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Q9P2I0

- CPSF2_HUMAN

UniProt

Q9P2I0 - CPSF2_HUMAN

Protein

Cleavage and polyadenylation specificity factor subunit 2

Gene

CPSF2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (16 Aug 2004)
      Previous versions | rss
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    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. Involved in the histone 3' end pre-mRNA processing.2 Publications

    GO - Molecular functioni

    1. hydrolase activity Source: InterPro
    2. protein binding Source: UniProtKB
    3. RNA binding Source: UniProtKB-KW

    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: InterPro
    5. mRNA export from nucleus Source: Reactome
    6. mRNA polyadenylation Source: InterPro
    7. mRNA splicing, via spliceosome Source: Reactome
    8. RNA splicing Source: Reactome
    9. termination of RNA polymerase II transcription Source: Reactome
    10. 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_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 2
    Alternative name(s):
    Cleavage and polyadenylation specificity factor 100 kDa subunit
    Short name:
    CPSF 100 kDa subunit
    Gene namesi
    Name:CPSF2
    Synonyms:CPSF100, KIAA1367
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:2325. CPSF2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi67 – 671H → A: Inhibits histone 3'-end processing. 1 Publication
    Mutagenesisi289 – 2891D → A: Does not inhibit histone 3'-end processing. 1 Publication
    Mutagenesisi543 – 5431R → A: Inhibits histone 3'-end processing. 1 Publication

    Organism-specific databases

    PharmGKBiPA26842.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 782782Cleavage and polyadenylation specificity factor subunit 2PRO_0000074393Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei419 – 4191Phosphoserine2 Publications
    Modified residuei420 – 4201Phosphoserine2 Publications
    Modified residuei423 – 4231Phosphoserine3 Publications
    Modified residuei660 – 6601Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9P2I0.
    PaxDbiQ9P2I0.
    PeptideAtlasiQ9P2I0.
    PRIDEiQ9P2I0.

    PTM databases

    PhosphoSiteiQ9P2I0.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9P2I0.
    BgeeiQ9P2I0.
    CleanExiHS_CPSF2.
    GenevestigatoriQ9P2I0.

    Organism-specific databases

    HPAiHPA024238.

    Interactioni

    Subunit structurei

    Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with CPSF3, CSTF2 and SYMPK.3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CSTF2P332402EBI-1043224,EBI-711360
    SYMPKQ927972EBI-1043224,EBI-1051992

    Protein-protein interaction databases

    BioGridi119826. 36 interactions.
    DIPiDIP-42500N.
    IntActiQ9P2I0. 10 interactions.
    MINTiMINT-1697677.
    STRINGi9606.ENSP00000298875.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9P2I0.
    SMRiQ9P2I0. Positions 6-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1236.
    HOGENOMiHOG000264343.
    HOVERGENiHBG051106.
    InParanoidiQ9P2I0.
    KOiK14402.
    OMAiHEERIKW.
    OrthoDBiEOG741Z1H.
    PhylomeDBiQ9P2I0.
    TreeFamiTF106131.

    Family and domain databases

    Gene3Di3.60.15.10. 3 hits.
    InterProiIPR001279. Beta-lactamas-like.
    IPR022712. Beta_Casp.
    IPR027075. CPSF2.
    IPR025069. Cpsf2_C.
    IPR011108. RMMBL.
    [Graphical view]
    PANTHERiPTHR11203:SF5. PTHR11203:SF5. 1 hit.
    PfamiPF10996. Beta-Casp. 1 hit.
    PF13299. CPSF100_C. 1 hit.
    PF00753. Lactamase_B. 1 hit.
    PF07521. RMMBL. 1 hit.
    [Graphical view]
    SMARTiSM01027. Beta-Casp. 1 hit.
    SM00849. Lactamase_B. 1 hit.
    [Graphical view]
    SUPFAMiSSF56281. SSF56281. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    Q9P2I0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTSIIKLTTL SGVQEESALC YLLQVDEFRF LLDCGWDEHF SMDIIDSLRK    50
    HVHQIDAVLL SHPDPLHLGA LPYAVGKLGL NCAIYATIPV YKMGQMFMYD 100
    LYQSRHNTED FTLFTLDDVD AAFDKIQQLK FSQIVNLKGK GHGLSITPLP 150
    AGHMIGGTIW KIVKDGEEEI VYAVDFNHKR EIHLNGCSLE MLSRPSLLIT 200
    DSFNATYVQP RRKQRDEQLL TNVLETLRGD GNVLIAVDTA GRVLELAQLL 250
    DQIWRTKDAG LGVYSLALLN NVSYNVVEFS KSQVEWMSDK LMRCFEDKRN 300
    NPFQFRHLSL CHGLSDLARV PSPKVVLASQ PDLECGFSRD LFIQWCQDPK 350
    NSIILTYRTT PGTLARFLID NPSEKITEIE LRKRVKLEGK ELEEYLEKEK 400
    LKKEAAKKLE QSKEADIDSS DESDIEEDID QPSAHKTKHD LMMKGEGSRK 450
    GSFFKQAKKS YPMFPAPEER IKWDEYGEII KPEDFLVPEL QATEEEKSKL 500
    ESGLTNGDEP MDQDLSDVPT KCISTTESIE IKARVTYIDY EGRSDGDSIK 550
    KIINQMKPRQ LIIVHGPPEA SQDLAECCRA FGGKDIKVYM PKLHETVDAT 600
    SETHIYQVRL KDSLVSSLQF CKAKDAELAW IDGVLDMRVS KVDTGVILEE 650
    GELKDDGEDS EMQVEAPSDS SVIAQQKAMK SLFGDDEKET GEESEIIPTL 700
    EPLPPHEVPG HQSVFMNEPR LSDFKQVLLR EGIQAEFVGG VLVCNNQVAV 750
    RRTETGRIGL EGCLCQDFYR IRDLLYEQYA IV 782
    Length:782
    Mass (Da):88,487
    Last modified:August 16, 2004 - v2
    Checksum:iF67B4813B9883CE8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti289 – 2891D → G in AAH70095. (PubMed:15489334)Curated
    Sequence conflicti654 – 6541K → R in AAH70095. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001627 mRNA. Translation: BAG50953.1.
    CH471061 Genomic DNA. Translation: EAW81480.1.
    BC070095 mRNA. Translation: AAH70095.1.
    AB037788 mRNA. Translation: BAA92605.1.
    AL442079 mRNA. Translation: CAC09445.1.
    CCDSiCCDS9902.1.
    RefSeqiNP_059133.1. NM_017437.2.
    XP_005267824.1. XM_005267767.1.
    UniGeneiHs.657632.
    Hs.736541.

