GenomeNet

Database: UniProt
Entry: Q8R5A0
LinkDB: Q8R5A0
Original site: Q8R5A0 
ID   SMYD2_MOUSE             Reviewed;         433 AA.
AC   Q8R5A0; Q3UBQ2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   13-FEB-2019, entry version 114.
DE   RecName: Full=N-lysine methyltransferase SMYD2;
DE            EC=2.1.1.-;
DE   AltName: Full=Histone methyltransferase SMYD2;
DE            EC=2.1.1.43;
DE   AltName: Full=SET and MYND domain-containing protein 2;
GN   Name=Smyd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP   TYR-240, AND INTERACTION WITH SIN3A AND HDAC1.
RX   PubMed=16805913; DOI=10.1186/1476-4598-5-26;
RA   Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.;
RT   "Identification and characterization of Smyd2: a split SET/MYND
RT   domain-containing histone H3 lysine 36-specific methyltransferase that
RT   interacts with the Sin3 histone deacetylase complex.";
RL   Mol. Cancer 5:26-26(2006).
RN   [4]
RP   TISSUE SPECIFICITY, INTERACTION WITH RNA POLYMERASE II AND HELZ, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20305823; DOI=10.1371/journal.pone.0009748;
RA   Diehl F., Brown M.A., van Amerongen M.J., Novoyatleva T.,
RA   Wietelmann A., Harriss J., Ferrazzi F., Bottger T., Harvey R.P.,
RA   Tucker P.W., Engel F.B.;
RT   "Cardiac deletion of Smyd2 is dispensable for mouse heart
RT   development.";
RL   PLoS ONE 5:E9748-E9748(2010).
CC   -!- FUNCTION: Protein-lysine N-methyltransferase that methylates both
CC       histones and non-histone proteins, including p53/TP53 and RB1.
CC       Specifically methylates histone H3 'Lys-4' (H3K4me) and
CC       dimethylates histone H3 'Lys-36' (H3K36me2). Shows even higher
CC       methyltransferase activity on p53/TP53. Monomethylates 'Lys-370'
CC       of p53/TP53, leading to decreased DNA-binding activity and
CC       subsequent transcriptional regulation activity of p53/TP53.
CC       Monomethylates RB1 at 'Lys-860'. {ECO:0000269|PubMed:16805913}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:16805913};
CC   -!- SUBUNIT: Interacts (via MYND-type zinc finger) with EPB41L3.
CC       Interacts (via SET domain) with p53/TP53. Interacts with RB1 and
CC       HSP90AA1 (By similarity). Interacts with RNA polymerase II and
CC       HELZ. Interacts with SIN3A and HDAC1. {ECO:0000250,
CC       ECO:0000269|PubMed:16805913, ECO:0000269|PubMed:20305823}.
CC   -!- INTERACTION:
CC       P04637:TP53 (xeno); NbExp=3; IntAct=EBI-15612527, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC       brain tissue. During cardiac development, it is differentially
CC       expressed with highest expression in the neonatal heart while very
CC       low expression is detected at E12.5 and adult. Specifically
CC       expressed in cardiomyocytes (at protein level).
CC       {ECO:0000269|PubMed:20305823}.
CC   -!- MISCELLANEOUS: Although specifically expressed in cardiomyocytes,
CC       a conditional deletion in heart does not lead to any visible
CC       phenotype. {ECO:0000305|PubMed:20305823}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE29912.1; Type=Miscellaneous discrepancy; Note=Deletion within an exon that does not correspond to an intron.; Evidence={ECO:0000305};
DR   EMBL; AK150857; BAE29912.1; ALT_SEQ; mRNA.
DR   EMBL; BC023119; AAH23119.1; -; mRNA.
DR   CCDS; CCDS35821.1; -.
DR   RefSeq; NP_081072.1; NM_026796.1.
DR   UniGene; Mm.156895; -.
DR   PDB; 3QWV; X-ray; 2.03 A; A=1-433.
DR   PDB; 3QWW; X-ray; 1.80 A; A=1-433.
DR   PDBsum; 3QWV; -.
DR   PDBsum; 3QWW; -.
DR   ProteinModelPortal; Q8R5A0; -.
DR   SMR; Q8R5A0; -.
DR   BioGrid; 230559; 2.
DR   DIP; DIP-60503N; -.
DR   IntAct; Q8R5A0; 1.
DR   STRING; 10090.ENSMUSP00000027897; -.
DR   iPTMnet; Q8R5A0; -.
DR   PhosphoSitePlus; Q8R5A0; -.
DR   EPD; Q8R5A0; -.
DR   MaxQB; Q8R5A0; -.
DR   PaxDb; Q8R5A0; -.
DR   PeptideAtlas; Q8R5A0; -.
DR   PRIDE; Q8R5A0; -.
DR   Ensembl; ENSMUST00000027897; ENSMUSP00000027897; ENSMUSG00000026603.
DR   GeneID; 226830; -.
DR   KEGG; mmu:226830; -.
DR   UCSC; uc007eax.1; mouse.
DR   CTD; 56950; -.
DR   MGI; MGI:1915889; Smyd2.
DR   eggNOG; KOG2084; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000157082; -.
DR   HOGENOM; HOG000007850; -.
DR   HOVERGEN; HBG098536; -.
DR   InParanoid; Q8R5A0; -.
DR   KO; K11426; -.
DR   OMA; AVQEIHP; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; Q8R5A0; -.
DR   TreeFam; TF106487; -.
