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P67809

- YBOX1_HUMAN

UniProt

P67809 - YBOX1_HUMAN

Protein

Nuclease-sensitive element-binding protein 1

Gene

YBX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Mediates pre-mRNA alternative splicing regulation. Binds to splice sites in pre-mRNA and regulates splice site selection. Binds and stabilizes cytoplasmic mRNA. Contributes to the regulation of translation by modulating the interaction between the mRNA and eukaryotic initiation factors By similarity. Regulates the transcription of numerous genes. Its transcriptional activity on the multidrug resistance gene MDR1 is enhanced in presence of the APEX1 acetylated form at 'Lys-6' and 'Lys-7'. Binds to promoters that contain a Y-box (5'-CTGATTGGCCAA-3'), such as MDR1 and HLA class II genes. Promotes separation of DNA strands that contain mismatches or are modified by cisplatin. Has endonucleolytic activity and can introduce nicks or breaks into double-stranded DNA (in vitro). May play a role in DNA repair. Component of the CRD-mediated complex that promotes MYC mRNA stability. Binds preferentially to the 5'-[CU]CUGCG-3' motif in vitro.By similarity
    The secreted form acts as an extracellular mitogen and stimulates cell migration and proliferation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei219 – 2202Cleavage; by 20S proteasomal protease

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB
    2. double-stranded DNA binding Source: ProtInc
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. RNA binding Source: UniProtKB
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. single-stranded DNA binding Source: ProtInc

    GO - Biological processi

    1. CRD-mediated mRNA stabilization Source: UniProtKB
    2. gene expression Source: Reactome
    3. in utero embryonic development Source: Ensembl
    4. mRNA splicing, via spliceosome Source: Reactome
    5. negative regulation of striated muscle cell differentiation Source: Ensembl
    6. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
    7. positive regulation of cell division Source: UniProtKB-KW
    8. regulation of transcription, DNA-templated Source: UniProtKB
    9. RNA splicing Source: Reactome
    10. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Activator, Mitogen, Repressor

    Keywords - Biological processi

    mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_467. mRNA Splicing - Major Pathway.
    SignaLinkiP67809.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclease-sensitive element-binding protein 1
    Alternative name(s):
    CCAAT-binding transcription factor I subunit A
    Short name:
    CBF-A
    DNA-binding protein B
    Short name:
    DBPB
    Enhancer factor I subunit A
    Short name:
    EFI-A
    Y-box transcription factor
    Y-box-binding protein 1
    Short name:
    YB-1
    Gene namesi
    Name:YBX1
    Synonyms:NSEP1, YB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:8014. YBX1.

    Subcellular locationi

    Cytoplasm. Nucleus. Cytoplasmic granule. Secreted
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles between nucleus and cytoplasm. Predominantly cytoplasmic in proliferating cells. Cytotoxic stress and DNA damage enhance translocation to the nucleus. Localized with DDX1, MBNL1 and TIAL1 in stress granules upon stress. Secreted by mesangial and monocytic cells after inflammatory challenges. Translocates from the cytoplasm to the nucleus after and colocalizes with APEX1 in nuclear speckles after genotoxic stress.

    GO - Cellular componenti

    1. CRD-mediated mRNA stability complex Source: UniProtKB
    2. cytoplasm Source: HPA
    3. cytoplasmic stress granule Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProtKB
    5. histone pre-mRNA 3'end processing complex Source: UniProtKB
    6. intracellular membrane-bounded organelle Source: HPA
    7. nuclear membrane Source: HPA
    8. nucleoplasm Source: Reactome
    9. nucleus Source: ProtInc
    10. ribonucleoprotein complex Source: UniProtKB
    11. U12-type spliceosomal complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus, Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi102 – 1021S → A: Loss of phosphorylation by PKB/AKT1. Inhibits translocation to the nucleus and tumor cell growth. 1 Publication
    Mutagenesisi301 – 3011K → A: Abrogates unconventional secretion. 1 Publication
    Mutagenesisi304 – 3041K → A: Abrogates unconventional secretion. 1 Publication

