LOCUS       NP_006035               1215 aa            linear   PRI 05-MAY-2025
DEFINITION  protein deacetylase HDAC6 isoform b [Homo sapiens].
ACCESSION   NP_006035
VERSION     NP_006035.2
DBSOURCE    REFSEQ: accession NM_006044.4
KEYWORDS    RefSeq; MANE Select.
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   Leslie,K.A., Lekka,C., Richardson,S.J., Russell,M.A. and
            Morgan,N.G.
  TITLE     Regulation of STAT1 Signaling in Human Pancreatic beta-Cells by the
            Lysine Deacetylase HDAC6: A New Therapeutic Opportunity in Type 1
            Diabetes?
  JOURNAL   Diabetes 73 (9), 1473-1485 (2024)
   PUBMED   38869827
  REMARK    GeneRIF: Regulation of STAT1 Signaling in Human Pancreatic
            beta-Cells by the Lysine Deacetylase HDAC6: A New Therapeutic
            Opportunity in Type 1 Diabetes?
REFERENCE   2  (residues 1 to 1215)
  AUTHORS   Rana,P.S., Ignatz-Hoover,J.J., Kim,B.G., Malek,E., Federov,Y.,
            Adams,D., Chan,T. and Driscoll,J.J.
  TITLE     HDAC6 Inhibition Releases HR23B to Activate Proteasomes, Expand the
            Tumor Immunopeptidome and Amplify T-cell Antimyeloma Activity
  JOURNAL   Cancer Res Commun 4 (6), 1517-1532 (2024)
   PUBMED   38747592
  REMARK    GeneRIF: HDAC6 Inhibition Releases HR23B to Activate Proteasomes,
            Expand the Tumor Immunopeptidome and Amplify T-cell Antimyeloma
            Activity.
REFERENCE   3  (residues 1 to 1215)
  AUTHORS   Luo,C., Wen,B., Liu,J. and Yang,W.
  TITLE     HDAC6-mediated deacetylation of FLOT2 maintains stability and
            tumorigenic function of FLOT2 in nasopharyngeal carcinoma
  JOURNAL   Zhong Nan Da Xue Xue Bao Yi Xue Ban 49 (5), 687-697 (2024)
   PUBMED   39174882
  REMARK    GeneRIF: HDAC6-mediated deacetylation of FLOT2 maintains stability
            and tumorigenic function of FLOT2 in nasopharyngeal carcinoma.
REFERENCE   4  (residues 1 to 1215)
  AUTHORS   Zhang,T., Tong,Y., Zhu,R., Liang,Y., Zhang,J., Hu,C., He,M., Hu,Z.,
            Shen,Z., Niu,J., Zhang,J., Yu,Y., Jin,B., Lei,S., Zeng,Z., Wu,Y.,
            Cheng,Z., Xiao,Z., Guo,B., Zhao,S., Xu,G., Pan,W. and Chen,T.
  TITLE     HDAC6-dependent deacetylation of NGF dictates its ubiquitination
            and maintains primordial follicle dormancy
  JOURNAL   Theranostics 14 (6), 2345-2366 (2024)
   PUBMED   38646645
  REMARK    GeneRIF: HDAC6-dependent deacetylation of NGF dictates its
            ubiquitination and maintains primordial follicle dormancy.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1215)
  AUTHORS   Zhao,W., Wu,Y., Wang,S., Zhao,F., Liu,W., Xue,Z., Zhang,L.,
            Wang,J., Han,M., Li,X. and Huang,B.
  TITLE     HTRA1 promotes EMT through the HDAC6/Ac-alpha-tubulin pathway in
            human GBM cells
  JOURNAL   CNS Neurosci Ther 30 (2), e14605 (2024)
   PUBMED   38334007
  REMARK    GeneRIF: HTRA1 promotes EMT through the HDAC6/Ac-alpha-tubulin
            pathway in human GBM cells.
REFERENCE   6  (residues 1 to 1215)
  AUTHORS   Mahlknecht,U., Schnittger,S., Landgraf,F., Schoch,C., Ottmann,O.G.,
            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,K.D., Fischle,W., Verdin,E. and Bardwell,V.J.
  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,C.M., Hassig,C.A. and Schreiber,S.L.
  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,M.J. and Kadonaga,J.T.
  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 DC377684.1, AJ011972.1,
            AC231533.2 and AL137696.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Feb 26, 2001 this sequence version replaced NP_006035.1.
            
            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].
            
            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 :: SRR1660805.144770.1,
                                           SRR1660803.117327.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA1965299, SAMEA1966682
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000334136.11/ ENSP00000334061.5
            RefSeq Select criteria :: based on manual assertion, conservation,
                                      expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..1215
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="X"
                     /map="Xp11.23"
     Protein         1..1215
                     /product="protein deacetylase HDAC6 isoform b"
                     /EC_number="3.5.1.98"
                     /note="protein phosphatase 1, regulatory subunit 90;
                     tubulin-lysine deacetylase HDAC6; E3 ubiquitin-protein
                     ligase HDAC6; alpha-tubulin deacetylase HDAC6; protein
                     deacetylase HDAC6"
                     /calculated_mol_wt=131289
     Region          1..44
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            22
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            33
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2V5; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          67..76
                     /region_name="Nuclear export signal.
                     /evidence=ECO:0000250|UniProtKB:Q9Z2V5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          87..404
                     /region_name="Histone deacetylase 1"
                     /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"
     Region          445..464
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          482..800
                     /region_name="Histone deacetylase 2"
                     /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"
     Region          842..863
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          919..932
                     /region_name="SE14-1.
                     /evidence=ECO:0000269|PubMed:39567688"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          933..946
                     /region_name="SE14-2.
                     /evidence=ECO:0000269|PubMed:39567688"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          947..960
                     /region_name="SE14-3.
                     /evidence=ECO:0000269|PubMed:39567688"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          961..974
                     /region_name="SE14-4.
                     /evidence=ECO:0000269|PubMed:39567688"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          975..988
                     /region_name="SE14-5.
                     /evidence=ECO:0000269|PubMed:39567688"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          989..1002
                     /region_name="SE14-6.
                     /evidence=ECO:0000269|PubMed:39567688"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          994..1047
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1016
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1021
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1027
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1031
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1034
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1035
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Site            1040
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|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:460464"
     Region          1154..1156
                     /region_name="Ubiquitin binding.
                     /evidence=ECO:0000269|Ref.43"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     Region          1182..1189
                     /region_name="Ubiquitin binding.
                     /evidence=ECO:0000269|Ref.43"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9UBN7.2)"
     CDS             1..1215
                     /gene="HDAC6"
                     /gene_synonym="CPBHM; HD6; JM21; KDAC6; PPP1R90"
                     /coded_by="NM_006044.4:107..3754"
                     /note="isoform b is encoded by transcript variant 5"
                     /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
//
