HXD13_HUMAN
ID HXD13_HUMAN Reviewed; 343 AA.
AC P35453;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 3.
DT 03-AUG-2022, entry version 194.
DE RecName: Full=Homeobox protein Hox-D13;
DE AltName: Full=Homeobox protein Hox-4I;
GN Name=HOXD13; Synonyms=HOX4I;
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=8614804; DOI=10.1126/science.272.5261.548;
RA Muragaki Y., Mundlos S., Upton J., Olsen B.R.;
RT "Altered growth and branching patterns in synpolydactyly caused by
RT mutations in HOXD13.";
RL Science 272:548-551(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Arai Y., Arai K., Kita K., Miwa H., Kamada N., Ohki M.;
RT "The t(2:11)(q31:p15) translocation in acute myeloid leukemia fuses NUP98
RT nucleoporin gene to HOXD13 homeobox gene.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 276-341.
RX PubMed=1675198; DOI=10.1016/0888-7543(91)90482-t;
RA D'Esposito M., Morelli F., Acampora D., Migliaccio E., Simeone A.,
RA Boncinelli E.;
RT "EVX2, a human homeobox gene homologous to the even-skipped segmentation
RT gene, is localized at the 5' end of HOX4 locus on chromosome 2.";
RL Genomics 10:43-50(1991).
RN [5]
RP INVOLVEMENT IN VACTERL.
RX PubMed=19006232; DOI=10.1002/ajmg.a.32426;
RA Garcia-Barcelo M.-M., Wong K.K., Lui V.C., Yuan Z.W., So M.T., Ngan E.S.,
RA Miao X.P., Chung P.H., Khong P.L., Tam P.K.;
RT "Identification of a HOXD13 mutation in a VACTERL patient.";
RL Am. J. Med. Genet. A 146:3181-3185(2008).
RN [6]
RP INVOLVEMENT IN BDSDO, AND VARIANT BDSDO LYS-325.
RX PubMed=23995701; DOI=10.1101/gr.157610.113;
RA Ibrahim D.M., Hansen P., Roedelsperger C., Stiege A.C., Doelken S.C.,
RA Horn D., Jaeger M., Janetzki C., Krawitz P., Leschik G., Wagner F.,
RA Scheuer T., Schmidt-von Kegler M., Seemann P., Timmermann B.,
RA Robinson P.N., Mundlos S., Hecht J.;
RT "Distinct global shifts in genomic binding profiles of limb malformation-
RT associated HOXD13 mutations.";
RL Genome Res. 23:2091-2102(2013).
RN [7]
RP VARIANT SPD1 ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-57 INS.
RX PubMed=8817328; DOI=10.1093/hmg/5.7.945;
RA Akarsu A.N., Stoilov I., Yilmaz E., Sayli B.S., Sarfarazi M.;
RT "Genomic structure of HOXD13 gene: a nine polyalanine duplication causes
RT synpolydactyly in two unrelated families.";
RL Hum. Mol. Genet. 5:945-952(1996).
RN [8]
RP VARIANT SPD1 TRP-306.
RX PubMed=12414828; DOI=10.1136/jmg.39.11.852;
RA Debeer P., Bacchelli C., Scambler P.J., De Smet L., Fryns J.-P.,
RA Goodman F.R.;
RT "Severe digital abnormalities in a patient heterozygous for both a novel
RT missense mutation in HOXD13 and a polyalanine tract expansion in HOXA13.";
RL J. Med. Genet. 39:852-856(2002).
RN [9]
RP VARIANTS BDE1 CYS-316 AND LEU-322, AND VARIANT BDD CYS-316.
RX PubMed=12649808; DOI=10.1086/374721;
RA Johnson D., Kan S.H., Oldridge M., Trembath R.C., Roche P., Esnouf R.M.,
RA Giele H., Wilkie A.O.;
RT "Missense mutations in the homeodomain of HOXD13 are associated with
RT brachydactyly types D and E.";
RL Am. J. Hum. Genet. 72:984-997(2003).
RN [10]
RP VARIANT SPD1 ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-ALA-57 INS, AND VARIANT
RP 57-ALA-ALA-58 DEL.
RX PubMed=16222680; DOI=10.1002/ajmg.a.30971;
RA Kjaer K.W., Hansen L., Eiberg H., Utkus A., Skovgaard L.T., Leicht P.,
RA Opitz J.M., Tommerup N.;
RT "A 72-year-old Danish puzzle resolved -- comparative analysis of phenotypes
RT in families with different-sized HOXD13 polyalanine expansions.";
RL Am. J. Med. Genet. A 138:328-339(2005).
