ID FOXN1_HUMAN Reviewed; 648 AA. AC O15353; B2R9Q7; O15352; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 193. DE RecName: Full=Forkhead box protein N1; DE AltName: Full=Winged-helix transcription factor nude; GN Name=FOXN1; Synonyms=RONU, WHN; 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 [GENOMIC DNA / MRNA], AND VARIANT VAL-283. RC TISSUE=Thymus; RX PubMed=9321431; DOI=10.1007/s002510050312; RA Schorpp M., Hofmann M., Dear T.N., Boehm T.; RT "Characterization of mouse and human nude genes."; RL Immunogenetics 46:509-515(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 [3] 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 [4] RP INVOLVEMENT IN TIDAND, AND VARIANT TIDAND 255-ARG--ALA-648 DEL. RX PubMed=10206641; DOI=10.1038/18997; RA Frank J., Pignata C., Panteleyev A.A., Prowse D.M., Baden H., Weiner L., RA Gaetaniello L., Ahmad W., Pozzi N., Cserhalmi-Friedman P.B., Aita V.M., RA Uyttendaele H., Gordon D., Ott J., Brissette J.L., Christiano A.M.; RT "Exposing the human nude phenotype."; RL Nature 398:473-474(1999). RN [5] RP FUNCTION, INVOLVEMENT IN TIDAND, AND VARIANT TIDAND 255-ARG--ALA-648 DEL. RX PubMed=21507891; DOI=10.1136/jmg.2011.089532; RA Vigliano I., Gorrese M., Fusco A., Vitiello L., Amorosi S., Panico L., RA Ursini M.V., Calcagno G., Racioppi L., Del Vecchio L., Pignata C.; RT "FOXN1 mutation abrogates prenatal T-cell development in humans."; RL J. Med. Genet. 48:413-416(2011). RN [6] RP INVOLVEMENT IN TIDAND. RX PubMed=25173801; DOI=10.1016/j.clim.2014.08.005; RA Chou J., Massaad M.J., Wakim R.H., Bainter W., Dbaibo G., Geha R.S.; RT "A novel mutation in FOXN1 resulting in SCID: a case report and literature RT review."; RL Clin. Immunol. 155:30-32(2014). RN [7] RP REVIEW. RX PubMed=23874334; DOI=10.3389/fimmu.2013.00187; RA Romano R., Palamaro L., Fusco A., Giardino G., Gallo V., Del Vecchio L., RA Pignata C.; RT "FOXN1: a master regulator gene of thymic epithelial development program."; RL Front. Immunol. 4:187-187(2013). RN [8] RP REVIEW. RX PubMed=24432845; DOI=10.3109/08830185.2013.870171; RA Palamaro L., Romano R., Fusco A., Giardino G., Gallo V., Pignata C.; RT "FOXN1 in organ development and human diseases."; RL Int. Rev. Immunol. 33:83-93(2014). RN [9] RP VARIANTS TIDAND 255-ARG--ALA-648 DEL AND TRP-320. RX PubMed=20978268; DOI=10.1182/blood-2010-06-292490; RA Markert M.L., Marques J.G., Neven B., Devlin B.H., McCarthy E.A., RA Chinn I.K., Albuquerque A.S., Silva S.L., Pignata C., de Saint Basile G., RA Victorino R.M., Picard C., Debre M., Mahlaoui N., Fischer A., Sousa A.E.; RT "First use of thymus transplantation therapy for FOXN1 deficiency RT (nude/SCID): a report of 2 cases."; RL Blood 117:688-696(2011). RN [10] RP VARIANT TIDAND 255-ARG--ALA-648 DEL. RX PubMed=28636882; DOI=10.1016/j.gene.2017.06.033; RA Radha Rama Devi A., Panday N.N., Naushad S.M.; RT "FOXN1 Italian founder mutation in Indian family: Implications in prenatal RT diagnosis."; RL Gene 627:222-225(2017). RN [11] RP VARIANTS TLIND LYS-169; 255-ARG--ALA-648 DEL; TRP-320; ASN-321; PRO-325 AND RP 474-GLN--ALA-648 DEL, AND INVOLVEMENT IN TLIND. RX PubMed=31447097; DOI=10.1016/j.ajhg.2019.07.014; RA Bosticardo M., Yamazaki Y., Cowan J., Giardino G., Corsino C., Scalia G., RA Prencipe R., Ruffner M., Hill D.A., Sakovich I., Yemialyanava I., Tam J.S., RA Padem N., Elder M.E., Sleasman J.W., Perez E., Niebur H., Seroogy C.M., RA Sharapova S., Gebbia J., Kleiner G.I., Peake J., Abbott J.K., Gelfand E.W., RA Crestani E., Biggs C., Butte M.J., Hartog N., Hayward A., Chen K., RA Heimall J., Seeborg F., Bartnikas L.M., Cooper M.A., Pignata C., RA Bhandoola A., Notarangelo L.D.; RT "Heterozygous FOXN1 variants cause low TRECs and severe T cell lymphopenia, RT revealing a crucial role of FOXN1 in supporting early thymopoiesis."; RL Am. J. Hum. Genet. 