DACT2_HUMAN
ID DACT2_HUMAN Reviewed; 774 AA.
AC Q5SW24; Q2NKJ2; Q569G0; Q8WYW2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Dapper homolog 2;
DE AltName: Full=Dapper antagonist of catenin 2;
GN Name=DACT2; Synonyms=C6orf116; ORFNames=PP13671;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Placenta;
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: Involved in regulation of intracellular signaling pathways
CC during development. Negatively regulates the Nodal signaling pathway,
CC possibly by promoting the lysosomal degradation of Nodal receptors,
CC such as TGFBR1. May be involved in control of the morphogenetic
CC behavior of kidney ureteric bud cells by keeping cells epithelial and
CC restraining their mesenchymal character. May play an inhibitory role in
CC the re-epithelialization of skin wounds by attenuating TGF-beta
CC signaling (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Can form homodimers and heterodimers with DACT1 or DACT3.
CC Interacts with CSNK1D, PKA catalytic subunit, PKC-type kinase, CSNK2B,
CC DVL1, DVL2, DVL3, VANGL1, VANGL2, TGFBR1, CTNNB1, CTNND2, CTNND1, LEF1,
CC TCF7, TCF7L1 and HDAC1 (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q5SW24-3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11994826, EBI-3867333;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5SW24-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SW24-2; Sequence=VSP_032596;
CC Name=3;
CC IsoId=Q5SW24-3; Sequence=VSP_032595;
CC Name=4;
CC IsoId=Q5SW24-4; Sequence=VSP_032597, VSP_032598;
CC -!- DOMAIN: The C-terminal PDZ-binding motif may mediate interaction with
CC the PDZ domains of DSH (Dishevelled) family proteins. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the dapper family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI11791.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL55843.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF318336; AAL55843.1; ALT_FRAME; mRNA.
DR EMBL; AL606970; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC092498; AAH92498.1; -; mRNA.
DR EMBL; BC111764; AAI11765.1; -; mRNA.
DR EMBL; BC111790; AAI11791.1; ALT_INIT; mRNA.
DR CCDS; CCDS47519.1; -. [Q5SW24-1]
DR CCDS; CCDS69241.1; -. [Q5SW24-4]
DR CCDS; CCDS75554.1; -. [Q5SW24-2]
DR RefSeq; NP_001273279.1; NM_001286350.1. [Q5SW24-2]
DR RefSeq; NP_001273280.1; NM_001286351.1. [Q5SW24-4]
DR RefSeq; NP_999627.2; NM_214462.4. [Q5SW24-1]
DR AlphaFoldDB; Q5SW24; -.
DR BioGRID; 127953; 17.
DR IntAct; Q5SW24; 2.
DR STRING; 9606.ENSP00000355760; -.
DR iPTMnet; Q5SW24; -.
DR PhosphoSitePlus; Q5SW24; -.
DR BioMuta; DACT2; -.
DR DMDM; 74743909; -.
DR MassIVE; Q5SW24; -.
DR PaxDb; Q5SW24; -.
DR PeptideAtlas; Q5SW24; -.
DR PRIDE; Q5SW24; -.
DR ProteomicsDB; 63960; -. [Q5SW24-1]
DR ProteomicsDB; 63961; -. [Q5SW24-2]
DR ProteomicsDB; 63962; -. [Q5SW24-3]
DR ProteomicsDB; 63963; -. [Q5SW24-4]
DR Antibodypedia; 33560; 65 antibodies from 21 providers.
DR DNASU; 168002; -.
DR Ensembl; ENST00000366795.4; ENSP00000355760.3; ENSG00000164488.12. [Q5SW24-1]
DR Ensembl; ENST00000366796.7; ENSP00000355761.2; ENSG00000164488.12. [Q5SW24-4]
DR Ensembl; ENST00000607983.1; ENSP00000476434.1; ENSG00000164488.12. [Q5SW24-3]
DR Ensembl; ENST00000610183.1; ENSP00000476573.1; ENSG00000164488.12. [Q5SW24-2]
DR GeneID; 168002; -.
DR KEGG; hsa:168002; -.
DR MANE-Select; ENST00000366795.4; ENSP00000355760.3; NM_214462.5; NP_999627.2.
DR UCSC; uc003qwq.5; human. [Q5SW24-1]
DR CTD; 168002; -.
DR DisGeNET; 168002; -.
DR GeneCards; DACT2; -.
DR HGNC; HGNC:21231; DACT2.
DR HPA; ENSG00000164488; Tissue enhanced (brain, placenta).
DR MIM; 608966; gene.
DR neXtProt; NX_Q5SW24; -.
DR OpenTargets; ENSG00000164488; -.
DR PharmGKB; PA134934623; -.
DR VEuPathDB; HostDB:ENSG00000164488; -.
DR eggNOG; ENOG502QVT3; Eukaryota.
DR GeneTree; ENSGT00950000183181; -.
DR HOGENOM; CLU_086692_0_0_1; -.
