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Q92945

- FUBP2_HUMAN

UniProt

Q92945 - FUBP2_HUMAN

Protein

Far upstream element-binding protein 2

Gene

KHSRP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 4 (30 Nov 2010)
      Previous versions | rss
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    Functioni

    Binds to the dendritic targeting element and may play a role in mRNA trafficking By similarity. Part of a ternary complex that binds to the downstream control sequence (DCS) of the pre-mRNA. Mediates exon inclusion in transcripts that are subject to tissue-specific alternative splicing. May interact with single-stranded DNA from the far-upstream element (FUSE). May activate gene expression. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly by recruiting degradation machinery to ARE-containing mRNAs.By similarity3 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. poly(A) RNA binding Source: UniProtKB

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA metabolic process Source: Reactome
    3. mRNA processing Source: ProtInc
    4. mRNA transport Source: UniProtKB-KW
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. RNA metabolic process Source: Reactome
    7. RNA splicing Source: UniProtKB
    8. RNA splicing, via transesterification reactions Source: UniProtKB
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA processing, mRNA splicing, mRNA transport, Transcription, Transcription regulation, Transport

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_18355. ATF4 activates genes.
    REACT_25042. KSRP destabilizes mRNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Far upstream element-binding protein 2
    Short name:
    FUSE-binding protein 2
    Alternative name(s):
    KH type-splicing regulatory protein
    Short name:
    KSRP
    p75
    Gene namesi
    Name:KHSRP
    Synonyms:FUBP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:6316. KHSRP.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: A small proportion is also found in the cytoplasm of neuronal cell bodies and dendrites.By similarity

    GO - Cellular componenti

    1. cytoplasmic stress granule Source: Ensembl
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleoplasm Source: Reactome
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30097.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 711710Far upstream element-binding protein 2PRO_0000050137Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine3 Publications
    Modified residuei87 – 871N6-acetyllysineBy similarity
    Modified residuei100 – 1001Phosphothreonine1 Publication
    Modified residuei181 – 1811Phosphoserine7 Publications
    Modified residuei184 – 1841PhosphoserineBy similarity
    Modified residuei193 – 1931Phosphoserine1 Publication
    Modified residuei274 – 2741Phosphoserine2 Publications
    Modified residuei480 – 4801Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylation at Ser-193 leads to the unfolding of the unstable KH domain 1, creating a site for 14-3-3 YWHAZ binding, which promotes nuclear localization and impairs the RNA degradation function.9 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ92945.
    PaxDbiQ92945.
    PRIDEiQ92945.

    2D gel databases

    REPRODUCTION-2DPAGEQ92945.

    PTM databases

    PhosphoSiteiQ92945.

    Miscellaneous databases

    PMAP-CutDBQ92945.

    Expressioni

    Tissue specificityi

    Detected in neural and non-neural cell lines.

    Gene expression databases

    ArrayExpressiQ92945.
    BgeeiQ92945.
    CleanExiHS_KHSRP.
    GenevestigatoriQ92945.

    Organism-specific databases

    HPAiHPA034739.
    HPA056518.

    Interactioni

    Subunit structurei

    Part of a ternary complex containing FUBP2, PTBP1, PTBP2 and HNRPH1. Interacts with PARN.2 Publications

    Protein-protein interaction databases

    BioGridi114139. 49 interactions.
    DIPiDIP-48484N.
    IntActiQ92945. 15 interactions.
    MINTiMINT-2813544.
    STRINGi9606.ENSP00000381216.