    Genome annotation databases

    GeneIDi53981.
    KEGGihsa:53981.
    UCSCiuc001yah.2. human.

    Polymorphism databases

    DMDMi51338827.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK001627 mRNA. Translation: BAG50953.1 .
    CH471061 Genomic DNA. Translation: EAW81480.1 .
    BC070095 mRNA. Translation: AAH70095.1 .
    AB037788 mRNA. Translation: BAA92605.1 .
    AL442079 mRNA. Translation: CAC09445.1 .
    CCDSi CCDS9902.1.
    RefSeqi NP_059133.1. NM_017437.2.
    XP_005267824.1. XM_005267767.1.
    UniGenei Hs.657632.
    Hs.736541.

    3D structure databases

    ProteinModelPortali Q9P2I0.
    SMRi Q9P2I0. Positions 6-404.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119826. 36 interactions.
    DIPi DIP-42500N.
    IntActi Q9P2I0. 10 interactions.
    MINTi MINT-1697677.
    STRINGi 9606.ENSP00000298875.

    PTM databases

    PhosphoSitei Q9P2I0.

    Polymorphism databases

    DMDMi 51338827.

    Proteomic databases

    MaxQBi Q9P2I0.
    PaxDbi Q9P2I0.
    PeptideAtlasi Q9P2I0.
    PRIDEi Q9P2I0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 53981.
    KEGGi hsa:53981.
    UCSCi uc001yah.2. human.

    Organism-specific databases

    CTDi 53981.
    GeneCardsi GC14P092588.
    HGNCi HGNC:2325. CPSF2.
    HPAi HPA024238.
    MIMi 606028. gene.
    neXtProti NX_Q9P2I0.
    PharmGKBi PA26842.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1236.
    HOGENOMi HOG000264343.
    HOVERGENi HBG051106.
    InParanoidi Q9P2I0.
    KOi K14402.
    OMAi HEERIKW.
    OrthoDBi EOG741Z1H.
    PhylomeDBi Q9P2I0.
    TreeFami TF106131.

    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 CPSF2. human.
    GeneWikii CPSF2.
    GenomeRNAii 53981.
    NextBioi 56268.
    PROi Q9P2I0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9P2I0.
    Bgeei Q9P2I0.
    CleanExi HS_CPSF2.
    Genevestigatori Q9P2I0.

    Family and domain databases

    Gene3Di 3.60.15.10. 3 hits.
    InterProi IPR001279. Beta-lactamas-like.
    IPR022712. Beta_Casp.
    IPR027075. CPSF2.
    IPR025069. Cpsf2_C.
    IPR011108. RMMBL.
    [Graphical view ]
    PANTHERi PTHR11203:SF5. PTHR11203:SF5. 1 hit.
    Pfami PF10996. Beta-Casp. 1 hit.
    PF13299. CPSF100_C. 1 hit.
    PF00753. Lactamase_B. 1 hit.
    PF07521. RMMBL. 1 hit.
    [Graphical view ]
    SMARTi SM01027. Beta-Casp. 1 hit.
    SM00849. Lactamase_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56281. SSF56281. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "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].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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].
      Tissue: Testis.
    4. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
      DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 204-782.
      Tissue: Brain.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 279-782.
      Tissue: Lymph node.
    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. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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 CPSF3; CSTF2 AND SYMPK, MUTAGENESIS OF HIS-67; ASP-289 AND ARG-543.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419; SER-420; SER-423 AND SER-660, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "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-419; SER-420 AND SER-423, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCPSF2_HUMAN
    AccessioniPrimary (citable) accession number: Q9P2I0
    Secondary accession number(s): B3KME1, Q6NSJ1, Q9H3W7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: August 16, 2004
    Last modified: October 1, 2014
    This is version 108 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3