MO4L2_PANTR
ID MO4L2_PANTR Reviewed; 288 AA.
AC A5A6J5;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Mortality factor 4-like protein 2;
GN Name=MORF4L2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=17574350; DOI=10.1016/j.gene.2007.04.013;
RA Sakate R., Suto Y., Imanishi T., Tanoue T., Hida M., Hayasaka I.,
RA Kusuda J., Gojobori T., Hashimoto K., Hirai M.;
RT "Mapping of chimpanzee full-length cDNAs onto the human genome unveils
RT large potential divergence of the transcriptome.";
RL Gene 399:1-10(2007).
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex which
CC is involved in transcriptional activation of select genes principally
CC by acetylation of nucleosomal histone H4 and H2A. This modification may
CC both alter nucleosome - DNA interactions and promote interaction of the
CC modified histones with other proteins which positively regulate
CC transcription. This complex may be required for the activation of
CC transcriptional programs associated with oncogene and proto-oncogene
CC mediated growth induction, tumor suppressor mediated growth arrest and
CC replicative senescence, apoptosis, and DNA repair. The NuA4 complex
CC ATPase and helicase activities seem to be, at least in part,
CC contributed by the association of RUVBL1 and RUVBL2 with EP400. NuA4
CC may also play a direct role in DNA repair when directly recruited to
CC sites of DNA damage. Also a component of the MSIN3A complex which acts
CC to repress transcription by deacetylation of nucleosomal histones (By
CC similarity). {ECO:0000250}.
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 and VPS72/YL1. The NuA4 complex interacts with MYC and the
CC adenovirus E1A protein. MORF4L1 may also participate in the formation
CC of NuA4 related complexes which lack the KAT5/TIP60 catalytic subunit,
CC but which include the SWI/SNF related protein SRCAP. Component of the
CC MSIN3A histone deacetylase complex, which includes SIN3A, HDAC2,
CC ARID4B, MORF4L1, RBBP4/RbAp48, and RBBP7/RbAp46. Interacts with MRFAP1
CC and RB1. May also interact with one or more as yet undefined members of
CC the TLE (transducin-like enhancer of split) family of transcriptional
CC repressors (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00972}.
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DR EMBL; AB222123; BAF62368.1; -; mRNA.
DR RefSeq; NP_001092032.1; NM_001098562.1.
DR RefSeq; XP_009437670.1; XM_009439395.1.
DR RefSeq; XP_009437671.1; XM_009439396.1.
DR RefSeq; XP_009437672.1; XM_009439397.1.
DR RefSeq; XP_009437673.1; XM_009439398.1.
DR RefSeq; XP_009437674.1; XM_009439399.1.
DR RefSeq; XP_009437675.1; XM_009439400.1.
DR RefSeq; XP_009437676.1; XM_009439401.1.
DR RefSeq; XP_009437677.1; XM_009439402.1.
DR RefSeq; XP_009437678.1; XM_009439403.1.
DR RefSeq; XP_009437679.1; XM_009439404.1.
DR RefSeq; XP_009437680.1; XM_009439405.1.
DR RefSeq; XP_009437681.1; XM_009439406.1.
DR RefSeq; XP_009437682.1; XM_009439407.1.
DR AlphaFoldDB; A5A6J5; -.
DR SMR; A5A6J5; -.
DR STRING; 9598.ENSPTRP00000042777; -.
DR PaxDb; A5A6J5; -.
DR GeneID; 465783; -.
DR KEGG; ptr:465783; -.
DR CTD; 9643; -.
DR eggNOG; KOG3001; Eukaryota.
DR HOGENOM; CLU_039566_4_0_1; -.
DR InParanoid; A5A6J5; -.
DR OrthoDB; 1624495at2759; -.
DR TreeFam; TF323400; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0000123; C:histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0043968; P:histone H2A acetylation; IBA:GO_Central.
DR GO; GO:0043967; P:histone H4 acetylation; IBA:GO_Central.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.274.30; -; 1.
DR InterPro; IPR008676; MRG.
DR InterPro; IPR038217; MRG_C_sf.
DR InterPro; IPR026541; MRG_dom.
DR InterPro; IPR038012; MRGX.
DR PANTHER; PTHR10880; PTHR10880; 1.
DR PANTHER; PTHR10880:SF25; PTHR10880:SF25; 1.
DR Pfam; PF05712; MRG; 1.
DR PROSITE; PS51640; MRG; 1.
PE 2: Evidence at transcript level;
KW Chromatin regulator; DNA damage; DNA repair; Growth regulation; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..288
FT /note="Mortality factor 4-like protein 2"
FT /id="PRO_0000297552"
FT DOMAIN 117..288
FT /note="MRG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00972"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15014"
SQ SEQUENCE 288 AA; 32308 MW; C9EFF517C76A565D CRC64;
MSSRKQGSQP RGQQSAEEEN FKKPTRSNMQ RSKMRGASSG KKTAGPQQKN LEPALPGRWG
GRSAENPPSG SVRKTRKNKQ KTPGNGDGGS TSEAPQPPRK KRARADPTVE SEEAFKNRME
VKVKIPEELK PWLVEDWDLV TRQKQLFQLP AKKNVDAILE EYANCKKSQG NVDNKEYAVN
EVVAGIKEYF NVMLGTQLLY KFERPQYAEI LLAHPDAPMS QVYGAPHLLR LFVRIGAMLA
YTPLDEKSLA LLLGYLHDFL KYLAKNSASL FTASDYKVAS AEYHRKAL