    Structurei

    Secondary structure

    1
    711
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi132 – 1343
    Helixi141 – 1444
    Beta strandi146 – 1516
    Helixi153 – 1597
    Turni161 – 1633
    Helixi165 – 17410
    Beta strandi179 – 1835
    Beta strandi188 – 1947
    Helixi198 – 21619
    Beta strandi234 – 2407
    Turni242 – 2443
    Turni245 – 2495
    Turni251 – 2533
    Helixi254 – 2618
    Beta strandi265 – 2695
    Beta strandi271 – 2733
    Beta strandi275 – 2795
    Beta strandi281 – 2877
    Helixi289 – 30214
    Beta strandi306 – 3083
    Turni317 – 3193
    Beta strandi325 – 3306
    Turni331 – 3333
    Helixi334 – 3385
    Beta strandi340 – 3423
    Helixi343 – 35210
    Beta strandi355 – 3584
    Beta strandi363 – 37513
    Helixi376 – 39318
    Beta strandi400 – 4056
    Turni413 – 4153
    Beta strandi427 – 4326
    Helixi433 – 4353
    Turni436 – 4383
    Turni441 – 4444
    Helixi446 – 4538
    Beta strandi454 – 4607
    Beta strandi472 – 4798
    Helixi481 – 49414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HH2NMR-A424-525[»]
    2HH3NMR-A318-418[»]
    2JVZNMR-A233-396[»]
    2OPUNMR-A130-218[»]
    2OPVNMR-A221-305[»]
    4B8TNMR-A317-418[»]
    ProteinModelPortaliQ92945.
    SMRiQ92945. Positions 130-503.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ92945.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini144 – 20865KH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini233 – 29967KH 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini322 – 38665KH 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini424 – 49168KH 4PROSITE-ProRule annotationAdd
    BLAST
    Repeati571 – 582121Add
    BLAST
    Repeati617 – 628122Add
    BLAST
    Repeati643 – 654123Add
    BLAST
    Repeati673 – 684124Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni571 – 6841144 X 12 AA imperfect repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi7 – 6761Gly/Pro-richAdd
    BLAST
    Compositional biasi68 – 496429Gly-richAdd
    BLAST
    Compositional biasi498 – 612115Ala/Gly/Pro-richAdd
    BLAST

    Domaini

    KH domains KH 3 and KH 4 behave as independent binding modules and can interact with different regions of the AU-rich RNA targets of degradation.

    Sequence similaritiesi

    Belongs to the KHSRP family.Curated
    Contains 4 KH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG300923.
    HOGENOMiHOG000231552.
    HOVERGENiHBG000625.
    InParanoidiQ92945.
    KOiK13210.
    OMAiGPMGPFN.
    OrthoDBiEOG77Q4WB.
    PhylomeDBiQ92945.
    TreeFamiTF313654.

    Family and domain databases

    Gene3Di3.30.1370.10. 4 hits.
    InterProiIPR015096. DUF1897.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view]
    PfamiPF09005. DUF1897. 2 hits.
    PF00013. KH_1. 4 hits.
    [Graphical view]
    SMARTiSM00322. KH. 4 hits.
    [Graphical view]
    SUPFAMiSSF54791. SSF54791. 4 hits.
    PROSITEiPS50084. KH_TYPE_1. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q92945-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDYSTGGPP PGPPPPAGGG GGAGGAGGGP PPGPPGAGDR GGGGPGGGGP    50
    GGGSAGGPSQ PPGGGGPGIR KDAFADAVQR ARQIAAKIGG DAATTVNNST 100
    PDFGFGGQKR QLEDGDQPES KKLASQGDSI SSQLGPIHPP PRTSMTEEYR 150
    VPDGMVGLII GRGGEQINKI QQDSGCKVQI SPDSGGLPER SVSLTGAPES 200
    VQKAKMMLDD IVSRGRGGPP GQFHDNANGG QNGTVQEIMI PAGKAGLVIG 250
    KGGETIKQLQ ERAGVKMILI QDGSQNTNVD KPLRIIGDPY KVQQACEMVM 300
    DILRERDQGG FGDRNEYGSR IGGGIDVPVP RHSVGVVIGR SGEMIKKIQN 350
    DAGVRIQFKQ DDGTGPEKIA HIMGPPDRCE HAARIINDLL QSLRSGPPGP 400
    PGGPGMPPGG RGRGRGQGNW GPPGGEMTFS IPTHKCGLVI GRGGENVKAI 450
    NQQTGAFVEI SRQLPPNGDP NFKLFIIRGS PQQIDHAKQL IEEKIEGPLC 500
    PVGPGPGGPG PAGPMGPFNP GPFNQGPPGA PPHAGGPPPH QYPPQGWGNT 550
    YPQWQPPAPH DPSKAAAAAA DPNAAWAAYY SHYYQQPPGP VPGPAPAPAA 600
    PPAQGEPPQP PPTGQSDYTK AWEEYYKKIG QQPQQPGAPP QQDYTKAWEE 650
    YYKKQAQVAT GGGPGAPPGS QPDYSAAWAE YYRQQAAYYG QTPGPGGPQP 700
    PPTQQGQQQA Q 711
    Length:711
    Mass (Da):73,115
    Last modified:November 30, 2010 - v4
    Checksum:iAB0B7C0B5B938114
    GO

