ID   HDAC1_PONAB             Reviewed;         482 AA.
AC   Q5RAG0;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   02-SEP-2026, entry version 132.
DE   RecName: Full=Histone deacetylase 1;
DE            Short=HD1;
DE            EC=3.5.1.98 {ECO:0000250|UniProtKB:Q13547};
DE   AltName: Full=Protein deacetylase HDAC1;
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
DE   AltName: Full=Protein deacylase HDAC1;
DE            EC=3.5.1.- {ECO:0000250|UniProtKB:Q13547};
GN   Name=HDAC1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone deacetylase that catalyzes the deacetylation of
CC       lysine residues on the N-terminal part of the core histones (H2A, H2B,
CC       H3 and H4). Histone deacetylation gives a tag for epigenetic repression
CC       and plays an important role in transcriptional regulation, cell cycle
CC       progression and developmental events. Histone deacetylases act via the
CC       formation of large multiprotein complexes (By similarity). Acts as a
CC       component of the histone deacetylase NuRD complex which participates in
CC       the remodeling of chromatin (By similarity). As part of the SIN3B
CC       complex is recruited downstream of the constitutively active genes
CC       transcriptional start sites through interaction with histones and
CC       mitigates histone acetylation and RNA polymerase II progression within
CC       transcribed regions contributing to the regulation of transcription (By
CC       similarity). Also functions as a deacetylase for non-histone targets,
CC       such as NR1D2, RELA, SP1, SP3, STAT3, ZNF76 and TSHZ3 (By similarity).
CC       Deacetylates SP proteins, SP1 and SP3, and regulates their function (By
CC       similarity). Component of the BRG1-RB1-HDAC1 complex, which negatively
CC       regulates the CREST-mediated transcription in resting neurons (By
CC       similarity). Upon calcium stimulation, HDAC1 is released from the
CC       complex and CREBBP is recruited, which facilitates transcriptional
CC       activation (By similarity). Deacetylates TSHZ3 and regulates its
CC       transcriptional repressor activity (By similarity). Deacetylates 'Lys-
CC       310' in RELA and thereby inhibits the transcriptional activity of NF-
CC       kappa-B (By similarity). Deacetylates NR1D2 and abrogates the effect of
CC       KAT5-mediated relieving of NR1D2 transcription repression activity (By
CC       similarity). Component of a RCOR/GFI/KDM1A/HDAC complex that
CC       suppresses, via histone deacetylase (HDAC) recruitment, a number of
CC       genes implicated in multilineage blood cell development. Involved in
CC       CIART-mediated transcriptional repression of the circadian
CC       transcriptional activator: CLOCK-BMAL1 heterodimer. Required for the
CC       transcriptional repression of circadian target genes, such as PER1,
CC       mediated by the large PER complex or CRY1 through histone
CC       deacetylation. In addition to protein deacetylase activity, also has
CC       protein-lysine deacylase activity: acts as a protein decrotonylase and
CC       delactylase by mediating decrotonylation ((2E)-butenoyl) and
CC       delactylation (lactoyl) of histones, respectively (By similarity).
CC       {ECO:0000250|UniProtKB:O09106, ECO:0000250|UniProtKB:Q13547}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-acetyl-L-lysyl-[histone] + H2O = L-lysyl-[histone] +
CC         acetate; Xref=Rhea:RHEA:58196, Rhea:RHEA-COMP:9845, Rhea:RHEA-
CC         COMP:11338, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; EC=3.5.1.98;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58197;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-acetyl-L-lysyl-[protein] + H2O = L-lysyl-[protein] +
CC         acetate; Xref=Rhea:RHEA:58108, Rhea:RHEA-COMP:9752, Rhea:RHEA-
CC         COMP:10731, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:61930; Evidence={ECO:0000250|UniProtKB:Q13547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:58109;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-(2E)-butenoyl-L-lysyl-[protein] + H2O = (2E)-2-butenoate
CC         + L-lysyl-[protein]; Xref=Rhea:RHEA:69172, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15377, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:35899, ChEBI:CHEBI:137954;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69173;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(6)-[(S)-lactoyl]-L-lysyl-[protein] + H2O = (S)-lactate + L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:81387, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:19466, ChEBI:CHEBI:15377, ChEBI:CHEBI:16651,
CC         ChEBI:CHEBI:29969, ChEBI:CHEBI:231527;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:81388;
CC         Evidence={ECO:0000250|UniProtKB:Q13547};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:O15379};
CC   -!- ACTIVITY REGULATION: Inositol tetraphosphate (1D-myo-inositol 1,4,5,6-
CC       tetrakisphosphate) may act as an intermolecular glue between HDAC1 and
CC       N-Cor repressor complex components. {ECO:0000250|UniProtKB:O15379}.
