OBF1_MOUSE
ID OBF1_MOUSE Reviewed; 256 AA.
AC Q64693;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=POU domain class 2-associating factor 1 {ECO:0000305};
DE AltName: Full=B-cell-specific coactivator OBF-1;
DE AltName: Full=BOB-1;
DE Short=BOB1;
DE AltName: Full=OCA-B;
DE AltName: Full=OCT-binding factor 1;
GN Name=Pou2af1 {ECO:0000312|MGI:MGI:105086}; Synonyms=Obf-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=8530384; DOI=10.1074/jbc.270.50.29870;
RA Pfisterer P., Zwilling S., Hess J., Wirth T.;
RT "Functional characterization of the murine homolog of the B cell-specific
RT coactivator BOB.1/OBF.1.";
RL J. Biol. Chem. 270:29870-29880(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8657574; DOI=10.1093/nar/24.10.1913;
RA Schubart D.B., Sauter P., Massa S., Friedl E.M., Schwarzenbach H.,
RA Matthias P.;
RT "Gene structure and characterization of the murine homologue of the B cell-
RT specific transcriptional coactivator OBF-1.";
RL Nucleic Acids Res. 24:1913-1920(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8868069; DOI=10.1515/bchm3.1996.377.2.139;
RA Knoepfel L., Georgiev O., Nielsen P., Schaffner W.;
RT "Cloning and characterization of the murine B-cell specific transcriptional
RT coactivator Bob1.";
RL Biol. Chem. Hoppe-Seyler 377:139-145(1996).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND INDUCTION BY LPS.
RX PubMed=23045607; DOI=10.1084/jem.20111504;
RA Karnowski A., Chevrier S., Belz G.T., Mount A., Emslie D., D'Costa K.,
RA Tarlinton D.M., Kallies A., Corcoran L.M.;
RT "B and T cells collaborate in antiviral responses via IL-6, IL-21, and
RT transcriptional activator and coactivator, Oct2 and OBF-1.";
RL J. Exp. Med. 209:2049-2064(2012).
CC -!- FUNCTION: Transcriptional coactivator that specifically associates with
CC either POU2F1/OCT1 or POU2F2/OCT2. It boosts the POU2F1/OCT1 mediated
CC promoter activity and to a lesser extent, that of POU2F2/OCT2. It has
CC no intrinsic DNA-binding activity. It recognizes the POU domains of
CC POU2F1/OCT1 and POU2F2/OCT2. It is essential for the response of B-
CC cells to antigens and required for the formation of germinal centers
CC (PubMed:23045607). Regulates IL6 expression in B cells as POU2F2/OCT2
CC coactivator (PubMed:23045607). {ECO:0000269|PubMed:23045607}.
CC -!- SUBUNIT: Interacts with POU2F1/OCT1 and POU2F2/OCT2; the interaction
CC increases POU2F1 and POU2F2 transactivation activity.
CC {ECO:0000250|UniProtKB:Q16633}.
CC -!- INTERACTION:
CC Q64693; P48025: Syk; NbExp=2; IntAct=EBI-943530, EBI-300116;
CC Q64693; Q8IUQ4: SIAH1; Xeno; NbExp=5; IntAct=EBI-943530, EBI-747107;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: B-cell specific. {ECO:0000305|PubMed:23045607}.
CC -!- INDUCTION: In B cells, expression is highly increased upon activation
CC by LPS or CpG. {ECO:0000269|PubMed:23045607}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000250|UniProtKB:Q16633}.
CC -!- DISRUPTION PHENOTYPE: Mutants show severely reduced or absent germinal
CC center B cells in the lung-draining lymphatic nodes when infected by
CC influenza virus. {ECO:0000269|PubMed:23045607}.
CC -!- SIMILARITY: Belongs to the POU2AF1 family. {ECO:0000305}.
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DR EMBL; Z54283; CAA91058.1; -; mRNA.
DR EMBL; U43788; AAC52618.1; -; mRNA.
DR CCDS; CCDS23176.1; -.
DR PIR; S63588; S63588.
DR RefSeq; NP_035266.1; NM_011136.2.
DR AlphaFoldDB; Q64693; -.
DR SMR; Q64693; -.
DR DIP; DIP-977N; -.
DR IntAct; Q64693; 3.
DR STRING; 10090.ENSMUSP00000034554; -.
DR iPTMnet; Q64693; -.
DR PhosphoSitePlus; Q64693; -.
DR PaxDb; Q64693; -.
DR PRIDE; Q64693; -.
DR ProteomicsDB; 293823; -.
DR Antibodypedia; 4401; 663 antibodies from 41 providers.
DR DNASU; 18985; -.
DR Ensembl; ENSMUST00000034554; ENSMUSP00000034554; ENSMUSG00000032053.
DR GeneID; 18985; -.
DR KEGG; mmu:18985; -.
DR UCSC; uc009plg.1; mouse.
DR CTD; 5450; -.
DR MGI; MGI:105086; Pou2af1.
DR VEuPathDB; HostDB:ENSMUSG00000032053; -.
DR eggNOG; ENOG502R5JD; Eukaryota.
DR GeneTree; ENSGT00390000017499; -.
DR HOGENOM; CLU_095920_0_0_1; -.
DR InParanoid; Q64693; -.
DR OMA; GQPCIDM; -.
DR OrthoDB; 1172888at2759; -.
DR PhylomeDB; Q64693; -.
DR TreeFam; TF332565; -.
DR BioGRID-ORCS; 18985; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Pou2af1; mouse.
DR PRO; PR:Q64693; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q64693; protein.
DR Bgee; ENSMUSG00000032053; Expressed in peripheral lymph node and 65 other tissues.
DR ExpressionAtlas; Q64693; baseline and differential.
DR Genevisible; Q64693; MM.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0098586; P:cellular response to virus; IMP:UniProtKB.
DR GO; GO:0002314; P:germinal center B cell differentiation; IMP:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR DisProt; DP00008; -.
DR InterPro; IPR015389; PD-C2-AF1.
DR Pfam; PF09310; PD-C2-AF1; 1.
PE 1: Evidence at protein level;
KW Nucleus; Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..256
FT /note="POU domain class 2-associating factor 1"
FT /id="PRO_0000058019"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 50
FT /note="V -> G (in Ref. 1; CAA91058)"
FT /evidence="ECO:0000305"
FT CONFLICT 97..98
FT /note="QP -> HA (in Ref. 1; CAA91058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 256 AA; 27692 MW; 392E894517EA25E9 CRC64;
MLWQKSTAPE QAPAPPRPYQ GVRVKEPVKE LLRRKRGHTS VGAAGPPTAV VLPHQPLATY
STVGPSCLDM EVSASTVTEE GTLCAGWLSQ PAPATLQPLA PWTPYTEYVS HEAVSCPYST
DMYVQPVCPS YTVVGPSSVL TYASPPLITN VTPRSTATPA VGPQLEGPEH QAPLTYFPWP
QPLSTLPTSS LQYQPPAPTL SGPQFVQLPI SIPEPVLQDM DDPRRAISSL TIDKLLLEEE
ESNTYELNHT LSVEGF
