{PDOC52052}
{PS52052; PEHE}
{BEGIN}
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* PEHE domain profile *
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The PEHE  domain,  named after four highly conserved characteristic amino acid
residues (P,  E,  H, E) is found in subunits of two protein complexes, MSL and
NSL, involved  in  histone  acetylation  in both vertebrates and invertebrates
[1,2]:

 - Animal  Male-specific lethal 1 (MSL1), a non-catalytic component of the MSL
   histone acetyltransferase  complex,  a  multiprotein  complex that mediates
   histone H4  acetylation  at  'Lys-16'  (H4K16ac),  an  epigenetic mark that
   prevents chromatin compaction.
 - Vertebrate  KAT8 regulatory NSL complex subunit 1 (KANSL1), a non-catalytic
   component of  the  NSL  histone  acetyltransferase  complex, a multiprotein
   complex that  mediates  histone  H4  acetylation  at  'Lys-5'-  and 'Lys-8'
   (H4K5ac and H4K8ac) at transcription start sites and promotes transcription
   initiation.
 - Vertebrate KAT8 regulatory NSL complex subunit 1-like protein (KANSL1L).

The N-terminal half the PEHE domain, which contains a beta strand, an extended
region, and a long alpha helix (see <PDB:4DNC>), interacts with the HAT domain
(see <PDOC51726>) of the KAT8 histone acetyltransferase (also known as MOF and
MYST1), a  subunit  of  both MSL and NSL complexes. The C-terminal half of the
MSL1 PEHE  domain  forms a short helical hairpin and wraps around the MSL3 MRG
domain (see <PDOC51640>) as an extended chain (see <PDB:2Y0N>) [2,3,4,5].

The profile we developed covers the entire PEHE domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2024 / First entry.

[ 1] Marin I.
     "Evolution of chromatin-remodeling complexes: comparative genomics
     reveals the  ancient origin of 'novel' compensasome genes."
     J. Mol. Evol. 56:527-539(2003).
     PubMed=12698291; DOI=10.1007/s00239-002-2422-1
[ 2] Panagopoulos I., Gorunova L., Bjerkehagen B., Heim S.
     "Novel KAT6B-KANSL1 fusion gene identified by RNA sequencing in
     retroperitoneal  leiomyoma with t(10;17)(q22;q21)."
     PLoS One. 10:E0117010-E0117010(2015).
     PubMed=25621995; DOI=10.1371/journal.pone.0117010
[ 3] Morales V., Straub T., Neumann M.F., Mengus G., Akhtar A.,
     Becker P.B.
     "Functional integration of the histone acetyltransferase MOF into the
     dosage  compensation complex."
     EMBO. J. 23:2258-2268(2004).
     PubMed=15141166; DOI=10.1038/sj.emboj.7600235
[ 4] Kadlec J., Hallacli E., Lipp M., Holz H., Sanchez-Weatherby J.,
     Cusack S., Akhtar A.
     "Structural basis for MOF and MSL3 recruitment into the dosage
     compensation  complex by MSL1."
     Nat. Struct. Mol. Biol. 18:142-149(2011).
     PubMed=21217699; DOI=10.1038/nsmb.1960
[ 5] Huang J., Wan B., Wu L., Yang Y., Dou Y., Lei M.
     "Structural insight into the regulation of MOF in the male-specific
     lethal complex  and the non-specific lethal complex."
     Cell. Res. 22:1078-1081(2012).
     PubMed=22547026; DOI=10.1038/cr.2012.72

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