ID PO2F2_HUMAN Reviewed; 479 AA. AC P09086; Q16648; Q7M4M8; Q9BRS4; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 02-OCT-2024, entry version 234. DE RecName: Full=POU domain, class 2, transcription factor 2 {ECO:0000305}; DE AltName: Full=Lymphoid-restricted immunoglobulin octamer-binding protein NF-A2; DE AltName: Full=Octamer-binding protein 2; DE Short=Oct-2; DE AltName: Full=Octamer-binding transcription factor 2; DE Short=OTF-2; GN Name=POU2F2 {ECO:0000312|HGNC:HGNC:9213}; Synonyms=OCT2, OTF2; 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] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [MRNA] OF RP 450-479 (ISOFORM 1). RX PubMed=3265124; DOI=10.1101/gad.2.12a.1570; RA Clerc R.G., Corcoran L.M., Lebowitz J.H., Baltimore D., Sharp P.A.; RT "The B-cell-specific Oct-2 protein contains POU box- and homeo box-type RT domains."; RL Genes Dev. 2:1570-1581(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=B-cell lymphoma; RX PubMed=2904654; DOI=10.1038/336551a0; RA Scheidereit C., Cromlish J.A., Gerster T., Kawakami K., Balmaceda C.-G., RA Currie R.A., Roder R.G.; RT "A human lymphoid-specific transcription factor that activates RT immunoglobulin genes is a homoeobox protein."; RL Nature 336:551-557(1988). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Lymph; 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 2-479 (ISOFORM 1). RC TISSUE=B-cell; RX PubMed=2904653; DOI=10.1038/336544a0; RA Mueller M.M., Ruppert S., Schaffner W., Matthias P.; RT "A cloned octamer transcription factor stimulates transcription from RT lymphoid-specific promoters in non-B cells."; RL Nature 336:544-551(1988). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-161, AND FUNCTION. RX PubMed=2328728; DOI=10.1002/j.1460-2075.1990.tb08282.x; RA Muller-Immergluck M.M., Schaffner W., Matthias P.; RT "Transcription factor Oct-2A contains functionally redundant activating RT domains and works selectively from a promoter but not from a remote RT enhancer position in non-lymphoid (HeLa) cells."; RL EMBO J. 9:1625-1634(1990). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-377. RX PubMed=7888080; DOI=10.1515/bchm3.1994.375.10.675; RA Matsuo K., Clay O., Kuenzler P., Georgiev O., Urbanek P., Schaffner W.; RT "Short introns interrupting the Oct-2 POU domain may prevent recombination RT between POU family genes without interfering with potential POU domain RT 'shuffling' in evolution."; RL Biol. Chem. Hoppe-Seyler 375:675-683(1994). RN [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 240-387, AND FUNCTION. RX PubMed=2901913; DOI=10.1016/0092-8674(88)90016-5; RA Ko H.-S., Fast P., McBride W., Staudt L.M.; RT "A human protein specific for the immunoglobulin octamer DNA motif contains RT a functional homeobox domain."; RL Cell 55:135-144(1988). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] OF 468-479 (ISOFORM 5), AND FUNCTION. RX PubMed=1739980; DOI=10.1016/0092-8674(92)90150-b; RA Tanaka M., Lai J.