Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6NZM9

- HDAC4_MOUSE

UniProt

Q6NZM9 - HDAC4_MOUSE

Protein

Histone deacetylase 4

Gene

Hdac4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Involved in muscle maturation via its interaction with the myocyte enhancer factors such as MEF2A, MEF2C and MEF2D By similarity.By similarity

    Catalytic activityi

    Hydrolysis of an N(6)-acetyl-lysine residue of a histone to yield a deacetylated histone.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi664 – 6641ZincBy similarity
    Metal bindingi666 – 6661ZincBy similarity
    Metal bindingi672 – 6721ZincBy similarity
    Metal bindingi743 – 7431ZincBy similarity
    Active sitei795 – 7951By similarity

    GO - Molecular functioni

    1. core promoter binding Source: Ensembl
    2. DNA binding Source: MGI
    3. NAD-dependent histone deacetylase activity (H3-K14 specific) Source: UniProtKB-EC
    4. NAD-dependent histone deacetylase activity (H3-K18 specific) Source: UniProtKB-EC
    5. NAD-dependent histone deacetylase activity (H3-K9 specific) Source: UniProtKB-EC
    6. NAD-dependent histone deacetylase activity (H4-K16 specific) Source: UniProtKB-EC
    7. potassium ion binding Source: Ensembl
    8. protein binding Source: UniProtKB
    9. protein deacetylase activity Source: MGI
    10. protein kinase binding Source: UniProtKB
    11. sequence-specific DNA binding Source: Ensembl
    12. transcription corepressor activity Source: MGI
    13. transcription factor binding Source: UniProtKB
    14. zinc ion binding Source: Ensembl

    GO - Biological processi

    1. chromatin remodeling Source: Ensembl
    2. negative regulation of cell proliferation Source: MGI
    3. negative regulation of glycolytic process Source: BHF-UCL
    4. negative regulation of myotube differentiation Source: Ensembl
    5. negative regulation of osteoblast differentiation Source: MGI
    6. negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    7. negative regulation of transcription, DNA-templated Source: MGI
    8. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    9. osteoblast development Source: MGI
    10. peptidyl-lysine deacetylation Source: Ensembl
    11. positive regulation of cell proliferation Source: Ensembl
    12. positive regulation of protein sumoylation Source: UniProtKB
    13. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    14. positive regulation of transcription, DNA-templated Source: BHF-UCL
    15. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    16. regulation of cardiac muscle contraction by calcium ion signaling Source: MGI
    17. regulation of protein binding Source: Ensembl
    18. regulation of skeletal muscle fiber development Source: MGI
    19. regulation of striated muscle cell differentiation Source: MGI
    20. response to denervation involved in regulation of muscle adaptation Source: BHF-UCL
    21. response to drug Source: Ensembl
    22. response to interleukin-1 Source: Ensembl
    23. skeletal system development Source: MGI
    24. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Hydrolase, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Histone deacetylase 4 (EC:3.5.1.98)
    Short name:
    HD4
    Gene namesi
    Name:Hdac4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:3036234. Hdac4.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Shuttles between the nucleus and the cytoplasm. Upon muscle cells differentiation, it accumulates in the nuclei of myotubes, suggesting a positive role of nuclear HDAC4 in muscle differentiation. The export to cytoplasm depends on the interaction with a 14-3-3 chaperone protein and is due to its phosphorylation at Ser-245, Ser-465 and Ser-629 by CaMK4 and SIK1. The nuclear localization probably depends on sumoylation By similarity.By similarity

