GenomeNet

Database: UniProt
Entry: Q86TU7
LinkDB: Q86TU7
Original site: Q86TU7 
ID   SETD3_HUMAN             Reviewed;         594 AA.
AC   Q86TU7; A0PJU3; A5PLP0; B4DZE8; Q0VAQ2; Q659C0; Q86TU8; Q96GY9;
AC   Q9H5U5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   10-APR-2019, entry version 134.
DE   RecName: Full=Actin-histidine N-methyltransferase {ECO:0000305};
DE            EC=2.1.1.85 {ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964};
DE   AltName: Full=SET domain-containing protein 3 {ECO:0000305};
DE            Short=hSETD3 {ECO:0000303|PubMed:28442573};
GN   Name=SETD3 {ECO:0000303|PubMed:30526847, ECO:0000303|PubMed:30626964,
GN   ECO:0000312|HGNC:HGNC:20493};
GN   Synonyms=C14orf154 {ECO:0000312|HGNC:HGNC:20493};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Placenta;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Lung, and Testis;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12508121; DOI=10.1038/nature01348;
RA   Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA   Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA   Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S.,
RA   Sun H., Du H., Pepin K., Artiguenave F., Robert C., Cruaud C.,
RA   Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P.,
RA   Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N.,
RA   Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C.,
RA   Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S.,
RA   Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B.,
RA   Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M.,
RA   Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S.,
RA   Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D.,
RA   Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A.,
RA   Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA   Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA   Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L.,
RA   Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J.,
RA   Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W.,
RA   Quetier F., Waterston R., Hood L., Weissenbach J.;
RT   "The DNA sequence and analysis of human chromosome 14.";
RL   Nature 421:601-607(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Eye;
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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 215-594 (ISOFORM 1).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, UBIQUITINATION,
RP   PHOSPHORYLATION, AND MUTAGENESIS OF 37-SER--GLY-42; 181-SER--THR-185;
RP   260-THR--SER-264; 373-THR--SER-378; 512-SER--SER-517 AND
RP   565-SER--SER-569.
RX   PubMed=28442573; DOI=10.1074/jbc.M117.778001;
RA   Cheng X., Hao Y., Shu W., Zhao M., Zhao C., Wu Y., Peng X., Yao P.,
RA   Xiao D., Qing G., Pan Z., Yin L., Hu D., Du H.N.;
RT   "Cell cycle-dependent degradation of the methyltransferase SETD3
RT   attenuates cell proliferation and liver tumorigenesis.";
RL   J. Biol. Chem. 292:9022-9033(2017).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=30526847; DOI=10.7554/eLife.37921;
RA   Kwiatkowski S., Seliga A.K., Vertommen D., Terreri M., Ishikawa T.,
RA   Grabowska I., Tiebe M., Teleman A.A., Jagielski A.K.,
RA   Veiga-da-Cunha M., Drozak J.;
RT   "SETD3 protein is the actin-specific histidine N-methyltransferase.";
RL   Elife 7:0-0(2018).
RN   [12] {ECO:0000244|PDB:3SMT}
RP   X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 2-498 IN COMPLEX WITH
RP   S-ADENOSYL-L-METHIONINE.
RA   Zeng H., Dong A., Walker J.R., Loppnau P., Bountra C., Weigelt J.,
RA   Arrowsmith C.H., Edwards A.M., Min J., Wu H.;
RT   "Crystal structure of human SET domain-containing protein 3.";
RL   Submitted (JUN-2011) to the PDB data bank.
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 21-503 IN COMPLEX WITH ACTIN
RP   AND S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR
RP   LOCATION, DOMAIN, AND MUTAGENESIS OF TYR-313.
RX   PubMed=30626964; DOI=10.1038/s41586-018-0821-8;
RA   Wilkinson A.W., Diep J., Dai S., Liu S., Ooi Y.S., Song D., Li T.M.,
RA   Horton J.R., Zhang X., Liu C., Trivedi D.V., Ruppel K.M.,
RA   Vilches-Moure J.G., Casey K.M., Mak J., Cowan T., Elias J.E.,
RA   Nagamine C.M., Spudich J.A., Cheng X., Carette J.E., Gozani O.;
RT   "SETD3 is an actin histidine methyltransferase that prevents primary
RT   dystocia.";
RL   Nature 0:0-0(2019).
CC   -!- FUNCTION: Protein-histidine N-methyltransferase that specifically
CC       mediates methylation of actin at 'His-73' (PubMed:30526847,
CC       PubMed:30626964). Histidine methylation of actin is required for
CC       smooth muscle contraction of the laboring uterus during delivery
CC       (PubMed:30626964). Does not have protein-lysine N-
CC       methyltransferase activity and probably only catalyzes histidine
CC       methylation of actin (PubMed:30626964).