    Organism-specific databases

    PharmGKBiPA31791.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 324323Nuclease-sensitive element-binding protein 1PRO_0000100219Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei102 – 1021Phosphoserine; by PKB/AKT12 Publications
    Cross-linki137 – 137Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
    Modified residuei162 – 1621Phosphotyrosine1 Publication
    Modified residuei165 – 1651Phosphoserine4 Publications
    Modified residuei167 – 1671Phosphoserine3 Publications
    Modified residuei174 – 1741Phosphoserine5 Publications
    Modified residuei176 – 1761Phosphoserine5 Publications
    Modified residuei301 – 3011N6-acetyllysine1 Publication
    Modified residuei304 – 3041N6-acetyllysine1 Publication
    Modified residuei314 – 3141Phosphoserine1 Publication

    Post-translational modificationi

    Ubiquitinated by RBBP6; leading to a decrease of YBX1 transcactivational ability.1 Publication
    In the absence of phosphorylation the protein is retained in the cytoplasm.8 Publications
    Cleaved by a 20S proteasomal protease in response to agents that damage DNA. Cleavage takes place in the absence of ubiquitination and ATP. The resulting N-terminal fragment accumulates in the nucleus By similarity.By similarity

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP67809.
    PaxDbiP67809.
    PRIDEiP67809.

    PTM databases

    PhosphoSiteiP67809.

    Miscellaneous databases

    PMAP-CutDBP67809.

    Expressioni

    Gene expression databases

    BgeeiP67809.
    CleanExiHS_YBX1.
    GenevestigatoriP67809.

    Organism-specific databases

    HPAiCAB005875.
    HPA040304.
    HPA057159.

    Interactioni

    Subunit structurei

    Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1 By similarity. Component of the coding region determinant (CRD)-mediated complex, composed of DHX9, HNRNPU, IGF2BP1, SYNCRIP and YBX1. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the U11/U12 snRNPs that are part of the U12-type spliceosome. Interacts with IGF2BP1 and RBBP6. Component of cytoplasmic messenger ribonucleoprotein particles (mRNPs). Interacts with AKT1, MBNL1, SFRS9, ALYREF/THOC4, MSH2, XRCC5, WRN and NCL. Can bind to DNA as a homomeric form, (EFI-A)n or as a heteromeric form in association with EFI-B. Homodimer in the presence of ATP. Interacts (via C-terminus) with APEX1 (via N-terminus); the interaction is increased with APEX1 acetylated at 'Lys-6' and 'Lys-7'. Interacts with AGO1 and AGO2. Interacts with ANKRD2.By similarity14 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTCFQ087052EBI-354065,EBI-932806From a different organism.
    DHX9Q0821110EBI-354065,EBI-352022
    EP300Q094722EBI-354065,EBI-447295
    FBXO33Q7Z6M25EBI-354065,EBI-8555452
    HNRNPDQ14103-43EBI-354065,EBI-432545
    LSM3P623102EBI-354065,EBI-348239
    PITX2Q996973EBI-354065,EBI-1175211

    Protein-protein interaction databases

    BioGridi110959. 140 interactions.
    DIPiDIP-29405N.
    IntActiP67809. 194 interactions.
    MINTiMINT-5001202.
    STRINGi9606.ENSP00000361626.

    Structurei

    Secondary structure

    1
    324
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi56 – 6712
    Turni68 – 714
    Beta strandi72 – 776
    Turni78 – 814
    Beta strandi82 – 876
    Helixi88 – 903
    Beta strandi108 – 1158
    Beta strandi117 – 1259

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H95NMR-A52-129[»]
    ProteinModelPortaliP67809.
    SMRiP67809. Positions 52-129.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP67809.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini61 – 12565CSDAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni15 – 7157Interaction with ss-DNAAdd
    BLAST

    Sequence similaritiesi

    Contains 1 CSD (cold-shock) domain.Curated

    Phylogenomic databases

    eggNOGiCOG1278.
    HOGENOMiHOG000116439.
    HOVERGENiHBG008757.
    InParanoidiP67809.
    KOiK09276.
    OMAiYRRRRYP.
    PhylomeDBiP67809.
    TreeFamiTF317306.