-S., Herr W.; RT "Promoter-selective activation domains in Oct-1 and Oct-2 direct RT differential activation of an snRNA and mRNA promoter."; RL Cell 68:755-767(1992). RN [10] RP IDENTIFICATION (ISOFORM 5), AND TISSUE SPECIFICITY. RX PubMed=3072196; DOI=10.1002/j.1460-2075.1988.tb03319.x; RA Schreiber E., Matthias P., Mueller M.M., Schaffner W.; RT "Identification of a novel lymphoid specific octamer binding protein (OTF- RT 2B) by proteolytic clipping bandshift assay (PCBA)."; RL EMBO J. 7:4221-4229(1988). RN [11] RP FUNCTION, INTERACTION WITH POU2AF1, AND DNA-BINDING. RC TISSUE=Spleen; RX PubMed=7859290; DOI=10.1016/0092-8674(95)90500-6; RA Strubin M., Newell J.W., Matthias P.; RT "OBF-1, a novel B cell-specific coactivator that stimulates immunoglobulin RT promoter activity through association with octamer-binding proteins."; RL Cell 80:497-506(1995). RN [12] RP INTERACTION WITH NR3C1; AR AND PGR. RX PubMed=10480874; DOI=10.1074/jbc.274.38.26713; RA Prefontaine G.G., Walther R., Giffin W., Lemieux M.E., Pope L., RA Hache R.J.G.; RT "Selective binding of steroid hormone receptors to octamer transcription RT factors determines transcriptional synergism at the mouse mammary tumor RT virus promoter."; RL J. Biol. Chem. 274:26713-26719(1999). RN [13] RP STRUCTURE BY NMR OF 297-359. RX PubMed=7914745; DOI=10.1021/bi00199a005; RA Sivaraja M., Botfield M.C., Mueller M., Jancso A., Weiss M.A.; RT "Solution structure of a POU-specific homeodomain: 3D-NMR studies of human RT B-cell transcription factor Oct-2."; RL Biochemistry 33:9845-9855(1994). CC -!- FUNCTION: Transcription factor that specifically binds to the octamer CC motif (5'-ATTTGCAT-3') (PubMed:2904654, PubMed:7859290). Regulates IL6 CC expression in B cells with POU2AF1 (By similarity). Regulates CC transcription in a number of tissues in addition to activating CC immunoglobulin gene expression (PubMed:2901913, PubMed:2904654). CC Modulates transcription transactivation by NR3C1, AR and PGR CC (PubMed:10480874). {ECO:0000250|UniProtKB:Q00196, CC ECO:0000269|PubMed:10480874, ECO:0000269|PubMed:2328728, CC ECO:0000269|PubMed:2901913, ECO:0000269|PubMed:2904654, CC ECO:0000269|PubMed:7859290}. CC -!- FUNCTION: [Isoform 5]: Activates the U2 small nuclear RNA (snRNA) CC promoter. {ECO:0000269|PubMed:1739980}. CC -!- ACTIVITY REGULATION: Transactivation activity is enhanced by CC transcriptional coactivator POU2AF1. {ECO:0000250|UniProtKB:Q00196}. CC -!- SUBUNIT: Interacts with NR3C1, AR and PGR (PubMed:10480874). Interacts CC with POU2AF1; the interaction increases POU2F2 transactivation activity CC (PubMed:7859290). {ECO:0000269|PubMed:10480874, CC ECO:0000269|PubMed:7859290}. CC -!- INTERACTION: CC P09086-4; P35548: MSX2; NbExp=3; IntAct=EBI-12918396, EBI-6447480; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P09086-1; Sequence=Displayed; CC Name=2; CC IsoId=P09086-2; Sequence=VSP_002325; CC Name=3; CC IsoId=P09086-3; Sequence=VSP_002324; CC Name=4; CC IsoId=P09086-4; Sequence=VSP_002324, VSP_007848, VSP_007849; CC Name=5; Synonyms=Oct-2B; CC IsoId=P09086-5; Sequence=VSP_032187; CC -!- TISSUE SPECIFICITY: Isoform 3 is B-cell specific. Isoform 5 is CC expressed in B-cells and the immunoglobulin-expressing T-cell line CC MOLT-4, but not in the T-cell line BW5147. {ECO:0000269|PubMed:2904654, CC ECO:0000269|PubMed:3072196}. CC -!- MISCELLANEOUS: [Isoform 5]: Incomplete sequence. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA32039.