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Q86YP4

- P66A_HUMAN

UniProt

Q86YP4 - P66A_HUMAN

Protein

Transcriptional repressor p66-alpha

Gene

GATAD2A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    Transcriptional repressor. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B.2 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri411 – 46454GATA-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein binding, bridging Source: UniProtKB
    3. sequence-specific DNA binding Source: InterPro
    4. sequence-specific DNA binding transcription factor activity Source: InterPro
    5. zinc ion binding Source: InterPro

    GO - Biological processi

    1. anterior neuropore closure Source: Ensembl
    2. blood vessel development Source: Ensembl
    3. DNA methylation Source: UniProtKB
    4. embryonic body morphogenesis Source: Ensembl
    5. in utero embryonic development Source: Ensembl
    6. negative regulation of transcription, DNA-templated Source: UniProtKB
    7. neural fold formation Source: Ensembl
    8. programmed cell death Source: Ensembl
    9. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_953. RNA Polymerase I Transcription Initiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transcriptional repressor p66-alpha
    Short name:
    Hp66alpha
    Alternative name(s):
    GATA zinc finger domain-containing protein 2A
    Gene namesi
    Name:GATAD2A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:29989. GATAD2A.

    Subcellular locationi

    Nucleus speckle 2 Publications
    Note: Speckled nuclear localization requires both CR1 and CR2 regions.

    GO - Cellular componenti

    1. nuclear speck Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB
    3. NuRD complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi149 – 1491K → R: Disruption of MBD2-binding, loss of enhancement of MBD2-mediated repression and loss of speckled nuclear localization. 1 Publication

    Organism-specific databases

    PharmGKBiPA142671746.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 633633Transcriptional repressor p66-alphaPRO_0000083500Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei49 – 491Phosphothreonine5 Publications
    Modified residuei100 – 1001Phosphoserine6 Publications
    Modified residuei107 – 1071Phosphoserine6 Publications
    Modified residuei114 – 1141Phosphoserine3 Publications
    Modified residuei189 – 1891Phosphothreonine1 Publication
    Modified residuei340 – 3401Phosphoserine1 Publication
    Modified residuei343 – 3431Phosphoserine1 Publication
    Modified residuei546 – 5461Phosphoserine2 Publications
    Modified residuei548 – 5481Phosphoserine2 Publications
    Modified residuei598 – 5981Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86YP4.
    PaxDbiQ86YP4.
    PRIDEiQ86YP4.

    PTM databases

    PhosphoSiteiQ86YP4.

    Miscellaneous databases

    PMAP-CutDBQ86YP4.

    Expressioni

    Tissue specificityi

    Ubiquitous, both in fetal and adult tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ86YP4.
    BgeeiQ86YP4.
    CleanExiHS_GATAD2A.
    GenevestigatoriQ86YP4.

    Organism-specific databases

    HPAiHPA006759.
    HPA024373.

    Interactioni

    Subunit structurei

    Binds MBD2 and MBD3. Interaction with MBD2 is required for the enhancement of MBD2-mediated repression and for targeting to the chromatin. Component of the MeCP1 histone deacetylase complex. Interacts with histone tails, including that of histones H2A, H2B, H3 and H4. This interaction is reduced by histone acetylation.3 Publications

    Protein-protein interaction databases

    BioGridi120172. 22 interactions.
    IntActiQ86YP4. 15 interactions.
    MINTiMINT-1387810.
    STRINGi9606.ENSP00000351552.

    Structurei

    Secondary structure

    1
    633
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi138 – 16831

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L2LNMR-A137-178[»]
    ProteinModelPortaliQ86YP4.
    SMRiQ86YP4. Positions 137-178.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 17835CR1; MBD2-bindingAdd
    BLAST
    Regioni340 – 480141CR2; histone tail-bindingAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili139 – 17436Sequence AnalysisAdd
    BLAST

    Domaini

    Both CR1 and CR2 regions are required for speckled nuclear localization.

    Sequence similaritiesi

    Contains 1 GATA-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri411 – 46454GATA-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG252421.
    HOGENOMiHOG000074070.
    HOVERGENiHBG053401.
    OMAiLVNIPQP.
    PhylomeDBiQ86YP4.
    TreeFamiTF321369.

