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P25490

- TYY1_HUMAN

UniProt

P25490 - TYY1_HUMAN

Protein

Transcriptional repressor protein YY1

Gene

YY1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 169 (01 Oct 2014)
      Sequence version 2 (15 Dec 1998)
      Previous versions | rss
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    Functioni

    Multifunctional transcription factor that exhibits positive and negative control on a large number of cellular and viral genes by binding to sites overlapping the transcription start site. Binds to the consensus sequence 5'-CCGCCATNTT-3'; some genes have been shown to contain a longer binding motif allowing enhanced binding; the initial CG dinucleotide can be methylated greatly reducing the binding affinity. The effect on transcription regulation is depending upon the context in which it binds and diverse mechanisms of action include direct activation or repression, indirect activation or repression via cofactor recruitment, or activation or repression by disruption of binding sites or conformational DNA changes. Its activity is regulated by transcription factors and cytoplasmic proteins that have been shown to abrogate or completely inhibit YY1-mediated activation or repression. For example, it acts as a repressor in absence of adenovirus E1A protein but as an activator in its presence. Acts synergistically with the SMAD1 and SMAD4 in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (PubMed:15329343). Binds to SMAD binding elements (SBEs) (5'-GTCT/AGAC-3') within BMP response element (BMPRE) of cardiac activating regions. May play an important role in development and differentiation. Proposed to recruit the PRC2/EED-EZH2 complex to target genes that are transcriptional repressed. Involved in DNA repair. In vitro, binds to DNA recombination intermediate structures (Holliday junctions).1 Publication
    Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair; proposed to target the INO80 complex to YY1-responsive elements.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi298 – 2981Zinc 1
    Metal bindingi303 – 3031Zinc 1
    Metal bindingi316 – 3161Zinc 1
    Metal bindingi320 – 3201Zinc 1
    Metal bindingi327 – 3271Zinc 2
    Metal bindingi330 – 3301Zinc 2
    Metal bindingi343 – 3431Zinc 2
    Metal bindingi347 – 3471Zinc 2
    Metal bindingi355 – 3551Zinc 3
    Metal bindingi360 – 3601Zinc 3
    Metal bindingi373 – 3731Zinc 3
    Metal bindingi377 – 3771Zinc 3
    Metal bindingi385 – 3851Zinc 4
    Metal bindingi390 – 3901Zinc 4
    Metal bindingi403 – 4031Zinc 4
    Metal bindingi407 – 4071Zinc 4

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri296 – 32025C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri325 – 34723C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri353 – 37725C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri383 – 40725C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. DNA binding Source: MGI
    2. four-way junction DNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA binding Source: MGI
    5. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
    6. sequence-specific DNA binding transcription factor activity Source: ProtInc
    7. transcription coactivator activity Source: ProtInc
    8. transcription corepressor activity Source: ProtInc
    9. transcription regulatory region DNA binding Source: MGI
    10. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. anterior/posterior pattern specification Source: Ensembl
    2. camera-type eye morphogenesis Source: Ensembl
    3. cell differentiation Source: UniProtKB-KW
    4. cellular response to DNA damage stimulus Source: UniProtKB
    5. cellular response to UV Source: UniProtKB
    6. chromosome organization Source: Ensembl
    7. double-strand break repair via homologous recombination Source: UniProtKB
    8. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    9. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    10. response to prostaglandin F Source: Ensembl
    11. response to UV-C Source: UniProtKB
    12. RNA localization Source: Ensembl
    13. spermatogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Differentiation, DNA damage, DNA recombination, DNA repair, Spermatogenesis, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiP25490.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional repressor protein YY1
    Alternative name(s):
    Delta transcription factor
    INO80 complex subunit S
    NF-E1
    Yin and yang 1
    Short name:
    YY-1
    Gene namesi
    Name:YY1
    Synonyms:INO80S
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:12856. YY1.

    Subcellular locationi

    Nucleus matrix 3 Publications
    Note: Associated with the nuclear matrix.

    GO - Cellular componenti

    1. Ino80 complex Source: UniProtKB
    2. nuclear matrix Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. PcG protein complex Source: Ensembl
    5. transcription factor complex Source: Ensembl

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37445.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 414414Transcriptional repressor protein YY1PRO_0000047190Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei118 – 1181Phosphoserine3 Publications
    Modified residuei247 – 2471Phosphoserine3 Publications
    Modified residuei378 – 3781Phosphothreonine1 Publication

    Post-translational modificationi

    Transiently poly-ADP-ribosylated by PARP1 upon DNA damage, with the effect of decreasing affinity of YY1 to its cognate DNA binding sites.
    Ubiquitinated.1 Publication

    Keywords - PTMi

    ADP-ribosylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP25490.
    PaxDbiP25490.
    PeptideAtlasiP25490.
    PRIDEiP25490.