105:549-561(2019). RN [12] RP VARIANT TIDTA 363-TRP--PRO-368 DELINS CYS, INVOLVEMENT IN TIDTA, VARIANTS RP SER-242 AND SER-430, CHARACTERIZATION OF VARIANT TIDTA 363-TRP--PRO-368 RP DELINS CYS, CHARACTERIZATION OF VARIANTS SER-242 AND SER-430, AND RP CHARACTERIZATION OF VARIANT TIDAND TRP-320. RX PubMed=31566583; DOI=10.1172/jci127565; RA Du Q., Huynh L.K., Coskun F., Molina E., King M.A., Raj P., Khan S., RA Dozmorov I., Seroogy C.M., Wysocki C.A., Padron G.T., Yates T.R., RA Markert M.L., de la Morena M.T., van Oers N.S.; RT "FOXN1 compound heterozygous mutations cause selective thymic hypoplasia in RT humans."; RL J. Clin. Invest. 129:4724-4738(2019). CC -!- FUNCTION: Transcriptional regulator which regulates the development, CC differentiation, and function of thymic epithelial cells (TECs) both in CC the prenatal and postnatal thymus. Acts as a master regulator of the CC TECs lineage development and is required from the onset of CC differentiation in progenitor TECs in the developing fetus to the final CC differentiation steps through which TECs mature to acquire their full CC functionality. Regulates, either directly or indirectly the expression CC of a variety of genes that mediate diverse aspects of thymus CC development and function, including MHC Class II, DLL4, CCL25, CTSL, CC CD40 and PAX1. Regulates the differentiation of the immature TECs into CC functional cortical TECs (cTECs) and medullary TECs (mTECs). Essential CC for maintenance of mTECs population in the postnatal thymus. Involved CC in the morphogenesis and maintenance of the three-dimensional thymic CC microstructure which is necessary for a fully functional thymus. Plays CC an important role in the maintenance of hematopoiesis and particularly CC T lineage progenitors within the bone marrow niche with age. Essential CC for the vascularization of the thymus anlage. Promotes the terminal CC differentiation of epithelial cells in the epidermis and hair CC follicles, partly by negatively regulating the activity of protein CC kinase C (By similarity). Plays a crucial role in the early prenatal CC stages of T-cell ontogeny (PubMed:21507891). CC {ECO:0000250|UniProtKB:Q61575, ECO:0000269|PubMed:21507891}. CC -!- INTERACTION: CC O15353; P32320: CDA; NbExp=3; IntAct=EBI-11319000, EBI-9250559; CC O15353; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-11319000, EBI-396137; CC O15353; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-11319000, EBI-9679045; CC O15353; P49639: HOXA1; NbExp=3; IntAct=EBI-11319000, EBI-740785; CC O15353; Q68G74: LHX8; NbExp=3; IntAct=EBI-11319000, EBI-8474075; CC O15353; O60336: MAPKBP1; NbExp=3; IntAct=EBI-11319000, EBI-947402; CC O15353; Q13526: PIN1; NbExp=3; IntAct=EBI-11319000, EBI-714158; CC O15353; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-11319000, EBI-11995806; CC O15353; Q08117-2: TLE5; NbExp=3; IntAct=EBI-11319000, EBI-11741437; CC O15353; Q12933: TRAF2; NbExp=3; IntAct=EBI-11319000, EBI-355744; CC O15353; O75865-2: TRAPPC6A; NbExp=3; IntAct=EBI-11319000, EBI-8451480; CC O15353; Q9BXA7: TSSK1B; NbExp=4; IntAct=EBI-11319000, EBI-6423734; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- TISSUE SPECIFICITY: Expressed in thymus. CC -!