CC   -!- SUBUNIT: Part of the core histone deacetylase (HDAC) complex composed
CC       of HDAC1, HDAC2, RBBP4 and RBBP7, the core complex associates with
CC       SIN3, SAP18 and SAP30 to form the SIN3 HDAC complex. Component of the
CC       nucleosome remodeling and deacetylase (NuRD) repressor complex,
CC       composed of core proteins MTA1, MTA2, MTA3, RBBP4, RBBP7, HDAC1, HDAC2,
CC       MBD2, MBD3, and peripherally associated proteins CDK2AP1, CDK2AP2,
CC       GATAD2A, GATAD2B, CHD3, CHD4 and CHD5. The exact stoichiometry of the
CC       NuRD complex is unknown, and some subunits such as MBD2 and MBD3,
CC       GATAD2A and GATAD2B, and CHD3, CHD4 and CHD5 define mutually exclusive
CC       NuRD complexes (By similarity). Component of a BHC histone deacetylase
CC       complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST
CC       and PHF21A/BHC80 (By similarity). The BHC complex may also contain
CC       ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I (By similarity). Component of a
CC       mSin3A corepressor complex that contains SIN3A, SAP130, SUDS3/SAP45,
CC       ARID4B/SAP180, HDAC1 and HDAC2 (By similarity). Found in a trimeric
CC       complex with APBB1 and TSHZ3; the interaction between HDAC1 and APBB1
CC       is mediated by TSHZ3 (By similarity). Forms a complex comprising APPL1,
CC       RUVBL2, APPL2, CTNNB1 and HDAC2 (By similarity). Component of a
CC       RCOR/GFI/KDM1A/HDAC complex (By similarity). Part of a complex composed
CC       of TRIM28, HDAC1, HDAC2 and EHMT2 (By similarity). Part of a complex
CC       containing at least CDYL, MIER1, MIER2, HDAC1 and HDAC2 (By
CC       similarity). The large PER complex involved in the histone
CC       deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A (By
CC       similarity). Associates with the 9-1-1 complex; interacts with HUS1 (By
CC       similarity). Found in a complex with DNMT3A and HDAC7. Found in a
CC       complex with YY1, SIN3A and GON4L (By similarity). Identified in a
CC       histone deacetylase complex that contains DNTTIP1, HDAC1 and MIDEAS;
CC       this complex assembles into a tetramer that contains four copies of
CC       each protein chain (By similarity). Found in a complex composed of at
CC       least SINHCAF, SIN3A, HDAC1, SAP30, RBBP4, OGT and TET1 (By
CC       similarity). Component of the SIN3B complex, which includes SIN3B,
CC       HDAC1, PHF12 and MORF4L1 (By similarity). Interacts with GFI1; the
CC       interaction is direct. Interacts directly with GFI1B (By similarity).
CC       Interacts with TSHZ3 (via N-terminus); the interaction is direct (By
CC       similarity). Interacts with APEX1; the interaction is not dependent on
CC       the acetylated status of APEX1 (By similarity). Interacts with BANP.
