MYCN_HUMAN
ID MYCN_HUMAN Reviewed; 464 AA.
AC P04198; Q53XS5; Q6LDT9;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 2.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=N-myc proto-oncogene protein;
DE AltName: Full=Class E basic helix-loop-helix protein 37;
DE Short=bHLHe37;
GN Name=MYCN; Synonyms=BHLHE37, NMYC;
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].
RX PubMed=2869488; DOI=10.1073/pnas.83.6.1772;
RA Stanton L.W., Schwab M., Bishop J.M.;
RT "Nucleotide sequence of the human N-myc gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 83:1772-1776(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3510398; DOI=10.1038/319073a0;
RA Kohl N.E., Legouy E., DePinho R.A., Nisen P.D., Smith R.K., Gee C.E.,
RA Alt F.W.;
RT "Human N-myc is closely related in organization and nucleotide sequence to
RT c-myc.";
RL Nature 319:73-77(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2834684;
RA Ibson J.M., Rabbitts P.H.;
RT "Sequence of a germ-line N-myc gene and amplification as a mechanism of
RT activation.";
RL Oncogene 2:399-402(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40.
RX PubMed=3437890; DOI=10.1128/mcb.7.12.4266-4272.1987;
RA Stanton L.W., Bishop J.M.;
RT "Alternative processing of RNA transcribed from NMYC.";
RL Mol. Cell. Biol. 7:4266-4272(1987).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 71-464.
RX PubMed=3008339; DOI=10.1126/science.3008339;
RA Slamon D.J., Boone T.C., Seeger R.C., Keith D.E., Chazin V., Lee H.C.,
RA Souza L.M.;
RT "Identification and characterization of the protein encoded by the human N-
RT myc oncogene.";
RL Science 232:768-772(1986).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-464.
RX PubMed=2987858; DOI=10.1093/nar/13.7.2545;
RA Michitsch R.W., Melera P.W.;
RT "Nucleotide sequence of the 3' exon of the human N-myc gene.";
RL Nucleic Acids Res. 13:2545-2558(1985).
RN [11]
RP PHOSPHORYLATION AT SER-261 AND SER-263 BY CK2.
RX PubMed=1425701; DOI=10.1111/j.1432-1033.1992.tb17367.x;
RA Hagiwara T., Nakaya K., Nakamura Y., Nakajima H., Nishimura S., Taya Y.;
RT "Specific phosphorylation of the acidic central region of the N-myc protein
RT by casein kinase II.";
RL Eur. J. Biochem. 209:945-950(1992).
RN [12]
RP INTERACTION WITH KDM5A AND KDM5B.
RX PubMed=17311883; DOI=10.1101/gad.1523007;
RA Secombe J., Li L., Carlos L., Eisenman R.N.;
RT "The Trithorax group protein Lid is a trimethyl histone H3K4 demethylase
RT required for dMyc-induced cell growth.";
RL Genes Dev. 21:537-551(2007).
RN [13]
RP INTERACTION WITH HUWE1.
RX PubMed=18488021; DOI=10.1038/ncb1727;
RA Zhao X., Heng J.I.-T., Guardavaccaro D., Jiang R., Pagano M., Guillemot F.,
RA Iavarone A., Lasorella A.;
RT "The HECT-domain ubiquitin ligase Huwe1 controls neural differentiation and
RT proliferation by destabilizing the N-Myc oncoprotein.";
RL Nat. Cell Biol. 10:643-653(2008).
RN [14]
RP FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH NCYM, AND PHOSPHORYLATION.
RX PubMed=24391509; DOI=10.1371/journal.pgen.1003996;
RA Suenaga Y., Islam S.M., Alagu J., Kaneko Y., Kato M., Tanaka Y., Kawana H.,
RA Hossain S., Matsumoto D., Yamamoto M., Shoji W., Itami M., Shibata T.,
RA Nakamura Y., Ohira M., Haraguchi S., Takatori A., Nakagawara A.;
RT "NCYM, a Cis-antisense gene of MYCN, encodes a de novo evolved protein that
RT inhibits GSK3beta resulting in the stabilization of MYCN in human
RT neuroblastomas.";
RL PLoS Genet. 10:E1003996-E1003996(2014).
RN [15]
RP 9AATAD MOTIF.
RX PubMed=34342803; DOI=10.1007/s12015-021-10225-8;
RA Piskacek M., Otasevic T., Repko M., Knight A.;
RT "The 9aaTAD Activation Domains in the Yamanaka Transcription Factors Oct4,
RT Sox2, Myc, and Klf4.";
RL Stem. Cell. Rev. Rep. 17:1934-1936(2021).
