KAT5_PONAB
ID KAT5_PONAB Reviewed; 461 AA.
AC Q5RBG4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Histone acetyltransferase KAT5 {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000250|UniProtKB:Q92993};
DE AltName: Full=60 kDa Tat-interactive protein {ECO:0000250|UniProtKB:Q92993};
DE Short=Tip60 {ECO:0000250|UniProtKB:Q92993};
DE AltName: Full=Histone acetyltransferase HTATIP;
DE AltName: Full=Lysine acetyltransferase 5;
DE AltName: Full=Protein 2-hydroxyisobutyryltransferase KAT5 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92993};
DE AltName: Full=Protein acetyltransferase KAT5 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92993};
DE AltName: Full=Protein crotonyltransferase KAT5 {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92993};
GN Name=KAT5 {ECO:0000250|UniProtKB:Q92993};
GN Synonyms=HTATIP, TIP60 {ECO:0000250|UniProtKB:Q92993};
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: Catalytic subunit of the NuA4 histone acetyltransferase
CC complex, a multiprotein complex involved in transcriptional activation
CC of select genes principally by acetylation of nucleosomal histones H2A
CC and H4. Histone acetylation alters nucleosome-DNA interactions and
CC promotes interaction of the modified histones with other proteins which
CC positively regulate transcription. The NuA4 histone acetyltransferase
CC complex is required for the activation of transcriptional programs
CC associated with proto-oncogene mediated growth induction, tumor
CC suppressor mediated growth arrest and replicative senescence,
CC apoptosis, and DNA repair. The NuA4 complex plays a direct role in
CC repair of DNA double-strand breaks (DSBs) by promoting homologous
CC recombination (HR): the complex inhibits TP53BP1 binding to chromatin
CC via MBTD1, which recognizes and binds histone H4 trimethylated at 'Lys-
CC 20' (H4K20me), and KAT5 that catalyzes acetylation of 'Lys-15' of
CC histone H2A (H2AK15ac), thereby blocking the ubiquitination mark
CC required for TP53BP1 localization at DNA breaks. Also involved in DSB
CC repair by mediating acetylation of 'Lys-5' of histone H2AX (H2AXK5ac),
CC promoting NBN/NBS1 assembly at the sites of DNA damage (By similarity).
CC The NuA4 complex plays a key role in hematopoietic stem cell
CC maintenance and is required to maintain acetylated H2A.Z/H2AZ1 at MYC
CC target genes. The NuA4 complex is also required for spermatid
CC development by promoting acetylation of histones: histone
CC hyperacetylation is required for histone replacement during the
CC transition from round to elongating spermatids (By similarity).
CC Component of a SWR1-like complex that specifically mediates the removal
CC of histone H2A.Z/H2AZ1 from the nucleosome. Also acetylates non-histone
CC proteins, such as ARNTL/BMAL1, ATM, AURKB, CHKA, CGAS, ERCC4/XPF,
CC LPIN1, NDC80/HEC1, NR1D2, RAN, SOX4, FOXP3, ULK1 and RUBCNL/Pacer.
CC Directly acetylates and activates ATM. Promotes nucleotide excision
CC repair (NER) by mediating acetylation of ERCC4/XPF, thereby promoting
CC formation of the ERCC4-ERCC1 complex. Relieves NR1D2-mediated
CC inhibition of APOC3 expression by acetylating NR1D2. Acts as a
CC regulator of regulatory T-cells (Treg) by catalyzing FOXP3 acetylation,
CC thereby promoting FOXP3 transcriptional repressor activity. Involved in
CC skeletal myoblast differentiation by mediating acetylation of SOX4.