    Sequence cautioni

    The sequence AAH85004.1 differs from that shown. Reason: Aberrant splicing.
    The sequence AAC50892.1 differs from that shown. Reason: Frameshift at positions 304, 309, 466 and 473.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti46 – 461G → C in AAB53222. (PubMed:9136930)Curated
    Sequence conflicti46 – 461G → C in AAD29861. (PubMed:10087204)Curated
    Sequence conflicti96 – 961V → G in AAC50892. (PubMed:8940189)Curated
    Sequence conflicti406 – 4072MP → I in AAC50892. (PubMed:8940189)Curated
    Sequence conflicti422 – 4221Missing in AAC50892. (PubMed:8940189)Curated
    Sequence conflicti487 – 4882AK → CR in AAC50892. (PubMed:8940189)Curated
    Sequence conflicti694 – 6963GPG → VP in AAC50892. (PubMed:8940189)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94832 mRNA. Translation: AAB53222.1.
    AC011491 Genomic DNA. No translation available.
    AC011539 Genomic DNA. No translation available.
    BC085004 mRNA. Translation: AAH85004.1. Sequence problems.
    AF093747, AF093745 Genomic DNA. Translation: AAD29861.1.
    AF093748 Genomic DNA. Translation: AAD29862.1.
    U69126 mRNA. Translation: AAC50892.1. Frameshift.
    AB209662 mRNA. Translation: BAD92899.1.
    CCDSiCCDS45936.1.
    RefSeqiNP_003676.2. NM_003685.2.
    UniGeneiHs.727344.

    Genome annotation databases

    EnsembliENST00000398148; ENSP00000381216; ENSG00000088247.
    GeneIDi8570.
    KEGGihsa:8570.
    UCSCiuc002mer.4. human.

    Polymorphism databases

    DMDMi313104306.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U94832 mRNA. Translation: AAB53222.1 .
    AC011491 Genomic DNA. No translation available.
    AC011539 Genomic DNA. No translation available.
    BC085004 mRNA. Translation: AAH85004.1 . Sequence problems.
    AF093747 , AF093745 Genomic DNA. Translation: AAD29861.1 .
    AF093748 Genomic DNA. Translation: AAD29862.1 .
    U69126 mRNA. Translation: AAC50892.1 . Frameshift.
    AB209662 mRNA. Translation: BAD92899.1 .
    CCDSi CCDS45936.1.
    RefSeqi NP_003676.2. NM_003685.2.
    UniGenei Hs.727344.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HH2 NMR - A 424-525 [» ]
    2HH3 NMR - A 318-418 [» ]
    2JVZ NMR - A 233-396 [» ]
    2OPU NMR - A 130-218 [» ]
    2OPV NMR - A 221-305 [» ]
    4B8T NMR - A 317-418 [» ]
    ProteinModelPortali Q92945.
    SMRi Q92945. Positions 130-503.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114139. 49 interactions.
    DIPi DIP-48484N.
    IntActi Q92945. 15 interactions.
    MINTi MINT-2813544.
    STRINGi 9606.ENSP00000381216.

    Chemistry

    ChEMBLi CHEMBL1795105.

    PTM databases

    PhosphoSitei Q92945.

    Polymorphism databases

    DMDMi 313104306.

    2D gel databases

    REPRODUCTION-2DPAGE Q92945.

    Proteomic databases

    MaxQBi Q92945.
    PaxDbi Q92945.
    PRIDEi Q92945.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398148 ; ENSP00000381216 ; ENSG00000088247 .
    GeneIDi 8570.
    KEGGi hsa:8570.
    UCSCi uc002mer.4. human.

    Organism-specific databases

    CTDi 8570.
    GeneCardsi GC19M006413.
    H-InvDB HIX0040083.
    HGNCi HGNC:6316. KHSRP.
    HPAi HPA034739.
    HPA056518.
    MIMi 603445. gene.
    neXtProti NX_Q92945.
    PharmGKBi PA30097.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300923.
    HOGENOMi HOG000231552.
    HOVERGENi HBG000625.
    InParanoidi Q92945.
    KOi K13210.
    OMAi GPMGPFN.
    OrthoDBi EOG77Q4WB.
    PhylomeDBi Q92945.
    TreeFami TF313654.

