BMI1A_DANRE
ID BMI1A_DANRE Reviewed; 320 AA.
AC Q8JIR0; Q7ZWG4;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Polycomb complex protein BMI-1-A;
DE AltName: Full=Polycomb group RING finger protein 4-A;
GN Name=bmi1a; Synonyms=bmi1, pcgf4a, psc1;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH CBX2, DEVELOPMENTAL STAGE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12051733; DOI=10.1016/s0006-291x(02)00497-7;
RA Kawamura A., Yokota S., Yamada K., Inoue H., Inohaya K., Yamazaki K.,
RA Yasumasu I., Higashinakagawa T.;
RT "pc1 and psc1, zebrafish homologs of Drosophila Polycomb and Posterior sex
RT combs, encode nuclear proteins capable of complex interactions.";
RL Biochem. Biophys. Res. Commun. 294:456-463(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development. PcG PRC1 complex acts via chromatin remodeling and
CC modification of histones; it mediates monoubiquitination of histone H2A
CC 'Lys-119', rendering chromatin heritably changed in its expressibility.
CC In the PRC1 complex, it is required to stimulate the E3 ubiquitin-
CC protein ligase activity of rnf2. {ECO:0000250|UniProtKB:P35226}.
CC -!- SUBUNIT: Component of a PRC1-like complex (By similarity). Homodimer.
CC Interacts with cbx2. {ECO:0000250|UniProtKB:P35226,
CC ECO:0000269|PubMed:12051733}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12051733}.
CC -!- DEVELOPMENTAL STAGE: Maternally derived transcript is detected at high
CC levels at 1 and 3 hours post-fertilization (hpf). Not detectable at 6
CC and 9 hpf. Detected at intermediate levels at 12 and 15 hpf. Highly
CC expressed at 18 and 24 hpf, after which expression decreases again.
CC Detected in the anterior embryo at the 6 somites stage. Detected in
CC hindbrain, rhombomeres and telencephalon at the 18 somites stage.
CC Restricted to the anterior embryo, including brain, otic vesicles, and
CC optic stalks in 24 hpf embryo. Detected in pectoral fin buds in 48 hpf
CC embryo. {ECO:0000269|PubMed:12051733}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC01266.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB074153; BAC01266.1; ALT_INIT; mRNA.
DR EMBL; BC049423; AAH49423.1; -; mRNA.
DR RefSeq; NP_919347.1; NM_194366.1.
DR AlphaFoldDB; Q8JIR0; -.
DR SMR; Q8JIR0; -.
DR BioGRID; 80329; 3.
DR STRING; 7955.ENSDARP00000106943; -.
DR PaxDb; Q8JIR0; -.
DR GeneID; 321505; -.
DR KEGG; dre:321505; -.
DR CTD; 321505; -.
DR ZFIN; ZDB-GENE-030131-224; bmi1a.
DR eggNOG; KOG2660; Eukaryota.
DR InParanoid; Q8JIR0; -.
DR OrthoDB; 1344247at2759; -.
DR PhylomeDB; Q8JIR0; -.
DR TreeFam; TF324206; -.
DR Reactome; R-DRE-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-DRE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-DRE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-DRE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-DRE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-DRE-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-DRE-8943724; Regulation of PTEN gene transcription.
DR Reactome; R-DRE-8953750; Transcriptional Regulation by E2F6.
DR ChiTaRS; bmi1a; zebrafish.
DR PRO; PR:Q8JIR0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0031519; C:PcG protein complex; ISS:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0021549; P:cerebellum development; IGI:ZFIN.
DR GO; GO:0035701; P:hematopoietic stem cell migration; IMP:ZFIN.
DR GO; GO:0036353; P:histone H2A-K119 monoubiquitination; ISS:UniProtKB.
DR GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060215; P:primitive hemopoiesis; IMP:ZFIN.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR032443; RAWUL.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR Pfam; PF16207; RAWUL; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Metal-binding; Nucleus; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..320
FT /note="Polycomb complex protein BMI-1-A"
FT /id="PRO_0000296630"
FT ZN_FING 18..57
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 234..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 81..95
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 238..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 320 AA; 36539 MW; F55CBACD9A235FEA CRC64;
MHRTTRIKIT ELNPHLMCVL CGGYFIDATT IIECLHSFCK MCIVRYLETS KYCPICDVQV
HKTKPLLNIR SDKTLQDIVY KLVPGLFKNE MKRRRDFYAE HPSVDAANGS NEDRGEVADE
DKRIITDDEI ISLSIEFFDH RAQQQGCTEE RQKEEVNNKR YLQCPAAMTV MHLRKFLRSK
MDIPPTYQIE VMYEDEPLKD YYTLMDIAYI YTWRRNGPLP LKYRVRPSCK KMKITHPQEG
LNNANRSESD SASDKACSPA GVPSTSSPLP SPSTLVQPSQ PHFTHISSPI NGTTMTSPNR
QFNFSKVRKS ALNGSSTSSG