CC       {ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidyl-[protein] + S-adenosyl-L-methionine = H(+) +
CC         N(tele)-methyl-L-histidyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:19369, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:11600,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16367, ChEBI:CHEBI:29979,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.85;
CC         Evidence={ECO:0000269|PubMed:30526847,
CC         ECO:0000269|PubMed:30626964};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19370;
CC         Evidence={ECO:0000269|PubMed:30526847,
CC         ECO:0000269|PubMed:30626964};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.752 uM for beta-actin {ECO:0000269|PubMed:30526847};
CC         KM=0.116 uM for S-adenosyl-L-methionine
CC         {ECO:0000269|PubMed:30526847};
CC         Vmax=9.091 nmol/min/mg enzyme with beta-actin as substrate
CC         {ECO:0000269|PubMed:30526847};
CC         Vmax=8.649 nmol/min/mg enzyme with S-adenosyl-L-methionine as
CC         substrate {ECO:0000269|PubMed:30526847};
CC         Note=Kcat is 0.65 min(-1) with beta-actin as substrate
CC         (PubMed:30526847). Kcat is 0.61 min(-1) with S-adenosyl-L-
CC         methionine as substrate (PubMed:30526847).
CC         {ECO:0000269|PubMed:30526847};
CC   -!- SUBUNIT: Interacts with MYOD1. {ECO:0000250|UniProtKB:Q91WC0}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28442573,
CC       ECO:0000269|PubMed:30626964}. Nucleus
CC       {ECO:0000269|PubMed:28442573}. Note=Localizes mainly in the
CC       cytoplasm. {ECO:0000269|PubMed:28442573}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q86TU7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86TU7-2; Sequence=VSP_021190, VSP_021193;
CC       Name=3;
CC         IsoId=Q86TU7-3; Sequence=VSP_021191, VSP_021192;
CC   -!- DEVELOPMENTAL STAGE: Protein levels peak in S phase and are lowest
CC       during M phase (at protein level). {ECO:0000269|PubMed:28442573}.
CC   -!- DOMAIN: The SET domain specifically recognizes and binds actin,
CC       suggesting that it does not accommodate substrates diverging from
CC       actin. {ECO:0000269|PubMed:30626964}.
CC   -!- PTM: Phosphorylated by GSK3B, which is required for recognition by
CC       the SCF(FBXW7) complex and subsequent degradation.
CC       {ECO:0000269|PubMed:28442573}.
CC   -!- PTM: Ubiquitinated by the SCF(FBXW7) complex following
CC       phosphorylation by GSK3B, leading to its degration by the
CC       proteasome. {ECO:0000269|PubMed:28442573}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SETD3 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00898}.
CC   -!- CAUTION: Was initially reported to have histone methyltransferase
CC       activity and methylate 'Lys-4' and 'Lys-36' of histone H3 (H3K4me
CC       and H3K36me) (By similarity). However, this conclusion was based
CC       on mass spectrometry data wherin mass shifts were inconsistent
CC       with a bona fide methylation event (PubMed:30626964). In vitro,
CC       the protein-lysine methyltransferase activity is weak compared to
CC       the protein-histidine methyltransferase activity
CC       (PubMed:30526847). {ECO:0000250|UniProtKB:Q91WC0,
CC       ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15525.1; Type=Frameshift; Positions=486, 495; Evidence={ECO:0000305};
DR   EMBL; BX161441; CAD61911.1; -; mRNA.
DR   EMBL; BX161471; CAD61927.1; -; mRNA.
DR   EMBL; AK026680; BAB15525.1; ALT_FRAME; mRNA.
DR   EMBL; AK302882; BAG64060.1; -; mRNA.
DR   EMBL; AL110504; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL132819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471061; EAW81664.1; -; Genomic_DNA.
DR   EMBL; CH471061; EAW81665.1; -; Genomic_DNA.
DR   EMBL; BC009054; AAH09054.2; -; mRNA.
DR   EMBL; BC120967; AAI20968.1; -; mRNA.
DR   EMBL; BC120968; AAI20969.1; -; mRNA.
DR   EMBL; BC127624; AAI27625.1; -; mRNA.
DR   EMBL; BC127625; AAI27626.1; -; mRNA.
DR   EMBL; BC142995; AAI42996.1; -; mRNA.
DR   EMBL; BC148251; AAI48252.1; -; mRNA.
DR   EMBL; AL359581; CAH56365.1; -; mRNA.
DR   CCDS; CCDS9951.1; -. [Q86TU7-1]
DR   CCDS; CCDS9952.1; -. [Q86TU7-2]
DR   PIR; T50614; T50614.
