GenomeNet

Database: UniProt
Entry: Q9UMQ3
LinkDB: Q9UMQ3
Original site: Q9UMQ3 
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   27-MAR-2024, entry version 192.
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; 9606-ENSP00000281437; -.
DR   PeptideAtlas; Q9UMQ3; -.
DR   ProteomicsDB; 85192; -.
DR   Antibodypedia; 19208; 104 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   AGR; HGNC:956; -.
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; AQEPKAH; -.
DR   OrthoDB; 4204245at2759; -.
DR   PhylomeDB; Q9UMQ3; -.
DR   TreeFam; TF350735; -.
DR   PathwayCommons; Q9UMQ3; -.
DR   SignaLink; Q9UMQ3; -.
DR   BioGRID-ORCS; 8538; 11 hits in 1171 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 118 other cell types or 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   Gene3D; 1.10.10.60; Homeodomain-like; 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   PANTHER; PTHR24333:SF14; BARX HOMEOBOX 2; 1.
DR   PANTHER; PTHR24333; HOMEO BOX HB9 LIKE A-RELATED; 1.
DR   Pfam; PF00046; Homeodomain; 1.
DR   PRINTS; PR00024; HOMEOBOX.
DR   PRINTS; PR00031; HTHREPRESSR.
DR   SMART; SM00389; HOX; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 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
//
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