PO4F2_HUMAN
ID PO4F2_HUMAN Reviewed; 409 AA.
AC Q12837; B1PJR6; B2RC84; Q13883; Q14987;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=POU domain, class 4, transcription factor 2 {ECO:0000305};
DE AltName: Full=Brain-specific homeobox/POU domain protein 3B;
DE Short=Brain-3B;
DE Short=Brn-3B;
GN Name=POU4F2 {ECO:0000312|HGNC:HGNC:9219}; Synonyms=BRN3B;
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 1), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=7691107; DOI=10.1016/0896-6273(93)90079-7;
RA Xiang M., Zhou L.-J., Peng Y., Eddy R.L., Shows T.B., Nathans J.;
RT "Brn-3b: a POU domain gene expressed in a subset of retinal ganglion
RT cells.";
RL Neuron 11:689-701(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=8332509; DOI=10.1093/nar/21.12.2946;
RA Ring C.J.A., Latchman D.S.;
RT "The human Brn-3b POU transcription factor shows only limited homology to
RT the Brn-3a/RDC-1 factor outside the conserved POU domain.";
RL Nucleic Acids Res. 21:2946-2946(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 7-409 (ISOFORM 1), FUNCTION, SUBCELLULAR
RP LOCATION, MOTIF, AND MUTAGENESIS OF 171-HIS--HIS-185.
RC TISSUE=Testis;
RX PubMed=19266028; DOI=10.1371/journal.pgen.1000397;
RA Salichs E., Ledda A., Mularoni L., Alba M.M., de la Luna S.;
RT "Genome-wide analysis of histidine repeats reveals their role in the
RT localization of human proteins to the nuclear speckles compartment.";
RL PLoS Genet. 5:E1000397-E1000397(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 274-391 (ISOFORM 1/2).
RX PubMed=8234287; DOI=10.1073/pnas.90.21.10260;
RA Bhargava A.K., Li Z., Weissman S.M.;
RT "Differential expression of four members of the POU family of proteins in
RT activated and phorbol 12-myristate 13-acetate-treated Jurkat T cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:10260-10264(1993).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=11526481; DOI=10.1038/sj.onc.1204491;
RA Dennis J.H., Budhram-Mahadeo V., Latchman D.S.;
RT "The Brn-3b POU family transcription factor regulates the cellular growth,
RT proliferation, and anchorage dependence of MCF7 human breast cancer
RT cells.";
RL Oncogene 20:4961-4971(2001).
RN [9]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=23805044;
RA Zhang L., Wahlin K., Li Y., Masuda T., Yang Z., Zack D.J., Esumi N.;
RT "RIT2, a neuron-specific small guanosine triphosphatase, is expressed in
RT retinal neuronal cells and its promoter is modulated by the POU4
RT transcription factors.";
RL Mol. Vis. 19:1371-1386(2013).
CC -!- FUNCTION: Tissue-specific DNA-binding transcription factor involved in
CC the development and differentiation of target cells (PubMed:19266028,
CC PubMed:23805044). Functions either as activator or repressor modulating
CC the rate of target gene transcription through RNA polymerase II enzyme
CC in a promoter-dependent manner (PubMed:19266028, PubMed:23805044).
CC Binds to the consensus octamer motif 5'-AT[A/T]A[T/A]T[A/T]A-3' of
CC promoter of target genes. Plays a fundamental role in the gene
CC regulatory network essential for retinal ganglion cell (RGC)
CC differentiation. Binds to an octamer site to form a ternary complex
CC with ISL1; cooperates positively with ISL1 and ISL2 to potentiate
CC transcriptional activation of RGC target genes being involved in RGC
CC fate commitment in the developing retina and RGC axon formation and
CC pathfinding. Inhibits DLX1 and DLX2 transcriptional activities
CC preventing DLX1- and DLX2-mediated ability to promote amacrine cell
CC fate specification. In cooperation with TP53 potentiates
CC transcriptional activation of BAX promoter activity increasing neuronal
CC cell apoptosis. Negatively regulates BAX promoter activity in the
CC absence of TP53. Acts as a transcriptional coactivator via its
CC interaction with the transcription factor ESR1 by enhancing its effect
CC on estrogen response element (ERE)-containing promoter. Antagonizes the
CC transcriptional stimulatory activity of POU4F1 by preventing its
CC binding to an octamer motif. Involved in TNFSF11-mediated terminal
CC osteoclast differentiation (By similarity).