DR InParanoid; Q5SW24; -.
DR OMA; NSCYPAK; -.
DR OrthoDB; 242694at2759; -.
DR PhylomeDB; Q5SW24; -.
DR TreeFam; TF331300; -.
DR PathwayCommons; Q5SW24; -.
DR SignaLink; Q5SW24; -.
DR SIGNOR; Q5SW24; -.
DR BioGRID-ORCS; 168002; 10 hits in 1067 CRISPR screens.
DR GenomeRNAi; 168002; -.
DR Pharos; Q5SW24; Tbio.
DR PRO; PR:Q5SW24; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5SW24; protein.
DR Bgee; ENSG00000164488; Expressed in placenta and 98 other tissues.
DR Genevisible; Q5SW24; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008013; F:beta-catenin binding; ISS:UniProtKB.
DR GO; GO:0070097; F:delta-catenin binding; ISS:UniProtKB.
DR GO; GO:0051018; F:protein kinase A binding; ISS:UniProtKB.
DR GO; GO:0005080; F:protein kinase C binding; ISS:UniProtKB.
DR GO; GO:0008134; F:transcription factor binding; ISS:UniProtKB.
DR GO; GO:0003382; P:epithelial cell morphogenesis; ISS:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0072061; P:inner medullary collecting duct development; ISS:UniProtKB.
DR GO; GO:0007162; P:negative regulation of cell adhesion; ISS:UniProtKB.
DR GO; GO:1900108; P:negative regulation of nodal signaling pathway; ISS:UniProtKB.
DR GO; GO:0043588; P:skin development; ISS:UniProtKB.
DR InterPro; IPR024853; Dact2.
DR InterPro; IPR024843; Dapper.
DR PANTHER; PTHR15919; PTHR15919; 1.
DR PANTHER; PTHR15919:SF13; PTHR15919:SF13; 1.
DR Pfam; PF15268; Dapper; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Reference proteome.
FT CHAIN 1..774
FT /note="Dapper homolog 2"
FT /id="PRO_0000326199"
FT REGION 188..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..319
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 67..93
FT /evidence="ECO:0000255"
FT MOTIF 771..774
FT /note="PDZ-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 409..458
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..710
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..408
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032595"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032596"
FT VAR_SEQ 220..280
FT /note="GDLDRALPADTGLQKASADAELLGLLCQGVDIPLHVPDPKYRQDLVSQGGRE
FT VYPYPSPLH -> ELCNAPGELDMHAPPAGCTSSSLTGVGSGLRGKCGLCGCQLPFCSV
FT NTSSKTKSSGISRQQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032597"
FT VAR_SEQ 281..774
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_032598"
FT VARIANT 351
FT /note="E -> G (in dbSNP:rs6925614)"
FT /id="VAR_059969"
FT VARIANT 541
FT /note="T -> P (in dbSNP:rs10945501)"
FT /id="VAR_059970"
FT CONFLICT 138
FT /note="S -> F (in Ref. 3; AAH92498)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="A -> E (in Ref. 1; AAL55843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 774 AA; 82700 MW; 0DA03DE7E12FE611 CRC64;
MWTPGGPPGS AGWDRRRLGA RLRAAFAGLQ ELQGLRATQQ ERVRGALALQ PPPAPAAPCG
PHGLHGPEQQ LEAALAALQE QLSRLRQQDI GLKTHLDQLD LQISKLQLDV GTASGEALDS
DSRPSSGFYE MSDGGSCSLS TSCASVCSDH ISPSLGSLLP VAQAHKARPS MGDWRPRSVD
ETTVPAWRPQ ATEEGARPPG SVEDAGQPWG TFWPRPVSTG DLDRALPADT GLQKASADAE
LLGLLCQGVD IPLHVPDPKY RQDLVSQGGR EVYPYPSPLH AVALQSPLFV LTKETPQRGG
PSFPRESPRG PAGLNTIQTG PVLEAGPARA RAYIDRLLHL WGRETPAKGS EGEQGPLRHA
ASPSPQRQGG WSTDGGGRLL VFAPGREDEG GPAQSRGAGR GGPQQQGYMP LEGPQQSGSL
PEEGSKPSNS CVLRETMVQA SPSSKAQQTP SAQDYGRGNI ISPSRMLDKS PSPASGHFAH
PSFAASLKMG PPKSKAEKIK RSPMDKVLRF ARQPLLLLDR PEGAHAAPQP SLEWDPAHWP
TGRGGLQRRP ALAWEAPGRS CSESTLYPMP VLVPLAVAPQ ESHRTSAQAL FPFEASLLTS
VARRKHRRWQ STVEISARAR LASCPESNLG PPRPVARRAG GPLARGRPSL VRQDAYTRSD
SEPSKHSAEC DPRFPSVIPE TSEGESSDHT TNRFGDRESS SSDEEGGAQS RDCDLALGYV
AAGHAELAWT QEAPVSSGPL LSPVPKLCRI KASKALKKKI RRFQPTALKV MTMV
