ID FA50A_HUMAN Reviewed; 339 AA. AC Q14320; A8KAQ4; B2R997; Q5HY37; Q6PJH5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 27-MAR-2024, entry version 174. DE RecName: Full=Protein FAM50A; DE AltName: Full=Protein HXC-26; DE AltName: Full=Protein XAP-5; GN Name=FAM50A; Synonyms=DXS9928E, HXC26, XAP5; 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], AND TISSUE SPECIFICITY. RX PubMed=9339379; DOI=10.1006/geno.1997.4912; RA Mazzarella R., Pengue G., Yoon J., Jones J., Schlessinger D.; RT "Differential expression of XAP5, a candidate disease gene."; RL Genomics 45:216-219(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C., RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., RA Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Colon, and Placenta; 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 [GENOMIC DNA / MRNA] OF 15-339. RC TISSUE=Skeletal muscle; RX PubMed=9039504; DOI=10.1093/dnares/3.5.337; RA Toyoda A., Sakai T., Sugiyama Y., Kusuda J., Hashimoto K., Maeda H.; RT "Isolation and analysis of a novel gene, HXC-26, adjacent to the rab GDP RT dissociation inhibitor gene located at human chromosome Xq28 region."; RL DNA Res. 3:337-340(1996). RN [7] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 66-339. RX PubMed=8733135; DOI=10.1093/hmg/5.5.659; RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., Zuo L., RA Heiner C., Burough F.W., Ripetto M., Schlessinger D., D'Urso M.; RT "Long-range sequence analysis in Xq28: thirteen known and six candidate RT genes in 219.4 kb of high GC DNA between the RCP/GCP and G6PD loci."; RL Hum. Mol. Genet. 5:659-668(1996). RN [8] RP PROTEIN SEQUENCE OF 159-170, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Fetal brain cortex; RA Lubec G., Chen W.-Q., Sun Y.; RL Submitted (DEC-2008) to UniProtKB. RN [9] 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 [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-100, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [12] RP FUNCTION, INTERACTION WITH EFTUD2 AND DDX41, TISSUE SPECIFICITY, RP SUBCELLULAR LOCATION, INVOLVEMENT IN MRXSA, VARIANTS MRXSA GLY-206; RP GLY-254; ASN-255; GLY-255 AND TRP-273, CHARACTERIZATION OF VARIANTS MRXSA RP GLY-206; GLY-254; ASN-255; GLY-255 AND TRP-273, AND CHARACTERIZATION OF RP VARIANTS VAL-137 AND LYS-143. RX PubMed=32703943; DOI=10.1038/s41467-020-17452-6; RA Lee Y.R., Khan K., Armfield-Uhas K., Srikanth S., Thompson N.A., Pardo M., RA Yu L., Norris J.W., Peng Y., Gripp K.W., Aleck K.A., Li C., Spence E., RA Choi T.I., Kwon S.J., Park H.M., Yu D., Do Heo W., Mooney M.R., Baig S.M., RA Wentzensen I.M., Telegrafi A., McWalter K., Moreland T., Roadhouse C., RA Ramsey K., Lyons M.J., Skinner C., Alexov E., Katsanis N., Stevenson R.E., RA Choudhary J.S., Adams D.J., Kim C.H., Davis E.E., Schwartz C.E.; RT "Mutations in FAM50A suggest that Armfield XLID syndrome is a RT spliceosomopathy."; RL Nat. Commun. 11:3698-3698(2020). CC -!- FUNCTION: Probably involved in the regulation of pre-mRNA splicing. CC {ECO:0000269|PubMed:32703943}. CC -!- SUBUNIT: Interacts with EFTUD2, a component of the spliceosome U5 CC complex (PubMed:32703943). Interacts with DDX41, a component of the CC spliceosome C complex (PubMed:32703943). {ECO:0000269|PubMed:32703943}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:32703943}. CC -!