ID PO2F1_HUMAN Reviewed; 743 AA. AC P14859; B1AL91; B1AL93; B4E029; J3KP77; Q5TBT7; Q6PK46; Q8NEU9; Q9BPV1; DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2003, sequence version 2. DT 27-MAR-2024, entry version 250. DE RecName: Full=POU domain, class 2, transcription factor 1; DE AltName: Full=NF-A1; DE AltName: Full=Octamer-binding protein 1; DE Short=Oct-1; DE AltName: Full=Octamer-binding transcription factor 1; DE Short=OTF-1; GN Name=POU2F1; Synonyms=OCT1, OTF1; 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 PARTIAL NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6). RC TISSUE=Teratocarcinoma; RX PubMed=2905684; DOI=10.1101/gad.2.12a.1582; RA Sturm R.A., Das G., Herr W.; RT "The ubiquitous octamer-binding protein Oct-1 contains a POU domain with a RT homeo box subdomain."; RL Genes Dev. 2:1582-1599(1988). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=B-cell lymphoma; RX PubMed=12663137; DOI=10.1016/s0165-2478(02)00179-7; RA Luchina N.N., Krivega I.V., Pankratova E.V.; RT "Human Oct-1L isoform has tissue-specific expression pattern similar to RT Oct-2."; RL Immunol. Lett. 85:237-241(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Thymus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 93-653 (ISOFORM 4). RC TISSUE=Lung, Lymph, and Skin; 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 [7] RP PHOSPHORYLATION AT SER-385, MUTAGENESIS OF SER-385, AND FUNCTION IN RP DNA-BINDING ACTIVITY. RX PubMed=1684878; DOI=10.1126/science.1684878; RA Segil N., Roberts S.B., Heintz N.; RT "Mitotic phosphorylation of the Oct-1 homeodomain and regulation of Oct-1 RT DNA binding activity."; RL Science 254:1814-1816(1991). RN [8] 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 [9] 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 [10] RP INTERACTION WITH HCFC1. RX PubMed=10629049; DOI=10.1128/mcb.20.3.919-928.2000; RA Mahajan S.S., Wilson A.C.; RT "Mutations in host cell factor 1 separate its role in cell proliferation RT from recruitment of VP16 and LZIP."; RL Mol. Cell. Biol. 20:919-928(2000). RN [11] RP PHOSPHORYLATION. RX PubMed=14612514; RA Schild-Poulter C., Shih A., Yarymowich N.C., Hache R.J.G.; RT "Down-regulation of histone H2B by DNA-dependent protein kinase in response RT to DNA damage through modulation of octamer transcription factor 1."; RL Cancer Res. 63:7197-7205(2003). RN [12] RP REVIEW ON HERPES INFECTION. RX PubMed=12826401; DOI=10.1016/s0968-0004(03)00088-4; RA Wysocka J., Herr W.; RT "The herpes simplex virus VP16-induced complex: the makings of a regulatory RT switch."; RL Trends Biochem. Sci. 28:294-304(2003). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [14] RP INTERACTION WITH HUMAN HERPESVIRUS 8 PROTEIN RTA/ORF50 (MICROBIAL RP INFECTION). RX PubMed=17537858; DOI=10.1128/jvi.00265-07; RA Carroll K.D., Khadim F., Spadavecchia S., Palmeri D., Lukac D.M.; RT "Direct interactions of Kaposi's sarcoma-associated herpesvirus/human RT herpesvirus 8 ORF50/Rta protein with the cellular protein octamer-1 and DNA RT are critical for specifying transactivation of a delayed-early promoter and RT stimulating viral reactivation."; RL J. Virol. 81:8451-8467(2007). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-270; SER-283 AND SER-448, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [16] 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 [17] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [18] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-276 AND SER-448, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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). RN [21] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [22] RP STRUCTURE BY NMR OF 284-359. RX PubMed=8479524; DOI=10.1038/362852a0; RA Dekker N., Cox M., Boelens R., Verrijzer C.P., van der Vliet P.C., RA Kaptein R.; RT "Solution structure of the POU-specific DNA-binding domain of Oct-1."; RL Nature 362:852-855(1993). RN [23] RP STRUCTURE BY NMR OF 284-354. RX PubMed=8462099; DOI=10.1016/0092-8674(93)90171-l; RA Assa-Munt N., Mortishire-Smith R.J., Aurora R., Herr W., Wright P.E.; RT "The solution structure of the Oct-1 POU-specific domain reveals a striking RT similarity to the bacteriophage lambda repressor DNA-binding domain."; RL Cell 73:193-205(1993). RN [24] RP STRUCTURE BY NMR OF 378-437. RX PubMed=7663141; DOI=10.1007/bf00417488; RA Cox M., van Tilborg P.J.A., de Laat W., Boelens R., van Leeuwen H.C., RA van der Vliet P.C., Kaptein R.; RT "Solution structure of the Oct-1 POU homeodomain determined by NMR and RT restrained molecular dynamics."; RL J. Biomol. NMR 6:23-32(1995). RN [25] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 284-439. RX PubMed=8156594; DOI=10.1016/0092-8674(94)90231-3; RA Klemm J.D., Rould M.A., Aurora R., Herr W., Pabo C.O.; RT "Crystal structure of the Oct-1 POU domain bound to an octamer site: DNA RT recognition with tethered DNA-binding modules."; RL Cell 77:21-32(1994). RN [26] RP VARIANT [LARGE SCALE ANALYSIS] PHE-88. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Transcription factor that binds to the octamer motif (5'- CC ATTTGCAT-3') and activates the promoters of the genes for some small CC nuclear RNAs (snRNA) and of genes such as those for histone H2B and CC immunoglobulins. Modulates transcription transactivation by NR3C1, AR CC and PGR. {ECO:0000269|PubMed:10480874, ECO:0000269|PubMed:1684878, CC ECO:0000269|PubMed:7859290}. CC -!- FUNCTION: (Microbial infection) In case of human herpes simplex virus CC (HSV) infection, POU2F1 forms a multiprotein-DNA complex with the viral CC transactivator protein VP16 and HCFC1 thereby enabling the CC transcription of the viral immediate early genes. CC {ECO:0000305|PubMed:12826401}. CC -!- SUBUNIT: Interacts with POU2AF1; the interaction increases POU2F1 CC transactivation activity (PubMed:7859290). Interacts with NR3C1, AR, CC PGR and HCFC1. {ECO:0000269|PubMed:10480874, CC ECO:0000269|PubMed:10629049, ECO:0000269|PubMed:7859290}. CC -!- SUBUNIT: (Microbial infection) Associates with the herpes simplex virus CC VP16-induced complex; binding to HCFC1 activates the viral CC transcriptional activator VP16 for association with POU2F1, to form a CC multiprotein-DNA complex responsible for activating transcription of CC the viral immediate early genes. {ECO:0000269|PubMed:10629049}. CC -!- SUBUNIT: (Microbial infection) Interacts with human herpesvirus 8 CC (KSHV) protein RTA/ORF50; this interaction enhances RTA/ORF50-mediated CC transactivation of several viral promoters including K-bZIP promoter. CC {ECO:0000269|PubMed:17537858}. CC -!