    Family and domain databases

    Gene3Di2.40.50.140. 1 hit.
    InterProiIPR019844. Cold-shock_CS.
    IPR011129. Cold_shock_prot.
    IPR002059. CSP_DNA-bd.
    IPR012340. NA-bd_OB-fold.
    [Graphical view]
    PfamiPF00313. CSD. 1 hit.
    [Graphical view]
    PRINTSiPR00050. COLDSHOCK.
    SMARTiSM00357. CSP. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    PROSITEiPS00352. COLD_SHOCK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P67809-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSEAETQQP PAAPPAAPAL SAADTKPGTT GSGAGSGGPG GLTSAAPAGG    50
    DKKVIATKVL GTVKWFNVRN GYGFINRNDT KEDVFVHQTA IKKNNPRKYL 100
    RSVGDGETVE FDVVEGEKGA EAANVTGPGG VPVQGSKYAA DRNHYRRYPR 150
    RRGPPRNYQQ NYQNSESGEK NEGSESAPEG QAQQRRPYRR RRFPPYYMRR 200
    PYGRRPQYSN PPVQGEVMEG ADNQGAGEQG RPVRQNMYRG YRPRFRRGPP 250
    RQRQPREDGN EEDKENQGDE TQGQQPPQRR YRRNFNYRRR RPENPKPQDG 300
    KETKAADPPA ENSSAPEAEQ GGAE 324
    Length:324
    Mass (Da):35,924
    Last modified:January 23, 2007 - v3
    Checksum:iDF0114BF974AEDB8
    GO

    Sequence cautioni

    The sequence AAA59949.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAA61308.1 differs from that shown. Reason: Frameshift at position 314.
    The sequence AAA35750.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti120 – 1201A → E in AAA61308. (PubMed:3174636)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24070 mRNA. Translation: AAA35750.1. Different initiation.
    J03827 mRNA. Translation: AAA61308.1. Frameshift.
    M83234 mRNA. Translation: AAA59949.1. Frameshift.
    L28809 mRNA. Translation: AAA20871.1.
    BC002411 mRNA. Translation: AAH02411.1.
    BC010430 mRNA. Translation: AAH10430.1.
    BC015208 mRNA. Translation: AAH15208.1.
    BC038384 mRNA. Translation: AAH38384.1.
    BC065571 mRNA. Translation: AAH65571.1.
    BC070084 mRNA. Translation: AAH70084.1.
    BC071708 mRNA. Translation: AAH71708.1.
    BC090038 mRNA. Translation: AAH90038.1.
    BC098435 mRNA. Translation: AAH98435.1.
    BC106045 mRNA. Translation: AAI06046.1.
    CCDSiCCDS470.1.
    PIRiI39382.
    S34426.
    RefSeqiNP_004550.2. NM_004559.3.
    UniGeneiHs.473583.

    Genome annotation databases

    EnsembliENST00000321358; ENSP00000361626; ENSG00000065978.
    GeneIDi4904.
    KEGGihsa:4904.
    UCSCiuc001chs.3. human.

    Polymorphism databases

    DMDMi54040031.

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M24070 mRNA. Translation: AAA35750.1 . Different initiation.
    J03827 mRNA. Translation: AAA61308.1 . Frameshift.
    M83234 mRNA. Translation: AAA59949.1 . Frameshift.
    L28809 mRNA. Translation: AAA20871.1 .
    BC002411 mRNA. Translation: AAH02411.1 .
    BC010430 mRNA. Translation: AAH10430.1 .
    BC015208 mRNA. Translation: AAH15208.1 .
    BC038384 mRNA. Translation: AAH38384.1 .
    BC065571 mRNA. Translation: AAH65571.1 .
    BC070084 mRNA. Translation: AAH70084.1 .
    BC071708 mRNA. Translation: AAH71708.1 .
    BC090038 mRNA. Translation: AAH90038.1 .
    BC098435 mRNA. Translation: AAH98435.1 .
    BC106045 mRNA. Translation: AAI06046.1 .
    CCDSi CCDS470.1.
    PIRi I39382.
    S34426.
    RefSeqi NP_004550.2. NM_004559.3.
    UniGenei Hs.473583.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H95 NMR - A 52-129 [» ]
    ProteinModelPortali P67809.
    SMRi P67809. Positions 52-129.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110959. 140 interactions.
    DIPi DIP-29405N.
    IntActi P67809. 194 interactions.
    MINTi MINT-5001202.
    STRINGi 9606.ENSP00000361626.

    PTM databases

    PhosphoSitei P67809.

    Polymorphism databases

    DMDMi 54040031.

    Proteomic databases

    MaxQBi P67809.
    PaxDbi P67809.
    PRIDEi P67809.

    Protocols and materials databases

    DNASUi 4904.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000321358 ; ENSP00000361626 ; ENSG00000065978 .
    GeneIDi 4904.
    KEGGi hsa:4904.
    UCSCi uc001chs.3. human.

