ID NANOG_HUMAN Reviewed; 305 AA. AC Q9H9S0; D3DUU4; Q2TTG0; Q6JZS5; DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 2. DT 27-MAR-2024, entry version 183. DE RecName: Full=Homeobox protein NANOG; DE AltName: Full=Homeobox transcription factor Nanog; DE Short=hNanog; GN Name=NANOG; 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), VARIANT ASN-82, AND TISSUE RP SPECIFICITY. RC TISSUE=Embryonic stem cell; RX PubMed=12787504; DOI=10.1016/s0092-8674(03)00393-3; RA Mitsui K., Tokuzawa Y., Itoh H., Segawa K., Murakami M., Takahashi K., RA Maruyama M., Maeda M., Yamanaka S.; RT "The homeoprotein Nanog is required for maintenance of pluripotency in RT mouse epiblast and ES cells."; RL Cell 113:631-642(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Embryonic stem cell; RX PubMed=14990856; DOI=10.1634/stemcells.22-2-169; RA Clark A.T., Rodriguez R.T., Bodnar M.S., Abeyta M.J., Cedars M.I., RA Turek P.J., Firpo M.T., Reijo Pera R.A.; RT "Human STELLAR, NANOG, and GDF3 genes are expressed in pluripotent cells RT and map to chromosome 12p13, a hotspot for teratocarcinoma."; RL Stem Cells 22:169-179(2004). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, DNA-BINDING, RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC TISSUE=Embryonic stem cell; RX PubMed=16391521; DOI=10.1038/emm.2005.73; RA Kim J.S., Kim J., Kim B.S., Chung H.Y., Lee Y.Y., Park C.-S., Lee Y.S., RA Lee Y.H., Chung I.Y.; RT "Identification and functional characterization of an alternative splice RT variant within the fourth exon of human nanog."; RL Exp. Mol. Med. 37:601-607(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ASN-82. RC TISSUE=Teratocarcinoma; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ASN-82. 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP TISSUE SPECIFICITY. RX PubMed=12787505; DOI=10.1016/s0092-8674(03)00392-1; RA Chambers I., Colby D., Robertson M., Nichols J., Lee S., Tweedie S., RA Smith A.; RT "Functional expression cloning of Nanog, a pluripotency sustaining factor RT in embryonic stem cells."; RL Cell 113:643-655(2003). RN [7] RP DEVELOPMENTAL STAGE. RX PubMed=15108323; DOI=10.1002/dvdy.20034; RA Hart A.H., Hartley L., Ibrahim M., Robb L.; RT "Identification, cloning and expression analysis of the pluripotency RT promoting Nanog genes in mouse and human."; RL Dev. Dyn. 230:187-198(2004). RN [8] RP FUNCTION. RX PubMed=16000880; DOI=10.1038/emm.2005.33; RA Oh J.-H., Do H.-J., Yang H.-M., Moon S.-Y., Cha K.-Y., Chung H.-M., RA Kim J.-H.; RT "Identification of a putative transactivation domain in human Nanog."; RL Exp. Mol. Med. 37:250-254(2005). RN [9] RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY. RX PubMed=15982323; DOI=10.1111/j.1365-2559.2005.02182.x; RA Hoei-Hansen C.E., Almstrup K., Nielsen J.E., Brask Sonne S., Graem N., RA Skakkebaek N.E., Leffers H., Rajpert-De Meyts E.; RT "Stem cell pluripotency factor NANOG is expressed in human fetal gonocytes, RT testicular carcinoma in situ and germ cell tumours."; RL Histopathology 47:48-56(2005). RN [10] RP DEVELOPMENTAL STAGE. RX PubMed=15582778; DOI=10.1016/j.mod.2004.08.008; RA Hatano S.Y., Tada M., Kimura H., Yamaguchi S., Kono T., Nakano T., RA Suemori H., Nakatsuji N., Tada T.; RT "Pluripotential competence of cells associated with Nanog activity."; RL Mech. Dev. 122:67-79(2005). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE. RX PubMed=15983365; DOI=10.1634/stemcells.2005-0080; RA Hyslop L.A., Stojkovic M., Armstrong L., Walter T., Stojkovic P., RA Przyborski S., Herbert M., Murdoch A., Strachan T., Lako M.; RT "Downregulation of NANOG induces differentiation of human embryonic stem RT cells to extraembryonic lineages."; RL Stem Cells 23:1035-1043(2005). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH PCGF1. RX PubMed=26687479; DOI=10.1038/srep18388; RA Oliviero G., Munawar N., Watson A., Streubel G., Manning G., Bardwell V., RA Bracken A.P., Cagney G.; RT "The variant Polycomb Repressor Complex 1 component PCGF1 interacts with a RT pluripotency sub-network that includes DPPA4, a regulator of RT embryogenesis."; RL Sci. Rep. 5:18388-18388(2015). RN [13] RP STRUCTURE BY NMR OF 75-157. RG Center for eukaryotic structural genomics (CESG); RT "Solution structure of human stem cell transcription factor NANOG."; RL Submitted (MAR-2010) to the PDB data bank. RN [14] RP X-RAY CRYSTALLOGRAPHY (3.30 ANGSTROMS) OF 94-162 IN COMPLEX WITH DNA, RP DNA-BINDING, MUTAGENESIS OF PHE-102; LEU-122; GLN-124; MET-125; TYR-136; RP LYS-137; LYS-140; THR-141; GLN-144; ASN-145; ARG-147; MET-148 AND LYS-151, RP AND FUNCTION. RX PubMed=25825768; DOI=10.1073/pnas.1502855112; RA Hayashi Y., Caboni L., Das D., Yumoto F., Clayton T., Deller M.C., RA Nguyen P., Farr C.L., Chiu H.J., Miller M.D., Elsliger M.A., Deacon A.M., RA Godzik A., Lesley S.A., Tomoda K., Conklin B.R., Wilson I.A., Yamanaka S., RA Fletterick R.J.; RT "Structure-based discovery of NANOG variant with enhanced properties to RT promote self-renewal and reprogramming of pluripotent stem cells."; RL Proc. Natl. Acad. Sci. U.S.A. 112:4666-4671(2015). RN [15] RP VARIANT ASN-82. RX PubMed=15233988; DOI=10.1016/j.ygeno.2004.02.014; RA Booth H.A., Holland P.W.; RT "Eleven daughters of NANOG."; RL Genomics 84:229-238(2004). CC -!- FUNCTION: Transcription regulator involved in inner cell mass and CC embryonic stem (ES) cells proliferation and self-renewal. Imposes CC pluripotency on ES cells and prevents their differentiation towards CC extraembryonic endoderm and trophectoderm lineages. Blocks bone CC morphogenetic protein-induced mesoderm differentiation of ES cells by CC physically interacting with SMAD1 and interfering with the recruitment CC of coactivators to the active SMAD transcriptional complexes. Acts as a CC transcriptional activator or repressor. Binds optimally to the DNA CC consensus sequence 5'-TAAT[GT][GT]-3' or 5'-[CG][GA][CG]C[GC]ATTAN[GC]- CC 3'. Binds to the POU5F1/OCT4 promoter (PubMed:25825768). Able to CC autorepress its expression in differentiating (ES) cells: binds to its CC own promoter following interaction with ZNF281/ZFP281, leading to CC recruitment of the NuRD complex and subsequent repression of CC expression. When overexpressed, promotes cells to enter into S phase CC and proliferation. {ECO:0000269|PubMed:15983365, CC ECO:0000269|PubMed:16000880, ECO:0000269|PubMed:16391521, CC ECO:0000269|PubMed:25825768}. CC -!