    GO - Cellular componenti

    1. A band Source: Ensembl
    2. actomyosin Source: MGI
    3. cytoplasm Source: BHF-UCL
    4. cytosol Source: MGI
    5. histone deacetylase complex Source: Ensembl
    6. neuromuscular junction Source: MGI
    7. nucleus Source: BHF-UCL
    8. transcriptional repressor complex Source: Ensembl
    9. Z disc Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10761076Histone deacetylase 4PRO_0000281033Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei245 – 2451Phosphoserine; by CaMK4 and SIK11 Publication
    Modified residuei349 – 3491PhosphoserineBy similarity
    Modified residuei465 – 4651Phosphoserine; by CaMK4 and SIK13 Publications
    Cross-linki556 – 556Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
    Modified residuei562 – 5621PhosphoserineBy similarity
    Modified residuei629 – 6291Phosphoserine; by CaMK4By similarity
    Modified residuei630 – 6301PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by CaMK4 at Ser-245, Ser-465 and Ser-629. Phosphorylation at other residues by CaMK2D is required for the interaction with 14-3-3. Phosphorylation at Ser-349 impairs the binding of ANKRA2 but generates a high-affinity docking site for 14-3-3 By similarity.By similarity
    Sumoylation on Lys-556 is promoted by the E3 SUMO-protein ligase RANBP2, and prevented by phosphorylation by CaMK4.3 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ6NZM9.
    PRIDEiQ6NZM9.

    PTM databases

    PhosphoSiteiQ6NZM9.

    Expressioni

    Gene expression databases

    BgeeiQ6NZM9.
    CleanExiMM_HDAC4.
    GenevestigatoriQ6NZM9.

    Interactioni

    Subunit structurei

    Interacts with HDAC7. Homodimer. Homodimerization via its N-terminal domain. Interacts with MEF2C and NR2C1. Interacts with a 14-3-3 chaperone protein in a phosphorylation dependent manner. Interacts with BTBD14B. Interacts with KDM5B. Interacts with ANKRA2. Interacts with EP300 in the presence of TFAP2C By similarity. Interacts with AHRR. Interacts with MYOCD.By similarity2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Runx2Q087753EBI-646397,EBI-903354

    Protein-protein interaction databases

    BioGridi229009. 14 interactions.
    DIPiDIP-36317N.
    IntActiQ6NZM9. 6 interactions.
    MINTiMINT-5183788.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6NZM9.
    SMRiQ6NZM9. Positions 62-128, 649-1023.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni117 – 312196Interaction with MEF2ABy similarityAdd
    BLAST
    Regioni652 – 1076425Histone deacetylaseBy similarityAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili66 – 169104Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi1043 – 107634Nuclear export signalBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi464 – 49936Gln-richAdd
    BLAST
    Compositional biasi561 – 5688Poly-Glu

    Domaini

    The nuclear export sequence mediates the shuttling between the nucleus and the cytoplasm.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0123.
    GeneTreeiENSGT00530000062809.
    HOGENOMiHOG000232065.
    HOVERGENiHBG057100.
    InParanoidiQ6NZM9.
    KOiK11406.
    OMAiVSFGGHR.
    OrthoDBiEOG7RFTH5.
    PhylomeDBiQ6NZM9.
    TreeFamiTF106174.

    Family and domain databases

    Gene3Di3.40.800.20. 1 hit.
    InterProiIPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view]
    PANTHERiPTHR10625. PTHR10625. 1 hit.
    PfamiPF12203. HDAC4_Gln. 1 hit.
    PF00850. Hist_deacetyl. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSiPR01270. HDASUPER.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6NZM9-1) [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