RN [16] {ECO:0007744|PDB:5G1X}
RP X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS) OF 28-89 IN COMPLEX WITH AURKA,
RP INTERACTION WITH AURKA AND FBXW7, MUTAGENESIS OF PHE-28; TYR-29; PHE-35;
RP TYR-36; 52-LYS--LEU-56; GLU-73; TRP-77 AND TRP-88, REGION, AND
RP PHOSPHORYLATION.
RX PubMed=27837025; DOI=10.1073/pnas.1610626113;
RA Richards M.W., Burgess S.G., Poon E., Carstensen A., Eilers M., Chesler L.,
RA Bayliss R.;
RT "Structural basis of N-Myc binding by Aurora-A and its destabilization by
RT kinase inhibitors.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:13726-13731(2016).
RN [17]
RP VARIANTS FGLDS1 HIS-393; SER-393 AND HIS-394.
RX PubMed=15821734; DOI=10.1038/ng1546;
RA van Bokhoven H., Celli J., van Reeuwijk J., Rinne T., Glaudemans B.,
RA van Beusekom E., Rieu P., Newbury-Ecob R.A., Chiang C., Brunner H.G.;
RT "MYCN haploinsufficiency is associated with reduced brain size and
RT intestinal atresias in Feingold syndrome.";
RL Nat. Genet. 37:465-467(2005).
RN [18]
RP INVOLVEMENT IN FGLDS1.
RX PubMed=16906565; DOI=10.1002/ajmg.a.31407;
RA Teszas A., Meijer R., Scheffer H., Gyuris P., Kosztolanyi G.,
RA van Bokhoven H., Kellermayer R.;
RT "Expanding the clinical spectrum of MYCN-related Feingold syndrome.";
RL Am. J. Med. Genet. A 140:2254-2256(2006).
CC -!- FUNCTION: Positively regulates the transcription of MYCNOS in
CC neuroblastoma cells. {ECO:0000269|PubMed:24391509}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Binds DNA as a heterodimer with MAX. Interacts with KDM5A,
CC KDM5B and HUWE1. Interacts with MYCNOS. Interacts with AURKA;
CC interaction is phospho-independent and triggers AURKA activation; AURKA
CC competes with FBXW7 for binding to unphosphorylated MYCN but not for
CC binding to unphosphorylated MYCN (PubMed:27837025). Interacts with
CC FBXW7; FBXW7 competes with AURKA for binding to unphosphorylated MYCN
CC but not for binding to phosphorylated MYCN (PubMed:27837025).
CC {ECO:0000269|PubMed:17311883, ECO:0000269|PubMed:18488021,
CC ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:27837025}.
CC -!- INTERACTION:
CC P04198; O14965: AURKA; NbExp=12; IntAct=EBI-878369, EBI-448680;
CC P04198; Q8N726: CDKN2A; NbExp=3; IntAct=EBI-878369, EBI-625922;
CC P04198; P61244: MAX; NbExp=10; IntAct=EBI-878369, EBI-751711;
CC P04198; Q13287: NMI; NbExp=3; IntAct=EBI-878369, EBI-372942;
CC P04198; Q96EB6: SIRT1; NbExp=3; IntAct=EBI-878369, EBI-1802965;
CC P04198; Q13105: ZBTB17; NbExp=3; IntAct=EBI-878369, EBI-372156;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed in the neuronal cells of the cerebrum,
CC neuroblastomas and thyroid tumors (at protein level).
CC {ECO:0000269|PubMed:24391509}.
CC -!- DEVELOPMENTAL STAGE: Expressed during fetal development.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:34342803}.
CC -!- PTM: Phosphorylated by GSK3-beta which may promote its degradation
CC (PubMed:24391509). Phosphorylated by AURKA (PubMed:27837025).
CC {ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:27837025}.
CC -!- DISEASE: Note=Amplification of the N-MYC gene is associated with a
CC variety of human tumors, most frequently neuroblastoma, where the level
CC of amplification appears to increase as the tumor progresses.
CC {ECO:0000269|PubMed:2834684}.
CC -!- DISEASE: Feingold syndrome 1 (FGLDS1) [MIM:164280]: A syndrome
CC characterized by variable combinations of esophageal and duodenal
CC atresias, microcephaly, learning disability, intellectual disability,
CC and limb malformations. Hand and foot abnormalities may include
CC hypoplastic thumbs, clinodactyly of second and fifth fingers,
CC syndactyly (characteristically between second and third and fourth and
CC fifth toes), and shortened or absent middle phalanges. Cardiac and
CC renal malformations, vertebral anomalies, and deafness have also been
CC described. {ECO:0000269|PubMed:15821734, ECO:0000269|PubMed:16906565}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA36371.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA68678.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/NMYCID112.html";
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DR EMBL; X03294; CAA27037.1; -; Genomic_DNA.