- TISSUE SPECIFICITY: Widely expressed in fetal and adult tissues. Mostly CC abundant in fetal brain, liver and kidney; in the adult, high levels CC were also observed in heart, skeletal muscle, spleen, thymus, prostate CC and small intestine. Expressed in fetal cerebellum and hypothalamus. CC Low expression is observed in fetal temporal lobe (PubMed:32703943). CC {ECO:0000269|PubMed:32703943, ECO:0000269|PubMed:9339379}. CC -!- DISEASE: Intellectual developmental disorder, X-linked, syndromic, CC Armfield type (MRXSA) [MIM:300261]: An X-linked recessive disorder CC characterized by global developmental delay with impaired intellectual CC development, walking difficulties and poor or absent speech. Affected CC individuals display a distinctive phenotype characterized by postnatal CC growth retardation, variable head circumference with a prominent CC forehead and dysmorphic facial features, ocular abnormalities, and CC seizures. {ECO:0000269|PubMed:32703943}. Note=The disease is caused by CC variants affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the FAM50 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AD001530; AAB81663.1; -; mRNA. DR EMBL; AK293119; BAF85808.1; -; mRNA. DR EMBL; AK313697; BAG36444.1; -; mRNA. DR EMBL; BX936365; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471172; EAW72708.1; -; Genomic_DNA. DR EMBL; BC000028; AAH00028.1; -; mRNA. DR EMBL; BC015499; AAH15499.1; -; mRNA. DR EMBL; D83389; BAA11907.1; -; Genomic_DNA. DR EMBL; D83260; BAA11871.1; -; mRNA. DR EMBL; L44140; AAA92649.1; -; Genomic_DNA. DR CCDS; CCDS14751.1; -. DR PIR; JC5276; JC5276. DR RefSeq; NP_004690.1; NM_004699.3. DR PDB; 8C6J; EM; 2.80 A; CF=1-339. DR PDBsum; 8C6J; -. DR AlphaFoldDB; Q14320; -. DR EMDB; EMD-16452; -. DR SMR; Q14320; -. DR BioGRID; 114578; 111. DR IntAct; Q14320; 7. DR MINT; Q14320; -. DR STRING; 9606.ENSP00000377225; -. DR GlyGen; Q14320; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q14320; -. DR MetOSite; Q14320; -. DR PhosphoSitePlus; Q14320; -. DR BioMuta; FAM50A; -. DR DMDM; 12231058; -. DR EPD; Q14320; -. DR jPOST; Q14320; -. DR MassIVE; Q14320; -. DR MaxQB; Q14320; -. DR PaxDb; 9606-ENSP00000377225; -. DR PeptideAtlas; Q14320; -. DR ProteomicsDB; 59964; -. DR Pumba; Q14320; -. DR Antibodypedia; 488; 216 antibodies from 29 providers. DR DNASU; 9130; -. DR Ensembl; ENST00000393600.8; ENSP00000377225.3; ENSG00000071859.15. DR GeneID; 9130; -. DR KEGG; hsa:9130; -. DR MANE-Select; ENST00000393600.8; ENSP00000377225.3; NM_004699.4; NP_004690.1. DR UCSC; uc004fll.4; human. DR AGR; HGNC:18786; -. DR CTD; 9130; -. DR DisGeNET; 9130; -. DR GeneCards; FAM50A; -. DR HGNC; HGNC:18786; FAM50A. DR HPA; ENSG00000071859; Low tissue specificity. DR MalaCards; FAM50A; -. DR MIM; 300261; phenotype. DR MIM; 300453; gene. DR neXtProt; NX_Q14320; -. DR OpenTargets; ENSG00000071859; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA134984709; -. DR VEuPathDB; HostDB:ENSG00000071859; -. DR eggNOG; KOG2894; Eukaryota. DR GeneTree; ENSGT00390000004735; -. DR HOGENOM; CLU_037985_1_1_1; -. DR InParanoid; Q14320; -. DR OMA; DFIWVFL; -. DR OrthoDB; 1102160at2759; -. DR PhylomeDB; Q14320; -. DR TreeFam; TF314738; -. DR PathwayCommons; Q14320; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q14320; -. DR BioGRID-ORCS; 9130; 162 hits in 783 CRISPR screens. DR ChiTaRS; FAM50A; human. DR GeneWiki; FAM50A; -. DR GenomeRNAi; 9130; -. DR Pharos; Q14320; Tbio. DR PRO; PR:Q14320; -. DR Proteomes; UP000005640; Chromosome X. DR RNAct; Q14320; Protein. DR Bgee; ENSG00000071859; Expressed in sural nerve and 192 other cell types or tissues. DR ExpressionAtlas; Q14320; baseline and differential. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central. DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW. DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB. DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW. DR GO; GO:0007283; P:spermatogenesis; NAS:UniProtKB. DR InterPro; IPR048337; FAM50A/XAP5_C. DR InterPro; IPR007005; XAP5. DR PANTHER; PTHR12722:SF2; PROTEIN FAM50A; 1. DR PANTHER; PTHR12722; XAP-5 PROTEIN-RELATED; 1. DR Pfam; PF04921; XAP5; 1. DR Genevisible; Q14320; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant; KW Intellectual disability; Isopeptide bond; mRNA processing; mRNA splicing; KW Nucleus; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..339 FT /note="Protein FAM50A" FT /id="PRO_0000068284" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 121..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 152..155 FT /note="Nuclear localization signal" FT /evidence="ECO:0000255" FT COMPBIAS 14..31 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 125..143 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 144..177 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:22814378" FT CROSSLNK 100 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VARIANT 137 FT /note="A -> V (it rescues craniofacial patterning defects FT in zebrafish morphant embryos; dbSNP:rs149558328)" FT /evidence="ECO:0000269|PubMed:32703943" FT /id="VAR_084563" FT VARIANT 143 FT /note="E -> K (it rescues craniofacial patterning defects FT in zebrafish morphant embryos; dbSNP:rs782017549)" FT /evidence="ECO:0000269|PubMed:32703943" FT /id="VAR_084564" FT VARIANT 206 FT /note="W -> G (in MRXSA; uncertain significance; does not FT affect FAM50A protein levels in patient cells; does not FT affect localization to the nucleus; dbSNP:rs2068793121)" FT /evidence="ECO:0000269|PubMed:32703943" FT /id="VAR_084565" FT VARIANT 254 FT /note="E -> G (in MRXSA; hypomorphic variant; does not FT fully rescue craniofacial patterning defects in zebrafish FT morphant embryos; does not affect FAM50A protein levels in FT patient cells; does not affect localization to the nucleus; FT dbSNP:rs2068797150)" FT /evidence="ECO:0000269|PubMed:32703943" FT /id="VAR_084566" FT VARIANT 255 FT /note="D -> G (in MRXSA; hypomorphic variant; does not FT fully rescue craniofacial patterning defects in zebrafish FT morphant embryos; does not affect localization to the FT nucleus; dbSNP:rs2068797192)" FT /evidence="ECO:0000269|PubMed:32703943" FT /id="VAR_084567" FT VARIANT 255 FT /note="D -> N (in MRXSA; hypomorphic variant; does not FT fully rescue craniofacial patterning defects in zebrafish FT morphant embryos; dbSNP:rs2068797171)" FT /evidence="ECO:0000269|PubMed:32703943" FT /id="VAR_084568" FT VARIANT 273 FT /note="R -> W (in MRXSA; hypomorphic variant; does not FT fully rescue craniofacial patterning defects in zebrafish FT morphant embryos; dbSNP:rs2068798311)" FT /evidence="ECO:0000269|PubMed:32703943" FT /id="VAR_084569" FT CONFLICT 166 FT /note="F -> S (in Ref. 2; BAF85808)" FT /evidence="ECO:0000305" FT CONFLICT 330 FT /note="E -> G (in Ref. 2; BAF85808)" FT /evidence="ECO:0000305" SQ SEQUENCE 339 AA; 40242 MW; 88BCA57E49B0AA32 CRC64; MAQYKGAASE AGRAMHLMKK REKQREQMEQ MKQRIAEENI MKSNIDKKFS AHYDAVEAEL KSSTVGLVTL NDMKAKQEAL VKEREKQLAK KEQSKELQMK LEKLREKERK KEAKRKISSL SFTLEEEEEG GEEEEEAAMY EEEMEREEIT TKKRKLGKNP DVDTSFLPDR DREEEENRLR EELRQEWEAK QEKIKSEEIE ITFSYWDGSG HRRTVKMRKG NTMQQFLQKA LEILRKDFSE LRSAGVEQLM YIKEDLIIPH HHSFYDFIVT KARGKSGPLF NFDVHDDVRL LSDATVEKDE SHAGKVVLRS WYEKNKHIFP ASRWEPYDPE KKWDKYTIR //