- SUBUNIT: Interacts with SMAD1 (By similarity). Interacts with SALL4 (By CC similarity). Interacts with ZNF281/ZFP281 (By similarity). Interacts CC with PCGF1 (PubMed:26687479). Interacts with ESRRB; reciprocally CC modulates their transcriptional activities (By similarity). Interacts CC with NSD2 (By similarity). {ECO:0000250|UniProtKB:Q80Z64, CC ECO:0000269|PubMed:26687479}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, CC ECO:0000269|PubMed:15983365}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9H9S0-1; Sequence=Displayed; CC Name=2; Synonyms=Nanog-delta 48; CC IsoId=Q9H9S0-2; Sequence=VSP_021688; CC -!- TISSUE SPECIFICITY: Expressed in testicular carcinoma and derived germ CC cell tumors (at protein level). Expressed in fetal gonads, ovary and CC testis. Also expressed in ovary teratocarcinoma cell line and CC testicular embryonic carcinoma. Not expressed in many somatic organs CC and oocytes. {ECO:0000269|PubMed:12787504, ECO:0000269|PubMed:12787505, CC ECO:0000269|PubMed:14990856, ECO:0000269|PubMed:15982323, CC ECO:0000269|PubMed:16391521}. CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic stem (ES) and carcinoma CC (EC) cells. Expressed in inner cell mass (ICM) of the blastocyst and CC gonocytes between 14 and 19 weeks of gestation (at protein level). Not CC expressed in oocytes, unfertilized oocytes, 2-16 cell embryos and early CC morula (at protein level). Expressed in embryonic stem cells (ES). CC Expression decreases with ES differentiation. CC {ECO:0000269|PubMed:15108323, ECO:0000269|PubMed:15582778, CC ECO:0000269|PubMed:15982323, ECO:0000269|PubMed:15983365, CC ECO:0000269|PubMed:16391521}. CC -!- MISCELLANEOUS: Exists an other tandem duplicated non-processed CC pseudogene (NANOGP1) and 10 other NANOG-related nucleotide sequences CC located on different chromosomes, all of which are processed CC pseudogenes lacking introns (NANOGP2 to NANOGP11); except NANOGP8 which CC is a retrogene. CC -!- SIMILARITY: Belongs to the Nanog homeobox family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Nanog entry; CC URL="https://en.wikipedia.org/wiki/Nanog"; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/46540/NANOG"; 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; AB093576; BAC76999.1; -; mRNA. DR EMBL; AY230262; AAP49529.1; -; mRNA. DR EMBL; AY578089; AAT81526.1; -; mRNA. DR EMBL; AK022643; BAB14151.1; -; mRNA. DR EMBL; CH471116; EAW88649.1; -; Genomic_DNA. DR EMBL; CH471116; EAW88651.1; -; Genomic_DNA. DR CCDS; CCDS31736.1; -. [Q9H9S0-1] DR CCDS; CCDS73436.1; -. [Q9H9S0-2] DR RefSeq; NP_001284627.1; NM_001297698.1. [Q9H9S0-2] DR RefSeq; NP_079141.2; NM_024865.3. [Q9H9S0-1] DR PDB; 2KT0; NMR; -; A=75-157. DR PDB; 4RBO; X-ray; 3.30 A; A/D=94-162. DR PDBsum; 2KT0; -. DR PDBsum; 4RBO; -. DR AlphaFoldDB; Q9H9S0; -. DR BMRB; Q9H9S0; -. DR SMR; Q9H9S0; -. DR BioGRID; 123000; 240. DR CORUM; Q9H9S0; -. DR IntAct; Q9H9S0; 3. DR MINT; Q9H9S0; -. DR STRING; 9606.ENSP00000229307; -. DR ChEMBL; CHEMBL3580527; -. DR iPTMnet; Q9H9S0; -. DR PhosphoSitePlus; Q9H9S0; -. DR BioMuta; NANOG; -. DR DMDM; 118573073; -. DR EPD; Q9H9S0; -. DR jPOST; Q9H9S0; -. DR MassIVE; Q9H9S0; -. DR PaxDb; 9606-ENSP00000229307; -. DR PeptideAtlas; Q9H9S0; -. DR Antibodypedia; 4521; 1430 antibodies from 49 providers. DR CPTC; Q9H9S0; 3 antibodies. DR DNASU; 79923; -. DR Ensembl; ENST00000229307.9; ENSP00000229307.4; ENSG00000111704.11. [Q9H9S0-1] DR Ensembl; ENST00000526286.1; ENSP00000435288.1; ENSG00000111704.11. [Q9H9S0-2] DR GeneID; 79923; -. DR KEGG; hsa:79923; -. DR MANE-Select; ENST00000229307.9; ENSP00000229307.4; NM_024865.4; NP_079141.2. DR UCSC; uc009zfy.2; human. [Q9H9S0-1] DR