RN [11]
RP VARIANT BDSD 57-ALA--ALA-62 DEL, VARIANT SDTY5 ARG-325, CHARACTERIZATION OF
RP VARIANT BDSD 57-ALA--ALA-62 DEL, AND CHARACTERIZATION OF VARIANT SDTY5
RP ARG-325.
RX PubMed=17236141; DOI=10.1086/511387;
RA Zhao X., Sun M., Zhao J., Leyva J.A., Zhu H., Yang W., Zeng X., Ao Y.,
RA Liu Q., Liu G., Lo W.H.Y., Jabs E.W., Amzel L.M., Shan X., Zhang X.;
RT "Mutations in HOXD13 underlie syndactyly type V and a novel brachydactyly-
RT syndactyly syndrome.";
RL Am. J. Hum. Genet. 80:361-371(2007).
RN [12]
RP VARIANTS SPD1 GLN-306 AND GLY-306, CHARACTERIZATION OF VARIANTS SPD1
RP GLN-306 AND GLY-306, CHARACTERIZATION OF VARIANT BDE1 LEU-322, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=24789103; DOI=10.1371/journal.pone.0096192;
RA Dai L., Liu D., Song M., Xu X., Xiong G., Yang K., Zhang K., Meng H.,
RA Guo H., Bai Y.;
RT "Mutations in the homeodomain of HOXD13 cause syndactyly type 1-c in two
RT Chinese families.";
RL PLoS ONE 9:E96192-E96192(2014).
RN [13]
RP VARIANT SPD1 ARG-313, AND CHARACTERIZATION OF VARIANT SPD1 ARG-313.
RX PubMed=26581570; DOI=10.1002/ajmg.a.37464;
RA Ibrahim D.M., Tayebi N., Knaus A., Stiege A.C., Sahebzamani A., Hecht J.,
RA Mundlos S., Spielmann M.;
RT "A homozygous HOXD13 missense mutation causes a severe form of
RT synpolydactyly with metacarpal to carpal transformation.";
RL Am. J. Med. Genet. A 170:615-621(2016).
CC -!- FUNCTION: Sequence-specific transcription factor that binds gene
CC promoters and activates their transcription (PubMed:24789103). Part of
CC a developmental regulatory system that provides cells with specific
CC positional identities on the anterior-posterior axis (By similarity).
CC {ECO:0000250|UniProtKB:P24344, ECO:0000269|PubMed:24789103}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:24789103}.
CC -!- POLYMORPHISM: The poly-Ala region is polymorphic (11 to 15 residues) in
CC the normal population and is expanded to about 22-29 residues in SPD1
CC and syndactyly type 5 patients.
CC -!- DISEASE: Synpolydactyly 1 (SPD1) [MIM:186000]: Limb malformation that
CC shows a characteristic manifestation in both hands and feet. This
CC condition is inherited as an autosomal dominant trait with reduced
CC penetrance. {ECO:0000269|PubMed:12414828, ECO:0000269|PubMed:16222680,
CC ECO:0000269|PubMed:24789103, ECO:0000269|PubMed:26581570,
CC ECO:0000269|PubMed:8817328}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Brachydactyly D (BDD) [MIM:113200]: A form of brachydactyly.
CC Brachydactyly defines a group of inherited malformations characterized
CC by shortening of the digits due to abnormal development of the
CC phalanges and/or the metacarpals. Brachydactyly type D is characterized
CC by short and broad terminal phalanges of the thumbs and big toes.
CC {ECO:0000269|PubMed:12649808}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Syndactyly 5 (SDTY5) [MIM:186300]: A form of syndactyly, a
CC congenital anomaly of the hand or foot marked by persistence of the
CC webbing between adjacent digits that are more or less completely
CC attached. The characteristic finding in SDTY5 is the presence of an
CC associated metacarpal and metatarsal fusion. The metacarpals and
CC metatarsals most commonly fused are the 4th and 5th or the 3rd and 4th.
CC Soft tissue syndactyly usually affects the 3rd and 4th fingers and the
CC 2nd and 3rd toes. {ECO:0000269|PubMed:17236141}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- DISEASE: Brachydactyly-syndactyly syndrome (BDSD) [MIM:610713]: A
CC disease characterized by generalized shortening of the hands and feet,
CC broad and short distal phalanges of the thumbs, and cutaneous
CC syndactyly of toes 2 and 3. The limb phenotypes observed in this
CC syndrome overlap those of brachydactyly types A4, D, E and syndactyly
CC type 1. {ECO:0000269|PubMed:17236141}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Brachydactyly E1 (BDE1) [MIM:113300]: A form of brachydactyly.
CC Brachydactyly defines a group of inherited malformations characterized
CC by shortening of the digits due to abnormal development of the
CC phalanges and/or the metacarpals. Brachydactyly type E is characterized
CC by shortening of the fingers mainly in the metacarpals and metatarsals.
