SMYD4_MOUSE
ID SMYD4_MOUSE Reviewed; 799 AA.
AC Q8BTK5; A2BDD0; Q3U3Z8; Q501N5; Q5SWN4; Q69Z60; Q8BMP3;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=SET and MYND domain-containing protein 4;
DE EC=2.1.1.-;
GN Name=Smyd4; Synonyms=Kiaa1936;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Pituitary;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP TYR-65; VAL-208; LYS-226; GLU-397; ALA-458; THR-486; VAL-527 AND ILE-553.
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-799 (ISOFORM 1).
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=30110327; DOI=10.1371/journal.pgen.1007578;
RA Xiao D., Wang H., Hao L., Guo X., Ma X., Qian Y., Chen H., Ma J., Zhang J.,
RA Sheng W., Shou W., Huang G., Ma D.;
RT "The roles of SMYD4 in epigenetic regulation of cardiac development in
RT zebrafish.";
RL PLoS Genet. 14:e1007578-e1007578(2018).
CC -!- FUNCTION: Plays a critical role in cardiac development (By similarity).
CC Acts as a key epigenetic regulator of gene expression during cardiac
CC development via its dual activities as a methyltransferase and negative
CC regulator of HDAC1 (By similarity). {ECO:0000250|UniProtKB:Q08C84,
CC ECO:0000250|UniProtKB:Q8IYR2}.
CC -!- SUBUNIT: Interacts (via MYND-type zinc finger) with HDAC1.
CC {ECO:0000250|UniProtKB:Q8IYR2}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:30110327}. Cytoplasm
CC {ECO:0000269|PubMed:30110327}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8BTK5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BTK5-2; Sequence=VSP_017580;
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AK030380; BAC26933.1; -; mRNA.
DR EMBL; AK089959; BAC41013.1; -; mRNA.
DR EMBL; AK154507; BAE32637.1; -; mRNA.
DR EMBL; AL591496; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL603834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC095952; AAH95952.1; -; mRNA.
DR EMBL; BC130220; AAI30221.1; -; mRNA.
DR EMBL; AK173306; BAD32584.1; -; mRNA.
DR CCDS; CCDS48848.1; -. [Q8BTK5-1]
DR RefSeq; NP_001096081.1; NM_001102611.1. [Q8BTK5-1]
DR RefSeq; XP_006533600.1; XM_006533537.3. [Q8BTK5-2]
DR AlphaFoldDB; Q8BTK5; -.
DR SMR; Q8BTK5; -.
DR STRING; 10090.ENSMUSP00000047505; -.
DR iPTMnet; Q8BTK5; -.
DR PhosphoSitePlus; Q8BTK5; -.
DR EPD; Q8BTK5; -.
DR MaxQB; Q8BTK5; -.
DR PaxDb; Q8BTK5; -.
DR PRIDE; Q8BTK5; -.
DR ProteomicsDB; 261382; -. [Q8BTK5-1]
DR ProteomicsDB; 261383; -. [Q8BTK5-2]
DR Antibodypedia; 22811; 222 antibodies from 28 providers.
DR Ensembl; ENSMUST00000044530; ENSMUSP00000047505; ENSMUSG00000018809. [Q8BTK5-1]
DR GeneID; 319822; -.
DR KEGG; mmu:319822; -.
DR UCSC; uc007kdm.1; mouse. [Q8BTK5-1]
DR CTD; 114826; -.
DR MGI; MGI:2442796; Smyd4.
DR VEuPathDB; HostDB:ENSMUSG00000018809; -.
DR eggNOG; KOG2084; Eukaryota.
DR GeneTree; ENSGT00730000111079; -.
DR HOGENOM; CLU_021727_0_0_1; -.
DR InParanoid; Q8BTK5; -.
DR OMA; FDCTCPA; -.
DR OrthoDB; 1278034at2759; -.
DR PhylomeDB; Q8BTK5; -.
DR TreeFam; TF106441; -.
DR BioGRID-ORCS; 319822; 3 hits in 75 CRISPR screens.
DR ChiTaRS; Smyd4; mouse.
DR PRO; PR:Q8BTK5; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8BTK5; protein.
DR Bgee; ENSMUSG00000018809; Expressed in ureter smooth muscle and 165 other tissues.
DR Genevisible; Q8BTK5; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042826; F:histone deacetylase binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd10536; SET_SMYD4; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044421; SMYD4_SET.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR002893; Znf_MYND.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF01753; zf-MYND; 1.
DR SUPFAM; SSF48452; SSF48452; 2.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytoplasm; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transferase; Zinc;
KW Zinc-finger.
FT CHAIN 1..799
FT /note="SET and MYND domain-containing protein 4"
FT /id="PRO_0000227785"
FT DOMAIN 233..570
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT ZN_FING 296..335
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 112..114
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 296
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 318
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 331
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 535..536
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9H7B4"
FT BINDING 569
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT BINDING 591
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT VAR_SEQ 1..133
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_017580"
FT VARIANT 65
FT /note="N -> Y (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 208
FT /note="I -> V (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 226
FT /note="T -> K (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 397
FT /note="G -> E (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 458
FT /note="D -> A (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 486
FT /note="A -> T (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 527
FT /note="I -> V (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT VARIANT 553
FT /note="V -> I (in strain: Czech II)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT CONFLICT 363
FT /note="V -> D (in Ref. 1; BAC26933)"
FT /evidence="ECO:0000305"
FT CONFLICT 374
FT /note="V -> I (in Ref. 1; BAC41013)"
FT /evidence="ECO:0000305"
FT CONFLICT 751
FT /note="A -> P (in Ref. 1; BAC26933)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 799 AA; 88538 MW; 6C4CAA5AC7B5874A CRC64;
MDLPVDEWKS YLLKKWASLP KSVQDTISTA ETLSDIFLPS SSLLQPEDEM FLKELSSSYS
VEKDNDAPLF YREEGNRKFQ EKEYTDAAVL YSKGVSHSRP NTEDISLCYA NRSAALFHLG
QYEACLKDIV EAGMHGYPER LQPKMMVRKT ECLVNLGRLQ EARQTISDLE SSLTAKPTLV
LSSYQILQRN VQHLKIKIQE KETLPEPIPA ALTNAFEDIA LGEENTQISG ASLSVSLCTH
PLKGRHLVAT KDILPGELLV KEDAFVSVLI PGEMPRPHHC LENKWDTRVT SGDLYCHRCL
KHTLATVPCG SCSYAKYCSQ ECMQQAWDLY HSTECSLGGL LLTLGVFCHV ALRMTLLARF
EDVDRVVRML CDEVGSTDTC LPESKNLVKA FDYTSQGESE EKSKIGEPPI PGCNVNGKYG
SNYNAIFSLL PHTEKHSPEH RFICAISVSA LCRQLKADSV QAQTLKSPKL KAVTPGLCAD
LTVWGAAMLR HMLQLQCNAQ AITSICHTGS NESIITNSRQ IRLATGIFPV VSLLNHSCRP
NTSVSFTGTV ATVRAAQRIA KGQEILHCYG PHESRMGVAE RQQRLSSQYF FDCRCGACHA
ETLRAAAAPR WEAFCCKTCR ALMQGNDVLS CSNESCTNSV SRDQLVSRLQ DLQQQVCMAQ
KLLRTGKPEQ AIQQLLRCRE AAESFLSAEH TVLGEIEDGL AQAHATLGNW LKSAAHVQKS
LQVVETRHGP SSVEIGHELF KLAQVLFNGL AVPEALSAIW KAERILLVHC GPESEEVREL
REMRSCLLDS SFVPVGPLV