    PTM databases

    PhosphoSiteiP25490.

    Miscellaneous databases

    PMAP-CutDBP25490.

    Expressioni

    Gene expression databases

    ArrayExpressiP25490.
    BgeeiP25490.
    CleanExiHS_YY1.
    GenevestigatoriP25490.

    Organism-specific databases

    HPAiCAB009392.
    HPA001119.

    Interactioni

    Subunit structurei

    Found in a complex with SMAD1 and SMAD4. Interacts with YAF2 through the region encompassing the first and second zinc fingers. Component of the chromatin remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80. Interacts with EED and EZH2; the interactions are indicative for an association with the PRC2/EED-EZH2 complex. Interacts with SFMBT2.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P032593EBI-765538,EBI-6947456From a different organism.
    ACTL6AO960195EBI-765538,EBI-355018
    ARRB1P494074EBI-765538,EBI-743313
    E1AQ8JSK44EBI-765538,EBI-7453955From a different organism.
    INO80Q9ULG15EBI-765538,EBI-769345
    PRKDCP785272EBI-765538,EBI-352053
    RUVBL1Q9Y2654EBI-765538,EBI-353675
    RUVBL2Q9Y2305EBI-765538,EBI-352939
    RybpQ8CCI52EBI-765538,EBI-929290From a different organism.

    Protein-protein interaction databases

    BioGridi113360. 119 interactions.
    DIPiDIP-150N.
    IntActiP25490. 41 interactions.
    MINTiMINT-157439.
    STRINGi9606.ENSP00000262238.

    Structurei

    Secondary structure

    1
    414
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi207 – 2115
    Beta strandi220 – 2245
    Beta strandi306 – 3094
    Helixi310 – 3178
    Helixi318 – 3203
    Turni328 – 3303
    Beta strandi333 – 3364
    Helixi337 – 3437
    Helixi344 – 3463
    Turni358 – 3603
    Beta strandi363 – 3653
    Helixi367 – 37812
    Turni397 – 4004
    Helixi401 – 4077

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UBDX-ray2.50C291-414[»]
    1ZNMNMR-A352-379[»]
    4C5IX-ray2.59C199-228[»]
    ProteinModelPortaliP25490.
    SMRiP25490. Positions 295-408.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP25490.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 170170Interaction with the SMAD1/SMAD4 complexAdd
    BLAST
    Regioni257 – 34185Involved in nuclear matrix associationAdd
    BLAST
    Regioni295 – 414120Binding to DNAAdd
    BLAST
    Regioni333 – 37139Involved in repression of activated transcriptionAdd
    BLAST
    Regioni371 – 39727Involved in masking transactivation domainAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi43 – 5311Asp/Glu-rich (acidic)Add
    BLAST
    Compositional biasi54 – 6916Gly-richAdd
    BLAST
    Compositional biasi70 – 8011Poly-HisAdd
    BLAST
    Compositional biasi159 – 17012Gly/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the YY transcription factor family.Curated
    Contains 4 C2H2-type zinc fingers.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri296 – 32025C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri325 – 34723C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri353 – 37725C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri383 – 40725C2H2-type 4PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5048.
    HOGENOMiHOG000008232.
    HOVERGENiHBG006823.
    InParanoidiP25490.
    KOiK09201.
    OMAiDIDHESV.
    PhylomeDBiP25490.
    TreeFamiTF106493.