- DISEASE: T-cell immunodeficiency, congenital alopecia, and nail CC dystrophy (TIDAND) [MIM:601705]: A disorder characterized by the CC association of congenital alopecia, severe T-cell immunodeficiency, and CC ridging and pitting of all nails. {ECO:0000269|PubMed:10206641, CC ECO:0000269|PubMed:20978268, ECO:0000269|PubMed:21507891, CC ECO:0000269|PubMed:25173801, ECO:0000269|PubMed:28636882, CC ECO:0000269|PubMed:31566583}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: T-cell lymphopenia, infantile, with or without nail dystrophy, CC autosomal dominant (TLIND) [MIM:618806]: An autosomal dominant disorder CC characterized by decreased numbers of T cells, particularly cytotoxic CC CD8+ T cells, and increased susceptibility to recurrent infections, CC mainly respiratory viral infections. Additional features may include CC impaired thymic development, skin abnormalities, such as atopic CC dermatitis, and nail dystrophy. {ECO:0000269|PubMed:31447097}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- DISEASE: T-cell immunodeficiency with thymic aplasia (TIDTA) CC [MIM:242700]: An autosomal recessive disorder characterized by CC selective hypo- or aplasia of the thymus, T-cell immunodeficiency due CC to impaired T-cell development, and increased susceptibility to viral CC infections. {ECO:0000269|PubMed:31566583}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- WEB RESOURCE: Name=FOXN1base; Note=FOXN1 mutation db; CC URL="http://structure.bmc.lu.se/idbase/FOXN1base/"; 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; Y11741; CAA72417.1; -; Genomic_DNA. DR EMBL; Y11742; CAA72417.1; JOINED; Genomic_DNA. DR EMBL; Y11743; CAA72417.1; JOINED; Genomic_DNA. DR EMBL; Y11744; CAA72417.1; JOINED; Genomic_DNA. DR EMBL; Y11745; CAA72417.1; JOINED; Genomic_DNA. DR EMBL; Y11746; CAA72417.1; JOINED; Genomic_DNA. DR EMBL; Y11739; CAA72416.1; -; mRNA. DR EMBL; AK313878; BAG36604.1; -; mRNA. DR EMBL; CH471159; EAW51092.1; -; Genomic_DNA. DR CCDS; CCDS11232.1; -. DR RefSeq; NP_003584.2; NM_003593.2. DR RefSeq; XP_005258103.1; XM_005258046.3. DR PDB; 5OCN; X-ray; 2.70 A; A/B/C/D/E/F/G/H=270-366. DR PDB; 6EL8; X-ray; 1.61 A; A/D=270-366. DR PDBsum; 5OCN; -. DR PDBsum; 6EL8; -. DR AlphaFoldDB; O15353; -. DR SMR; O15353; -. DR BioGRID; 114034; 38. DR IntAct; O15353; 36. DR MINT; O15353; -. DR STRING; 9606.ENSP00000226247; -. DR iPTMnet; O15353; -. DR PhosphoSitePlus; O15353; -. DR BioMuta; FOXN1; -. DR jPOST; O15353; -. DR MassIVE; O15353; -. DR MaxQB; O15353; -. DR PaxDb; 9606-ENSP00000226247; -. DR PeptideAtlas; O15353; -. DR ProteomicsDB; 48606; -. DR Antibodypedia; 14085; 319 antibodies from 36 providers. DR DNASU; 8456; -. DR Ensembl; ENST00000226247.2; ENSP00000226247.2; ENSG00000109101.8. DR Ensembl; ENST00000577936.2; ENSP00000462159.2; ENSG00000109101.8. DR Ensembl; ENST00000579795.6; ENSP00000464645.1; ENSG00000109101.8. DR GeneID; 8456; -. DR KEGG; hsa:8456; -. DR MANE-Select; ENST00000579795.6; ENSP00000464645.1; NM_001369369.1; NP_001356298.1. DR UCSC; uc002hbj.4; human. DR AGR; HGNC:12765; -. DR CTD; 8456; -. DR DisGeNET; 