- INTERACTION: CC P14859; Q9H4B4: PLK3; NbExp=3; IntAct=EBI-624770, EBI-751877; CC P14859; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-624770, EBI-1389308; CC P14859; P08047: SP1; NbExp=7; IntAct=EBI-624770, EBI-298336; CC P14859; Q02446: SP4; NbExp=5; IntAct=EBI-624770, EBI-10198587; CC P14859-6; O15145: ARPC3; NbExp=3; IntAct=EBI-11526590, EBI-351829; CC P14859-6; P49407: ARRB1; NbExp=3; IntAct=EBI-11526590, EBI-743313; CC P14859-6; Q03060-25: CREM; NbExp=3; IntAct=EBI-11526590, EBI-12884642; CC P14859-6; P55197-2: MLLT10; NbExp=3; IntAct=EBI-11526590, EBI-12853322; CC P14859-6; P23511-2: NFYA; NbExp=5; IntAct=EBI-11526590, EBI-11061759; CC P14859-6; P14859-6: POU2F1; NbExp=3; IntAct=EBI-11526590, EBI-11526590; CC P14859-6; P78424: POU6F2; NbExp=3; IntAct=EBI-11526590, EBI-12029004; CC P14859-6; O43314-2: PPIP5K2; NbExp=3; IntAct=EBI-11526590, EBI-12906508; CC P14859-6; P86480: PRR20D; NbExp=3; IntAct=EBI-11526590, EBI-12754095; CC P14859-6; Q8TAD8: SNIP1; NbExp=3; IntAct=EBI-11526590, EBI-749336; CC P14859-6; Q9Y343: SNX24; NbExp=3; IntAct=EBI-11526590, EBI-727113; CC P14859-6; Q02446: SP4; NbExp=3; IntAct=EBI-11526590, EBI-10198587; CC P14859-6; Q6ZVD7: STOX1; NbExp=3; IntAct=EBI-11526590, EBI-3923644; CC P14859-6; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-11526590, EBI-10180829; CC P14859-6; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-11526590, EBI-742550; CC P14859-6; Q15911-2: ZFHX3; NbExp=3; IntAct=EBI-11526590, EBI-10237226; CC P14859-6; O95789-4: ZMYM6; NbExp=3; IntAct=EBI-11526590, EBI-12949277; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=P14859-1; Sequence=Displayed; CC Name=2; Synonyms=Oct-1L, lymphocyte-specific; CC IsoId=P14859-2; Sequence=VSP_002320; CC Name=3; CC IsoId=P14859-3; Sequence=VSP_013421; CC Name=6; CC IsoId=P14859-6; Sequence=VSP_043195; CC Name=4; CC IsoId=P14859-4; Sequence=VSP_013422, VSP_013423; CC Name=5; CC IsoId=P14859-5; Sequence=VSP_043195, VSP_043196; CC -!- TISSUE SPECIFICITY: Ubiquitous. Isoform 2 is lymphocyte-specific. CC -!- PTM: Phosphorylated by PRKDC. {ECO:0000269|PubMed:14612514, CC ECO:0000269|PubMed:1684878}. CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-2 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; X13403; CAA31767.1; -; mRNA. DR EMBL; AY113189; AAM77920.1; -; mRNA. DR EMBL; AK303201; BAG64291.1; -; mRNA. DR EMBL; AL136984; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL359962; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL451050; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471067; EAW90786.1; -; Genomic_DNA. DR EMBL; CH471067; EAW90788.1; -; Genomic_DNA. DR EMBL; BC001664; AAH01664.1; -; mRNA. DR EMBL; BC003571; AAH03571.1; -; mRNA. DR EMBL; BC007388; AAH07388.1; -; mRNA. DR EMBL; BC052274; AAH52274.1; -; mRNA. DR CCDS; CCDS1259.2; -. [P14859-6] DR CCDS; CCDS55655.1; -. [P14859-5] DR CCDS; CCDS55656.1; -. [P14859-2] DR PIR; A47001; A47001. DR RefSeq; NP_001185712.1; NM_001198783.1. [P14859-2] DR RefSeq; NP_001185715.1; NM_001198786.1. [P14859-5] DR RefSeq; NP_002688.3; NM_002697.3. [P14859-6] DR RefSeq; XP_011507956.1; XM_011509654.2. [P14859-1] DR PDB; 1CQT; X-ray; 3.20 A; A/B=278-439. DR PDB; 1E3O; X-ray; 1.90 A; C=280-438. DR PDB; 1GT0; X-ray; 2.60 A; C=280-438. DR PDB; 1HF0; X-ray; 2.70 A; A/B=280-438. DR PDB; 1O4X; NMR; -; A=280-442. DR PDB; 1OCT; X-ray; 3.00 A; C=284-439. DR PDB; 1POG; NMR; -; A=378-437. DR PDB; 1POU; NMR; -; A=284-354. DR PDBsum; 1CQT; -. DR PDBsum; 1E3O; -. DR PDBsum; 1GT0; -. DR PDBsum; 1HF0; -. DR PDBsum; 1O4X; -. DR PDBsum; 1OCT; -. DR PDBsum; 1POG; -. DR PDBsum; 1POU; -. DR AlphaFoldDB; P14859; -. DR EMDB; EMD-26258; -. DR EMDB; EMD-26260; -. DR EMDB; EMD-40683; -. DR EMDB; EMD-40686; -. DR SMR; P14859; -. DR BioGRID; 111447; 171. DR CORUM; P14859; -. DR DIP; DIP-226N; -. DR IntAct; P14859; 55. DR MINT; P14859; -. DR STRING; 9606.ENSP00000356840; -. DR BindingDB; P14859; -. DR ChEMBL; CHEMBL3509601; -. DR DrugBank; DB01203; Nadolol. DR