GenomeNet

Database: RefSeq
Entry: NP_001308156
LinkDB: NP_001308156
Original site: NP_001308156 
LOCUS       NP_001308156            1215 aa            linear   PRI 04-MAR-2019
DEFINITION  histone deacetylase 6 isoform b [Homo sapiens].
ACCESSION   NP_001308156 XP_005272622
VERSION     NP_001308156.1
DBSOURCE    REFSEQ: accession NM_001321227.1
KEYWORDS    RefSeq.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 1215)
  AUTHORS   Cheng M, Cai W, Huang W, Chen Y, Wu Z, Luo P and Yan W.
  TITLE     Histone deacetylase 6 regulated expression of IL-8 is involved in
            the doxorubicin (Dox) resistance of osteosarcoma cells via
            modulating ABCB1 transcription
  JOURNAL   Eur. J. Pharmacol. 840, 1-8 (2018)
   PUBMED   30273544
  REMARK    GeneRIF: Histone deacetylase 6 regulated expression of IL-8 is
            involved in the doxorubicin (Dox) resistance of osteosarcoma cells
            via modulating ABCB1 transcription
REFERENCE   2  (residues 1 to 1215)
  AUTHORS   Li A, Chen P, Leng Y and Kang J.
  TITLE     Histone deacetylase 6 regulates the immunosuppressive properties of
            cancer-associated fibroblasts in breast cancer through the
            STAT3-COX2-dependent pathway
  JOURNAL   Oncogene 37 (45), 5952-5966 (2018)
   PUBMED   29980788
  REMARK    GeneRIF: our findings indicated that fibroblastic HDAC6 was a vital
            epigenetic mediator involved in programming an immunosuppressive
            tumor microenvironment that dampens antitumor immunity in breast
            cancer
REFERENCE   3  (residues 1 to 1215)
  AUTHORS   Cosenza M and Pozzi S.
  TITLE     The Therapeutic Strategy of HDAC6 Inhibitors in Lymphoproliferative
            Disease
  JOURNAL   Int J Mol Sci 19 (8), E2337 (2018)
   PUBMED   30096875
  REMARK    GeneRIF: In this review, we describe the HDACs, their inhibitors,
            and the recent advances of HDAC6 inhibitors, their mechanisms of
            action and role in lymphoproliferative disorders.
            Review article
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1215)
  AUTHORS   Porter NJ, Wagner FF and Christianson DW.
  TITLE     Entropy as a Driver of Selectivity for Inhibitor Binding to Histone
            Deacetylase 6
  JOURNAL   Biochemistry 57 (26), 3916-3924 (2018)
   PUBMED   29775292
  REMARK    GeneRIF: Thus, favorable binding entropy contributes to HDAC6
            selectivity. Notably, cyclohexenyl hydroxamate 2 represents a
            promising lead for derivatization with capping groups that may
            further enhance its impressive 313-fold thermodynamic selectivity
            for HDAC6 inhibition.
REFERENCE   5  (residues 1 to 1215)
  AUTHORS   Pinazza M, Ghisi M, Minuzzo S, Agnusdei V, Fossati G, Ciminale V,
            Pezze L, Ciribilli Y, Pilotto G, Venturoli C, Amadori A and
            Indraccolo S.
  TITLE     Histone deacetylase 6 controls Notch3 trafficking and degradation
            in T-cell acute lymphoblastic leukemia cells
  JOURNAL   Oncogene 37 (28), 3839-3851 (2018)
   PUBMED   29643474
  REMARK    GeneRIF: These results connect HDAC6 activity to regulation of
            total and surface Notch3 levels.
REFERENCE   6  (residues 1 to 1215)
  AUTHORS   Mahlknecht U, Schnittger S, Landgraf F, Schoch C, Ottmann OG,
            Hiddemann W and Hoelzer D.
  TITLE     Assignment of the human histone deacetylase 6 gene (HDAC6) to X
            chromosome p11.23 by in situ hybridization
  JOURNAL   Cytogenet. Cell Genet. 93 (1-2), 135-136 (2001)
   PUBMED   11474198
REFERENCE   7  (residues 1 to 1215)
  AUTHORS   Huynh KD, Fischle W, Verdin E and Bardwell VJ.
  TITLE     BCoR, a novel corepressor involved in BCL-6 repression
  JOURNAL   Genes Dev. 14 (14), 1810-1823 (2000)
   PUBMED   10898795
REFERENCE   8  (residues 1 to 1215)
  AUTHORS   Grozinger CM, Hassig CA and Schreiber SL.
  TITLE     Three proteins define a class of human histone deacetylases related
            to yeast Hda1p
  JOURNAL   Proc. Natl. Acad. Sci. U.S.A. 96 (9), 4868-4873 (1999)
   PUBMED   10220385
REFERENCE   9  (residues 1 to 1215)
  AUTHORS   Pazin MJ and Kadonaga JT.
  TITLE     What's up and down with histone deacetylation and transcription?
  JOURNAL   Cell 89 (3), 325-328 (1997)
   PUBMED   9150131
  REMARK    Review article
REFERENCE   10 (residues 1 to 1215)
  AUTHORS   Wolffe,A.P.
  TITLE     Transcriptional control. Sinful repression
  JOURNAL   Nature 387 (6628), 16-17 (1997)
   PUBMED   9139815
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from AC231533.2.
            On Mar 18, 2016 this sequence version replaced XP_005272622.1.
            
