PO3F2_HUMAN
ID PO3F2_HUMAN Reviewed; 443 AA.
AC P20265; Q14960; Q86V54; Q9UJL0;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 4.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=POU domain, class 3, transcription factor 2;
DE AltName: Full=Brain-specific homeobox/POU domain protein 2;
DE Short=Brain-2;
DE Short=Brn-2;
DE AltName: Full=Nervous system-specific octamer-binding transcription factor N-Oct-3;
DE AltName: Full=Octamer-binding protein 7;
DE Short=Oct-7;
DE AltName: Full=Octamer-binding transcription factor 7;
DE Short=OTF-7;
GN Name=POU3F2; Synonyms=BRN2, OCT7, OTF7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8441633; DOI=10.1093/nar/21.2.253;
RA Schreiber E., Tobler A., Malipiero U., Schaffner W., Fontana A.;
RT "cDNA cloning of human N-Oct3, a nervous-system specific POU domain
RT transcription factor binding to the octamer DNA motif.";
RL Nucleic Acids Res. 21:253-258(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Liver;
RX PubMed=7651733;
RA Angus J., Thomson F., Murphy K., Baker E., Sutherland G.R., Parsons P.G.,
RA Sturm R.A.;
RT "The brn-2 gene regulates the melanocytic phenotype and tumorigenic
RT potential of human melanoma cells.";
RL Oncogene 11:691-700(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 280-404.
RC TISSUE=Brain;
RX PubMed=2739723; DOI=10.1038/340035a0;
RA He X., Treacy M.N., Simmons D.M., Ingraham H.A., Swanson L.W.,
RA Rosenfeld M.G.;
RT "Expression of a large family of POU-domain regulatory genes in mammalian
RT brain development.";
RL Nature 340:35-42(1989).
RN [6]
RP INTERACTION WITH PQBP1.
RC TISSUE=Brain;
RX PubMed=10332029; DOI=10.1093/hmg/8.6.977;
RA Waragai M., Lammers C.-H., Takeuchi S., Imafuku I., Udagawa Y.,
RA Kanazawa I., Kawabata M., Mouradian M.M., Okazawa H.;
RT "PQBP-1, a novel polyglutamine tract binding protein, inhibits
RT transcription activation by Brn-2 and affects cell survival.";
RL Hum. Mol. Genet. 8:977-987(1999).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-341, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Transcription factor that plays a key role in neuronal
CC differentiation (By similarity). Binds preferentially to the
CC recognition sequence which consists of two distinct half-sites,
CC ('GCAT') and ('TAAT'), separated by a non-conserved spacer region of 0,
CC 2, or 3 nucleotides (By similarity). Acts as a transcriptional
CC activator when binding cooperatively with SOX4, SOX11, or SOX12 to gene
CC promoters (By similarity). The combination of three transcription
CC factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram
CC fibroblasts and other somatic cells into induced neuronal (iN) cells in
CC vitro (By similarity). Acts downstream of ASCL1, accessing chromatin
CC that has been opened by ASCL1, and promotes transcription of neuronal
CC genes (By similarity). {ECO:0000250|UniProtKB:P31360,
CC ECO:0000250|UniProtKB:P56222}.
CC -!- SUBUNIT: Interacts with PQBP1 (PubMed:10332029). Interaction with ISL1
CC (By similarity). {ECO:0000250|UniProtKB:P31360,
CC ECO:0000269|PubMed:10332029}.
CC -!- INTERACTION:
CC P20265; Q09472: EP300; NbExp=3; IntAct=EBI-1167176, EBI-447295;
CC P20265; P23760: PAX3; NbExp=2; IntAct=EBI-1167176, EBI-1167564;
CC P20265; P20265: POU3F2; NbExp=2; IntAct=EBI-1167176, EBI-1167176;
CC P20265; P56693: SOX10; NbExp=3; IntAct=EBI-1167176, EBI-1167533;
CC P20265; P20226: TBP; NbExp=2; IntAct=EBI-1167176, EBI-355371;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=3;
CC Name=N-OCT 3;
CC IsoId=P20265-1; Sequence=Displayed;
CC Name=N-OCT 5A;
CC IsoId=P20265-2; Sequence=VSP_018749;
CC Name=N-OCT 5B;
CC IsoId=P20265-3; Sequence=VSP_018750;
CC -!- TISSUE SPECIFICITY: Expressed specifically in the neuroectodermal cell
CC lineage.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-3
CC subfamily. {ECO:0000305}.
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DR EMBL; Z11933; CAA77990.1; -; mRNA.
DR EMBL; L37868; AAB59611.1; -; Genomic_DNA.
DR EMBL; AL022395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051699; AAH51699.2; -; mRNA.
DR CCDS; CCDS5040.1; -. [P20265-1]
DR PIR; S29334; S29334.
DR RefSeq; NP_005595.2; NM_005604.3. [P20265-1]
DR AlphaFoldDB; P20265; -.
DR SASBDB; P20265; -.
DR SMR; P20265; -.
DR BioGRID; 111450; 15.
DR IntAct; P20265; 7.
DR STRING; 9606.ENSP00000329170; -.
DR BindingDB; P20265; -.
DR ChEMBL; CHEMBL4189; -.
DR iPTMnet; P20265; -.
DR PhosphoSitePlus; P20265; -.
DR BioMuta; POU3F2; -.
DR DMDM; 78100757; -.
DR EPD; P20265; -.
DR jPOST; P20265; -.
DR MassIVE; P20265; -.
DR MaxQB; P20265; -.
