DUX4C_HUMAN
ID DUX4C_HUMAN Reviewed; 374 AA.
AC Q6RFH8;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Double homeobox protein 4C;
DE AltName: Full=Double homeobox protein 4, centromeric;
DE Short=DUX4c;
DE AltName: Full=Double homeobox protein 4-like protein 9;
GN Name=DUX4L9; Synonyms=DUX4C;
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], FUNCTION, INTERACTION WITH MYF5,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=19829708; DOI=10.1371/journal.pone.0007482;
RA Ansseau E., Laoudj-Chenivesse D., Marcowycz A., Tassin A., Vanderplanck C.,
RA Sauvage S., Barro M., Mahieu I., Leroy A., Leclercq I., Mainfroid V.,
RA Figlewicz D., Mouly V., Butler-Browne G., Belayew A., Coppee F.;
RT "DUX4c is up-regulated in FSHD. It induces the MYF5 protein and human
RT myoblast proliferation.";
RL PLoS ONE 4:E7482-E7482(2009).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=18723017; DOI=10.1016/j.expneurol.2008.07.022;
RA Bosnakovski D., Lamb S., Simsek T., Xu Z., Belayew A., Perlingeiro R.,
RA Kyba M.;
RT "DUX4c, an FSHD candidate gene, interferes with myogenic regulators and
RT abolishes myoblast differentiation.";
RL Exp. Neurol. 214:87-96(2008).
RN [4]
RP FUNCTION.
RX PubMed=24145033; DOI=10.1074/jbc.m113.504522;
RA Dmitriev P., Stankevicins L., Ansseau E., Petrov A., Barat A., Dessen P.,
RA Robert T., Turki A., Lazar V., Labourer E., Belayew A., Carnac G.,
RA Laoudj-Chenivesse D., Lipinski M., Vassetzky Y.S.;
RT "Defective regulation of microRNA target genes in myoblasts from
RT facioscapulohumeral dystrophy patients.";
RL J. Biol. Chem. 288:34989-35002(2013).
CC -!- FUNCTION: May be involved in transcriptional regulation (By
CC similarity). Down-regulates MYOD1 expression and may up-regulate MYF5
CC expression. May regulate microRNA (miRNA) transcription, up-regulating
CC the expression of some myogenic miRNAs, including MIR1-1, MIR133A2,
CC MIR133B and MIR206. Impairs the differentiation of myoblasts and may be
CC involved in muscle regeneration. {ECO:0000250,
CC ECO:0000269|PubMed:18723017, ECO:0000269|PubMed:19829708,
CC ECO:0000269|PubMed:24145033}.
CC -!- SUBUNIT: May interact with MYF5; regulates MYF5 expression.
CC -!- INTERACTION:
CC Q6RFH8; O94829: IPO13; NbExp=2; IntAct=EBI-11599882, EBI-747310;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108,
CC ECO:0000269|PubMed:19829708}.
CC -!- TISSUE SPECIFICITY: Expressed in muscles, as well as in primary
CC myoblasts and myotubes (at protein level).
CC {ECO:0000269|PubMed:19829708}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated during myoblasts differentiation (at
CC protein level). {ECO:0000269|PubMed:19829708}.
CC -!- DISEASE: Note=Up-regulated in myoblasts of facioscapulohumeral muscular
CC dystrophy (FSHD) patients (at protein level).
CC {ECO:0000269|PubMed:19829708}.
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DR EMBL; AY500824; AAS15569.1; -; Genomic_DNA.
DR EMBL; AF146191; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q6RFH8; -.
DR SMR; Q6RFH8; -.
DR IntAct; Q6RFH8; 51.
DR iPTMnet; Q6RFH8; -.
DR PhosphoSitePlus; Q6RFH8; -.
DR BioMuta; HGNC:33855; -.
DR DMDM; 74710112; -.
DR MassIVE; Q6RFH8; -.
DR PeptideAtlas; Q6RFH8; -.
DR PRIDE; Q6RFH8; -.
DR GeneCards; DUX4L9; -.
DR HGNC; HGNC:33855; DUX4L9.
DR MIM; 615581; gene.
DR neXtProt; NX_Q6RFH8; -.
DR InParanoid; Q6RFH8; -.
DR PhylomeDB; Q6RFH8; -.
DR PathwayCommons; Q6RFH8; -.
DR SignaLink; Q6RFH8; -.
DR Pharos; Q6RFH8; Tdark.
DR PRO; PR:Q6RFH8; -.
DR Proteomes; UP000005640; Unplaced.
DR RNAct; Q6RFH8; protein.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00086; homeodomain; 2.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR000047; HTH_motif.
DR Pfam; PF00046; Homeodomain; 2.
DR PRINTS; PR00031; HTHREPRESSR.
DR SMART; SM00389; HOX; 2.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 2.
PE 1: Evidence at protein level;
KW DNA-binding; Homeobox; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..374
FT /note="Double homeobox protein 4C"
FT /id="PRO_0000405256"
FT DNA_BIND 19..78
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 94..153
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 72..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..96
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 374 AA; 39442 MW; B7F4ED12BED46821 CRC64;
MALPTPSDST LPAEARGRGR RRRLVWTPSQ SEALRACFER NPYPGIATRE RLAQAIGIPE
PRVQIWFQNE RSRQLRQHRR ESRPWPGRRG PPEGRRKRTA VTGSQTALLL RAFEKDRFPG
IAAREELARE TGLPESRIQI WFQNRRARHP GQGGRAPAQA GGLCSAAPGG GHPAPSWVAF
AHTGAWGTGL PAPHVPCAPG ALPQGAFVSQ AARAAPALQP SQAAPAEGIS QPAPARGDFA
YAAPAPPDGA LSHPQAPRWP PHPGKSREDR DPQRDGLPGP CAVAQPGPAQ AGPQGQGVLA
PPTSQGSPWW GWGRGPQVAG AAWEPQAGAA PPPQPAPPDA SAASTDASHP GASQPLQEPG
RSSTVTSSLL YELL
