GenomeNet

Database: UniProt
Entry: Q9NZS3_HUMAN
LinkDB: Q9NZS3_HUMAN
Original site: Q9NZS3_HUMAN 
ID   Q9NZS3_HUMAN            Unreviewed;      1066 AA.
AC   Q9NZS3;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   24-JAN-2024, entry version 93.
DE   RecName: Full=histone deacetylase {ECO:0000256|ARBA:ARBA00012111};
DE            EC=3.5.1.98 {ECO:0000256|ARBA:ARBA00012111};
DE   Flags: Fragment;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|EMBL:AAF36540.1};
RN   [1] {ECO:0000313|EMBL:AAF36540.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Placenta {ECO:0000313|EMBL:AAF36540.1};
RA   Govindan M.V., Warriar N.;
RT   "Human GR AF-1 specific histone deacetylase.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 2
CC       subfamily. {ECO:0000256|ARBA:ARBA00007738}.
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DR   EMBL; AF174499; AAF36540.1; -; mRNA.
DR   AlphaFoldDB; Q9NZS3; -.
DR   GO; GO:0000118; C:histone deacetylase complex; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR   GO; GO:0004407; F:histone deacetylase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0010605; P:negative regulation of macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd10003; HDAC6-dom2; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000286; His_deacetylse.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR017320; Histone_deAcase_II_euk.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR001607; Znf_UBP.
DR   PANTHER; PTHR45364:SF8; HISTONE DEACETYLASE 5; 1.
DR   PANTHER; PTHR45364; HISTONE DEACETYLASE 9-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 2.
DR   Pfam; PF02148; zf-UBP; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   SMART; SM00290; ZnF_UBP; 1.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50271; ZF_UBP; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00502};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00502};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00502}.
FT   DOMAIN          962..1060
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50271"
FT   REGION          694..714
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAF36540.1"
SQ   SEQUENCE   1066 AA;  114285 MW;  7001E35AAC093346 CRC64;
     NSGMETTQYM NEGELRVLAD TYDSVYLHPN SYSCACLASG SVLRLVDAVL GAEIRNGMAI
     IRPPGHHAQH SLMDGYCMFN HVAVAARYAQ QKHRIRRVLI LDWDVHHGQG TQFTFDQDPS
     VLYFSIHRYE QGRFWPHLKA SNWSTTGFGQ GQGYTINVPW NQVGMRDADY IAAFLHVLLP
     VALEFQPQLV LVAAGFDALQ GDPKGEMAAT PAGFAQLTHL LMGLAGGKLI LSLEGGYNLR
     ALAEGVSASL HTLLGDPGPM LESPGAPCRS AQASVSCALE ALEPFWEVLV RSTETVERGH
     MGEDNVEESE EEGPWEPPVL PILTWPVLTS RTGLVYDQNM MNHCNLWDSH HPEVPQRILR
     IMCRLEELGL AGRCLTLTPR PATEAELLTC HSAEYVGHLR ATEKMKTREL HRESSNFDSI
     YICPSTFACA QLATGAACRL VEAVLSGEVL NGAAVVRPPG HHAEQDAACG FCFFNSVAVA
     ARHAQTISGH ALRILIVDWD VHHGNGTQHM FEDDPSVLYV SLHRYDHGTF FPMGDEGASS
     QIGRAAGTGF TVNVAWNGPR MGDADYLAAW HRLVLPIAYE FNPELVLVSA GFDAARGDPL
     GGCQVSPEGY AHLTHLLMGL ASGRIILILE GGYNLTSISE SMAACTRSLL GDPPPLLTLP
     RPPLSGALAS ITETIQVHAR YWCSLRVMKV EDREGPSSSK LVTKKAPQPA KPRLAERMTT
     REKKVLEAGM GKVTSASFGE ESTPGQTNSE TAVVALTQDQ PSEAATGGAT LAQTISEAAI
     GGAMLGQTTS EEAVGGATPD QTTSEETVGG AILDQTTSED AVGGATLGQT TSEEAVGGAT
     LAQTISEAAM EGATLDQTTS EEAPGGTELI QTPLASSTDH QTPPTSPGQG TTPQISPSTL
     IGSLRTLELG SESQGASESQ APGEENLLGE AAGGQDMADS MLMQGSRGLT DQAIFYAVTP
     LPWCPHLVAV CPIPAAGLDV TQPCGDCGTI QENWVCLSCY QVYCGRYING HMLQHHGNSG
     HPLVLSYIDL SAWCYYCQAY VHHQALLDVK NIAHQNKFGE DMPHPH
//
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