    Family and domain databases

    Gene3Di3.30.50.10. 1 hit.
    InterProiIPR000679. Znf_GATA.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    PROSITEiPS00344. GATA_ZN_FINGER_1. 1 hit.
    PS50114. GATA_ZN_FINGER_2. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86YP4-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTEEACRTRS QKRALERDPT EDDVESKKIK MERGLLASDL NTDGDMRVTP    50
    EPGAGPTQGL LRATEATAMA MGRGEGLVGD GPVDMRTSHS DMKSERRPPS 100
    PDVIVLSDNE QPSSPRVNGL TTVALKETST EALMKSSPEE RERMIKQLKE 150
    ELRLEEAKLV LLKKLRQSQI QKEATAQKPT GSVGSTVTTP PPLVRGTQNI 200
    PAGKPSLQTS SARMPGSVIP PPLVRGGQQA SSKLGPQASS QVVMPPLVRG 250
    AQQIHSIRQH SSTGPPPLLL APRASVPSVQ IQGQRIIQQG LIRVANVPNT 300
    SLLVNIPQPT PASLKGTTAT SAQANSTPTS VASVVTSAES PASRQAAAKL 350
    ALRKQLEKTL LEIPPPKPPA PEMNFLPSAA NNEFIYLVGL EEVVQNLLET 400
    QGRMSAATVL SREPYMCAQC KTDFTCRWRE EKSGAIMCEN CMTTNQKKAL 450
    KVEHTSRLKA AFVKALQQEQ EIEQRLLQQG TAPAQAKAEP TAAPHPVLKQ 500
    VIKPRRKLAF RSGEARDWSN GAVLQASSQL SRGSATTPRG VLHTFSPSPK 550
    LQNSASATAL VSRTGRHSER TVSAGKGSAT SNWKKTPLST GGTLAFVSPS 600
    LAVHKSSSAV DRQREYLLDM IPPRSIPQSA TWK 633
    Length:633
    Mass (Da):68,063
    Last modified:June 1, 2003 - v1
    Checksum:i64F0066B4BEFCB39
    GO
    Isoform 2 (identifier: Q86YP4-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         500-524: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:608
    Mass (Da):65,225
    Checksum:i751DB0FC42DA3BC8
    GO
    Isoform 3 (identifier: Q86YP4-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         401-401: Q → QA

    Note: No experimental confirmation available.

    Show »
    Length:634
    Mass (Da):68,134
    Checksum:i4C5D2B9CD5FE719E
    GO

    Sequence cautioni

    The sequence AAH11684.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA90939.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti432 – 4321K → E in BAA90939. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171R → Q.
    Corresponds to variant rs10426883 [ dbSNP | Ensembl ].
    VAR_059308
    Natural varianti296 – 2961N → S.
    Corresponds to variant rs2288851 [ dbSNP | Ensembl ].
    VAR_059309

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei401 – 4011Q → QA in isoform 3. 1 PublicationVSP_053410
    Alternative sequencei500 – 52425Missing in isoform 2. 1 PublicationVSP_010929Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY186731 mRNA. Translation: AAO31797.1.
    AC003030 Genomic DNA. No translation available.
    AC011448 Genomic DNA. No translation available.
    AC092067 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84819.1.
    BC011684 mRNA. Translation: AAH11684.1. Different initiation.
    BC012902 mRNA. Translation: AAH12902.2.
    AK000092 mRNA. Translation: BAA90939.1. Different initiation.
    AL390164 mRNA. Translation: CAB99095.1.
    CCDSiCCDS12402.2. [Q86YP4-1]
    PIRiT51878.
    RefSeqiNP_060130.3. NM_017660.3. [Q86YP4-1]
    XP_005260015.1. XM_005259958.1. [Q86YP4-3]
    XP_005260016.1. XM_005259959.2. [Q86YP4-3]
    XP_005260017.1. XM_005259960.2. [Q86YP4-3]
    XP_005260018.1. XM_005259961.1. [Q86YP4-3]
    UniGeneiHs.118964.

    Genome annotation databases

    EnsembliENST00000358713; ENSP00000351552; ENSG00000167491. [Q86YP4-1]
    ENST00000360315; ENSP00000353463; ENSG00000167491. [Q86YP4-1]
    ENST00000404158; ENSP00000384899; ENSG00000167491. [Q86YP4-3]
    GeneIDi54815.
    KEGGihsa:54815.
    UCSCiuc010xqt.2. human. [Q86YP4-1]
    uc010xqv.3. human.