CC       Interacts with BAZ2A/TIP5 (By similarity). Interacts with BCL6 (By
CC       similarity). Interacts with BCOR (By similarity). Interacts with
CC       BHLHE40/DEC1 (By similarity). Interacts with BRCC3; this interaction is
CC       enhanced in the presence of PWWP2B (By similarity). Interacts with
CC       BRMS1 (By similarity). Interacts with BRMS1L (By similarity). Interacts
CC       with C10orf90/FATS (via its N-terminal); the interaction prevents
CC       binding of HDAC1 to CDKN1A/p21 and facilitates the acetylation and
CC       stabilization of CDKN1A/p21. Interacts with CBFA2T3 (By similarity).
CC       Interacts with CCAR2 (By similarity). Interacts with CDK2AP1 (By
CC       similarity). Interacts with CHD3 (By similarity). Interacts with CHD4
CC       (By similarity). Interacts with CHFR (By similarity). Interacts with
CC       CIART. Interacts with CDKN1A/p21. Interacts with CDK5 complexed to
CC       CDK5R1 (p25). Interacts with CRY1 (By similarity). Interacts with DAXX
CC       (By similarity). Interacts with DDIT3/CHOP (By similarity). Interacts
CC       with DDX5 (By similarity). Interacts with DHX36; this interaction
CC       occurs in a RNA-dependent manner (By similarity). Interacts with DNMT1
CC       (By similarity). Interacts with DNTTIP1 (By similarity). Interacts with
CC       E4F1 (By similarity). Interacts with EP300 (By similarity). Interacts
CC       with ERCC6 (By similarity). Interacts with GATAD2A (By similarity).
CC       Interacts with HCFC1 (By similarity). Interacts with HDAC9 (By
CC       similarity). Interacts with HUS1 (By similarity). Interacts with INSM1
CC       (By similarity). Interacts with KDM4A (By similarity). Interacts with
CC       KDM5A; this interaction impairs histone deacetylation (By similarity).
CC       Interacts with KDM5B (By similarity). Interacts with KLF1 (By
CC       similarity). Interacts with MBD3L2 (By similarity). Interacts with
CC       MIER1 (By similarity). Interacts with NFE4 (By similarity). Interacts
CC       with NR4A2/NURR1 (By similarity). Interacts with NR1D2 (via C-terminus)
CC       (By similarity). Interacts with NRIP1. Interacts with NSD2 (By
CC       similarity). Interacts with PACS2 (By similarity). Interacts with PHB2
CC       (By similarity). Interacts with PPHLN1 (By similarity). Interacts with
CC       PRDM6 (By similarity). Interacts with PRDM16 (By similarity). Interacts
CC       with PWWP2A in a MTA1-dependent manner. Interacts with PWWP2B (By
CC       similarity). Interacts with RB1 (By similarity). Interacts with RERE.
CC       Interacts with SANBR (via the BTB domain). Interacts with SAMSN1 (By
CC       similarity). Interacts with SAP30L (By similarity). Interacts with
CC       SETDB1 (By similarity). Interacts with SIN3A (By similarity). Interacts
CC       with SMAD3 (By similarity). Interacts with SMAD4; positively regulated
CC       by ZBTB7A (By similarity). Interacts with SMARCAD1 (By similarity).
CC       Interacts with SMARCA4/BRG1 (By similarity). Interacts with SMYD2 (By
CC       similarity). Interacts with SMYD4 (via MYND-type zinc finger) (By
CC       similarity). Interacts with SP1; the interaction deacetylates SP1 and
CC       regulates its transcriptional activity (By similarity). Interacts with
CC       SP3; the interaction deacetylates SP3 and regulates its transcriptional
CC       activity (By similarity). In vitro, C(18) ceramides increase this
CC       interaction and the subsequent SP3 deacetylation and SP3-mediated
CC       repression of the TERT promoter (By similarity). Interacts with
CC       SPEN/MINT (By similarity). Interacts with SPHK2 (By similarity).