DR   BRENDA; 2.1.1.43; 3474.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
DR   ChiTaRS; Smyd2; mouse.
DR   EvolutionaryTrace; Q8R5A0; -.
DR   PRO; PR:Q8R5A0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   Bgee; ENSMUSG00000026603; Expressed in 290 organ(s), highest expression level in gastrocnemius.
DR   Genevisible; Q8R5A0; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0016571; P:histone methylation; IDA:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   Gene3D; 1.25.40.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
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; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; Complete proteome; Cytoplasm;
KW   Metal-binding; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    433       N-lysine methyltransferase SMYD2.
FT                                /FTId=PRO_0000218310.
FT   DOMAIN        7    241       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING      52     90       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   REGION       17     19       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      183    185       Peptide substrate binding. {ECO:0000250}.
FT   REGION      206    207       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   REGION      258    260       S-adenosyl-L-methionine binding.
FT                                {ECO:0000250}.
FT   BINDING     137    137       S-adenosyl-L-methionine.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00190}.
FT   BINDING     240    240       Peptide substrate; via carbonyl oxygen.
FT                                {ECO:0000250}.
FT   MOD_RES     283    283       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9NRG4}.
FT   MUTAGEN     240    240       Y->F: Abolishes methyltransferase
FT                                activity. {ECO:0000269|PubMed:16805913}.
FT   STRAND        9     13       {ECO:0000244|PDB:3QWW}.
FT   STRAND       19     25       {ECO:0000244|PDB:3QWW}.
FT   STRAND       32     37       {ECO:0000244|PDB:3QWW}.
FT   STRAND       39     43       {ECO:0000244|PDB:3QWW}.
FT   HELIX        45     47       {ECO:0000244|PDB:3QWW}.
FT   TURN         48     50       {ECO:0000244|PDB:3QWW}.
FT   TURN         53     55       {ECO:0000244|PDB:3QWW}.
FT   TURN         66     68       {ECO:0000244|PDB:3QWW}.
FT   STRAND       72     75       {ECO:0000244|PDB:3QWW}.
FT   HELIX        76     86       {ECO:0000244|PDB:3QWW}.
FT   TURN         87     89       {ECO:0000244|PDB:3QWW}.
FT   HELIX        90     95       {ECO:0000244|PDB:3QWW}.
FT   HELIX       104    118       {ECO:0000244|PDB:3QWW}.
FT   HELIX       124    126       {ECO:0000244|PDB:3QWW}.
FT   HELIX       131    133       {ECO:0000244|PDB:3QWW}.
FT   HELIX       138    140       {ECO:0000244|PDB:3QWW}.
FT   HELIX       143    160       {ECO:0000244|PDB:3QWW}.
FT   TURN        161    163       {ECO:0000244|PDB:3QWW}.
FT   HELIX       169    182       {ECO:0000244|PDB:3QWW}.
FT   STRAND      184    187       {ECO:0000244|PDB:3QWW}.
FT   STRAND      193    198       {ECO:0000244|PDB:3QWW}.
FT   HELIX       202    204       {ECO:0000244|PDB:3QWW}.
FT   STRAND      205    207       {ECO:0000244|PDB:3QWW}.
FT   STRAND      212    218       {ECO:0000244|PDB:3QWW}.
FT   STRAND      221    228       {ECO:0000244|PDB:3QWW}.
FT   STRAND      235    238       {ECO:0000244|PDB:3QWW}.
FT   HELIX       247    258       {ECO:0000244|PDB:3QWW}.
FT   HELIX       265    269       {ECO:0000244|PDB:3QWW}.
FT   HELIX       273    276       {ECO:0000244|PDB:3QWW}.
FT   HELIX       288    308       {ECO:0000244|PDB:3QWW}.
FT   TURN        309    311       {ECO:0000244|PDB:3QWW}.
FT   HELIX       314    328       {ECO:0000244|PDB:3QWW}.
FT   TURN        329    331       {ECO:0000244|PDB:3QWW}.
FT   HELIX       337    352       {ECO:0000244|PDB:3QWW}.
FT   HELIX       356    373       {ECO:0000244|PDB:3QWW}.
FT   HELIX       379    394       {ECO:0000244|PDB:3QWW}.
FT   HELIX       398    415       {ECO:0000244|PDB:3QWW}.
FT   HELIX       421    431       {ECO:0000244|PDB:3QWW}.
SQ   SEQUENCE   433 AA;  49567 MW;  5978E9A3FC2CDCE4 CRC64;
     MRAEARGGLE RFCSAGKGRG LRALRPFHVG DLLFSCPAYA CVLTVGERGH HCECCFARKE
     GLSKCGRCKQ AFYCDVECQK EDWPLHKLEC SSMVVLGENW NPSETVRLTA RILAKQKIHP
     ERTPSEKLLA VREFESHLDK LDNEKKDLIQ SDIAALHQFY SKYLEFPDHS SLVVLFAQVN
     CNGFTIEDEE LSHLGSAIFP DVALMNHSCC PNVIVTYKGT LAEVRAVQEI HPGDEVFTSY
     IDLLYPTEDR NDRLRDSYFF TCECRECTTK DKDKAKVEVR KLSSPPQAEA IRDMVRYARN
     VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC LYMQDWEGAL
     KYGQKIIKPY SKHYPVYSLN VASMWLKLGR LYMGLENKAA GEKALKKAIA IMEVAHGKDH
     PYISEIKQEI ESH
//
DBGET integrated database retrieval system