BARX2_HUMAN
ID BARX2_HUMAN Reviewed; 279 AA.
AC Q9UMQ3; O43518; Q6NT51;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Homeobox protein BarH-like 2;
GN Name=BARX2;
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].
RX PubMed=10854790; DOI=10.1016/s0378-1119(00)00169-4;
RA Krasner A., Wallace L., Thiagalingam A., Jones C., Lengauer C., Minahan L.,
RA Ma Y., Kalikin L., Feinberg A.P., Jabs E.W., Tunnacliffe A., Baylin S.B.,
RA Ball D.W., Nelkin B.D.;
RT "Cloning and chromosomal localization of the human BARX2 homeobox protein
RT gene.";
RL Gene 250:171-180(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10644443; DOI=10.1006/geno.1999.6037;
RA Hjalt T.A., Murray J.C.;
RT "The human BARX2 gene: genomic structure, chromosomal localization, and
RT single nucleotide polymorphisms.";
RL Genomics 62:456-459(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RA Lindon C., Goodbourn S.;
RT "Expression cloning of the human version of Barx2 as a cAMP response
RT element binding protein- (CREB)- interacting factor.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
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 [6]
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).
CC -!- FUNCTION: Transcription factor. Binds optimally to the DNA consensus
CC sequence 5'-YYTAATGRTTTTY-3'. May control the expression of neural
CC adhesion molecules such as L1 or Ng-CAM during embryonic development of
CC both the central and peripherical nervous system. May be involved in
CC controlling adhesive processes in keratinizing epithelia (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UMQ3; Q14192: FHL2; NbExp=3; IntAct=EBI-12053927, EBI-701903;
CC Q9UMQ3; Q13643: FHL3; NbExp=3; IntAct=EBI-12053927, EBI-741101;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Highly expressed in adult salivary gland and at
CC much lower levels in mammary gland, kidney and placenta.
CC -!- SIMILARITY: Belongs to the BAR homeobox family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC04705.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAC04705.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF09453.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF09453.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF031924; AAC04705.1; ALT_SEQ; mRNA.
DR EMBL; AF171222; AAF09453.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF171219; AAF09453.1; JOINED; Genomic_DNA.
DR EMBL; AF171220; AAF09453.1; JOINED; Genomic_DNA.
DR EMBL; AF171221; AAF09453.1; JOINED; Genomic_DNA.
DR EMBL; AJ243512; CAB50736.1; -; mRNA.
DR EMBL; AP003775; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471065; EAW67743.1; -; Genomic_DNA.
DR EMBL; BC069378; AAH69378.1; -; mRNA.
DR EMBL; BC111432; AAI11433.1; -; mRNA.
DR EMBL; BC111572; AAI11573.1; -; mRNA.
DR CCDS; CCDS8481.1; -.
DR RefSeq; NP_003649.2; NM_003658.4.
DR AlphaFoldDB; Q9UMQ3; -.
DR SMR; Q9UMQ3; -.
DR BioGRID; 114108; 3.
DR IntAct; Q9UMQ3; 2.
DR STRING; 9606.ENSP00000281437; -.
DR iPTMnet; Q9UMQ3; -.
DR PhosphoSitePlus; Q9UMQ3; -.
DR BioMuta; BARX2; -.
DR DMDM; 254763427; -.
DR jPOST; Q9UMQ3; -.
DR MassIVE; Q9UMQ3; -.
DR PaxDb; Q9UMQ3; -.
DR PeptideAtlas; Q9UMQ3; -.
DR PRIDE; Q9UMQ3; -.
DR ProteomicsDB; 85192; -.
DR Antibodypedia; 19208; 85 antibodies from 18 providers.
DR DNASU; 8538; -.
DR Ensembl; ENST00000281437.6; ENSP00000281437.4; ENSG00000043039.7.
DR GeneID; 8538; -.
DR KEGG; hsa:8538; -.
DR MANE-Select; ENST00000281437.6; ENSP00000281437.4; NM_003658.5; NP_003649.2.
DR UCSC; uc001qfc.5; human.
DR CTD; 8538; -.
DR DisGeNET; 8538; -.
DR GeneCards; BARX2; -.
DR HGNC; HGNC:956; BARX2.
DR HPA; ENSG00000043039; Tissue enhanced (esophagus, salivary gland, vagina).
DR MIM; 604823; gene.
DR neXtProt; NX_Q9UMQ3; -.
DR OpenTargets; ENSG00000043039; -.
DR PharmGKB; PA25260; -.
DR VEuPathDB; HostDB:ENSG00000043039; -.
DR eggNOG; KOG0488; Eukaryota.
DR GeneTree; ENSGT00940000159663; -.
DR HOGENOM; CLU_090214_0_0_1; -.
DR InParanoid; Q9UMQ3; -.
DR OMA; EIQLMGL; -.
DR OrthoDB; 1382174at2759; -.
DR PhylomeDB; Q9UMQ3; -.
DR TreeFam; TF350735; -.
DR PathwayCommons; Q9UMQ3; -.
DR SignaLink; Q9UMQ3; -.
DR BioGRID-ORCS; 8538; 10 hits in 1093 CRISPR screens.
DR ChiTaRS; BARX2; human.
DR GenomeRNAi; 8538; -.
DR Pharos; Q9UMQ3; Tbio.
DR PRO; PR:Q9UMQ3; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9UMQ3; protein.
DR Bgee; ENSG00000043039; Expressed in lower esophagus mucosa and 117 other tissues.
DR Genevisible; Q9UMQ3; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001502; P:cartilage condensation; IEA:Ensembl.
DR GO; GO:0014902; P:myotube differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR020479; Homeobox_metazoa.
DR InterPro; IPR000047; HTH_motif.
DR Pfam; PF00046; Homeodomain; 1.
DR PRINTS; PR00024; HOMEOBOX.
DR PRINTS; PR00031; HTHREPRESSR.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Homeobox; Nucleus; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..279
FT /note="Homeobox protein BarH-like 2"
FT /id="PRO_0000048838"
FT DNA_BIND 133..192
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 110..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..279
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 279 AA; 31188 MW; 8C2537E524528467 CRC64;
MHCHAELRLS SPGQLKAARR RYKTFMIDEI LSKETCDYFE KLSLYSVCPS LVVRPKPLHS
CTGSPSLRAY PLLSVITRQP TVISHLVPAT PGIAQALSCH QVTEAVSAEA PGGEALASSE
SETEQPTPRQ KKPRRSRTIF TELQLMGLEK KFQKQKYLST PDRLDLAQSL GLTQLQVKTW
YQNRRMKWKK MVLKGGQEAP TKPKGRPKKN SIPTSEEIEA EEKMNSQAQG QEQLEPSQGQ
EELCEAQEPK ARDVPLEMAE PPDPPQELPI PSSEPPPLS