    Organism-specific databases

    CTDi 4904.
    GeneCardsi GC01P043148.
    H-InvDB HIX0037767.
    HIX0172381.
    HGNCi HGNC:8014. YBX1.
    HPAi CAB005875.
    HPA040304.
    HPA057159.
    MIMi 154030. gene.
    neXtProti NX_P67809.
    PharmGKBi PA31791.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1278.
    HOGENOMi HOG000116439.
    HOVERGENi HBG008757.
    InParanoidi P67809.
    KOi K09276.
    OMAi YRRRRYP.
    PhylomeDBi P67809.
    TreeFami TF317306.

    Enzyme and pathway databases

    Reactomei REACT_467. mRNA Splicing - Major Pathway.
    SignaLinki P67809.

    Miscellaneous databases

    EvolutionaryTracei P67809.
    GeneWikii Y_box_binding_protein_1.
    GenomeRNAii 4904.
    NextBioi 18871.
    PMAP-CutDB P67809.
    PROi P67809.
    SOURCEi Search...

    Gene expression databases

    Bgeei P67809.
    CleanExi HS_YBX1.
    Genevestigatori P67809.

    Family and domain databases

    Gene3Di 2.40.50.140. 1 hit.
    InterProi IPR019844. Cold-shock_CS.
    IPR011129. Cold_shock_prot.
    IPR002059. CSP_DNA-bd.
    IPR012340. NA-bd_OB-fold.
    [Graphical view ]
    Pfami PF00313. CSD. 1 hit.
    [Graphical view ]
    PRINTSi PR00050. COLDSHOCK.
    SMARTi SM00357. CSP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    PROSITEi PS00352. COLD_SHOCK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two human genes isolated by a novel method encode DNA-binding proteins containing a common region of homology."
      Sakura H., Maekawa T., Imamoto F., Yasuda K., Ishii S.
      Gene 73:499-507(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Characterization of the cDNA encoding a protein binding to the major histocompatibility complex class II Y box."
      Didier D.K., Schiffenbauer J., Woulfe S.L., Zacheis M., Schwartz B.D.
      Proc. Natl. Acad. Sci. U.S.A. 85:7322-7326(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Full length cDNA sequence encoding a nuclease-sensitive element DNA binding protein."
      Kolluri R., Kinniburgh A.J.
      Nucleic Acids Res. 19:4771-4771(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "A human protein containing a 'cold shock' domain binds specifically to H-DNA upstream from the human gamma-globin genes."
      Horwitz E.M., Maloney K.A., Ley T.J.
      J. Biol. Chem. 269:14130-14139(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Bone marrow.
    5. "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: Adrenal cortex, Eye, Kidney, Muscle, Placenta, Skin, Testis and Uterus.
    6. Bienvenut W.V.
      Submitted (JAN-2010) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-53; 70-93; 102-137; 157-185; 205-231; 257-279 AND 305-324, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, PHOSPHORYLATION AT SER-165, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Ovarian carcinoma.
    7. "Nucleolin and YB-1 are required for JNK-mediated interleukin-2 mRNA stabilization during T-cell activation."
      Chen C.-Y., Gherzi R., Andersen J.S., Gaietta G., Juerchott K., Royer H.-D., Mann M., Karin M.
      Genes Dev. 14:1236-1248(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
    8. "Y box-binding factor promotes eosinophil survival by stabilizing granulocyte-macrophage colony-stimulating factor mRNA."
      Capowski E.E., Esnault S., Bhattacharya S., Malter J.S.
      J. Immunol. 167:5970-5976(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection."
      Raffetseder U., Frye B., Rauen T., Juerchott K., Royer H.-D., Jansen P.L., Mertens P.R.
      J. Biol. Chem. 278:18241-18248(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SFRS9, SUBCELLULAR LOCATION.
    10. "Regulation of alternative splicing by SRrp86 and its interacting proteins."
      Li J., Hawkins I.C., Harvey C.D., Jennings J.L., Link A.J., Patton J.G.
      Mol. Cell. Biol. 23:7437-7447(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SFRS12.
    11. "The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle."
      Kojic S., Medeot E., Guccione E., Krmac H., Zara I., Martinelli V., Valle G., Faulkner G.
      J. Mol. Biol. 339:313-325(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANKRD2.
    12. "YB-1 promotes strand separation in vitro of duplex DNA containing either mispaired bases or cisplatin modifications, exhibits endonucleolytic activities and binds several DNA repair proteins."
      Gaudreault I., Guay D., Lebel M.
      Nucleic Acids Res. 32:316-327(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INTERACTION WITH ALYREF/THOC4; NCL; XRCC5; WRN AND MSH2.
    13. "The human 18S U11/U12 snRNP contains a set of novel proteins not found in the U2-dependent spliceosome."