CC {ECO:0000250|UniProtKB:Q63934, ECO:0000269|PubMed:19266028,
CC ECO:0000269|PubMed:23805044}.
CC -!- SUBUNIT: Interacts with POU4F1; this interaction inhibits both POU4F1
CC DNA-binding and transcriptional activities. Interacts (C-terminus) with
CC ESR1 (via DNA-binding domain); this interaction increases the estrogen
CC receptor ESR1 transcriptional activity in a DNA- and ligand 17-beta-
CC estradiol-independent manner. Interacts (via C-terminus) with TP53 (via
CC N-terminus). Interacts with DLX1 (via homeobox DNA-binding domain);
CC this interaction suppresses DLX1-mediated transcriptional activity in
CC postnatal retina enhancing retinal ganglion cell (RGC) differentiation.
CC Interacts with DLX2 (via homeobox DNA-binding domain); this interaction
CC enhances RGC differentiation. Interacts (via C-terminus) with ISL1 (via
CC C-terminus). Interacts with ISL2. Interacts with LHX2.
CC {ECO:0000250|UniProtKB:Q63934}.
CC -!- INTERACTION:
CC Q12837; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-17236143, EBI-10173507;
CC Q12837; P05187: ALPP; NbExp=3; IntAct=EBI-17236143, EBI-1211484;
CC Q12837; P48745: CCN3; NbExp=3; IntAct=EBI-17236143, EBI-3904822;
CC Q12837; P15529-3: CD46; NbExp=3; IntAct=EBI-17236143, EBI-13046140;
CC Q12837; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-17236143, EBI-12261896;
CC Q12837; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-17236143, EBI-741528;
CC Q12837; Q9H2X0: CHRD; NbExp=3; IntAct=EBI-17236143, EBI-947551;
CC Q12837; Q6WN34-2: CHRDL2; NbExp=3; IntAct=EBI-17236143, EBI-12593838;
CC Q12837; P27658: COL8A1; NbExp=5; IntAct=EBI-17236143, EBI-747133;
CC Q12837; Q08AG9: CYP21A2; NbExp=3; IntAct=EBI-17236143, EBI-14156412;
CC Q12837; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-17236143, EBI-3867333;
CC Q12837; O60479: DLX3; NbExp=3; IntAct=EBI-17236143, EBI-3908248;
CC Q12837; Q9NVL1-2: FAM86C1P; NbExp=5; IntAct=EBI-17236143, EBI-12845222;
CC Q12837; P28799: GRN; NbExp=6; IntAct=EBI-17236143, EBI-747754;
CC Q12837; Q9BSH5: HDHD3; NbExp=3; IntAct=EBI-17236143, EBI-745201;
CC Q12837; Q4VC39: HIGD2B; NbExp=3; IntAct=EBI-17236143, EBI-12881610;
CC Q12837; P24592: IGFBP6; NbExp=3; IntAct=EBI-17236143, EBI-947015;
CC Q12837; Q6UW32: IGFL1; NbExp=3; IntAct=EBI-17236143, EBI-3870426;
CC Q12837; Q0VD86: INCA1; NbExp=3; IntAct=EBI-17236143, EBI-6509505;
CC Q12837; Q5T749: KPRP; NbExp=5; IntAct=EBI-17236143, EBI-10981970;
CC Q12837; Q15323: KRT31; NbExp=3; IntAct=EBI-17236143, EBI-948001;
CC Q12837; Q92764: KRT35; NbExp=3; IntAct=EBI-17236143, EBI-1058674;
CC Q12837; O76015: KRT38; NbExp=3; IntAct=EBI-17236143, EBI-1047263;
CC Q12837; P78385: KRT83; NbExp=3; IntAct=EBI-17236143, EBI-10221390;
CC Q12837; P60412: KRTAP10-11; NbExp=3; IntAct=EBI-17236143, EBI-10217483;
CC Q12837; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-17236143, EBI-10172150;
CC Q12837; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-17236143, EBI-10171774;
CC Q12837; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-17236143, EBI-10172052;
CC Q12837; P59990: KRTAP12-1; NbExp=3; IntAct=EBI-17236143, EBI-10210845;
CC Q12837; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-17236143, EBI-10176379;
CC Q12837; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-17236143, EBI-11953334;
CC Q12837; P60329: KRTAP12-4; NbExp=3; IntAct=EBI-17236143, EBI-10176396;
CC Q12837; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-17236143, EBI-10241252;