    Enzyme and pathway databases

    Reactomei REACT_18355. ATF4 activates genes.
    REACT_25042. KSRP destabilizes mRNA.

    Miscellaneous databases

    ChiTaRSi KHSRP. human.
    EvolutionaryTracei Q92945.
    GeneWikii KHSRP.
    GenomeRNAii 8570.
    NextBioi 32149.
    PMAP-CutDB Q92945.
    PROi Q92945.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q92945.
    Bgeei Q92945.
    CleanExi HS_KHSRP.
    Genevestigatori Q92945.

    Family and domain databases

    Gene3Di 3.30.1370.10. 4 hits.
    InterProi IPR015096. DUF1897.
    IPR004087. KH_dom.
    IPR004088. KH_dom_type_1.
    [Graphical view ]
    Pfami PF09005. DUF1897. 2 hits.
    PF00013. KH_1. 4 hits.
    [Graphical view ]
    SMARTi SM00322. KH. 4 hits.
    [Graphical view ]
    SUPFAMi SSF54791. SSF54791. 4 hits.
    PROSITEi PS50084. KH_TYPE_1. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A new regulatory protein, KSRP, mediates exon inclusion through an intronic splicing enhancer."
      Min H., Turck C.W., Nikolic J.M., Black D.L.
      Genes Dev. 11:1023-1036(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 72-85; 123-128; 267-281; 283-291; 348-359; 474-488; 489-494; 621-627; 629-646 AND 647-653, FUNCTION.
      Tissue: Neuroblastoma and Retinoblastoma.
    2. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      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: Ovary.
    4. "Mapping of the KHSRP gene to a region of conserved synteny on human chromosome 19p13.3 and mouse chromosome 17."
      Ring H.Z., Vameghi-Meyers V., Nikolic J.M., Min H., Black D.L., Francke U.
      Genomics 56:350-352(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-115 AND 573-711.
    5. "The far upstream element-binding proteins comprise an ancient family of single-strand DNA-binding transactivators."
      Davis-Smyth T., Duncan R.C., Zheng T., Michelotti G., Levens D.
      J. Biol. Chem. 271:31679-31687(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 60-711, FUNCTION.
      Tissue: B-cell lymphoma and Skeletal muscle.
    6. Lubec G., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 151-162; 321-331 AND 385-394, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Fetal brain cortex.
    7. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 183-566.
      Tissue: Brain.
    8. "Cooperative assembly of an hnRNP complex induced by a tissue-specific homolog of polypyrimidine tract binding protein."
      Markovtsov V., Nikolic J.M., Goldman J.A., Turck C.W., Chou M.-Y., Black D.L.
      Mol. Cell. Biol. 20:7463-7479(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PTBP1; PTBP2 AND HNRPH1.
    9. "A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery."
      Gherzi R., Lee K.-Y., Briata P., Wegmueller D., Moroni C., Karin M., Chen C.-Y.
      Mol. Cell 14:571-583(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARN.
    10. "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-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    13. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-100; SER-181 AND SER-274, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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].
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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-181, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "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 SER-181 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    19. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181; SER-274 AND SER-480, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "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].
    22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "The structure of the C-terminal KH domains of KSRP reveals a noncanonical motif important for mRNA degradation."
      Garcia-Mayoral M.F., Hollingworth D., Masino L., Diaz-Moreno I., Kelly G., Gherzi R., Chou C.F., Chen C.Y., Ramos A.
      Structure 15:485-498(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 218-418 AND 423-525.
    24. "Phosphorylation-mediated unfolding of a KH domain regulates KSRP localization via 14-3-3 binding."
      Diaz-Moreno I., Hollingworth D., Frenkiel T.A., Kelly G., Martin S., Howell S., Garcia-Mayoral M., Gherzi R., Briata P., Ramos A.
      Nat. Struct. Mol. Biol. 16:238-246(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 130-218 AND 221-305, PHOSPHORYLATION AT SER-193, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiFUBP2_HUMAN
    AccessioniPrimary (citable) accession number: Q92945
    Secondary accession number(s): O00301
    , Q59EZ9, Q5U4P6, Q9UNT5, Q9UQH5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 26, 2003
    Last sequence update: November 30, 2010
    Last modified: October 1, 2014
    This is version 140 of the entry and version 4 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 19
      Human chromosome 19: 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