    MSSQSHPDGL SGRDQPVELL NPARVNHMPS TVDVATALPL QVAPTAVPMD     50
    LRLDHQFSLP LEPALREQQL QQELLALKQK QQIQRQILIA EFQRQHEQLS 100
    RQHEAQLHEH IKQQQEMLAM KHQQELLEHQ RKLERHRQEQ ELEKQHREQK 150
    LQQLKNKEKG KESAVASTEV KMKLQEFVLN KKKALAHRNL NHCISSDPRY 200
    WYGKTQHSSL DQSSPPQSGV SASYNHPVLG MYDAKDDFPL RKTASEPNLK 250
    LRSRLKQKVA ERRSSPLLRR KDGPVATALK KRPLDVTDSA CSSAPGSGPS 300
    SPNSSSGNVS TENGIAPTVP SAPAETSLAH RLVTREGSVA PLPLYTSPSL 350
    PNITLGLPAT GPAAGAAGQQ DAERLALPAL QQRILFPGTH LTPYLSTSPL 400
    ERDGAAAHNP LLQHMVLLEQ PPTQTPLVTG LGALPLHSQS LVGADRVSPS 450
    IHKLRQHRPL GRTQSAPLPQ NAQALQHLVI QQQHQQFLEK HKQQFQQQQL 500
    HLSKIISKPS EPPRQPESHP EETEEELREH QALLDEPYLD RLPGQKEPSL 550
    AGVQVKQEPI ESEEEEAEAT RETEPGQRPA TEQELLFRQQ ALLLEQQRIH 600
    QLRNYQASME AAGIPVSFGS HRPLSRAQSS PASATFPMSV QEPPTKPRFT 650
    TGLVYDTLML KHQCTCGNTN SHPEHAGRIQ SIWSRLQETG LRGKCECIRG 700
    RKATLEELQT VHSEAHTLLY GTNPLNRQKL DSSLTSVFVR LPCGGVGVDS 750
    DTIWNEVHSS GAARLAVGCV VELVFKVATG ELKNGFAVVR PPGHHAEEST 800
    PMGFCYFNSV AVAAKLLQQR LNVSKILIVD WDVHHGNGTQ QAFYNDPNVL 850
    YMSLHRYDDG NFFPGSGAPD EVGTGPGVGF NVNMAFTGGL EPPMGDAEYL 900
    AAFRTVVMPI ANEFAPDVVL VSSGFDAVEG HPTPLGGYNL SAKCFGYLTK 950
    QLMGLAGGRL VLALEGGHDL TAICDASEAC VSALLGNELE PLPEKVLHQR 1000
    PNANAVHSME KVMDIHSKYW RCLQRLSSTV GHSLIEAQKC EKEEAETVTA 1050
    MASLSVGVKP AEKRSEEEPM EEEPPL 1076
    Length:1,076
    Mass (Da):118,562
    Last modified:July 5, 2004 - v1
    Checksum:iA3CCC3CCCBB903A0
    GO
    Isoform 2 (identifier: Q6NZM9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-171: Missing.
         732-732: S → SKKLLG

    Note: No experimental confirmation available.

    Show »
    Length:910
    Mass (Da):99,124
    Checksum:i80C1A8CA5567EE19
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti569 – 5691A → S in BAE33147. (PubMed:16141072)Curated
    Sequence conflicti904 – 9041R → K in BAE33147. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 171171Missing in isoform 2. 1 PublicationVSP_023952Add
    BLAST
    Alternative sequencei732 – 7321S → SKKLLG in isoform 2. 1 PublicationVSP_023953

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK029933 mRNA. Translation: BAE43272.1.
    AK155250 mRNA. Translation: BAE33147.1.
    AK162369 mRNA. Translation: BAE36877.1.
    BC066052 mRNA. Translation: AAH66052.1.
    CCDSiCCDS48324.1. [Q6NZM9-1]
    RefSeqiNP_997108.1. NM_207225.1. [Q6NZM9-1]
    UniGeneiMm.318567.

    Genome annotation databases

    EnsembliENSMUST00000008995; ENSMUSP00000008995; ENSMUSG00000026313. [Q6NZM9-1]
    GeneIDi208727.
    KEGGimmu:208727.
    UCSCiuc007cbe.2. mouse. [Q6NZM9-2]
    uc007cbf.2. mouse. [Q6NZM9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK029933 mRNA. Translation: BAE43272.1 .
    AK155250 mRNA. Translation: BAE33147.1 .
    AK162369 mRNA. Translation: BAE36877.1 .
    BC066052 mRNA. Translation: AAH66052.1 .
    CCDSi CCDS48324.1. [Q6NZM9-1 ]
    RefSeqi NP_997108.1. NM_207225.1. [Q6NZM9-1 ]
    UniGenei Mm.318567.