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; M36653; AAA36389.1; -; mRNA. DR EMBL; X53468; CAA37562.1; -; mRNA. DR EMBL; X53469; CAA37565.1; -; mRNA. DR EMBL; M36542; AAA36732.1; -; mRNA. DR EMBL; X13810; CAA32040.1; -; mRNA. DR EMBL; BT007438; AAP36106.1; -; mRNA. DR EMBL; BC006101; AAH06101.1; -; mRNA. DR EMBL; M36718; AAA59978.1; -; mRNA. DR EMBL; X13809; CAA32039.1; ALT_INIT; mRNA. DR EMBL; X81030; CAA56933.1; -; Genomic_DNA. DR CCDS; CCDS33035.1; -. [P09086-3] DR CCDS; CCDS56094.1; -. [P09086-2] DR CCDS; CCDS56095.1; -. [P09086-1] DR CCDS; CCDS58665.1; -. [P09086-4] DR PIR; A31753; A31753. DR PIR; A42098; A42098. DR RefSeq; NP_001193954.1; NM_001207025.2. [P09086-1] DR RefSeq; NP_001193955.1; NM_001207026.1. [P09086-2] DR RefSeq; NP_001234923.1; NM_001247994.1. [P09086-4] DR RefSeq; NP_002689.1; NM_002698.4. [P09086-3] DR PDB; 1HDP; NMR; -; A=297-359. DR PDBsum; 1HDP; -. DR AlphaFoldDB; P09086; -. DR SMR; P09086; -. DR BioGRID; 111448; 27. DR CORUM; P09086; -. DR DIP; DIP-51N; -. DR IntAct; P09086; 10. DR MINT; P09086; -. DR STRING; 9606.ENSP00000431603; -. DR BindingDB; P09086; -. DR ChEMBL; CHEMBL3509582; -. DR DrugBank; DB11799; Bictegravir. DR DrugBank; DB12500; Fedratinib. DR DrugBank; DB11757; Istradefylline. DR DrugBank; DB01203; Nadolol. DR GlyGen; P09086; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P09086; -. DR PhosphoSitePlus; P09086; -. DR BioMuta; POU2F2; -. DR DMDM; 123402; -. DR jPOST; P09086; -. DR MassIVE; P09086; -. DR PaxDb; 9606-ENSP00000431603; -. DR PeptideAtlas; P09086; -. DR ProteomicsDB; 52192; -. [P09086-1] DR ProteomicsDB; 52193; -. [P09086-2] DR ProteomicsDB; 52194; -. [P09086-3] DR ProteomicsDB; 52195; -. [P09086-4] DR ProteomicsDB; 52196; -. [P09086-5] DR Pumba; P09086; -. DR Antibodypedia; 3745; 685 antibodies from 43 providers. DR DNASU; 5452; -. DR Ensembl; ENST00000389341.9; ENSP00000373992.3; ENSG00000028277.22. [P09086-3] DR Ensembl; ENST00000526816.6; ENSP00000431603.3; ENSG00000028277.22. [P09086-1] DR Ensembl; ENST00000529067.5; ENSP00000437224.1; ENSG00000028277.22. [P09086-4] DR Ensembl; ENST00000529952.5; ENSP00000436988.1; ENSG00000028277.22. [P09086-2] DR GeneID; 5452; -. DR KEGG; hsa:5452; -. DR UCSC; uc002osn.4; human. [P09086-1] DR AGR; HGNC:9213; -. DR CTD; 5452; -. DR DisGeNET; 5452; -. DR GeneCards; POU2F2; -. DR HGNC; HGNC:9213; POU2F2. DR HPA; ENSG00000028277; Tissue enhanced (lymphoid). DR MIM; 164176; gene. DR neXtProt; NX_P09086; -. DR OpenTargets; ENSG00000028277; -. DR PharmGKB; PA33537; -. DR VEuPathDB; HostDB:ENSG00000028277; -. DR eggNOG; KOG3802; Eukaryota. DR GeneTree; ENSGT00940000160115; -. DR InParanoid; P09086; -. DR OrthoDB; 4250502at2759; -. DR PhylomeDB; P09086; -. DR TreeFam; TF316413; -. DR PathwayCommons; P09086; -. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR SignaLink; P09086; -. DR SIGNOR; P09086; -. DR BioGRID-ORCS; 5452; 22 hits in 1175 CRISPR screens. DR ChiTaRS; POU2F2; human. DR EvolutionaryTrace; P09086; -. DR GenomeRNAi; 5452; -. DR Pharos; P09086; Tbio. DR PRO; PR:P09086; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P09086; protein. DR Bgee; ENSG00000028277; Expressed in monocyte and 190 other cell types or tissues. DR ExpressionAtlas; P09086; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:MGI. 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:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISS:UniProtKB. DR GO; GO:0098586; P:cellular response to virus; ISS:UniProtKB. DR GO; GO:0006959; P:humoral immune response; TAS:ProtInc. DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. 