CC Catalyzes acetylation of APBB1/FE65, increasing its transcription
CC activator activity (By similarity). Promotes transcription elongation
CC during the activation phase of the circadian cycle by catalyzing
CC acetylation of ARNTL/BMAL1, promoting elongation of circadian
CC transcripts (By similarity). Together with GSK3 (GSK3A or GSK3B), acts
CC as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under
CC starvation conditions, leading to activate acetyltransferase activity
CC and promote acetylation of key autophagy regulators, such as ULK1 and
CC RUBCNL/Pacer. Acts as a regulator of the cGAS-STING innate antiviral
CC response by catalyzing acetylation the N-terminus of CGAS, thereby
CC promoting CGAS DNA-binding and activation. Also regulates lipid
CC metabolism by mediating acetylation of CHKA or LPIN1. Promotes
CC lipolysis of lipid droplets following glucose deprivation by mediating
CC acetylation of isoform 1 of CHKA, thereby promoting monomerization of
CC CHKA and its conversion into a tyrosine-protein kinase. Acts as a
CC regulator of fatty-acid-induced triacylglycerol synthesis by catalyzing
CC acetylation of LPIN1, thereby promoting the synthesis of
CC diacylglycerol. In addition to protein acetyltransferase, can use
CC different acyl-CoA substrates, such as (2E)-butenoyl-CoA (crotonyl-CoA)
CC and 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA), and is able to
CC mediate protein crotonylation and 2-hydroxyisobutyrylation,
CC respectively. Acts as a key regulator of chromosome segregation and
CC kinetochore-microtubule attachment during mitosis by mediating
CC acetylation or crotonylation of target proteins. Catalyzes acetylation
CC of AURKB at kinetochores, increasing AURKB activity and promoting
CC accurate chromosome segregation in mitosis. Acetylates RAN during
CC mitosis, promoting microtubule assembly at mitotic chromosomes.
CC Acetylates NDC80/HEC1 during mitosis, promoting robust kinetochore-
CC microtubule attachment. Catalyzes crotonylation of MAPRE1/EB1, thereby
CC ensuring accurate spindle positioning in mitosis (By similarity).
CC {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000250|UniProtKB:Q92993}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-butenoyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-
CC (2E)-butenoyl-L-lysyl-[protein]; Xref=Rhea:RHEA:53908, Rhea:RHEA-
CC COMP:9752, Rhea:RHEA-COMP:13707, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:137954; Evidence={ECO:0000250|UniProtKB:Q92993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53909;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = CoA + H(+) +
CC N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein]; Xref=Rhea:RHEA:24180,
CC Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15921, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:131780,
CC ChEBI:CHEBI:144968; Evidence={ECO:0000250|UniProtKB:Q92993};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24181;
CC Evidence={ECO:0000250|UniProtKB:Q92993};
CC -!- ACTIVITY REGULATION: Acyltransferase and acetyltransferase activities
CC are activated by phosphorylation and autoacetylation. Autoacetylation
CC activates the histone acetyltransferase activity.
CC {ECO:0000250|UniProtKB:Q92993}.
CC -!- SUBUNIT: Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41, VPS72/YL1 and MEAF6 (By similarity). KAT5/TIP60, EPC1,
CC and ING3 together constitute a minimal HAT complex termed Piccolo NuA4.
CC The NuA4 complex interacts with MYC. Interacts with ATM. Interacts with
CC JADE1. Interacts with PLA2G4A/CPLA2, EDNRA and HDAC7. Interacts with
CC the cytoplasmic tail of APP and APBB1/FE65. Interacts with TRIM24 and
CC TRIM68. Forms a complex with SENP6 and UBE2I in response to UV
CC irradiation. Identified in a complex with HINT1. Interacts with ATF2
CC and CUL3. Interacts with NR1D2 (via N-terminus). Component of a SWR1-
CC like complex (By similarity). Interacts with FOXP3 (By similarity).
CC Interacts with ZBTB49 (By similarity). Interacts with SRF (By
CC similarity). Interacts with ATF3; promoting autoacetylation and
CC deubiquitination by USP7. Interacts with EP300/p300; interaction
CC promotes KAT5 autoacetylation. Interacts with PRKDC; interaction is
CC impaired following KAT5 sumoylation (By similarity).