MoonProt; P14859; -. DR GlyCosmos; P14859; 15 sites, 2 glycans. DR GlyGen; P14859; 18 sites, 2 O-linked glycans (18 sites). DR iPTMnet; P14859; -. DR PhosphoSitePlus; P14859; -. DR BioMuta; POU2F1; -. DR DMDM; 28202257; -. DR EPD; P14859; -. DR jPOST; P14859; -. DR MassIVE; P14859; -. DR MaxQB; P14859; -. DR PaxDb; 9606-ENSP00000356840; -. DR PeptideAtlas; P14859; -. DR ProteomicsDB; 53085; -. [P14859-1] DR ProteomicsDB; 53086; -. [P14859-2] DR ProteomicsDB; 53087; -. [P14859-3] DR ProteomicsDB; 53088; -. [P14859-4] DR ProteomicsDB; 53089; -. [P14859-5] DR Pumba; P14859; -. DR Antibodypedia; 3616; 727 antibodies from 45 providers. DR DNASU; 5451; -. DR Ensembl; ENST00000367862.9; ENSP00000356836.5; ENSG00000143190.23. [P14859-2] DR Ensembl; ENST00000367866.7; ENSP00000356840.2; ENSG00000143190.23. [P14859-6] DR Ensembl; ENST00000429375.6; ENSP00000401217.2; ENSG00000143190.23. [P14859-5] DR Ensembl; ENST00000541643.7; ENSP00000441285.2; ENSG00000143190.23. [P14859-1] DR GeneID; 5451; -. DR KEGG; hsa:5451; -. DR MANE-Select; ENST00000367866.7; ENSP00000356840.2; NM_002697.4; NP_002688.3. [P14859-6] DR UCSC; uc001gec.4; human. [P14859-1] DR AGR; HGNC:9212; -. DR CTD; 5451; -. DR DisGeNET; 5451; -. DR GeneCards; POU2F1; -. DR HGNC; HGNC:9212; POU2F1. DR HPA; ENSG00000143190; Low tissue specificity. DR MIM; 164175; gene. DR neXtProt; NX_P14859; -. DR OpenTargets; ENSG00000143190; -. DR PharmGKB; PA33536; -. DR VEuPathDB; HostDB:ENSG00000143190; -. DR eggNOG; KOG3802; Eukaryota. DR GeneTree; ENSGT00940000157831; -. DR HOGENOM; CLU_013065_4_0_1; -. DR InParanoid; P14859; -. DR OMA; TPKRMDT; -. DR OrthoDB; 4250502at2759; -. DR PhylomeDB; P14859; -. DR TreeFam; TF316413; -. DR PathwayCommons; P14859; -. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes. DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation. DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter. DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression. DR SignaLink; P14859; -. DR SIGNOR; P14859; -. DR BioGRID-ORCS; 5451; 69 hits in 1184 CRISPR screens. DR ChiTaRS; POU2F1; human. DR EvolutionaryTrace; P14859; -. DR GeneWiki; POU2F1; -. DR GenomeRNAi; 5451; -. DR Pharos; P14859; Tbio. DR PRO; PR:P14859; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; P14859; Protein. DR Bgee; ENSG00000143190; Expressed in buccal mucosa cell and 193 other cell types or tissues. DR ExpressionAtlas; P14859; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA. 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:0090575; C:RNA polymerase II transcription regulator complex; IMP:CAFA. DR GO; GO:0003677; F:DNA binding; IDA:CAFA. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IC:BHF-UCL. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IMP:CAFA. 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; IDA:BHF-UCL. DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IMP:CAFA. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IC:BHF-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd00086; homeodomain; 1. DR DisProt; DP00231; -. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 1. DR IDEAL; IID00144; -. 