    Polymorphism databases

    DMDMi50401012.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY186731 mRNA. Translation: AAO31797.1 .
    AC003030 Genomic DNA. No translation available.
    AC011448 Genomic DNA. No translation available.
    AC092067 Genomic DNA. No translation available.
    CH471106 Genomic DNA. Translation: EAW84819.1 .
    BC011684 mRNA. Translation: AAH11684.1 . Different initiation.
    BC012902 mRNA. Translation: AAH12902.2 .
    AK000092 mRNA. Translation: BAA90939.1 . Different initiation.
    AL390164 mRNA. Translation: CAB99095.1 .
    CCDSi CCDS12402.2. [Q86YP4-1 ]
    PIRi T51878.
    RefSeqi NP_060130.3. NM_017660.3. [Q86YP4-1 ]
    XP_005260015.1. XM_005259958.1. [Q86YP4-3 ]
    XP_005260016.1. XM_005259959.2. [Q86YP4-3 ]
    XP_005260017.1. XM_005259960.2. [Q86YP4-3 ]
    XP_005260018.1. XM_005259961.1. [Q86YP4-3 ]
    UniGenei Hs.118964.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L2L NMR - A 137-178 [» ]
    ProteinModelPortali Q86YP4.
    SMRi Q86YP4. Positions 137-178.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120172. 22 interactions.
    IntActi Q86YP4. 15 interactions.
    MINTi MINT-1387810.
    STRINGi 9606.ENSP00000351552.

    PTM databases

    PhosphoSitei Q86YP4.

    Polymorphism databases

    DMDMi 50401012.

    Proteomic databases

    MaxQBi Q86YP4.
    PaxDbi Q86YP4.
    PRIDEi Q86YP4.

    Protocols and materials databases

    DNASUi 54815.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000358713 ; ENSP00000351552 ; ENSG00000167491 . [Q86YP4-1 ]
    ENST00000360315 ; ENSP00000353463 ; ENSG00000167491 . [Q86YP4-1 ]
    ENST00000404158 ; ENSP00000384899 ; ENSG00000167491 . [Q86YP4-3 ]
    GeneIDi 54815.
    KEGGi hsa:54815.
    UCSCi uc010xqt.2. human. [Q86YP4-1 ]
    uc010xqv.3. human.

    Organism-specific databases

    CTDi 54815.
    GeneCardsi GC19P019496.
    H-InvDB HIX0014940.
    HGNCi HGNC:29989. GATAD2A.
    HPAi HPA006759.
    HPA024373.
    MIMi 614997. gene.
    neXtProti NX_Q86YP4.
    PharmGKBi PA142671746.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG252421.
    HOGENOMi HOG000074070.
    HOVERGENi HBG053401.
    OMAi LVNIPQP.
    PhylomeDBi Q86YP4.
    TreeFami TF321369.

    Enzyme and pathway databases

    Reactomei REACT_953. RNA Polymerase I Transcription Initiation.

    Miscellaneous databases

    GenomeRNAii 54815.
    NextBioi 35478060.
    PMAP-CutDB Q86YP4.
    PROi Q86YP4.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86YP4.
    Bgeei Q86YP4.
    CleanExi HS_GATAD2A.
    Genevestigatori Q86YP4.

    Family and domain databases

    Gene3Di 3.30.50.10. 1 hit.
    InterProi IPR000679. Znf_GATA.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    PROSITEi PS00344. GATA_ZN_FINGER_1. 1 hit.
    PS50114. GATA_ZN_FINGER_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3."
      Brackertz M., Boeke J., Zhang R., Renkawitz R.
      J. Biol. Chem. 277:40958-40966(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH MBD2 AND MBD3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
      Tissue: Ovary and Skin.
    5. "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] OF 417-633 (ISOFORM 1).
      Tissue: Colon.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 465-633 (ISOFORM 2).
      Tissue: Brain.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "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-100; SER-107 AND SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone interaction."
      Brackertz M., Gong Z., Leers J., Renkawitz R.
      Nucleic Acids Res. 34:397-406(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MBD2 AND HISTONE TAILS, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-149.
    10. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100 AND SER-107, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-49; SER-100; SER-107; SER-114; SER-546; SER-548 AND SER-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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].
    14. "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 THR-49; SER-100; SER-107; SER-114; THR-189 AND SER-340, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "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 THR-49; SER-100; SER-107; SER-546 AND SER-548, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "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 THR-49; SER-100; SER-107 AND SER-343, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2-NuRD complex."
      Gnanapragasam M.N., Scarsdale J.N., Amaya M.L., Webb H.D., Desai M.A., Walavalkar N.M., Wang S.Z., Zu Zhu S., Ginder G.D., Williams D.C. Jr.
      Proc. Natl. Acad. Sci. U.S.A. 108:7487-7492(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 137-178 IN COMPLEX WITH MBD2, SUBUNIT, INTERACTION WITH MBD2.

    Entry informationi

    Entry nameiP66A_HUMAN
    AccessioniPrimary (citable) accession number: Q86YP4
    Secondary accession number(s): B5MC40
    , Q7L3J2, Q96F28, Q9NPU2, Q9NXS1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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