DR EMBL; X03295; CAA27038.1; -; Genomic_DNA.
DR EMBL; M13241; AAA36371.1; ALT_INIT; Genomic_DNA.
DR EMBL; M13228; AAA36370.1; -; Genomic_DNA.
DR EMBL; BT007384; AAP36048.1; -; mRNA.
DR EMBL; AC010145; AAY14952.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00885.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00886.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00887.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00888.1; -; Genomic_DNA.
DR EMBL; BC002712; AAH02712.1; -; mRNA.
DR EMBL; M18090; AAA59885.1; -; Genomic_DNA.
DR EMBL; X02363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Y00664; CAA68678.1; ALT_INIT; Genomic_DNA.
DR CCDS; CCDS1687.1; -.
DR PIR; A01355; TVHUMC.
DR PIR; A25744; TVHUM2.
DR RefSeq; NP_001280157.1; NM_001293228.1.
DR RefSeq; NP_001280160.1; NM_001293231.1.
DR RefSeq; NP_001280162.1; NM_001293233.1.
DR RefSeq; NP_005369.2; NM_005378.5.
DR RefSeq; XP_016859657.1; XM_017004168.1.
DR PDB; 5G1X; X-ray; 1.72 A; B=28-89.
DR PDBsum; 5G1X; -.
DR AlphaFoldDB; P04198; -.
DR SMR; P04198; -.
DR BioGRID; 110698; 64.
DR DIP; DIP-36822N; -.
DR IntAct; P04198; 17.
DR MINT; P04198; -.
DR STRING; 9606.ENSP00000281043; -.
DR ChEMBL; CHEMBL4523165; -.
DR iPTMnet; P04198; -.
DR PhosphoSitePlus; P04198; -.
DR BioMuta; MYCN; -.
DR DMDM; 127604; -.
DR EPD; P04198; -.
DR jPOST; P04198; -.
DR MassIVE; P04198; -.
DR PaxDb; P04198; -.
DR PeptideAtlas; P04198; -.
DR PRIDE; P04198; -.
DR ProteomicsDB; 51676; -.
DR Antibodypedia; 12867; 392 antibodies from 38 providers.
DR DNASU; 4613; -.
DR Ensembl; ENST00000281043.4; ENSP00000281043.3; ENSG00000134323.12.
DR GeneID; 4613; -.
DR KEGG; hsa:4613; -.
DR MANE-Select; ENST00000281043.4; ENSP00000281043.3; NM_005378.6; NP_005369.2.
DR UCSC; uc002rci.4; human.
DR CTD; 4613; -.
DR DisGeNET; 4613; -.
DR GeneCards; MYCN; -.
DR GeneReviews; MYCN; -.
DR HGNC; HGNC:7559; MYCN.
DR HPA; ENSG00000134323; Tissue enhanced (placenta).
DR MalaCards; MYCN; -.
DR MIM; 164280; phenotype.
DR MIM; 164840; gene.
DR neXtProt; NX_P04198; -.
DR OpenTargets; ENSG00000134323; -.
DR Orphanet; 391641; Feingold syndrome type 1.
DR Orphanet; 357027; Hereditary retinoblastoma.
DR Orphanet; 635; Neuroblastoma.
DR Orphanet; 357034; Non-hereditary retinoblastoma.
DR PharmGKB; PA31359; -.
DR VEuPathDB; HostDB:ENSG00000134323; -.
DR eggNOG; KOG2588; Eukaryota.
DR GeneTree; ENSGT00940000158432; -.
DR HOGENOM; CLU_052560_0_0_1; -.
DR InParanoid; P04198; -.
DR OMA; PFPINKR; -.
DR OrthoDB; 877891at2759; -.
DR PhylomeDB; P04198; -.
DR TreeFam; TF106001; -.
DR PathwayCommons; P04198; -.
DR Reactome; R-HSA-201556; Signaling by ALK.
DR SignaLink; P04198; -.
DR SIGNOR; P04198; -.
DR BioGRID-ORCS; 4613; 37 hits in 1103 CRISPR screens.
DR ChiTaRS; MYCN; human.
DR GeneWiki; N-Myc; -.
DR GenomeRNAi; 4613; -.
