,959
    Last modified:February 1, 1994 - v1
    Checksum:iB76595E9BF8FABBD
    GO
    Isoform 2 (identifier: P33240-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         235-251: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:560
    Mass (Da):59,251
    Checksum:iD76823A0FF6363B8
    GO

    Sequence cautioni

    The sequence CAI42681.1 differs from that shown. Reason: Erroneous gene model prediction.

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei235 – 25117Missing in isoform 2. 1 PublicationVSP_014841Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85085 mRNA. Translation: AAA35724.1.
    BT009778 mRNA. Translation: AAP88780.1.
    Z83819, Z95327 Genomic DNA. Translation: CAB06072.2.
    Z95327, Z83819 Genomic DNA. Translation: CAI42680.1.
    Z95327 Genomic DNA. Translation: CAI42681.1. Sequence problems.
    BC017712 mRNA. Translation: AAH17712.1.
    BC033135 mRNA. Translation: AAH33135.1.
    CCDSiCCDS14473.1. [P33240-1]
    PIRiA40220.
    RefSeqiNP_001316.1. NM_001325.2. [P33240-1]
    UniGeneiHs.132370.

    Genome annotation databases

    EnsembliENST00000372972; ENSP00000362063; ENSG00000101811. [P33240-1]
    GeneIDi1478.
    KEGGihsa:1478.
    UCSCiuc004egh.3. human. [P33240-1]
    uc004egi.3. human. [P33240-2]

    Polymorphism databases

    DMDMi461847.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M85085 mRNA. Translation: AAA35724.1 .
    BT009778 mRNA. Translation: AAP88780.1 .
    Z83819 , Z95327 Genomic DNA. Translation: CAB06072.2 .
    Z95327 , Z83819 Genomic DNA. Translation: CAI42680.1 .
    Z95327 Genomic DNA. Translation: CAI42681.1 . Sequence problems.
    BC017712 mRNA. Translation: AAH17712.1 .
    BC033135 mRNA. Translation: AAH33135.1 .
    CCDSi CCDS14473.1. [P33240-1 ]
    PIRi A40220.
    RefSeqi NP_001316.1. NM_001325.2. [P33240-1 ]
    UniGenei Hs.132370.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P1T NMR - A 8-111 [» ]
    2J8P NMR - A 531-577 [» ]
    ProteinModelPortali P33240.
    SMRi P33240. Positions 8-111, 529-577.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107860. 42 interactions.
    DIPi DIP-36129N.
    IntActi P33240. 19 interactions.
    MINTi MINT-1375144.
    STRINGi 9606.ENSP00000362063.

    PTM databases

    PhosphoSitei P33240.

    Polymorphism databases

    DMDMi 461847.

    Proteomic databases

    MaxQBi P33240.
    PaxDbi P33240.
    PRIDEi P33240.

    Protocols and materials databases

    DNASUi 1478.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000372972 ; ENSP00000362063 ; ENSG00000101811 . [P33240-1 ]
    GeneIDi 1478.
    KEGGi hsa:1478.
    UCSCi uc004egh.3. human. [P33240-1 ]
    uc004egi.3. human. [P33240-2 ]

    Organism-specific databases

    CTDi 1478.
    GeneCardsi GC0XP100075.
    HGNCi HGNC:2484. CSTF2.
    HPAi CAB004680.
    HPA000427.
    MIMi 300907. gene.
    neXtProti NX_P33240.
    PharmGKBi PA26986.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOGENOMi HOG000214373.
    HOVERGENi HBG051145.
    InParanoidi P33240.
    KOi K14407.
    OrthoDBi EOG7N63NZ.
    PhylomeDBi P33240.
    TreeFami TF314948.

    Enzyme and pathway databases

    Reactomei REACT_1096. Processing of Intronless Pre-mRNAs.
    REACT_1849. mRNA 3'-end processing.
    REACT_467. mRNA Splicing - Major Pathway.

    Miscellaneous databases

    EvolutionaryTracei P33240.
    GeneWikii CSTF2.
    GenomeRNAii 1478.
    NextBioi 6073.
    PROi P33240.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33240.
    Bgeei P33240.
    CleanExi HS_CSTF2.
    Genevestigatori P33240.

    Family and domain databases

    Gene3Di 3.30.70.330. 1 hit.
    InterProi IPR025742. CSTF2_hinge.
    IPR026896. CSTF_C.
    IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    [Graphical view ]
    Pfami PF14327. CSTF2_hinge. 1 hit.
    PF14304. CSTF_C. 1 hit.
    PF00076. RRM_1. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human 64-kDa polyadenylylation factor contains a ribonucleoprotein-type RNA binding domain and unusual auxiliary motifs."
      Takagaki Y., Macdonald C.C., Shenk T., Manley J.L.
      Proc. Natl. Acad. Sci. U.S.A. 89:1403-1407(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, RNA-BINDING.
    2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    3. "The DNA sequence of the human X chromosome."
      Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
      , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
      Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORMS 1 AND 2).
      Tissue: Kidney and Ovary.
    5. "RNA recognition by the human polyadenylation factor CstF."
      Takagaki Y., Manley J.L.
      Mol. Cell. Biol. 17:3907-3914(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, FUNCTION.
    6. "Increase in the 64-kDa subunit of the polyadenylation/cleavage stimulatory factor during the G0 to S phase transition."
      Martincic K., Campbell R., Edwalds-Gilbert G., Souan L., Lotze M.T., Milcarek C.
      Proc. Natl. Acad. Sci. U.S.A. 95:11095-11100(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    7. "Complex protein interactions within the human polyadenylation machinery identify a novel component."
      Takagaki Y., Manley J.L.
      Mol. Cell. Biol. 20:1515-1525(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CSTF3 AND SYMPK.
    8. "Evolutionarily conserved interaction between CstF-64 and PC4 links transcription, polyadenylation, and termination."
      Calvo O., Manley J.L.
      Mol. Cell 7:1013-1023(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RPO2TC1.
    9. "Association of human DEAD box protein DDX1 with a cleavage stimulation factor involved in 3'-end processing of pre-MRNA."
      Bleoo S., Sun X., Hendzel M.J., Rowe J.M., Packer M., Godbout R.
      Mol. Biol. Cell 12:3046-3059(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX1, SUBCELLULAR LOCATION.
    10. "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: INTERACTION WITH FIP1L1.
    11. "HSF1 modulation of Hsp70 mRNA polyadenylation via interaction with symplekin."
      Xing H., Mayhew C.N., Cullen K.E., Park-Sarge O.-K., Sarge K.D.
      J. Biol. Chem. 279:10551-10555(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HSF1.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    13. "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: INTERACTION WITH CPSF2 AND CPSF3.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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 SER-524, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "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.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "Recognition of GU-rich polyadenylation regulatory elements by human CstF-64 protein."
      Perez Canadillas J.M., Varani G.
      EMBO J. 22:2821-2830(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 8-111.
    21. "The C-terminal domains of vertebrate CstF-64 and its yeast orthologue Rna15 form a new structure critical for mRNA 3'-end processing."
      Qu X., Perez-Canadillas J.M., Agrawal S., De Baecke J., Cheng H., Varani G., Moore C.
      J. Biol. Chem. 282:2101-2115(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 531-577.

    Entry informationi

    Entry nameiCSTF2_HUMAN
    AccessioniPrimary (citable) accession number: P33240
    Secondary accession number(s): Q5H951, Q6LA74, Q8N502
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 143 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 X
      Human chromosome X: 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