CC Q12837; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-17236143, EBI-12196745;
CC Q12837; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-17236143, EBI-12805508;
CC Q12837; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-17236143, EBI-10241353;
CC Q12837; Q3LI59: KRTAP21-2; NbExp=3; IntAct=EBI-17236143, EBI-18395721;
CC Q12837; Q9BYR7: KRTAP3-2; NbExp=5; IntAct=EBI-17236143, EBI-751260;
CC Q12837; Q9BYQ6: KRTAP4-11; NbExp=3; IntAct=EBI-17236143, EBI-10302392;
CC Q12837; Q9BQ66: KRTAP4-12; NbExp=3; IntAct=EBI-17236143, EBI-739863;
CC Q12837; Q9BYR5: KRTAP4-2; NbExp=3; IntAct=EBI-17236143, EBI-10172511;
CC Q12837; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-17236143, EBI-11958132;
CC Q12837; Q9BYR2: KRTAP4-5; NbExp=3; IntAct=EBI-17236143, EBI-11993254;
CC Q12837; Q6L8G4: KRTAP5-11; NbExp=3; IntAct=EBI-17236143, EBI-11993296;
CC Q12837; Q6L8H2: KRTAP5-3; NbExp=3; IntAct=EBI-17236143, EBI-11974251;
CC Q12837; Q6L8H1: KRTAP5-4; NbExp=3; IntAct=EBI-17236143, EBI-11963072;
CC Q12837; Q6L8G9: KRTAP5-6; NbExp=3; IntAct=EBI-17236143, EBI-10250562;
CC Q12837; P26371: KRTAP5-9; NbExp=3; IntAct=EBI-17236143, EBI-3958099;
CC Q12837; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-17236143, EBI-12111050;
CC Q12837; Q9BYQ4: KRTAP9-2; NbExp=6; IntAct=EBI-17236143, EBI-1044640;
CC Q12837; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-17236143, EBI-1043191;
CC Q12837; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-17236143, EBI-11958364;
CC Q12837; Q5T751: LCE1C; NbExp=3; IntAct=EBI-17236143, EBI-12224199;
CC Q12837; Q5T754: LCE1F; NbExp=3; IntAct=EBI-17236143, EBI-11958008;
CC Q12837; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-17236143, EBI-11955689;
CC Q12837; P80188: LCN2; NbExp=3; IntAct=EBI-17236143, EBI-11911016;
CC Q12837; Q9UHV8: LGALS13; NbExp=3; IntAct=EBI-17236143, EBI-3957707;
CC Q12837; P50458: LHX2; NbExp=3; IntAct=EBI-17236143, EBI-12179869;
CC Q12837; Q6UXB3: LYPD2; NbExp=3; IntAct=EBI-17236143, EBI-18270828;
CC Q12837; Q9H3L0: MMADHC; NbExp=3; IntAct=EBI-17236143, EBI-11111575;
CC Q12837; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-17236143, EBI-10271199;
CC Q12837; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-17236143, EBI-17490746;
CC Q12837; Q92824-2: PCSK5; NbExp=6; IntAct=EBI-17236143, EBI-11956269;
CC Q12837; Q9NRY7: PLSCR2; NbExp=5; IntAct=EBI-17236143, EBI-3937430;
CC Q12837; P10745: RBP3; NbExp=3; IntAct=EBI-17236143, EBI-12806054;
CC Q12837; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-17236143, EBI-740343;
CC Q12837; P49795: RGS19; NbExp=3; IntAct=EBI-17236143, EBI-874907;
CC Q12837; Q9C004: SPRY4; NbExp=3; IntAct=EBI-17236143, EBI-354861;
CC Q12837; P01137: TGFB1; NbExp=3; IntAct=EBI-17236143, EBI-779636;
CC Q12837; Q8IWZ5: TRIM42; NbExp=5; IntAct=EBI-17236143, EBI-5235829;
CC Q12837; Q2TAL6: VWC2; NbExp=3; IntAct=EBI-17236143, EBI-11957238;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:7691107}. Nucleus
CC speckle {ECO:0000269|PubMed:19266028}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q63934}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Brn-3b long {ECO:0000303|PubMed:23805044}, Brn-3b-l
CC {ECO:0000303|PubMed:23805044};
CC IsoId=Q12837-1; Sequence=Displayed;
CC Name=2; Synonyms=Brn-3b short {ECO:0000303|PubMed:23805044}, Brn-3b-s
CC {ECO:0000303|PubMed:23805044};
CC IsoId=Q12837-2; Sequence=VSP_058837;
CC -!- TISSUE SPECIFICITY: Expressed in the brain (PubMed:7691107). Expressed
CC in the ganglion cell layer of the retina (PubMed:7691107).