            Summary: Histones play a critical role in transcriptional
            regulation, cell cycle progression, and developmental events.
            Histone acetylation/deacetylation alters chromosome structure and
            affects transcription factor access to DNA. The protein encoded by
            this gene belongs to class II of the histone deacetylase/acuc/apha
            family. It contains an internal duplication of two catalytic
            domains which appear to function independently of each other. This
            protein possesses histone deacetylase activity and represses
            transcription. [provided by RefSeq, Jul 2008].
            
            Sequence Note: The RefSeq transcript and protein were derived from
            genomic sequence to make the sequence consistent with the reference
            genome assembly. The genomic coordinates used for the transcript
            record were based on alignments.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: SRR1803613.148893.1,
                                           SRR1660805.71094.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..1215
                     /product="histone deacetylase 6 isoform b"
                     /EC_number="3.5.1.98"
                     /note="protein phosphatase 1, regulatory subunit 90"
                     /calculated_mol_wt=131289
     Site            22
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:23186163};
                     propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            33
                     /site_type="methylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Omega-N-methylarginine.
                     {ECO:0000250|UniProtKB:Q9Z2V5}; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          87..404
                     /region_name="Histone deacetylase 1"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          99..435
                     /region_name="HDAC6-dom1"
                     /note="Histone deacetylase 6, domain 1; cd11682"
                     /db_xref="CDD:212545"
     Site            order(215..216,224..225,253,255,346,384)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:212545"
     Site            order(253,255,346)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:212545"
     Region          482..800
                     /region_name="Histone deacetylase 2"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          485..835
                     /region_name="HDAC6-dom2"
                     /note="Histone deacetylase 6, domain 2; cd10003"
                     /db_xref="CDD:212527"
     Site            order(610..611,619..620,649,651,742,780)
                     /site_type="active"
                     /note="putative active site [active]"
                     /db_xref="CDD:212527"
     Site            order(649,651,742)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:212527"
     Site            1016
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphothreonine. {ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1021
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphothreonine. {ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1027
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphothreonine. {ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1031
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphothreonine. {ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1034
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphothreonine. {ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1035
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1040
                     /site_type="phosphorylation"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphothreonine. {ECO:0000244|PubMed:24275569};
                     propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          1133..1195
                     /region_name="zf-UBP"
                     /note="Zn-finger in ubiquitin-hydrolases and other
                     protein; pfam02148"
                     /db_xref="CDD:280334"
     Region          1154..1156
                     /region_name="Ubiquitin binding"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          1182..1189
                     /region_name="Ubiquitin binding"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     CDS             1..1215
                     /gene="HDAC6"
                     /gene_synonym="CPBHM; HD6; JM21; PPP1R90"
                     /coded_by="NM_001321227.1:288..3935"
                     /note="isoform b is encoded by transcript variant 3"
                     /db_xref="CCDS:CCDS14306.1"
                     /db_xref="GeneID:10013"
                     /db_xref="HGNC:HGNC:14064"
                     /db_xref="MIM:300272"
ORIGIN      
        1 mtstgqdstt trqrrsrqnp qsppqdssvt skrnikkgav prsipnlaev kkkgkmkklg
       61 qameedlivg lqgmdlnlea ealagtglvl deqlnefhcl wddsfpegpe rlhaikeqli
      121 qeglldrcvs fqarfaekee lmlvhsleyi dlmettqymn egelrvladt ydsvylhpns
      181 yscaclasgs vlrlvdavlg aeirngmaii rppghhaqhs lmdgycmfnh vavaaryaqq
      241 khrirrvliv dwdvhhgqgt qftfdqdpsv lyfsihryeq grfwphlkas nwsttgfgqg
      301 qgytinvpwn qvgmrdadyi aaflhvllpv alefqpqlvl vaagfdalqg dpkgemaatp
      361 agfaqlthll mglaggklil sleggynlra laegvsaslh tllgdpcpml espgapcrsa
      421 qasvscalea lepfwevlvr stetverdnm eednveesee egpweppvlp iltwpvlqsr
      481 tglvydqnmm nhcnlwdshh pevpqrilri mcrleelgla grcltltprp ateaelltch
      541 saeyvghlra tekmktrelh ressnfdsiy icpstfacaq latgaacrlv eavlsgevln
      601 gaavvrppgh haeqdaacgf cffnsvavaa rhaqtisgha lrilivdwdv hhgngtqhmf
      661 eddpsvlyvs lhrydhgtff pmgdegassq igraagtgft vnvawngprm gdadylaawh
      721 rlvlpiayef npelvlvsag fdaargdplg gcqvspegya hlthllmgla sgriilileg
      781 gynltsises maactrsllg dppplltlpr pplsgalasi tetiqvhrry wrslrvmkve
      841 dregpssskl vtkkapqpak prlaermttr ekkvleagmg kvtsasfgee stpgqtnset
      901 avvaltqdqp seaatggatl aqtiseaaig gamlgqttse eavggatpdq ttseetvgga
      961 ildqttseda vggatlgqtt seeavggatl aqttseaame gatldqttse eapggteliq
     1021 tplasstdhq tpptspvqgt tpqispstli gslrtlelgs esqgasesqa pgeenllgea
     1081 aggqdmadsm lmqgsrgltd qaifyavtpl pwcphlvavc pipaagldvt qpcgdcgtiq
     1141 enwvclscyq vycgryingh mlqhhgnsgh plvlsyidls awcyycqayv hhqalldvkn
     1201 iahqnkfged mphph
//
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