CC Wide variability in the number of digits affected occurs from person to
CC person, even in the same family. Some individuals are moderately short
CC of stature. Brachydactyly type E1 is characterized by shortening
CC limited to fourth metacarpals and/or metatarsals.
CC {ECO:0000269|PubMed:12649808, ECO:0000269|PubMed:24789103}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: VACTERL association (VACTERL) [MIM:192350]: VACTERL is an
CC acronym for vertebral anomalies, anal atresia, congenital cardiac
CC disease, tracheoesophageal fistula, renal anomalies, radial dysplasia,
CC and other limb defects. {ECO:0000269|PubMed:19006232}. Note=The gene
CC represented in this entry may be involved in disease pathogenesis.
CC -!- DISEASE: Brachydactyly-syndactyly-oligodactyly syndrome (BDSDO)
CC [MIM:610713]: A syndrome characterized by a complex brachydactyly-
CC syndactyly-oligodactyly phenotype. Limb anomalies include reduced
CC number of digits that are severely shortened, camptodactyly,
CC syndactyly, absence of terminal phalanges of the thumbs, and absence of
CC nails of the thumbs and toes. {ECO:0000269|PubMed:23995701}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the Abd-B homeobox family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-9 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC51635.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA95352.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA95352.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF005220; AAC51635.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF005219; AAC51635.1; JOINED; Genomic_DNA.
DR EMBL; AB032481; BAA95352.1; ALT_INIT; Genomic_DNA.
DR EMBL; AC009336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS2264.2; -.
DR PIR; B39065; B39065.
DR RefSeq; NP_000514.2; NM_000523.3.
DR AlphaFoldDB; P35453; -.
DR SMR; P35453; -.
DR BioGRID; 109479; 69.
DR IntAct; P35453; 21.
DR MINT; P35453; -.
DR STRING; 9606.ENSP00000376322; -.
DR GlyGen; P35453; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P35453; -.
DR PhosphoSitePlus; P35453; -.
DR BioMuta; HOXD13; -.
DR DMDM; 223590221; -.
DR EPD; P35453; -.
DR MassIVE; P35453; -.
DR MaxQB; P35453; -.
DR PaxDb; P35453; -.
DR PeptideAtlas; P35453; -.
DR PRIDE; P35453; -.
DR ProteomicsDB; 55065; -.
DR Antibodypedia; 33902; 250 antibodies from 32 providers.
DR DNASU; 3239; -.
DR Ensembl; ENST00000392539.4; ENSP00000376322.3; ENSG00000128714.6.
DR GeneID; 3239; -.
DR KEGG; hsa:3239; -.
DR MANE-Select; ENST00000392539.4; ENSP00000376322.3; NM_000523.4; NP_000514.2.
DR UCSC; uc002ukf.2; human.
DR CTD; 3239; -.
DR DisGeNET; 3239; -.
DR GeneCards; HOXD13; -.
DR HGNC; HGNC:5136; HOXD13.
DR HPA; ENSG00000128714; Group enriched (cervix, intestine, prostate, seminal vesicle, vagina).
DR MalaCards; HOXD13; -.
DR MIM; 113200; phenotype.
DR MIM; 113300; phenotype.
DR MIM; 142989; gene.
DR MIM; 186000; phenotype.
DR MIM; 186300; phenotype.
DR MIM; 192350; phenotype.
DR MIM; 610713; phenotype.
DR neXtProt; NX_P35453; -.
DR OpenTargets; ENSG00000128714; -.
DR Orphanet; 93387; Brachydactyly type E.
DR Orphanet; 93409; Brachydactyly-syndactyly, Zhao type.
DR Orphanet; 93385; NON RARE IN EUROPE: Brachydactyly type D.
DR Orphanet; 93406; Syndactyly type 5.
DR Orphanet; 295195; Synpolydactyly type 1.
DR Orphanet; 887; VACTERL/VATER association.
DR Orphanet; 295191; Zygodactyly type 3.
DR PharmGKB; PA29410; -.
DR VEuPathDB; HostDB:ENSG00000128714; -.
DR eggNOG; KOG0487; Eukaryota.
DR GeneTree; ENSGT00940000161457; -.
DR HOGENOM; CLU_059940_1_0_1; -.
DR InParanoid; P35453; -.
DR OMA; KECPAPA; -.
DR OrthoDB; 1190384at2759; -.
DR PhylomeDB; P35453; -.
DR TreeFam; TF330813; -.
DR PathwayCommons; P35453; -.
DR SignaLink; P35453; -.
DR SIGNOR; P35453; -.
DR BioGRID-ORCS; 3239; 249 hits in 1095 CRISPR screens.
DR ChiTaRS; HOXD13; human.
DR GeneWiki; HOXD13; -.
