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IID00492
UniprotQ92993
ProteinHistone acetyltransferase KAT5
GeneKAT5
OrganismHomo sapiens
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS
xml
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
513
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 1-80 Homo heptamer :
 Evidence X-RAY 4qqg A Reference
       Region 4qqg A 1-71 order
       Region 4qqg A 72-80 disorder
 Evidence X-RAY 4qqg B Reference
       Region 4qqg B 1-2 disorder
       Region 4qqg B 3-19 order
       Region 4qqg B 20-22 disorder
       Region 4qqg B 23-71 order
       Region 4qqg B 72-80 disorder
 Evidence X-RAY 4qqg C Reference
       Region 4qqg C 1-1 disorder
       Region 4qqg C 2-19 order
       Region 4qqg C 20-20 disorder
       Region 4qqg C 21-72 order
       Region 4qqg C 73-80 disorder
 Evidence X-RAY 4qqg D Reference
       Region 4qqg D 1-2 disorder
       Region 4qqg D 3-71 order
       Region 4qqg D 72-80 disorder
 Evidence X-RAY 4qqg E Reference
       Region 4qqg E 1-72 order
       Region 4qqg E 73-80 disorder
 Evidence X-RAY 4qqg F Reference
       Region 4qqg F 1-2 disorder
       Region 4qqg F 3-71 order
       Region 4qqg F 72-80 disorder
 Evidence X-RAY 4qqg G Reference
       Region 4qqg G 1-71 order
       Region 4qqg G 72-80 disorder
Seq 5-78 Monomer :
 Evidence NMR 2eko A Reference
       Region 2eko A 5-78 order
       Region 2eko A 52-52 high_rmsd
       Region 2eko A 74-78 high_rmsd
Seq 227-506 Monomer :
 Evidence X-RAY 2ou2 A Reference
       Region 2ou2 A 227-229 disorder
       Region 2ou2 A 230-426 order
       Region 2ou2 A 427-437 disorder
       Region 2ou2 A 438-474 order
       Region 2ou2 A 475-492 disorder
       Region 2ou2 A 493-504 order
       Region 2ou2 A 505-506 disorder
Seqphosphorylation
    199-199 Phosphoserine
    90-90 Phosphoserine; by CDK1 and CDK9
    86-86 Phosphoserine; by GSK3
Seqacetylation
    148-148 N6-acetyllysine; by autocatalysis
    327-327 N6-acetyllysine; by autocatalysis
    189-189 N6-acetyllysine; by autocatalysis
    187-187 N6-acetyllysine; by autocatalysis
    150-150 N6-acetyllysine; by autocatalysis
    120-120 N6-acetyllysine; by autocatalysis
    104-104 N6-acetyllysine; by autocatalysis
    52-52 N6-acetyllysine
 
Prediction
NeProc
Disorder 1-4,80-223,509-513
Order 5-79,224-487,492-508
ProS 1-4,80-93,107-158,164-167,183-189,204-215,509-513
AlphaFold
Disorder 1-5,73-149,155-224,510-513
Order 6-72,150-154,225-509
Pfam Hmmer
PF01853 285-477 1.8e-148
SEG 439-452
Function
Function in SwissProt
Catalytic subunit of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (PubMed:12776177, PubMed:15042092, PubMed:15121871, PubMed:15310756, PubMed:14966270, PubMed:16387653, PubMed:19909775, PubMed:15196461). This modification may both alter nucleosome-DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription (PubMed:12776177, PubMed:15042092, PubMed:15121871, PubMed:15310756, PubMed:14966270, PubMed:15196461). This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (PubMed:15196461). NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage (PubMed:15196461). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (PubMed:24463511). Also acetylates non-histone proteins, such as ATM, NR1D2, RAN, FOXP3, ULK1 and RUBCNL/Pacer (PubMed:16141325, PubMed:17360565, PubMed:17996965, PubMed:29040603, PubMed:30704899). Directly acetylates and activates ATM (PubMed:16141325). Relieves NR1D2-mediated inhibition of APOC3 expression by acetylating NR1D2 (PubMed:17996965). Promotes FOXP3 acetylation and positively regulates its transcriptional repressor activity (PubMed:17360565). Acetylates RAN at 'Lys-134' (PubMed:29040603). Together with GSK3 (GSK3A or GSK3B), acts as a regulator of autophagy: phosphorylated at Ser-86 by GSK3 under starvation conditions, leading to activate acetyltransferase activity and promote acetylation of key autophagy regulators, such as ULK1 and RUBCNL/Pacer (PubMed:30704899).