8456; -. DR GeneCards; FOXN1; -. DR HGNC; HGNC:12765; FOXN1. DR HPA; ENSG00000109101; Tissue enhanced (esophagus, skin, vagina). DR MalaCards; FOXN1; -. DR MIM; 242700; phenotype. DR MIM; 600838; gene. DR MIM; 601705; phenotype. DR MIM; 618806; phenotype. DR neXtProt; NX_O15353; -. DR OpenTargets; ENSG00000109101; -. DR Orphanet; 169095; Severe combined immunodeficiency due to FOXN1 deficiency. DR PharmGKB; PA37368; -. DR VEuPathDB; HostDB:ENSG00000109101; -. DR eggNOG; KOG2294; Eukaryota. DR GeneTree; ENSGT00940000158029; -. DR HOGENOM; CLU_031768_1_0_1; -. DR InParanoid; O15353; -. DR OMA; SHSLCEP; -. DR OrthoDB; 5385885at2759; -. DR PhylomeDB; O15353; -. DR TreeFam; TF329867; -. DR PathwayCommons; O15353; -. DR SignaLink; O15353; -. DR SIGNOR; O15353; -. DR BioGRID-ORCS; 8456; 15 hits in 1169 CRISPR screens. DR ChiTaRS; FOXN1; human. DR GeneWiki; FOXN1; -. DR GenomeRNAi; 8456; -. DR Pharos; O15353; Tbio. DR PRO; PR:O15353; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; O15353; Protein. DR Bgee; ENSG00000109101; Expressed in gingival epithelium and 58 other cell types or tissues. DR ExpressionAtlas; O15353; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IBA:GO_Central. DR GO; GO:0009887; P:animal organ morphogenesis; TAS:ProtInc. DR GO; GO:0048514; P:blood vessel morphogenesis; IEA:Ensembl. DR GO; GO:0006952; P:defense response; TAS:ProtInc. DR GO; GO:0008544; P:epidermis development; TAS:ProtInc. DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl. DR GO; GO:0030216; P:keratinocyte differentiation; IEA:Ensembl. DR GO; GO:0097535; P:lymphoid lineage cell migration into thymus; IEA:Ensembl. DR GO; GO:0035878; P:nail development; IEA:Ensembl. DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IDA:BHF-UCL. DR GO; GO:0051798; P:positive regulation of hair follicle development; IEA:Ensembl. DR GO; GO:1902232; P:regulation of positive thymic T cell selection; IEA:Ensembl. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0043029; P:T cell homeostasis; IEA:Ensembl. DR GO; GO:0002360; P:T cell lineage commitment; IEA:Ensembl. DR GO; GO:0097536; P:thymus epithelium morphogenesis; IEA:Ensembl. DR CDD; cd20056; FH_FOXN1; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR047401; FH_FOXN1. DR InterPro; IPR001766; Fork_head_dom. DR InterPro; IPR049624; FOXN1_4. DR InterPro; IPR030456; TF_fork_head_CS_2. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR InterPro; IPR036390; WH_DNA-bd_sf. DR PANTHER; PTHR46721; FORKHEAD BOX PROTEIN N1; 1. DR PANTHER; PTHR46721:SF1; FORKHEAD BOX PROTEIN N1; 1. DR Pfam; PF00250; Forkhead; 1. DR PRINTS; PR00053; FORKHEAD. DR SMART; SM00339; FH; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1. DR PROSITE; PS00658; FORK_HEAD_2; 1. DR PROSITE; PS50039; FORK_HEAD_3; 1. DR Genevisible; O15353; HS. PE 1: Evidence at protein level; KW 3D-structure; Developmental protein; Differentiation; Disease variant; KW DNA-binding; Hypotrichosis; Nucleus; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..648 FT /note="Forkhead box protein N1" FT /id="PRO_0000091866" FT DNA_BIND 271..367 FT /note="Fork-head" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00089" FT REGION 1..105 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 392..445 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 458..508 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 623..648 