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; IPR045703; POU2F1_C. DR InterPro; IPR000327; POU_dom. DR InterPro; IPR000972; TF_octamer. DR PANTHER; PTHR11636; POU DOMAIN; 1. DR PANTHER; PTHR11636:SF47; POU DOMAIN, CLASS 2, TRANSCRIPTION FACTOR 1; 1. DR Pfam; PF00046; Homeodomain; 1. DR Pfam; PF00157; Pou; 1. DR Pfam; PF19536; POU2F1_C; 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. DR Genevisible; P14859; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; DNA-binding; Homeobox; KW Nucleus; Phosphoprotein; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..743 FT /note="POU domain, class 2, transcription factor 1" FT /id="PRO_0000100707" FT DOMAIN 280..354 FT /note="POU-specific" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530" FT DNA_BIND 379..438 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 67..95 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 258..283 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 357..381 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 494..557 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..29 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 258..276 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 357..371 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 270 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 276 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 283 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 385 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:1684878" FT MOD_RES 448 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..20 FT /note="MNNPSETSKPSMESGDGNTG -> MKTRMKIFVMIHFHLMNS (in FT isoform 3)" FT /evidence="ECO:0000305" FT /id="VSP_013421" FT VAR_SEQ 1 FT /note="M -> MLDCSDYVLDSRM (in isoform 2)" FT /evidence="ECO:0000303|PubMed:12663137" FT /id="VSP_002320" FT VAR_SEQ 1 FT /note="M -> MADGGAASQDESSAAAAAAADSRM (in isoform 5 and FT isoform 6)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043195" FT VAR_SEQ 112..174 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043196" FT VAR_SEQ 641..653 FT /note="ALASGGSLPITSL -> GLLHGLENFLTKN (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_013422" FT VAR_SEQ 654..743 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_013423" FT VARIANT 88 FT /note="S -> F (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035816" FT MUTAGEN 385 FT /note="S->A: Loss of inhibition of DNA binding." FT /evidence="ECO:0000269|PubMed:1684878" FT CONFLICT 225 FT /note="L -> Q (in Ref. 1; CAA31767)" FT /evidence="ECO:0000305" FT CONFLICT 546 FT /note="T -> I (in Ref. 2; AAM77920)" FT /evidence="ECO:0000305" FT HELIX 285..301 FT /evidence="ECO:0007829|PDB:1E3O" FT HELIX 306..317 FT /evidence="ECO:0007829|PDB:1E3O" FT HELIX 323..331 FT /evidence="ECO:0007829|PDB:1E3O" FT HELIX 336..353 FT /evidence="ECO:0007829|PDB:1E3O" FT HELIX 388..400 FT /evidence="ECO:0007829|PDB:1E3O" FT HELIX 406..416 FT /evidence="ECO:0007829|PDB:1E3O" FT HELIX 420..434 FT /evidence="ECO:0007829|PDB:1E3O" SQ SEQUENCE 743 AA; 76472 MW; FAB27FFC79CF2276 CRC64; MNNPSETSKP SMESGDGNTG TQTNGLDFQK QPVPVGGAIS TAQAQAFLGH LHQVQLAGTS LQAAAQSLNV QSKSNEESGD SQQPSQPSQQ PSVQAAIPQT QLMLAGGQIT GLTLTPAQQQ LLLQQAQAQA QLLAAAVQQH SASQQHSAAG ATISASAATP MTQIPLSQPI QIAQDLQQLQ QLQQQNLNLQ QFVLVHPTTN LQPAQFIISQ TPQGQQGLLQ AQNLLTQLPQ QSQANLLQSQ PSITLTSQPA TPTRTIAATP IQTLPQSQST PKRIDTPSLE EPSDLEELEQ FAKTFKQRRI KLGFTQGDVG LAMGKLYGND FSQTTISRFE ALNLSFKNMC KLKPLLEKWL NDAENLSSDS SLSSPSALNS PGIEGLSRRR KKRTSIETNI RVALEKSFLE NQKPTSEEIT MIADQLNMEK EVIRVWFCNR RQKEKRINPP SSGGTSSSPI KAIFPSPTSL VATTPSLVTS SAATTLTVSP VLPLTSAAVT NLSVTGTSDT TSNNTATVIS TAPPASSAVT SPSLSPSPSA SASTSEASSA SETSTTQTTS TPLSSPLGTS QVMVTASGLQ TAAAAALQGA AQLPANASLA AMAAAAGLNP SLMAPSQFAA GGALLSLNPG TLSGALSPAL MSNSTLATIQ ALASGGSLPI TSLDATGNLV FANAGGAPNI VTAPLFLNPQ NLSLLTSNPV SLVSAAAASA GNSAPVASLH ATSTSAESIQ NSLFTVASAS GAASTTTTAS KAQ //