CC {ECO:0000269|PubMed:7691107}.
CC -!- DOMAIN: The N-terminal transcriptional activation region is sufficient
CC to induce transcriptional activity. {ECO:0000250|UniProtKB:Q63934}.
CC -!- DOMAIN: The POU-specific domain and POU homeodomain regions are
CC necessary for DNA-binding activity and transcriptional repression.
CC {ECO:0000250|UniProtKB:Q63934}.
CC -!- DOMAIN: The polyhistidine motif acts as a targeting signal to nuclear
CC speckles. {ECO:0000269|PubMed:19266028}.
CC -!- SIMILARITY: Belongs to the POU transcription factor family. Class-4
CC subfamily. {ECO:0000305}.
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DR EMBL; U06233; AAA16509.1; -; mRNA.
DR EMBL; AK314982; BAG37481.1; -; mRNA.
DR EMBL; AC093887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136344; AAI36345.1; -; mRNA.
DR EMBL; BC136345; AAI36346.1; -; mRNA.
DR EMBL; EU439706; ACA49233.1; -; mRNA.
DR EMBL; X71488; CAA50589.1; -; mRNA.
DR EMBL; L20434; AAA36393.1; -; mRNA.
DR CCDS; CCDS34074.1; -. [Q12837-1]
DR PIR; I38502; I38502.
DR RefSeq; NP_004566.2; NM_004575.2. [Q12837-1]
DR AlphaFoldDB; Q12837; -.
DR SMR; Q12837; -.
DR BioGRID; 111454; 77.
DR IntAct; Q12837; 71.
DR STRING; 9606.ENSP00000281321; -.
DR GlyGen; Q12837; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12837; -.
DR PhosphoSitePlus; Q12837; -.
DR BioMuta; POU4F2; -.
DR DMDM; 290457652; -.
DR MassIVE; Q12837; -.
DR PaxDb; Q12837; -.
DR PeptideAtlas; Q12837; -.
DR PRIDE; Q12837; -.
DR Antibodypedia; 16443; 168 antibodies from 24 providers.
DR DNASU; 5458; -.
DR Ensembl; ENST00000281321.3; ENSP00000281321.3; ENSG00000151615.3. [Q12837-1]
DR GeneID; 5458; -.
DR KEGG; hsa:5458; -.
DR MANE-Select; ENST00000281321.3; ENSP00000281321.3; NM_004575.3; NP_004566.2.
DR UCSC; uc003ikv.4; human. [Q12837-1]
DR CTD; 5458; -.
DR DisGeNET; 5458; -.
DR GeneCards; POU4F2; -.
DR HGNC; HGNC:9219; POU4F2.
DR HPA; ENSG00000151615; Tissue enriched (brain).
DR MIM; 113725; gene.
DR neXtProt; NX_Q12837; -.
DR OpenTargets; ENSG00000151615; -.
DR PharmGKB; PA33543; -.
DR VEuPathDB; HostDB:ENSG00000151615; -.
DR eggNOG; KOG1168; Eukaryota.
DR GeneTree; ENSGT00940000160339; -.
DR HOGENOM; CLU_013065_0_0_1; -.
DR InParanoid; Q12837; -.
DR OMA; THAPHMA; -.
DR OrthoDB; 929123at2759; -.
DR PhylomeDB; Q12837; -.
DR TreeFam; TF316413; -.
DR PathwayCommons; Q12837; -.
DR Reactome; R-HSA-6804759; Regulation of TP53 Activity through Association with Co-factors.
DR SignaLink; Q12837; -.
DR SIGNOR; Q12837; -.
DR BioGRID-ORCS; 5458; 8 hits in 1087 CRISPR screens.
DR GeneWiki; POU4F2; -.
DR GenomeRNAi; 5458; -.
DR Pharos; Q12837; Tbio.
DR PRO; PR:Q12837; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q12837; protein.
DR Bgee; ENSG00000151615; Expressed in secondary oocyte and 17 other tissues.
