MIER1_PONAB
ID MIER1_PONAB Reviewed; 512 AA.
AC Q5REE1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Mesoderm induction early response protein 1;
DE Short=Early response 1;
DE Short=Er1;
DE Short=Mi-er1;
GN Name=MIER1;
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=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Transcriptional repressor regulating the expression of a
CC number of genes including SP1 target genes. Probably functions through
CC recruitment of HDAC1 a histone deacetylase involved in chromatin
CC silencing (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with HDAC1. Part of a complex containing at least
CC CDYL, MIER1, MIER2, HDAC1 and HDAC2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH89866.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR857588; CAH89866.1; ALT_INIT; mRNA.
DR AlphaFoldDB; Q5REE1; -.
DR STRING; 9601.ENSPPYP00000001469; -.
DR Ensembl; ENSPPYT00000047828; ENSPPYP00000041036; ENSPPYG00000001261.
DR eggNOG; KOG4329; Eukaryota.
DR GeneTree; ENSGT01030000234573; -.
DR InParanoid; Q5REE1; -.
DR Proteomes; UP000001595; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017053; C:transcription repressor complex; ISS:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:InterPro.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR040138; MIER/MTA.
DR InterPro; IPR031169; MIER1.
DR InterPro; IPR045787; MIER1/3_C.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR PANTHER; PTHR10865; PTHR10865; 1.
DR PANTHER; PTHR10865:SF24; PTHR10865:SF24; 1.
DR Pfam; PF01448; ELM2; 1.
DR Pfam; PF19426; MIER1_beta_C; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 2: Evidence at transcript level;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..512
FT /note="Mesoderm induction early response protein 1"
FT /id="PRO_0000197143"
FT DOMAIN 180..278
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 283..335
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 75..173
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..284
FT /note="Interaction with HDAC1"
FT /evidence="ECO:0000250"
FT REGION 366..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..50
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..106
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..484
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 141
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 155
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 448
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT CROSSLNK 239
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
FT CROSSLNK 420
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q8N108"
SQ SEQUENCE 512 AA; 58013 MW; F78622C7FC507907 CRC64;
MAEPSVESSS PGGSATSDDH EFDPSADMLV HDFDDERTLE EEEMMEGETN FSSEIEDLAR
EGDMPIHELL SLYGYGSTVR LPEEDEEEEE EEEEGEDDED ADNDDNSGCS GENKEENIKD
SSGQEDETQS SNDDPSQSVA SQDAQEIIRP RRCKYFDTNS EVEEESEEDE DYIPSEDWKK
EIMVGSMFQA EIPVGICRYK ENEKVYENDD QLLWDPEYLP EDKVIIFLKD ASRRTGDEKG
VEAIPEGSHI KDNEQALYEL VKCNFDTEEA LRRLRFNVKA AREELSVWTE EECRNFEQGL
KAYGKDFHLI QANKVRTRSV GECVAFYYMW KKSERYDFFA QQTRFGKKKY NLHPGVTDYM
DRLLDESESA ASSRAPSPPP TASNSSNSQS EKEDGTVSTT NQNGVSSNGP GEILNKEEVK
VEGLHINGPT GGNKKPLHAD MDTNGYETDN LTTDPKLAHM TARNENDFDE KSERPAKRRR
VNSNGKESPG SSEFFQEAVS HGKFEELENT DD