CC       Interacts with SUV39H1 (By similarity). Interacts with TGIF (By
CC       similarity). Interacts with TGIF2 (By similarity). Interacts with TRAF6
CC       (By similarity). Interacts with TRIM28; the interaction recruits HDAC1
CC       to E2F1 and inhibits its acetylation (By similarity). Interacts with
CC       TSC22D3 isoform 1; this interaction affects HDAC1 activity on MYOG
CC       promoter and thus inhibits MYOD1 transcriptional activity (By
CC       similarity). Interacts with UHRF1 (By similarity). Interacts with UHRF2
CC       (By similarity). Interacts with ZBTB7A (By similarity). Interacts with
CC       ZMYND8 (By similarity). Interacts with ZMYND15. Interacts with ZNF431.
CC       Interacts with ZNF516; this interaction is enhanced in the presence of
CC       PWWP2B. Interacts with ZNF541 (By similarity). Interacts with ZNF638
CC       (By similarity). Interacts with ZNHIT1. Interacts with the non-histone
CC       region of MACROH2A1. Identified in a complex with HDAC2, KCTD19,
CC       DNTTIP1 and ZNF541. Interacts with MSX3 (By similarity). Interacts with
CC       VRK1 (By similarity). Interacts with SKOR2; the interaction is required
CC       for SKOR2 transcriptional repressor activity (By similarity).
CC       {ECO:0000250|UniProtKB:O09106, ECO:0000250|UniProtKB:Q13547}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q13547}.
CC   -!- PTM: Sumoylated on Lys-444 and Lys-476; which promotes enzymatic
CC       activity. Desumoylated by SENP1. {ECO:0000250|UniProtKB:Q13547}.
CC   -!- PTM: Phosphorylation on Ser-421 and Ser-423 promotes enzymatic activity
CC       and interactions with NuRD and SIN3 complexes. Phosphorylated by CDK5.
CC       {ECO:0000250|UniProtKB:Q13547}.
CC   -!- PTM: Ubiquitinated by CHFR and KCTD11, leading to its degradation by
CC       the proteasome. {ECO:0000250|UniProtKB:Q13547}.
CC   -!- SIMILARITY: Belongs to the histone deacetylase family. HD type 1
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR859057; CAH91250.1; -; mRNA.
DR   RefSeq; NP_001125738.1; NM_001132266.1.
DR   AlphaFoldDB; Q5RAG0; -.
DR   SMR; Q5RAG0; -.
DR   FunCoup; Q5RAG0; 3775.
DR   STRING; 9601.ENSPPYP00000001838; -.
DR   GeneID; 100172663; -.
DR   KEGG; pon:100172663; -.
DR   CTD; 3065; -.
DR   eggNOG; KOG1342; Eukaryota.
DR   InParanoid; Q5RAG0; -.
DR   OrthoDB; 1918432at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0016581; C:NuRD complex; ISS:UniProtKB.
DR   GO; GO:0070822; C:Sin3-type complex; IEA:UniProtKB-ARBA.
DR   GO; GO:0004407; F:histone deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0141221; F:histone deacetylase activity, hydrolytic mechanism; ISS:UniProtKB.
DR   GO; GO:0160009; F:histone decrotonylase activity; ISS:UniProtKB.
DR   GO; GO:0051059; F:NF-kappaB binding; IEA:UniProtKB-ARBA.
DR   GO; GO:0160008; F:protein decrotonylase activity; ISS:UniProtKB.
DR   GO; GO:0033558; F:protein lysine deacetylase activity; ISS:UniProtKB.
DR   GO; GO:0160216; F:protein lysine delactylase activity; ISS:UniProtKB.
DR   GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR   GO; GO:0031507; P:heterochromatin formation; IEA:UniProtKB-ARBA.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:UniProtKB-ARBA.
DR   GO; GO:0033148; P:positive regulation of intracellular estrogen receptor signaling pathway; IEA:UniProtKB-ARBA.
DR   CDD; cd10010; HDAC1; 1.
DR   FunFam; 3.40.800.20:FF:000003; Histone deacetylase; 1.
