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 27-MAR-2024, entry version 224. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7XRC; X-ray; 1.89 A; C=257-419. DR PDBsum; 7XRC; -. DR AlphaFoldDB; P20265; -. DR SASBDB; P20265; -. DR SMR; P20265; -. DR BioGRID; 111450; 16. DR IntAct; P20265; 8. 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; 9606-ENSP00000329170; -. DR PeptideAtlas; P20265; -. DR ProteomicsDB; 53737; -. [P20265-1] DR ProteomicsDB; 53738; -. [P20265-2] DR ProteomicsDB; 53739; -. [P20265-3] DR Pumba; P20265; -. DR Antibodypedia; 18892; 417 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 AGR; HGNC:9215; -. 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; RDAHEEP; -. DR OrthoDB; 4250502at2759; -. 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; 22 hits in 1172 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 60 other cell types or tissues. 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: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:0021897; P:forebrain astrocyte 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; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 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 PANTHER; PTHR11636; POU DOMAIN; 1. DR PANTHER; PTHR11636:SF115; POU DOMAIN, CLASS 3, TRANSCRIPTION FACTOR 2; 1. 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; Homeodomain-like; 1. DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 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. DR Genevisible; P20265; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative initiation; Differentiation; KW DNA-binding; Homeobox; Neurogenesis; Nucleus; Phosphoprotein; KW Reference proteome; Transcription; 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" FT HELIX 267..284 FT /evidence="ECO:0007829|PDB:7XRC" FT HELIX 288..299 FT /evidence="ECO:0007829|PDB:7XRC" FT HELIX 305..312 FT /evidence="ECO:0007829|PDB:7XRC" FT HELIX 318..335 FT /evidence="ECO:0007829|PDB:7XRC" FT HELIX 363..375 FT /evidence="ECO:0007829|PDB:7XRC" FT HELIX 381..390 FT /evidence="ECO:0007829|PDB:7XRC" FT HELIX 395..409 FT /evidence="ECO:0007829|PDB:7XRC" FT STRAND 411..413 FT /evidence="ECO:0007829|PDB:7XRC" 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 //