CC {ECO:0000250|UniProtKB:Q8CHK4, ECO:0000250|UniProtKB:Q92993}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92993}.
CC Chromosome {ECO:0000250|UniProtKB:Q92993}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q92993}. Chromosome, centromere, kinetochore
CC {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000250|UniProtKB:Q92993}. Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q92993}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q92993}. Note=Upon stimulation with EDN1, it is
CC exported from the nucleus to the perinuclear region and UV irradiation
CC induces translocation into punctuate subnuclear structures named
CC nuclear bodies. Transiently localizes to kinetochores in early mitosis.
CC Localizes to spindle poles when chromosomes align during metaphase (By
CC similarity). Localizes in the cytoplasm and nucleus of round spermatids
CC (By similarity). {ECO:0000250|UniProtKB:Q8CHK4,
CC ECO:0000250|UniProtKB:Q92993}.
CC -!- PTM: Phosphorylated on Ser-86 and Ser-90; enhanced during G2/M phase.
CC The phosphorylated form has a higher activity. Phosphorylation at Ser-
CC 90 by CDK1 or CDK9 is a prerequisite for phosphorylation at Ser-86 by
CC GSK3. Phosphorylation at Ser-86 by GSK3 (GSK3A or GSK3B) activates
CC acetyltransferase and acyltransferase activities. Phosphorylation at
CC Ser-90 by CDK9 promotes KAT5 recruitment to chromatin. Phosphorylation
CC by VRK1 following DNA damage promotes KAT5 association with chromatin
CC and histone acetyltransferase activity. {ECO:0000250|UniProtKB:Q92993}.
CC -!- PTM: Autoacetylated. Autoacetylation is required for histone
CC acetyltransferase activity. Autoacetylation at Lys-275 is facilitated
CC by interaction with EP300/p300: it prevents ubiquitination and
CC subsequent degradation by the proteasome and promotes acetylation of
CC target proteins. Deacetylated by HDAC3 and SIRT1. Deacetylation by
CC HDAC3 promotes its ubiquitination and cytoplasmic localization.
CC {ECO:0000250|UniProtKB:Q92993}.
CC -!- PTM: Sumoylated by UBE2I at Lys-378 and Lys-399, leading to increase of
CC its histone acetyltransferase activity in UV-induced DNA damage
CC response, as well as its translocation to nuclear bodies. Sumoylation
CC with SUMO2 by PIAS4 at Lys-378 promotes repair of DNA double-strand
CC breaks (DSBs) via homologous recombination (HR). Sumoylation by PIAS4
CC impairs interaction with PRKDC, inhibiting non-homologous end joining
CC (NHEJ)-mediated repair of DSBs, thereby facilitating HR. Desumoylated
CC by SENP3. {ECO:0000250|UniProtKB:Q92993}.
CC -!- PTM: Ubiquitinated by MDM2, leading to its proteasome-dependent
CC degradation. Ubiquitination is prevented by autoacetylation at Lys-275.
CC Ubiquitinated following deacetylation by HDAC3, leading to cytoplasmic
CC localization. Deubiquitinated by USP7 following interaction with ATF3,
CC promoting its stabilization. {ECO:0000250|UniProtKB:Q92993}.
CC -!- SIMILARITY: Belongs to the MYST (SAS/MOZ) family. {ECO:0000305}.
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DR EMBL; CR858684; CAH90896.1; -; mRNA.
DR RefSeq; NP_001127347.1; NM_001133875.1.
DR AlphaFoldDB; Q5RBG4; -.
DR SMR; Q5RBG4; -.
DR PRIDE; Q5RBG4; -.
DR GeneID; 100174410; -.
DR KEGG; pon:100174410; -.
DR CTD; 10524; -.