DR PaxDb; P20265; -.
DR PeptideAtlas; P20265; -.
DR PRIDE; P20265; -.
DR ProteomicsDB; 53737; -. [P20265-1]
DR ProteomicsDB; 53738; -. [P20265-2]
DR ProteomicsDB; 53739; -. [P20265-3]
DR Antibodypedia; 18892; 371 antibodies from 42 providers.
DR DNASU; 5454; -.
DR Ensembl; ENST00000328345.8; ENSP00000329170.5; ENSG00000184486.10. [P20265-1]
DR GeneID; 5454; -.
DR KEGG; hsa:5454; -.
DR MANE-Select; ENST00000328345.8; ENSP00000329170.5; NM_005604.4; NP_005595.2.
DR UCSC; uc003ppe.4; human. [P20265-1]
DR CTD; 5454; -.
DR DisGeNET; 5454; -.
DR GeneCards; POU3F2; -.
DR HGNC; HGNC:9215; POU3F2.
DR HPA; ENSG00000184486; Tissue enriched (brain).
DR MIM; 600494; gene.
DR neXtProt; NX_P20265; -.
DR OpenTargets; ENSG00000184486; -.
DR PharmGKB; PA33539; -.
DR VEuPathDB; HostDB:ENSG00000184486; -.
DR eggNOG; KOG3802; Eukaryota.
DR GeneTree; ENSGT00940000162208; -.
DR HOGENOM; CLU_013065_1_2_1; -.
DR InParanoid; P20265; -.
DR OMA; QHHGGEH; -.
DR OrthoDB; 752252at2759; -.
DR PhylomeDB; P20265; -.
DR TreeFam; TF316413; -.
DR PathwayCommons; P20265; -.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; P20265; -.
DR SIGNOR; P20265; -.
DR BioGRID-ORCS; 5454; 21 hits in 1094 CRISPR screens.
DR GeneWiki; POU3F2; -.
DR GenomeRNAi; 5454; -.
DR Pharos; P20265; Tbio.
DR PRO; PR:P20265; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P20265; protein.
DR Bgee; ENSG00000184486; Expressed in ganglionic eminence and 58 other tissues.
DR Genevisible; P20265; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0014002; P:astrocyte development; IEA:Ensembl.
DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IEA:Ensembl.
DR GO; GO:0008544; P:epidermis development; IEA:Ensembl.
DR GO; GO:0021869; P:forebrain ventricular zone progenitor cell division; IEA:Ensembl.
DR GO; GO:0021979; P:hypothalamus cell differentiation; IEA:Ensembl.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0007399; P:nervous system development; ISS:UniProtKB.
DR GO; GO:0061101; P:neuroendocrine cell differentiation; IEA:Ensembl.
DR GO; GO:0021985; P:neurohypophysis development; IEA:Ensembl.
DR GO; GO:0048666; P:neuron development; ISS:UniProtKB.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0048663; P:neuron fate commitment; ISS:UniProtKB.
DR GO; GO:0048665; P:neuron fate specification; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:MGI.
DR GO; GO:0040018; P:positive regulation of multicellular organism growth; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0045595; P:regulation of cell differentiation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR013847; POU.
DR InterPro; IPR000327; POU_dom.
DR InterPro; IPR016362; TF_POU_3.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
DR PIRSF; PIRSF002629; Transcription_factor_POU; 1.
DR PRINTS; PR00028; POUDOMAIN.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00352; POU; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS00035; POU_1; 1.
DR PROSITE; PS00465; POU_2; 1.
DR PROSITE; PS51179; POU_3; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative initiation; Differentiation; DNA-binding; Homeobox;
KW Neurogenesis; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..443
FT /note="POU domain, class 3, transcription factor 2"
FT /id="PRO_0000013495"
FT DOMAIN 262..336
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 354..413
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 64..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..153
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..252
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 341
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 1..199
FT /note="Missing (in isoform N-OCT 5B)"
FT /evidence="ECO:0000305"
FT /id="VSP_018750"
FT VAR_SEQ 1..180
FT /note="Missing (in isoform N-OCT 5A)"
FT /evidence="ECO:0000305"
FT /id="VSP_018749"
FT CONFLICT 26
FT /note="G -> A (in Ref. 1; CAA77990)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="S -> T (in Ref. 1 and 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="P -> S (in Ref. 4; AAH51699)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 443 AA; 46893 MW; D470360894D788C6 CRC64;
MATAASNHYS LLTSSASIVH AEPPGGMQQG AGGYREAQSL VQGDYGALQS NGHPLSHAHQ
WITALSHGGG GGGGGGGGGG GGGGGGGGDG SPWSTSPLGQ PDIKPSVVVQ QGGRGDELHG
PGALQQQHQQ QQQQQQQQQQ QQQQQQQQQR PPHLVHHAAN HHPGPGAWRS AAAAAHLPPS
MGASNGGLLY SQPSFTVNGM LGAGGQPAGL HHHGLRDAHD EPHHADHHPH PHSHPHQQPP
PPPPPQGPPG HPGAHHDPHS DEDTPTSDDL EQFAKQFKQR RIKLGFTQAD VGLALGTLYG
NVFSQTTICR FEALQLSFKN MCKLKPLLNK WLEEADSSSG SPTSIDKIAA QGRKRKKRTS
IEVSVKGALE SHFLKCPKPS AQEITSLADS LQLEKEVVRV WFCNRRQKEK RMTPPGGTLP
GAEDVYGGSR DTPPHHGVQT PVQ
