DMRT2_HUMAN
ID DMRT2_HUMAN Reviewed; 561 AA.
AC Q9Y5R5; B1ANC0; B9EGJ1; Q9NPG6; Q9NQR6;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Doublesex- and mab-3-related transcription factor 2;
DE AltName: Full=Doublesex-like 2 protein;
DE Short=DSXL-2;
GN Name=DMRT2; Synonyms=DSXL2;
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] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=10332030; DOI=10.1093/hmg/8.6.989;
RA Raymond C.S., Parker E.D., Kettlewell J.R., Brown L.G., Page D.C., Kusz K.,
RA Jaruzelska J., Reinberg Y., Flejter W.L., Bardwell V.J., Hirsch B.,
RA Zarkower D.;
RT "A region of human chromosome 9p required for testis development contains
RT two genes related to known sexual regulators.";
RL Hum. Mol. Genet. 8:989-996(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Kidney;
RX PubMed=10729224; DOI=10.1006/geno.2000.6120;
RA Ottolenghi C., Veitia R., Barbieri M., Fellous M., McElreavey K.;
RT "The human doublesex-related gene, DMRT2, is homologous to a gene involved
RT in somitogenesis and encodes a potential bicistronic transcript.";
RL Genomics 64:179-186(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=10857744; DOI=10.1006/geno.2000.6160;
RA Calvari V., Bertini V., De Grandi A., Peverali G., Zuffardi O.,
RA Ferguson-Smith M., Knudtzon J., Camerino G., Borsani G., Guioli S.;
RT "A new submicroscopic deletion that refines the 9p region for sex
RT reversal.";
RL Genomics 65:203-212(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-381.
RC TISSUE=Testis;
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: Transcriptional activator that directly regulates early
CC activation of the myogenic determination gene MYF5 by binding in a
CC sequence-specific manner to the early epaxial enhancer element of it.
CC Involved in somitogenesis during embryogenesis and somite development
CC and differentiation into sclerotome and dermomyotome. Required for the
CC initiation and/or maintenance of proper organization of the sclerotome,
CC dermomyotome and myotome (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y5R5; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-18072054, EBI-716006;
CC Q9Y5R5; Q08117-2: TLE5; NbExp=3; IntAct=EBI-18072054, EBI-11741437;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y5R5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5R5-2; Sequence=VSP_041248, VSP_041249;
CC Name=3;
CC IsoId=Q9Y5R5-3; Sequence=VSP_041247;
CC -!- TISSUE SPECIFICITY: Expressed in testis, kidney and skeletal muscle.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by DMRT2 bicistronic transcripts
CC (AF284223/AF284224) from non-overlapping reading frame, according to
CC PubMed:10729224. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by DMRT2 bicistronic transcripts
CC (AF284223/AF284224) from non-overlapping reading frame, according to
CC PubMed:10729224. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DMRT family. {ECO:0000305}.
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DR EMBL; AF130729; AAD40475.1; -; mRNA.
DR EMBL; AF284223; AAF86291.1; -; mRNA.
DR EMBL; AF284223; AAF86292.1; -; mRNA.
DR EMBL; AF284224; AAF86293.1; -; mRNA.
DR EMBL; AF284224; AAF86294.1; -; mRNA.
DR EMBL; AF284225; AAF86295.1; -; mRNA.
DR EMBL; Y19052; CAB59891.1; -; mRNA.
DR EMBL; AL358976; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471071; EAW58816.1; -; Genomic_DNA.
DR EMBL; BC136493; AAI36494.1; -; mRNA.
DR CCDS; CCDS6444.1; -. [Q9Y5R5-1]
DR CCDS; CCDS6445.1; -. [Q9Y5R5-2]
DR RefSeq; NP_001124337.1; NM_001130865.2. [Q9Y5R5-2]
DR RefSeq; NP_006548.1; NM_006557.6. [Q9Y5R5-2]
DR RefSeq; NP_870987.2; NM_181872.4. [Q9Y5R5-1]
DR RefSeq; XP_011515989.1; XM_011517687.1. [Q9Y5R5-1]
DR RefSeq; XP_011515992.1; XM_011517690.2. [Q9Y5R5-1]
DR RefSeq; XP_011515996.1; XM_011517694.2. [Q9Y5R5-3]
DR RefSeq; XP_016869702.1; XM_017014213.1. [Q9Y5R5-1]
DR RefSeq; XP_016869703.1; XM_017014214.1. [Q9Y5R5-1]
DR RefSeq; XP_016869704.1; XM_017014215.1. [Q9Y5R5-1]
DR RefSeq; XP_016869705.1; XM_017014216.1.
DR AlphaFoldDB; Q9Y5R5; -.
DR SMR; Q9Y5R5; -.
DR BioGRID; 115898; 4.
DR ELM; Q9Y5R5; -.
DR IntAct; Q9Y5R5; 2.
DR STRING; 9606.ENSP00000371686; -.
DR iPTMnet; Q9Y5R5; -.
DR PhosphoSitePlus; Q9Y5R5; -.
DR BioMuta; DMRT2; -.
DR DMDM; 334302783; -.
DR MassIVE; Q9Y5R5; -.
DR PaxDb; Q9Y5R5; -.
DR PeptideAtlas; Q9Y5R5; -.
DR PRIDE; Q9Y5R5; -.
DR Antibodypedia; 9092; 73 antibodies from 19 providers.
DR DNASU; 10655; -.