DR Genevisible; Q12837; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IGI:ARUK-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:ParkinsonsUK-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0048675; P:axon extension; IEA:Ensembl.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; ISS:UniProtKB.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
DR GO; GO:0071453; P:cellular response to oxygen levels; IEA:Ensembl.
DR GO; GO:1990791; P:dorsal root ganglion development; ISS:UniProtKB.
DR GO; GO:0007507; P:heart development; ISS:ARUK-UCL.
DR GO; GO:0030520; P:intracellular estrogen receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISS:UniProtKB.
DR GO; GO:0000165; P:MAPK cascade; IDA:UniProtKB.
DR GO; GO:1904178; P:negative regulation of adipose tissue development; IEA:Ensembl.
DR GO; GO:1902870; P:negative regulation of amacrine cell differentiation; ISS:UniProtKB.
DR GO; GO:0045596; P:negative regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045773; P:positive regulation of axon extension; ISS:UniProtKB.
DR GO; GO:0010666; P:positive regulation of cardiac muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:0045597; P:positive regulation of cell differentiation; ISS:UniProtKB.
DR GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISS:UniProtKB.
DR GO; GO:0043068; P:positive regulation of programmed cell death; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:ParkinsonsUK-UCL.
DR GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
DR GO; GO:0051090; P:regulation of DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0090259; P:regulation of retinal ganglion cell axon guidance; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd00093; HTH_XRE; 1.
DR Gene3D; 1.10.260.40; -; 1.
DR InterPro; IPR001387; Cro/C1-type_HTH.
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 Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00157; Pou; 1.
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 Activator; Alternative splicing; Apoptosis; Cytoplasm;
KW Developmental protein; Differentiation; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..409
FT /note="POU domain, class 4, transcription factor 2"
FT /id="PRO_0000100740"
FT DOMAIN 250..327
FT /note="POU-specific"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00530"
FT DNA_BIND 345..404
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 26..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..237
FT /note="Required for transcriptional activation"
FT /evidence="ECO:0000250|UniProtKB:Q63934"
FT REGION 153..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..409
FT /note="Required for DNA-binding and transcriptional
FT repression"
FT /evidence="ECO:0000250|UniProtKB:Q63934"
FT MOTIF 110..119
FT /note="POU-IV box"
FT MOTIF 171..185
FT /note="Nuclear speckle targeting signal"
FT /evidence="ECO:0000269|PubMed:19266028"
FT COMPBIAS 29..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..144
FT /note="Missing (in isoform 2)"
FT /id="VSP_058837"
FT VARIANT 40
FT /note="I -> T (in dbSNP:rs13152799)"
FT /id="VAR_059321"
FT MUTAGEN 171..185
FT /note="Missing: Absent from nuclear speckle; no change in
FT transcriptional activity."
FT /evidence="ECO:0000269|PubMed:19266028"
FT CONFLICT 54
FT /note="G -> GG (in Ref. 1; AAA16509 and 3; BAG37481/
FT AAI36345/AAI36346)"
FT /evidence="ECO:0000305"
FT CONFLICT 165
FT /note="S -> C (in Ref. 1; AAA16509)"
FT /evidence="ECO:0000305"
FT CONFLICT 182
FT /note="Missing (in Ref. 2; CAA50589)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 43087 MW; 42E2C174674E8DFC CRC64;
MMMMSLNSKQ AFSMPHGGSL HVEPKYSALH STSPGSSAPI APSASSPSSS SNAGGGGGGG
GGGGGGGGRS SSSSSSGSSG GGGSEAMRRA CLPTPPSNIF GGLDESLLAR AEALAAVDIV
SQSKSHHHHP PHHSPFKPDA TYHTMNTIPC TSAASSSSVP ISHPSALAGT HHHHHHHHHH
HHQPHQALEG ELLEHLSPGL ALGAMAGPDG AVVSTPAHAP HMATMNPMHQ AALSMAHAHG
LPSHMGCMSD VDADPRDLEA FAERFKQRRI KLGVTQADVG SALANLKIPG VGSLSQSTIC
RFESLTLSHN NMIALKPILQ AWLEEAEKSH REKLTKPELF NGAEKKRKRT SIAAPEKRSL
EAYFAIQPRP SSEKIAAIAE KLDLKKNVVR VWFCNQRQKQ KRMKYSAGI