      Will C.L., Schneider C., Hossbach M., Urlaub H., Rauhut R., Elbashir S., Tuschl T., Luehrmann R.
      RNA 10:929-941(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH THE U11/U12 SPLICEOSOME, IDENTIFICATION BY MASS SPECTROMETRY.
    14. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells."
      Sutherland B.W., Kucab J., Wu J., Lee C., Cheang M.C.U., Yorida E., Turbin D., Dedhar S., Nelson C., Pollak M., Leighton Grimes H., Miller K., Badve S., Huntsman D., Blake-Gilks C., Chen M., Pallen C.J., Dunn S.E.
      Oncogene 24:4281-4292(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-102, INTERACTION WITH AKT1, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-102.
    16. "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-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. "Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells."
      Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M., Urlaub H., Meister G.
      EMBO Rep. 8:1052-1060(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AGO1 AND AGO2.
    19. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
      Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
      Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Prostate cancer.
    20. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, INTERACTION WITH IGF2BP1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    21. "RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1."
      Chibi M., Meyer M., Skepu A., Rees D.J.G., Moolman-Smook J.C., Pugh D.J.
      J. Mol. Biol. 384:908-916(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBBP6, UBIQUITINATION.
    22. "MBNL1 associates with YB-1 in cytoplasmic stress granules."
      Onishi H., Kino Y., Morita T., Futai E., Sasagawa N., Ishiura S.
      J. Neurosci. Res. 86:1994-2002(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MBNL1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    23. "Regulatory role of human AP-endonuclease (APE1/Ref-1) in YB-1-mediated activation of the multidrug resistance gene MDR1."
      Chattopadhyay R., Das S., Maiti A.K., Boldogh I., Xie J., Hazra T.K., Kohno K., Mitra S., Bhakat K.K.
      Mol. Cell. Biol. 28:7066-7080(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, INTERACTION WITH APEX1.
    24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "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].
    26. "Y-box protein-1 is actively secreted through a non-classical pathway and acts as an extracellular mitogen."
      Frye B.C., Halfter S., Djudjaj S., Muehlenberg P., Weber S., Raffetseder U., En-Nia A., Knott H., Baron J.M., Dooley S., Bernhagen J., Mertens P.R.
      EMBO Rep. 10:783-789(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-301 AND LYS-304, ACETYLATION AT LYS-301 AND LYS-304.
    27. "Rapid and systematic analysis of the RNA recognition specificities of RNA-binding proteins."
      Ray D., Kazan H., Chan E.T., Pena Castillo L., Chaudhry S., Talukder S., Blencowe B.J., Morris Q., Hughes T.R.
      Nat. Biotechnol. 27:667-670(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING.
    28. "Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs."
      Weidensdorfer D., Stoehr N., Baude A., Lederer M., Koehn M., Schierhorn A., Buchmeier S., Wahle E., Huettelmaiery S.
      RNA 15:104-115(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, COMPONENT OF THE CRD-MEDIATED MRNA STABILIZATION COMPLEX, IDENTIFICATION IN A MRNP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    29. "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-102; SER-165; SER-167; SER-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    30. "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-165; SER-167; SER-174 AND SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    32. "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-165; SER-167; SER-174; SER-176 AND SER-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    33. "The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1."
      Kloks C.P.A.M., Spronk C.A.E.M., Lasonder E., Hoffmann A., Vuister G.W., Grzesiek S., Hilbers C.W.
      J. Mol. Biol. 316:317-326(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 52-129, INTERACTION WITH SS-DNA.

    Entry informationi

    Entry nameiYBOX1_HUMAN
    AccessioniPrimary (citable) accession number: P67809
    Secondary accession number(s): P16990
    , P16991, Q14972, Q15325, Q5FVF0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 11, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 124 of the entry and version 3 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 1
      Human chromosome 1: 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