DR Pharos; P04198; Tbio.
DR PRO; PR:P04198; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P04198; protein.
DR Bgee; ENSG00000134323; Expressed in ventricular zone and 163 other tissues.
DR ExpressionAtlas; P04198; baseline and differential.
DR Genevisible; P04198; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; TAS:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-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:0010629; P:negative regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:BHF-UCL.
DR GO; GO:1903800; P:positive regulation of miRNA maturation; IC:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR002418; Tscrpt_reg_Myc.
DR InterPro; IPR012682; Tscrpt_reg_Myc_N.
DR Pfam; PF00010; HLH; 1.
DR Pfam; PF01056; Myc_N; 1.
DR PIRSF; PIRSF001705; Myc_protein; 1.
DR PRINTS; PR00044; LEUZIPPRMYC.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Disease variant; DNA-binding; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..464
FT /note="N-myc proto-oncogene protein"
FT /id="PRO_0000127323"
FT DOMAIN 381..433
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 19..47
FT /note="Interaction with AURKA"
FT /evidence="ECO:0000269|PubMed:27837025"
FT REGION 61..89
FT /note="Interaction with AURKA and FBXW7"
FT /evidence="ECO:0000269|PubMed:27837025"
FT REGION 129..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..454
FT /note="Leucine-zipper"
FT MOTIF 76..84
FT /note="9aaTAD"
FT /evidence="ECO:0000269|PubMed:34342803"
FT COMPBIAS 259..278
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..392
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 261
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1425701"
FT MOD_RES 263
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000269|PubMed:1425701"
FT VARIANT 393
FT /note="R -> H (in FGLDS1; dbSNP:rs104893646)"
FT /evidence="ECO:0000269|PubMed:15821734"
FT /id="VAR_031952"
FT VARIANT 393
FT /note="R -> S (in FGLDS1; dbSNP:rs104893647)"
FT /evidence="ECO:0000269|PubMed:15821734"
FT /id="VAR_031953"
FT VARIANT 394
FT /note="R -> H (in FGLDS1; dbSNP:rs104893648)"
FT /evidence="ECO:0000269|PubMed:15821734"
FT /id="VAR_031954"
FT MUTAGEN 28
FT /note="F->A: Reduces interaction with AURKA; when
FT associated with A-35."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 29
FT /note="Y->A: Reduces interaction with AURKA; when
FT associated with A-36."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 35
FT /note="F->A: Reduces interaction with AURKA; when
FT associated with A-28."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 36
FT /note="Y->A: Reduces interaction with AURKA; when
FT associated with A-29."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 52..56
FT /note="KFELL->AAAAA: Does not affect AURKA binding."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 73
FT /note="E->K: Reduces binding to AURKA."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 77
FT /note="W->A: Reduces binding to AURKA."
FT /evidence="ECO:0000269|PubMed:27837025"
FT MUTAGEN 88
FT /note="W->A: Abrogates the interaction with AURKA."
FT /evidence="ECO:0000269|PubMed:27837025"
FT CONFLICT 227
FT /note="A -> P (in Ref. 2; CAA27037)"
FT /evidence="ECO:0000305"
FT CONFLICT 363
FT /note="I -> V (in Ref. 3; CAA68678)"
FT /evidence="ECO:0000305"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5G1X"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:5G1X"
SQ SEQUENCE 464 AA; 49561 MW; 560E885602E30DAD CRC64;
MPSCSTSTMP GMICKNPDLE FDSLQPCFYP DEDDFYFGGP DSTPPGEDIW KKFELLPTPP
LSPSRGFAEH SSEPPSWVTE MLLENELWGS PAEEDAFGLG GLGGLTPNPV ILQDCMWSGF
SAREKLERAV SEKLQHGRGP PTAGSTAQSP GAGAASPAGR GHGGAAGAGR AGAALPAELA
HPAAECVDPA VVFPFPVNKR EPAPVPAAPA SAPAAGPAVA SGAGIAAPAG APGVAPPRPG
GRQTSGGDHK ALSTSGEDTL SDSDDEDDEE EDEEEEIDVV TVEKRRSSSN TKAVTTFTIT
VRPKNAALGP GRAQSSELIL KRCLPIHQQH NYAAPSPYVE SEDAPPQKKI KSEASPRPLK
SVIPPKAKSL SPRNSDSEDS ERRRNHNILE RQRRNDLRSS FLTLRDHVPE LVKNEKAAKV
VILKKATEYV HSLQAEEHQL LLEKEKLQAR QQQLLKKIEH ARTC