    3D structure databases

    ProteinModelPortali Q6NZM9.
    SMRi Q6NZM9. Positions 62-128, 649-1023.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229009. 14 interactions.
    DIPi DIP-36317N.
    IntActi Q6NZM9. 6 interactions.
    MINTi MINT-5183788.

    PTM databases

    PhosphoSitei Q6NZM9.

    Proteomic databases

    PaxDbi Q6NZM9.
    PRIDEi Q6NZM9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000008995 ; ENSMUSP00000008995 ; ENSMUSG00000026313 . [Q6NZM9-1 ]
    GeneIDi 208727.
    KEGGi mmu:208727.
    UCSCi uc007cbe.2. mouse. [Q6NZM9-2 ]
    uc007cbf.2. mouse. [Q6NZM9-1 ]

    Organism-specific databases

    CTDi 9759.
    MGIi MGI:3036234. Hdac4.

    Phylogenomic databases

    eggNOGi COG0123.
    GeneTreei ENSGT00530000062809.
    HOGENOMi HOG000232065.
    HOVERGENi HBG057100.
    InParanoidi Q6NZM9.
    KOi K11406.
    OMAi VSFGGHR.
    OrthoDBi EOG7RFTH5.
    PhylomeDBi Q6NZM9.
    TreeFami TF106174.

    Miscellaneous databases

    NextBioi 372399.
    PROi Q6NZM9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6NZM9.
    CleanExi MM_HDAC4.
    Genevestigatori Q6NZM9.

    Family and domain databases

    Gene3Di 3.40.800.20. 1 hit.
    InterProi IPR000286. His_deacetylse.
    IPR023801. His_deacetylse_dom.
    IPR024643. Hist_deacetylase_Gln_rich_N.
    IPR017320. Histone_deAcase_II_euk.
    [Graphical view ]
    PANTHERi PTHR10625. PTHR10625. 1 hit.
    Pfami PF12203. HDAC4_Gln. 1 hit.
    PF00850. Hist_deacetyl. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037911. HDAC_II_euk. 1 hit.
    PRINTSi PR01270. HDASUPER.
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J and NOD.
      Tissue: Dendritic cell, Epididymis and Testis.
    2. "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] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Modulation of smooth muscle gene expression by association of histone acetyltransferases and deacetylases with myocardin."
      Cao D., Wang Z., Zhang C.L., Oh J., Xing W., Li S., Richardson J.A., Wang D.Z., Olson E.N.
      Mol. Cell. Biol. 25:364-376(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYOCD.
    4. "Molecular mechanism of transcriptional repression of AhR repressor involving ANKRA2, HDAC4, and HDAC5."
      Oshima M., Mimura J., Yamamoto M., Fujii-Kuriyama Y.
      Biochem. Biophys. Res. Commun. 364:276-282(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AHRR.
    5. "CaMKIIdelta isoforms differentially affect calcium handling but similarly regulate HDAC/MEF2 transcriptional responses."
      Zhang T., Kohlhaas M., Backs J., Mishra S., Phillips W., Dybkova N., Chang S., Ling H., Bers D.M., Maier L.S., Olson E.N., Brown J.H.
      J. Biol. Chem. 282:35078-35087(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY CAMK2D.
    6. "SIK1 is a class II HDAC kinase that promotes survival of skeletal myocytes."
      Berdeaux R., Goebel N., Banaszynski L., Takemori H., Wandless T., Shelton G.D., Montminy M.
      Nat. Med. 13:597-603(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-465 AND SER-465.
    7. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-465, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiHDAC4_MOUSE
    AccessioniPrimary (citable) accession number: Q6NZM9
    Secondary accession number(s): Q3TRZ9, Q3U2J3, Q3V3Y4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 20, 2007
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 92 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3