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; IPR001356; HD. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR009057; Homeodomain-like_sf. DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf. DR InterPro; IPR013847; POU. DR InterPro; IPR000327; POU_dom. DR InterPro; IPR050255; POU_domain_TF. DR InterPro; IPR000972; TF_octamer. DR PANTHER; PTHR11636; POU DOMAIN; 1. DR PANTHER; PTHR11636:SF46; POU DOMAIN, CLASS 2, TRANSCRIPTION FACTOR 2; 1. DR Pfam; PF00046; Homeodomain; 1. DR Pfam; PF00157; Pou; 1. DR PRINTS; PR00029; OCTAMER. 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. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Cytoplasm; DNA-binding; KW Homeobox; Nucleus; Proteomics identification; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1..479 FT /note="POU domain, class 2, transcription factor 2" FT /id="PRO_0000100714" FT DOMAIN 195..269 FT /note="POU-specific" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530" FT DNA_BIND 297..356 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..86 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 166..200 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 275..298 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 389..410 FT /note="Leucine-zipper" FT REGION 409..479 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 14..37 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 38..62 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 177..191 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 431..445 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 446..462 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 168..183 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:2904654, ECO:0000303|Ref.3" FT /id="VSP_002324" FT VAR_SEQ 400..416 FT /note="VTTLSSAVGTLHPSRTA -> AQTPALKAATRLSACQA (in isoform FT 4)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_007848" FT VAR_SEQ 417..479 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3" FT /id="VSP_007849" FT VAR_SEQ 468..479 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:3265124" FT /id="VSP_002325" FT VAR_SEQ 468..479 FT /note="PGLWWNPAPYQP -> STMVGLSSGLSPALMSNNPLATIQALASGGTLPLTS FT LDGSGNLVLGAAGAAPGSPSLVTSPLFLNHTGLPLLSAPPGVGLVSAAAAAVAASISSK FT SPGLSSSSSSSSSSSSSTCSDVAAQTPGGPGGPEAGSKAE (in isoform 5)" FT /evidence="ECO:0000303|PubMed:1739980" FT /id="VSP_032187" FT MUTAGEN 340..342 FT /note="VIR->FNP: Suppresses DNA-binding ability." FT HELIX 307..318 FT /evidence="ECO:0007829|PDB:1HDP" FT HELIX 324..331 FT /evidence="ECO:0007829|PDB:1HDP" FT TURN 332..335 FT /evidence="ECO:0007829|PDB:1HDP" FT HELIX 338..350 FT /evidence="ECO:0007829|PDB:1HDP" FT TURN 356..358 FT /evidence="ECO:0007829|PDB:1HDP" SQ SEQUENCE 479 AA; 51209 MW; 8DA661DC07644D43 CRC64; MVHSSMGAPE IRMSKPLEAE KQGLDSPSEH TDTERNGPDT NHQNPQNKTS PFSVSPTGPS TKIKAEDPSG DSAPAAPLPP QPAQPHLPQA QLMLTGSQLA GDIQQLLQLQ QLVLVPGHHL QPPAQFLLPQ AQQSQPGLLP TPNLFQLPQQ TQGALLTSQP RAGLPTQAVT RPTLPDPHLS HPQPPKCLEP PSHPEEPSDL EELEQFARTF KQRRIKLGFT QGDVGLAMGK LYGNDFSQTT ISRFEALNLS FKNMCKLKPL LEKWLNDAET MSVDSSLPSP NQLSSPSLGF DGLPGRRRKK RTSIETNVRF ALEKSFLANQ KPTSEEILLI AEQLHMEKEV IRVWFCNRRQ KEKRINPCSA APMLPSPGKP ASYSPHMVTP QGGAGTLPLS QASSSLSTTV TTLSSAVGTL HPSRTAGGGG GGGGAAPPLN SIPSVTPPPP ATTNSTNPSP QGSHSAIGLS GLNPSTGPGL WWNPAPYQP //