    Family and domain databases

    Gene3Di3.30.160.60. 4 hits.
    InterProiIPR017114. TF_Yin_yang.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00096. zf-C2H2. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037113. TF_Yin_yang. 1 hit.
    SMARTiSM00355. ZnF_C2H2. 4 hits.
    [Graphical view]
    PROSITEiPS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P25490-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASGDTLYIA TDGSEMPAEI VELHEIEVET IPVETIETTV VGEEEEEDDD    50
    DEDGGGGDHG GGGGHGHAGH HHHHHHHHHH PPMIALQPLV TDDPTQVHHH 100
    QEVILVQTRE EVVGGDDSDG LRAEDGFEDQ ILIPVPAPAG GDDDYIEQTL 150
    VTVAAAGKSG GGGSSSSGGG RVKKGGGKKS GKKSYLSGGA GAAGGGGADP 200
    GNKKWEQKQV QIKTLEGEFS VTMWSSDEKK DIDHETVVEE QIIGENSPPD 250
    YSEYMTGKKL PPGGIPGIDL SDPKQLAEFA RMKPRKIKED DAPRTIACPH 300
    KGCTKMFRDN SAMRKHLHTH GPRVHVCAEC GKAFVESSKL KRHQLVHTGE 350
    KPFQCTFEGC GKRFSLDFNL RTHVRIHTGD RPYVCPFDGC NKKFAQSTNL 400
    KSHILTHAKA KNNQ 414
    Length:414
    Mass (Da):44,713
    Last modified:December 15, 1998 - v2
    Checksum:i058C05A0AD2D04E6
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti65 – 651H → R in AAA59926. (PubMed:1946405)Curated
    Sequence conflicti196 – 1961G → R in AAA59467. (PubMed:1655281)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti380 – 3801D → Y De novo variant found in a patient with mental retardation. 1 Publication
    VAR_065086

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77698 mRNA. Translation: AAA59467.1.
    M76541 mRNA. Translation: AAA59926.1.
    Z14077 mRNA. Translation: CAA78455.1.
    BC037308 mRNA. Translation: AAH37308.1.
    BC065366 mRNA. Translation: AAH65366.1.
    CCDSiCCDS9957.1.
    PIRiA40350.
    RefSeqiNP_003394.1. NM_003403.4.
    UniGeneiHs.388927.
    Hs.603118.

    Genome annotation databases

    EnsembliENST00000262238; ENSP00000262238; ENSG00000100811.
    GeneIDi7528.
    KEGGihsa:7528.
    UCSCiuc001ygy.2. human.

    Polymorphism databases

    DMDMi3915889.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M77698 mRNA. Translation: AAA59467.1 .
    M76541 mRNA. Translation: AAA59926.1 .
    Z14077 mRNA. Translation: CAA78455.1 .
    BC037308 mRNA. Translation: AAH37308.1 .
    BC065366 mRNA. Translation: AAH65366.1 .
    CCDSi CCDS9957.1.
    PIRi A40350.
    RefSeqi NP_003394.1. NM_003403.4.
    UniGenei Hs.388927.
    Hs.603118.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UBD X-ray 2.50 C 291-414 [» ]
    1ZNM NMR - A 352-379 [» ]
    4C5I X-ray 2.59 C 199-228 [» ]
    ProteinModelPortali P25490.
    SMRi P25490. Positions 295-408.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113360. 119 interactions.
    DIPi DIP-150N.
    IntActi P25490. 41 interactions.
    MINTi MINT-157439.
    STRINGi 9606.ENSP00000262238.

    PTM databases

    PhosphoSitei P25490.

    Polymorphism databases

    DMDMi 3915889.

    Proteomic databases

    MaxQBi P25490.
    PaxDbi P25490.
    PeptideAtlasi P25490.
    PRIDEi P25490.

    Protocols and materials databases

    DNASUi 7528.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000262238 ; ENSP00000262238 ; ENSG00000100811 .
    GeneIDi 7528.
    KEGGi hsa:7528.
    UCSCi uc001ygy.2. human.

    Organism-specific databases

    CTDi 7528.
    GeneCardsi GC14P101161.
    HGNCi HGNC:12856. YY1.
    HPAi CAB009392.
    HPA001119.
    MIMi 600013. gene.
    neXtProti NX_P25490.
    PharmGKBi PA37445.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5048.
    HOGENOMi HOG000008232.
    HOVERGENi HBG006823.
    InParanoidi P25490.
    KOi K09201.
    OMAi DIDHESV.
    PhylomeDBi P25490.
    TreeFami TF106493.

    Enzyme and pathway databases

    SignaLinki P25490.

    Miscellaneous databases

    ChiTaRSi YY1. human.
    EvolutionaryTracei P25490.
    GeneWikii YY1.
    GenomeRNAii 7528.
    NextBioi 29449.
    PMAP-CutDB P25490.
    PROi P25490.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25490.
    Bgeei P25490.
    CleanExi HS_YY1.
    Genevestigatori P25490.