DR GenomeRNAi; 3239; -.
DR Pharos; P35453; Tbio.
DR PRO; PR:P35453; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P35453; protein.
DR Bgee; ENSG00000128714; Expressed in urethra and 31 other tissues.
DR Genevisible; P35453; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; ISS:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-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:0009952; P:anterior/posterior pattern specification; IEA:Ensembl.
DR GO; GO:0060602; P:branch elongation of an epithelium; IEA:Ensembl.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IEA:Ensembl.
DR GO; GO:0048619; P:embryonic hindgut morphogenesis; IEA:Ensembl.
DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
DR GO; GO:0060571; P:morphogenesis of an epithelial fold; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; IEA:Ensembl.
DR GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:ProtInc.
DR GO; GO:0033574; P:response to testosterone; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
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; IPR022067; HoxA13_N.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF12284; HoxA13_N; 1.
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 Developmental protein; Disease variant; DNA-binding; Homeobox; Nucleus;
KW Reference proteome; Transcription; Transcription regulation;
KW Triplet repeat expansion.
FT CHAIN 1..343
FT /note="Homeobox protein Hox-D13"
FT /id="PRO_0000200244"
FT DNA_BIND 276..335
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 57..63
FT /note="Missing (in BDSD; does not affect capacity to
FT transactivate EPHA7 promoter)"
FT /id="VAR_031649"
FT VARIANT 57..58
FT /note="Missing"
FT /evidence="ECO:0000269|PubMed:16222680"
FT /id="VAR_031648"
FT VARIANT 57
FT /note="A -> AAAAAAAAAA (in SPD1)"
FT /evidence="ECO:0000269|PubMed:16222680,
FT ECO:0000269|PubMed:8817328"
FT /id="VAR_003818"
FT VARIANT 252
FT /note="S -> A (in dbSNP:rs35290213)"
FT /id="VAR_031650"
FT VARIANT 306
FT /note="R -> G (in SPD1; decreases the transcriptional
FT activator activity; dbSNP:rs28933082)"
FT /evidence="ECO:0000269|PubMed:24789103"
FT /id="VAR_076833"
FT VARIANT 306
FT /note="R -> Q (in SPD1; decreases the transcriptional
FT activator activity; dbSNP:rs879255265)"
FT /evidence="ECO:0000269|PubMed:24789103"
FT /id="VAR_076834"
FT VARIANT 306
FT /note="R -> W (in SPD1; dbSNP:rs28933082)"
FT /evidence="ECO:0000269|PubMed:12414828"
FT /id="VAR_031651"
FT VARIANT 313
FT /note="T -> R (in SPD1; disrupts interaction with DNA;
FT dbSNP:rs1432063993)"
FT /evidence="ECO:0000269|PubMed:26581570"
FT /id="VAR_075400"
FT VARIANT 316
FT /note="S -> C (in BDE1 and BDD; dbSNP:rs28928892)"
FT /evidence="ECO:0000269|PubMed:12649808"
FT /id="VAR_015952"
FT VARIANT 322
FT /note="I -> L (in BDE1; decreases the transcriptional
FT activator activity; dbSNP:rs28928891)"
FT /evidence="ECO:0000269|PubMed:12649808,
FT ECO:0000269|PubMed:24789103"
FT /id="VAR_015953"
FT VARIANT 325
FT /note="Q -> K (in BDSDO; dbSNP:rs875989842)"
FT /evidence="ECO:0000269|PubMed:23995701"
FT /id="VAR_076835"
FT VARIANT 325
FT /note="Q -> R (in SDTY5; impairs capacity to transactivate
FT EPHA7 promoter; dbSNP:rs104893635)"
FT /evidence="ECO:0000269|PubMed:17236141,
FT ECO:0000269|PubMed:23995701"
FT /id="VAR_031652"
SQ SEQUENCE 343 AA; 36101 MW; CF34D0319021430A CRC64;
MSRAGSWDMD GLRADGGGAG GAPASSSSSS VAAAAASGQC RGFLSAPVFA GTHSGRAAAA
AAAAAAAAAA ASGFAYPGTS ERTGSSSSSS SSAVVAARPE APPAKECPAP TPAAAAAAPP
SAPALGYGYH FGNGYYSCRM SHGVGLQQNA LKSSPHASLG GFPVEKYMDV SGLASSSVPA
NEVPARAKEV SFYQGYTSPY QHVPGYIDMV STFGSGEPRH EAYISMEGYQ SWTLANGWNS
QVYCTKDQPQ GSHFWKSSFP GDVALNQPDM CVYRRGRKKR VPYTKLQLKE LENEYAINKF
INKDKRRRIS AATNLSERQV TIWFQNRRVK DKKIVSKLKD TVS
