PO2F2_HUMAN
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 03-AUG-2022, entry version 224.
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};
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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; 26.
DR CORUM; P09086; -.
DR DIP; DIP-51N; -.
DR IntAct; P09086; 9.
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 EPD; P09086; -.
DR jPOST; P09086; -.
DR MassIVE; P09086; -.
DR MaxQB; P09086; -.
DR PaxDb; P09086; -.
DR PeptideAtlas; P09086; -.
DR PRIDE; 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 Antibodypedia; 3745; 586 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 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; 873012at2759; -.
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; 16 hits in 1094 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 188 other tissues.
DR ExpressionAtlas; P09086; baseline and differential.
DR Genevisible; P09086; HS.
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; 1.10.260.40; -; 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; IPR000972; TF_octamer.
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; 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 3D-structure; Activator; Alternative splicing; Cytoplasm; DNA-binding;
KW Homeobox; Nucleus; Reference proteome; Transcription;
KW 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