DR   Gene3D; 3.40.800.20; Histone deacetylase domain; 1.
DR   InterPro; IPR003084; HDAC_I/II.
DR   InterPro; IPR000286; HDACs.
DR   InterPro; IPR023801; His_deacetylse_dom.
DR   InterPro; IPR037138; His_deacetylse_dom_sf.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR10625:SF49; HISTONE DEACETYLASE 1; 1.
DR   PANTHER; PTHR10625; HISTONE DEACETYLASE HDAC1-RELATED; 1.
DR   Pfam; PF00850; Hist_deacetyl; 1.
DR   PIRSF; PIRSF037913; His_deacetylse_1; 1.
DR   PRINTS; PR01270; HDASUPER.
DR   PRINTS; PR01271; HISDACETLASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Biological rhythms; Chromatin regulator; Hydrolase;
KW   Isopeptide bond; Metal-binding; Methylation; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; S-nitrosylation; Transcription;
KW   Transcription regulation; Ubl conjugation; Zinc.
FT   CHAIN           1..482
FT                   /note="Histone deacetylase 1"
FT                   /id="PRO_0000304730"
FT   REGION          9..321
FT                   /note="Histone deacetylase"
FT   REGION          390..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        390..400
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..416
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        417..427
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   BINDING         27
FT                   /ligand="1D-myo-inositol 1,4,5,6-tetrakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57627"
FT                   /evidence="ECO:0000250|UniProtKB:O15379"
FT   BINDING         31
FT                   /ligand="1D-myo-inositol 1,4,5,6-tetrakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57627"
FT                   /evidence="ECO:0000250|UniProtKB:O15379"
FT   BINDING         176
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O15379"
FT   BINDING         178
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O15379"
FT   BINDING         264
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:O15379"
FT   BINDING         270
FT                   /ligand="1D-myo-inositol 1,4,5,6-tetrakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57627"
FT                   /evidence="ECO:0000250|UniProtKB:O15379"
FT   MOD_RES         74
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         220
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         261
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P70288"
FT   MOD_RES         273
FT                   /note="S-nitrosocysteine"
FT                   /evidence="ECO:0000250|UniProtKB:P70288"
FT   MOD_RES         393
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         406
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q92769"
FT   MOD_RES         409
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         421
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         423
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   MOD_RES         432
FT                   /note="N6-methylated lysine; by EHMT2"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        74
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q92769"
FT   CROSSLNK        438
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        444
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        444
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        456
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92769"
FT   CROSSLNK        457
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        473
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q92769"
FT   CROSSLNK        476
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        476
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
FT   CROSSLNK        480
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13547"
SQ   SEQUENCE   482 AA;  55103 MW;  4D35B7C1ED7838D6 CRC64;
     MAQTQGTRRK VCYYYDGDVG NYYYGQGHPM KPHRIRMTHN LLLNYGLYRK MEIYRPHKAN
     AEEMTKYHSD DYIKFLRSIR PDNMSEYSKQ MQRFNVGEDC PVFDGLFEFC QLSTGGSVAS
     AVKLNKQQTD IAVNWAGGLH HAKKSEASGF CYVNDIVLAI LELLKYHQRV LYIDIDIHHG
     DGVEEAFYTT DRVMTVSFHK YGEYFPGTGD LRDIGAGKGK YYAVNYPLRD GIDDESYEAI
     FKPVMSKVME MFQPSAVVLQ CGSDSLSGDR LGCFNLTIKG HAKCVEFVKS FNLPMLMLGG
     GGYTIRNVAR CWTYETAVAL DTEIPNELPY NDYFEYFGPD FKLHISPSNM TNQNTNEYLE
     KIKQRLFENL RMLPHAPGVQ MQAIPEDAIP EESGDEDEDD PDKRISICSS DKRIACEEEF
     SDSEEEGEGG RKNSSNFKKA KRVKTEDEKE KDPEEKKEVT EEEKTKEEKP EAKGVKEEVK
     LA
//