DR InParanoid; Q5RBG4; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISS:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032777; C:Piccolo NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0000812; C:Swr1 complex; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0043998; F:H2A histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0004402; F:histone acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106226; F:peptide 2-hydroxyisobutyryltransferase activity; IEA:RHEA.
DR GO; GO:0140065; F:peptide butyryltransferase activity; ISS:UniProtKB.
DR GO; GO:0140064; F:peptide crotonyltransferase activity; ISS:UniProtKB.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISS:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006978; P:DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator; ISS:UniProtKB.
DR GO; GO:0006302; P:double-strand break repair; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; ISS:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:1905691; P:lipid droplet disassembly; ISS:UniProtKB.
DR GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR GO; GO:0018394; P:peptidyl-lysine acetylation; ISS:UniProtKB.
DR GO; GO:1902425; P:positive regulation of attachment of mitotic spindle microtubules to kinetochore; ISS:UniProtKB.
DR GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR GO; GO:0042753; P:positive regulation of circadian rhythm; ISS:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:1900051; P:positive regulation of histone exchange; ISS:UniProtKB.
DR GO; GO:0062033; P:positive regulation of mitotic sister chromatid segregation; ISS:UniProtKB.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0010867; P:positive regulation of triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
DR GO; GO:0007286; P:spermatid development; ISS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR002717; HAT_MYST-type.
DR InterPro; IPR037995; KAT5/Tip60.
DR InterPro; IPR025995; Tudor-knot.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR040706; Zf-MYST.
DR PANTHER; PTHR10615:SF183; PTHR10615:SF183; 1.
DR Pfam; PF01853; MOZ_SAS; 1.
DR Pfam; PF11717; Tudor-knot; 1.
DR Pfam; PF17772; zf-MYST; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51726; MYST_HAT; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Acyltransferase; Centromere; Chromatin regulator;
KW Chromosome; Cytoplasm; Cytoskeleton; DNA damage; DNA repair;
KW Growth regulation; Immunity; Innate immunity; Isopeptide bond; Kinetochore;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..461
FT /note="Histone acetyltransferase KAT5"
FT /id="PRO_0000245806"
FT DOMAIN 8..65
FT /note="Tudor-knot"
FT /evidence="ECO:0000255"
FT DOMAIN 175..452
FT /note="MYST-type HAT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT ZN_FING 208..233
FT /note="C2HC MYST-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01063"
FT REGION 70..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..461
FT /note="Interaction with ATF2"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT ACT_SITE 351
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 318..320
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 325..331
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 355
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT BINDING 364
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q9H7Z6"
FT MOD_RES 52
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 96
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 98
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 135
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 137
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT MOD_RES 275
FT /note="N6-acetyllysine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
FT CROSSLNK 399
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q92993"
SQ SEQUENCE 461 AA; 53077 MW; 5A0E9324550AF246 CRC64;
MAEVGEIIEG CRLPVLRRNQ DNEDEWPLAE ILSVKDISGR KLFYVHYIDF NKRLDEWVTH
ERLDLKKIQF PKKEAKTPTK NGLPGSRPGS PEREVKRKVE VVSPATPVPS ETAPASVFPQ
NGAARRAVAA QPGRKRKSNC LGTDEDSQDS SDGIPSAPRM TGSLVSDRSH DDIVTRMKNI
ECIELGRHRL KPWYFSPYPQ ELTTLPVLYL CEFCLKYGRS LKCLQRHLTK CDLRHPPGNE
IYRKGTISFF EIDGRKNKSY SQNLCLLAKC FLDHKTLYYD TDPFLFYVMT EYDCKGFHIV
GYFSKEKEST EDYNVACILT LPPYQRRGYG KLLIEFSYEL SKVEGKTGTP EKPLSDLGLL
SYRSYWSQTI LEILMGLKSE SGERPQITIN EISEITSIKK EDVISTLQYL NLINYYKGQY
ILTLSEDIVD GHERAMLKRL LRIDSKCLHF TPKDWSKRGK W