AGR; HGNC:20857; -. DR CTD; 79923; -. DR DisGeNET; 79923; -. DR GeneCards; NANOG; -. DR HGNC; HGNC:20857; NANOG. DR HPA; ENSG00000111704; Not detected. DR MIM; 607937; gene. DR neXtProt; NX_Q9H9S0; -. DR OpenTargets; ENSG00000111704; -. DR PharmGKB; PA134864904; -. DR VEuPathDB; HostDB:ENSG00000111704; -. DR eggNOG; KOG0491; Eukaryota. DR GeneTree; ENSGT00670000098076; -. DR HOGENOM; CLU_086240_0_0_1; -. DR InParanoid; Q9H9S0; -. DR OMA; AWSNHSW; -. DR OrthoDB; 4050836at2759; -. DR PhylomeDB; Q9H9S0; -. DR TreeFam; TF337402; -. DR PathwayCommons; Q9H9S0; -. DR Reactome; R-HSA-2892245; POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation. DR Reactome; R-HSA-2892247; POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation. DR Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells. DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling. DR Reactome; R-HSA-9754189; Germ layer formation at gastrulation. DR Reactome; R-HSA-9823739; Formation of the anterior neural plate. DR Reactome; R-HSA-9827857; Specification of primordial germ cells. DR SignaLink; Q9H9S0; -. DR SIGNOR; Q9H9S0; -. DR BioGRID-ORCS; 79923; 20 hits in 1103 CRISPR screens. DR EvolutionaryTrace; Q9H9S0; -. DR GeneWiki; Homeobox_protein_NANOG; -. DR GenomeRNAi; 79923; -. DR Pharos; Q9H9S0; Tbio. DR PRO; PR:Q9H9S0; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9H9S0; Protein. DR Bgee; ENSG00000111704; Expressed in primordial germ cell in gonad and 69 other cell types or tissues. DR ExpressionAtlas; Q9H9S0; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005730; C:nucleolus; IDA:BHF-UCL. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL. DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:HGNC-UCL. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISS:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB. DR GO; GO:0030154; P:cell differentiation; IEP:HGNC-UCL. DR GO; GO:0001714; P:endodermal cell fate specification; IDA:MGI. DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:HGNC-UCL. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0045595; P:regulation of cell differentiation; IMP:HGNC-UCL. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:HGNC-UCL. DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0035019; P:somatic stem cell population maintenance; IMP:UniProtKB. DR GO; GO:0019827; P:stem cell population maintenance; IEP:BHF-UCL. DR CDD; cd00086; homeodomain; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR InterPro; IPR009057; Homeobox-like_sf. DR InterPro; IPR017970; Homeobox_CS. DR InterPro; IPR001356; Homeobox_dom. DR PANTHER; PTHR24327; HOMEOBOX PROTEIN; 1. DR PANTHER; PTHR24327:SF79; HOMEOBOX PROTEIN NANOG-RELATED; 1. DR Pfam; PF00046; Homeodomain; 1. DR SMART; SM00389; HOX; 1. DR SUPFAM; SSF46689; Homeodomain-like; 1. DR PROSITE; PS00027; HOMEOBOX_1; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR Genevisible; Q9H9S0; HS. PE 1: Evidence at protein level; KW 3D-structure; Activator; Alternative splicing; Developmental protein; KW DNA-binding; Homeobox; Nucleus; Reference proteome; Repeat; Repressor; KW Transcription; Transcription regulation. FT CHAIN 1..305 FT /note="Homeobox protein NANOG" FT /id="PRO_0000261418" FT REPEAT 196..200 FT /note="1" FT REPEAT 201..205 FT /note="2" FT REPEAT 206..210 FT /note="3" FT REPEAT 216..220 FT /note="4" FT