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}.
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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 Genevisible; P14859; HS.
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.
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
//