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 42..56 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 405..435 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 69 FT /note="R -> C (in dbSNP:rs2071587)" FT /id="VAR_020025" FT VARIANT 169 FT /note="E -> K (in TLIND; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31447097" FT /id="VAR_083857" FT VARIANT 242 FT /note="P -> S (does not affect transcriptional activity as FT shown by a transcriptional reporter assay; FT dbSNP:rs140921495)" FT /evidence="ECO:0000269|PubMed:31566583" FT /id="VAR_083858" FT VARIANT 255..648 FT /note="Missing (in TIDAND and TLIND)" FT /evidence="ECO:0000269|PubMed:10206641, FT ECO:0000269|PubMed:20978268, ECO:0000269|PubMed:21507891, FT ECO:0000269|PubMed:28636882, ECO:0000269|PubMed:31447097" FT /id="VAR_083859" FT VARIANT 283 FT /note="A -> V" FT /evidence="ECO:0000269|PubMed:9321431" FT /id="VAR_010376" FT VARIANT 320 FT /note="R -> W (in TIDAND and TLIND; severely reduced FT transcriptional activity as shown by a transcriptional FT reporter assay; dbSNP:rs1288977950)" FT /evidence="ECO:0000269|PubMed:20978268, FT ECO:0000269|PubMed:31447097, ECO:0000269|PubMed:31566583" FT /id="VAR_083860" FT VARIANT 321 FT /note="H -> N (in TLIND; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31447097" FT /id="VAR_083861" FT VARIANT 325 FT /note="L -> P (in TLIND; uncertain significance)" FT /evidence="ECO:0000269|PubMed:31447097" FT /id="VAR_083862" FT VARIANT 363..368 FT /note="WKRKDP -> C (in TIDTA; decreased transcriptional FT activity as shown by a transcriptional reporter assay)" FT /evidence="ECO:0000269|PubMed:31566583" FT /id="VAR_083863" FT VARIANT 411 FT /note="R -> W (in dbSNP:rs2286520)" FT /id="VAR_021843" FT VARIANT 430 FT /note="P -> S (does not affect transcriptional activity as FT shown by a transcriptional reporter assay; FT dbSNP:rs61749867)" FT /evidence="ECO:0000269|PubMed:31566583" FT /id="VAR_083864" FT VARIANT 474..648 FT /note="Missing (in TLIND)" FT /evidence="ECO:0000269|PubMed:31447097" FT /id="VAR_083865" FT VARIANT 599 FT /note="A -> P (in dbSNP:rs532648)" FT /id="VAR_020026" FT HELIX 276..285 FT /evidence="ECO:0007829|PDB:6EL8" FT STRAND 287..293 FT /evidence="ECO:0007829|PDB:6EL8" FT HELIX 294..304 FT /evidence="ECO:0007829|PDB:6EL8" FT HELIX 307..310 FT /evidence="ECO:0007829|PDB:6EL8" FT HELIX 315..325 FT /evidence="ECO:0007829|PDB:6EL8" FT STRAND 329..332 FT /evidence="ECO:0007829|PDB:6EL8" FT STRAND 345..348 FT /evidence="ECO:0007829|PDB:6EL8" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:6EL8" FT HELIX 353..360 FT /evidence="ECO:0007829|PDB:6EL8" SQ SEQUENCE 648 AA; 68925 MW; F32F4C95627E60DE CRC64; MVSLPPPQSD VTLPGPTRLE GERQGDLMQA PGLPGSPAPQ SKHAGFSCSS FVSDGPPERT PSLPPHSPRI ASPGPEQVQG HCPAGPGPGP FRLSPSDKYP GFGFEEAAAS SPGRFLKGSH APFHPYKRPF HEDVFPEAET TLALKGHSFK TPGPLEAFEE IPVDVAEAEA FLPGFSAEAW CNGLPYPSQE HGPQVLGSEV KVKPPVLESG AGMFCYQPPL QHMYCSSQPP FHQYSPGGGS YPIPYLGSSH YQYQRMAPQA STDGHQPLFP KPIYSYSILI FMALKNSKTG SLPVSEIYNF MTEHFPYFKT APDGWKNSVR HNLSLNKCFE KVENKSGSSS RKGCLWALNP AKIDKMQEEL QKWKRKDPIA VRKSMAKPEE LDSLIGDKRE KLGSPLLGCP PPGLSGSGPI RPLAPPAGLS PPLHSLHPAP GPIPGKNPLQ DLLMGHTPSC YGQTYLHLSP GLAPPGPPQP LFPQPDGHLE LRAQPGTPQD SPLPAHTPPS HSAKLLAEPS PARTMHDTLL PDGDLGTDLD AINPSLTDFD FQGNLWEQLK DDSLALDPLV LVTSSPTSSS MPPPQPPPHC FPPGPCLTET GSGAGDLAAP GSGGSGALGD LHLTTLYSAF MELEPTPPTA PAGPSVYLSP SSKPVALA //