REPEAT 221..225 FT /note="5" FT REPEAT 226..230 FT /note="6" FT REPEAT 231..235 FT /note="7" FT REPEAT 236..240 FT /note="8" FT DNA_BIND 95..154 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..96 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 122..151 FT /note="Required for DNA-binding" FT /evidence="ECO:0000269|PubMed:25825768" FT REGION 196..240 FT /note="8 X repeats starting with a Trp in each unit" FT REGION 196..240 FT /note="Sufficient for transactivation activity" FT /evidence="ECO:0000250" FT REGION 241..305 FT /note="Sufficient for strong transactivation activity" FT /evidence="ECO:0000250" FT COMPBIAS 35..78 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 80..96 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 168..183 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:16391521" FT /id="VSP_021688" FT VARIANT 82 FT /note="K -> N (in dbSNP:rs2889551)" FT /evidence="ECO:0000269|PubMed:12787504, FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15233988, FT ECO:0000269|Ref.5" FT /id="VAR_029384" FT MUTAGEN 102 FT /note="F->A: No effect on POU5F1 promoter DNA-binding." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 122 FT /note="L->A: Increased POU5F1 promoter DNA-binding and FT protein stability." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 124 FT /note="Q->A: Decreased POU5F1 promoter DNA-binding and FT protein stability." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 125 FT /note="M->A: Decreased POU5F1 promoter DNA-binding and FT protein stability." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 136 FT /note="Y->A: Decreased POU5F1 promoter DNA-binding and FT protein stability." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 137 FT /note="K->A: Inhibits POU5F1 promoter DNA-binding." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 140 FT /note="K->A: Decreased POU5F1 promoter DNA-binding and FT protein stability." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 141 FT /note="T->A: Inhibits POU5F1 promoter DNA-binding." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 144 FT /note="Q->A: No effect on POU5F1 promoter DNA-binding. FT Decreased protein stability." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 145 FT /note="N->A: Inhibits POU5F1 promoter DNA-binding." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 147 FT /note="R->A: Inhibits POU5F1 promoter DNA-binding." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 148 FT /note="M->A: No effect on POU5F1 promoter DNA-binding. FT Increased protein stability." FT /evidence="ECO:0000269|PubMed:25825768" FT MUTAGEN 151 FT /note="K->A: Decreased POU5F1 promoter DNA-binding and FT protein stability." FT /evidence="ECO:0000269|PubMed:25825768" FT HELIX 104..116 FT /evidence="ECO:0007829|PDB:4RBO" FT STRAND 117..119 FT /evidence="ECO:0007829|PDB:2KT0" FT HELIX 122..131 FT /evidence="ECO:0007829|PDB:4RBO" FT HELIX 136..152 FT /evidence="ECO:0007829|PDB:4RBO" SQ SEQUENCE 305 AA; 34620 MW; AC3B2E067C591773 CRC64; MSVDPACPQS LPCFEASDCK ESSPMPVICG PEENYPSLQM SSAEMPHTET VSPLPSSMDL LIQDSPDSST SPKGKQPTSA EKSVAKKEDK VPVKKQKTRT VFSSTQLCVL NDRFQRQKYL SLQQMQELSN ILNLSYKQVK TWFQNQRMKS KRWQKNNWPK NSNGVTQKAS APTYPSLYSS YHQGCLVNPT GNLPMWSNQT WNNSTWSNQT QNIQSWSNHS WNTQTWCTQS WNNQAWNSPF YNCGEESLQS CMQFQPNSPA SDLEAALEAA GEGLNVIQQT TRYFSTPQTM DLFLNYSMNM QPEDV //