DR Ensembl; ENST00000259622.10; ENSP00000259622.6; ENSG00000173253.16. [Q9Y5R5-2]
DR Ensembl; ENST00000358146.7; ENSP00000350865.2; ENSG00000173253.16. [Q9Y5R5-1]
DR Ensembl; ENST00000382251.7; ENSP00000371686.3; ENSG00000173253.16. [Q9Y5R5-1]
DR Ensembl; ENST00000382255.7; ENSP00000371690.3; ENSG00000173253.16. [Q9Y5R5-2]
DR Ensembl; ENST00000412350.6; ENSP00000397494.2; ENSG00000173253.16. [Q9Y5R5-2]
DR Ensembl; ENST00000635183.1; ENSP00000489226.1; ENSG00000173253.16. [Q9Y5R5-2]
DR GeneID; 10655; -.
DR KEGG; hsa:10655; -.
DR MANE-Select; ENST00000358146.7; ENSP00000350865.2; NM_181872.6; NP_870987.2.
DR UCSC; uc003zhb.5; human. [Q9Y5R5-1]
DR CTD; 10655; -.
DR DisGeNET; 10655; -.
DR GeneCards; DMRT2; -.
DR HGNC; HGNC:2935; DMRT2.
DR HPA; ENSG00000173253; Tissue enhanced (kidney, lymphoid tissue, parathyroid gland).
DR MIM; 604935; gene.
DR neXtProt; NX_Q9Y5R5; -.
DR OpenTargets; ENSG00000173253; -.
DR PharmGKB; PA27382; -.
DR VEuPathDB; HostDB:ENSG00000173253; -.
DR eggNOG; KOG3815; Eukaryota.
DR GeneTree; ENSGT00940000156282; -.
DR HOGENOM; CLU_1224438_0_0_1; -.
DR InParanoid; Q9Y5R5; -.
DR OMA; YKFTIDR; -.
DR OrthoDB; 897429at2759; -.
DR PhylomeDB; Q9Y5R5; -.
DR TreeFam; TF317837; -.
DR PathwayCommons; Q9Y5R5; -.
DR SignaLink; Q9Y5R5; -.
DR BioGRID-ORCS; 10655; 12 hits in 1093 CRISPR screens.
DR GenomeRNAi; 10655; -.
DR Pharos; Q9Y5R5; Tbio.
DR PRO; PR:Q9Y5R5; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q9Y5R5; protein.
DR Bgee; ENSG00000173253; Expressed in kidney epithelium and 115 other tissues.
DR ExpressionAtlas; Q9Y5R5; baseline and differential.
DR Genevisible; Q9Y5R5; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0048706; P:embryonic skeletal system development; IEA:Ensembl.
DR GO; GO:0061055; P:myotome development; IEA:Ensembl.
DR GO; GO:2000287; P:positive regulation of myotome development; IEA:Ensembl.
DR GO; GO:0014807; P:regulation of somitogenesis; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0007548; P:sex differentiation; IBA:GO_Central.
DR Gene3D; 4.10.1040.10; -; 1.
DR InterPro; IPR001275; DM_DNA-bd.
DR InterPro; IPR036407; DM_DNA-bd_sf.
DR InterPro; IPR026607; DMRT.
DR PANTHER; PTHR12322; PTHR12322; 1.
DR Pfam; PF00751; DM; 1.
DR SMART; SM00301; DM; 1.
DR SUPFAM; SSF82927; SSF82927; 1.
DR PROSITE; PS40000; DM_1; 1.
DR PROSITE; PS50809; DM_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..561
FT /note="Doublesex- and mab-3-related transcription factor 2"
FT /id="PRO_0000207048"
FT DNA_BIND 123..170
FT /note="DM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00070"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..67
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..95
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..233
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10729224"
FT /id="VSP_041247"
FT VAR_SEQ 210..226
FT /note="GYRPIPAETYVGGTFPL -> VLLGLFYSYYVYIMNHL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10332030,
FT ECO:0000303|PubMed:10729224, ECO:0000303|PubMed:10857744"
FT /id="VSP_041248"
FT VAR_SEQ 227..561
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10332030,
FT ECO:0000303|PubMed:10729224, ECO:0000303|PubMed:10857744"
FT /id="VSP_041249"
FT VARIANT 381
FT /note="A -> P (in dbSNP:rs3824419)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_067719"
FT VARIANT 458
FT /note="E -> Q (in dbSNP:rs17641078)"
FT /id="VAR_067720"
FT CONFLICT 329
FT /note="A -> G (in Ref. 2; AAF86292/AAF86294/AAF86295)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="P -> H (in Ref. 2; AAF86292/AAF86294/AAF86295)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 561 AA; 61814 MW; 17D856C78EBB43CB CRC64;
MADPQAGSAA GDWEIDVESL ELEEDVCGAP RSTPPGPSPP PADGDCEDDE DDDGVDEDAE
EEGDGEEAGA SPGMPGQPEQ RGGPQPRPPL APQASPAGTG PRERCTPAGG GAEPRKLSRT
PKCARCRNHG VVSCLKGHKR FCRWRDCQCA NCLLVVERQR VMAAQVALRR QQATEDKKGL
SGKQNNFERK AVYQRQVRAP SLLAKSILEG YRPIPAETYV GGTFPLPPPV SDRMRKRRAF
ADKELENIML EREYKEREML ETSQAAALFL PNRMVPGPDY NSYKSAYSPS PVEPPSKDFC
NFLPTCLDLT MQYSGSGNME LISSNVSVAT TYRQYPLSSR FLVWPKCGPI SDTLLYQQCL
LNATTSVQAL KPGASWDLKG ARVQDGLSAE QDMMPSKLEG SLVLPHTPEI QTTRSDLQGH
QAVPERSAFS PPRRNFSPIV DTDSLAAQGH VLTKISKENT RHPLPLRHNP FHSLFQQTLT
DKSGPELKTP FVKEAFEETP KKHRECLVKD NQKYTFTIDR CAKDLFVAKQ VGTKLSVNEP
LSFSVESILK RPSSAITRVS Q
