FER3L_HUMAN
ID FER3L_HUMAN Reviewed; 166 AA.
AC Q96RJ6; Q495K0;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Fer3-like protein;
DE AltName: Full=Basic helix-loop-helix protein N-twist;
DE AltName: Full=Class A basic helix-loop-helix protein 31;
DE Short=bHLHa31;
DE AltName: Full=Nephew of atonal 3;
DE AltName: Full=Neuronal twist;
GN Name=FERD3L; Synonyms=BHLHA31, NATO3, NTWIST;
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=11472856; DOI=10.1016/s0925-4773(01)00437-3;
RA Segev E., Halachmi N., Salzberg A., Ben-Arie N.;
RT "Nato3 is an evolutionarily conserved bHLH transcription factor expressed
RT in the CNS of Drosophila and mouse.";
RL Mech. Dev. 106:197-202(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12217327; DOI=10.1006/dbio.2002.0753;
RA Verzi M.P., Anderson J.P., Dodou E., Kelly K.K., Greene S.B., North B.J.,
RA Cripps R.M., Black B.L.;
RT "N-twist, an evolutionarily conserved bHLH protein expressed in the
RT developing CNS, functions as a transcriptional inhibitor.";
RL Dev. Biol. 249:174-190(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 VARIANT [LARGE SCALE ANALYSIS] ARG-36.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Transcription factor that binds to the E-box and functions as
CC inhibitor of transcription. DNA binding requires dimerization with an E
CC protein. Inhibits transcription activation by ASCL1/MASH1 by
CC sequestering E proteins (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer with TCF3/E12. Interacts with the bHLH domain of
CC TCF3/E12 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q96RJ6; Q8IZU0: FAM9B; NbExp=4; IntAct=EBI-10183007, EBI-10175124;
CC Q96RJ6; O15481: MAGEB4; NbExp=3; IntAct=EBI-10183007, EBI-751857;
CC Q96RJ6; O43765: SGTA; NbExp=3; IntAct=EBI-10183007, EBI-347996;
CC Q96RJ6; P15884: TCF4; NbExp=4; IntAct=EBI-10183007, EBI-533224;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
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DR EMBL; AF369897; AAK72956.1; -; Genomic_DNA.
DR EMBL; AF517122; AAN04086.1; -; mRNA.
DR EMBL; CH236948; EAL24278.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93712.1; -; Genomic_DNA.
DR EMBL; BC069147; AAH69147.1; -; mRNA.
DR EMBL; BC101135; AAI01136.1; -; mRNA.
DR EMBL; BC101136; AAI01137.1; -; mRNA.
DR EMBL; BC101137; AAI01138.1; -; mRNA.
DR EMBL; BC101138; AAI01139.1; -; mRNA.
DR CCDS; CCDS5368.1; -.
DR RefSeq; NP_690862.1; NM_152898.2.
DR AlphaFoldDB; Q96RJ6; -.
DR SMR; Q96RJ6; -.
DR BioGRID; 128819; 16.
DR IntAct; Q96RJ6; 11.
DR STRING; 9606.ENSP00000275461; -.
DR PhosphoSitePlus; Q96RJ6; -.
DR BioMuta; FERD3L; -.
DR DMDM; 74752106; -.
DR MassIVE; Q96RJ6; -.
DR PaxDb; Q96RJ6; -.
DR PeptideAtlas; Q96RJ6; -.
DR PRIDE; Q96RJ6; -.
DR Antibodypedia; 11904; 87 antibodies from 20 providers.
DR DNASU; 222894; -.
DR Ensembl; ENST00000275461.3; ENSP00000275461.3; ENSG00000146618.3.
DR GeneID; 222894; -.
DR KEGG; hsa:222894; -.
DR MANE-Select; ENST00000275461.3; ENSP00000275461.3; NM_152898.2; NP_690862.1.
DR UCSC; uc003suo.1; human.
DR CTD; 222894; -.
DR DisGeNET; 222894; -.
DR GeneCards; FERD3L; -.
DR HGNC; HGNC:16660; FERD3L.
DR HPA; ENSG00000146618; Tissue enriched (brain).
DR MIM; 617578; gene.
DR neXtProt; NX_Q96RJ6; -.
DR OpenTargets; ENSG00000146618; -.
DR PharmGKB; PA134973730; -.
DR VEuPathDB; HostDB:ENSG00000146618; -.
DR eggNOG; KOG4029; Eukaryota.
DR GeneTree; ENSGT00940000161409; -.
DR HOGENOM; CLU_148882_0_0_1; -.
DR InParanoid; Q96RJ6; -.
DR OMA; LDGCSRQ; -.
DR OrthoDB; 1513995at2759; -.
DR PhylomeDB; Q96RJ6; -.
DR PathwayCommons; Q96RJ6; -.
DR SignaLink; Q96RJ6; -.
DR BioGRID-ORCS; 222894; 10 hits in 1087 CRISPR screens.
DR GenomeRNAi; 222894; -.
DR Pharos; Q96RJ6; Tbio.
DR PRO; PR:Q96RJ6; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96RJ6; protein.
DR Bgee; ENSG00000146618; Expressed in sural nerve and 23 other tissues.
DR Genevisible; Q96RJ6; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0048468; P:cell development; IEA:Ensembl.
DR GO; GO:0032502; P:developmental process; IBA:GO_Central.
DR GO; GO:0033504; P:floor plate development; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1904338; P:regulation of dopaminergic neuron differentiation; IEA:Ensembl.
DR GO; GO:0050767; P:regulation of neurogenesis; IEA:Ensembl.
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 Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..166
FT /note="Fer3-like protein"
FT /id="PRO_0000328682"
FT DOMAIN 101..153
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 57..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..80
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 36
FT /note="G -> R (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs775679607)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_042439"
FT CONFLICT 74
FT /note="G -> GE (in Ref. 5; AAI01136/AAI01137)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 166 AA; 19017 MW; 206F6EDE1F54C79C CRC64;
MAAYPESCVD TTVLDFVADL SLASPRRPLL CDFAPGVSLG DPALALREGR PRRMARFEEG
DPEEEECEVD QGDGEEEEEE ERGRGVSLLG RPKRKRVITY AQRQAANIRE RKRMFNLNEA
FDQLRRKVPT FAYEKRLSRI ETLRLAIVYI SFMTELLESC EKKESG