    Family and domain databases

    Gene3Di 3.30.160.60. 4 hits.
    InterProi IPR017114. TF_Yin_yang.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00096. zf-C2H2. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037113. TF_Yin_yang. 1 hit.
    SMARTi SM00355. ZnF_C2H2. 4 hits.
    [Graphical view ]
    PROSITEi PS00028. ZINC_FINGER_C2H2_1. 4 hits.
    PS50157. ZINC_FINGER_C2H2_2. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Transcriptional repression by YY1, a human GLI-Kruppel-related protein, and relief of repression by adenovirus E1A protein."
      Shi Y., Seto E., Chang L.-S., Shenk T.
      Cell 67:377-388(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    2. "Isolation of a candidate repressor/activator, NF-E1 (YY-1, delta), that binds to the immunoglobulin kappa 3' enhancer and the immunoglobulin heavy-chain mu E1 site."
      Park K., Atchison M.
      Proc. Natl. Acad. Sci. U.S.A. 88:9804-9808(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Foreskin.
    3. Whitson R.H., Huang T., Dang J., Itakura K.
      Submitted (JUL-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Brain and Lymph.
    5. "Targeting of the YY1 transcription factor to the nucleolus and the nuclear matrix in situ: the C-terminus is a principal determinant for nuclear trafficking."
      McNeil S., Guo B., Stein J.L., Lian J.B., Bushmeyer S., Seto E., Atchison M.L., Penman S., van Wijnen A.J., Stein G.S.
      J. Cell. Biochem. 68:500-510(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    6. "Yeast two-hybrid cloning of a novel zinc finger protein that interacts with the multifunctional transcription factor YY1."
      Kalenik J.L., Chen D., Bradley M.E., Chen S.-J., Lee T.-C.
      Nucleic Acids Res. 25:843-849(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH YAF2.
    7. "Poly(ADP-ribosyl)ation of transcription factor Yin Yang 1 under conditions of DNA damage."
      Oei S.L., Shi Y.
      Biochem. Biophys. Res. Commun. 285:27-31(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLY-ADP-RIBOSYLATION BY PARP1.
    8. "The polycomb group protein EED interacts with YY1, and both proteins induce neural tissue in Xenopus embryos."
      Satijn D.P.E., Hamer K.M., den Blaauwen J., Otte A.P.
      Mol. Cell. Biol. 21:1360-1369(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EZH2 AND EZH2.
    9. "SMAD-mediated modulation of YY1 activity regulates the BMP response and cardiac-specific expression of a GATA4/5/6-dependent chick Nkx2.5 enhancer."
      Lee K.H., Evans S., Ruan T.Y., Lassar A.B.
      Development 131:4709-4723(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH SMAD1 AND SMAD4.
    10. "Transcription factor YY1: structure, function, and therapeutic implications in cancer biology."
      Gordon S., Akopyan G., Garban H., Bonavida B.
      Oncogene 25:1125-1142(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.
    11. Cited for: FUNCTION, IDENTIFICATION IN THE INO80 COMPLEX.
    12. "A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
      Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
      Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA REPAIR, SUBCELLULAR LOCATION, DNA-BINDING, PROTEIN INTERACTION, IDENTIFICATION IN THE INO80 COMPLEX.
    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-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
      Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
      Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-247 AND THR-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "YY1's longer DNA-binding motifs."
      Kim J., Kim J.
      Genomics 93:152-158(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DNA-BINDING MOTIF.
    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-118 AND SER-247, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    18. "Development and validation of a method for profiling post-translational modification activities using protein microarrays."
      Del Rincon S.V., Rogers J., Widschwendter M., Sun D., Sieburg H.B., Spruck C.
      PLoS ONE 5:E11332-E11332(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    19. "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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
      Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
      J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
    22. "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-118, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Regulation of DU145 prostate cancer cell growth by Scm-like with four mbt domains 2."
      Lee K., Na W., Maeng J.H., Wu H., Ju B.G.
      J. Biosci. 38:105-112(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SFMBT2, SUBCELLULAR LOCATION.
    24. "Cocrystal structure of YY1 bound to the adeno-associated virus P5 initiator."
      Houbaviy H.B., Usheva A., Shenk T., Burley S.K.
      Proc. Natl. Acad. Sci. U.S.A. 93:13577-13582(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 304-414.
    25. Cited for: STRUCTURE BY NMR OF 353-379.
    26. Cited for: VARIANT TYR-380.

    Entry informationi

    Entry nameiTYY1_HUMAN
    AccessioniPrimary (citable) accession number: P25490
    Secondary accession number(s): Q14935
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: December 15, 1998
    Last modified: October 1, 2014
    This is version 169 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3