DR   RefSeq; NP_115609.2; NM_032233.2. [Q86TU7-1]
DR   RefSeq; NP_954574.1; NM_199123.1. [Q86TU7-2]
DR   RefSeq; XP_011535533.2; XM_011537231.2. [Q86TU7-1]
DR   RefSeq; XP_011535534.1; XM_011537232.2. [Q86TU7-1]
DR   RefSeq; XP_011535537.1; XM_011537235.1. [Q86TU7-2]
DR   RefSeq; XP_016877188.1; XM_017021699.1. [Q86TU7-1]
DR   RefSeq; XP_016877189.1; XM_017021700.1. [Q86TU7-1]
DR   UniGene; Hs.510407; -.
DR   PDB; 3SMT; X-ray; 2.04 A; A=2-498.
DR   PDB; 6MBJ; X-ray; 1.78 A; A/B=21-500, A/B=1-594.
DR   PDB; 6MBK; X-ray; 1.69 A; A/B=21-503, A/B=1-594.
DR   PDB; 6MBL; X-ray; 2.20 A; A=21-500, A=1-594.
DR   PDBsum; 3SMT; -.
DR   PDBsum; 6MBJ; -.
DR   PDBsum; 6MBK; -.
DR   PDBsum; 6MBL; -.
DR   ProteinModelPortal; Q86TU7; -.
DR   SMR; Q86TU7; -.
DR   BioGrid; 123940; 18.
DR   IntAct; Q86TU7; 3.
DR   MINT; Q86TU7; -.
DR   STRING; 9606.ENSP00000327436; -.
DR   iPTMnet; Q86TU7; -.
DR   PhosphoSitePlus; Q86TU7; -.
DR   BioMuta; SETD3; -.
DR   DMDM; 74750394; -.
DR   EPD; Q86TU7; -.
DR   jPOST; Q86TU7; -.
DR   MaxQB; Q86TU7; -.
DR   PaxDb; Q86TU7; -.
DR   PeptideAtlas; Q86TU7; -.
DR   PRIDE; Q86TU7; -.
DR   ProteomicsDB; 69732; -.
DR   ProteomicsDB; 69733; -. [Q86TU7-2]
DR   ProteomicsDB; 69734; -. [Q86TU7-3]
DR   Ensembl; ENST00000329331; ENSP00000327910; ENSG00000183576. [Q86TU7-2]
DR   Ensembl; ENST00000331768; ENSP00000327436; ENSG00000183576. [Q86TU7-1]
DR   GeneID; 84193; -.
DR   KEGG; hsa:84193; -.
DR   UCSC; uc001ygc.4; human. [Q86TU7-1]
DR   CTD; 84193; -.
DR   DisGeNET; 84193; -.
DR   EuPathDB; HostDB:ENSG00000183576.12; -.
DR   GeneCards; SETD3; -.
DR   HGNC; HGNC:20493; SETD3.
DR   HPA; HPA003591; -.
DR   HPA; HPA003639; -.
DR   MIM; 615671; gene.
DR   neXtProt; NX_Q86TU7; -.
DR   OpenTargets; ENSG00000183576; -.
DR   PharmGKB; PA134883013; -.
DR   eggNOG; KOG1337; Eukaryota.
DR   eggNOG; ENOG410Y7DR; LUCA.
DR   GeneTree; ENSGT00940000153577; -.
DR   HOGENOM; HOG000041319; -.
DR   HOVERGEN; HBG062823; -.
DR   InParanoid; Q86TU7; -.
DR   KO; K19199; -.
DR   OMA; CERADPN; -.
DR   OrthoDB; 489371at2759; -.
DR   PhylomeDB; Q86TU7; -.
DR   TreeFam; TF354226; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; SETD3; human.
DR   GenomeRNAi; 84193; -.
DR   PRO; PR:Q86TU7; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   Bgee; ENSG00000183576; Expressed in 239 organ(s), highest expression level in testis.
DR   ExpressionAtlas; Q86TU7; baseline and differential.
DR   Genevisible; Q86TU7; HS.
DR   GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); ISS:UniProtKB.
DR   GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0001102; F:RNA polymerase II activating transcription factor binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR   GO; GO:0010452; P:histone H3-K36 methylation; ISS:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; ISS:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0018023; P:peptidyl-lysine trimethylation; ISS:UniProtKB.
DR   GO; GO:0051149; P:positive regulation of muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   Gene3D; 3.90.1420.10; -; 1.
DR   InterPro; IPR025785; Hist-Lys_N-MeTrfase_SETD3.
DR   InterPro; IPR015353; Rubisco_LSMT_subst-bd.
DR   InterPro; IPR036464; Rubisco_LSMT_subst-bd_sf.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF09273; Rubis-subs-bind; 1.
DR   Pfam; PF00856; SET; 1.
DR   SUPFAM; SSF81822; SSF81822; 1.
DR   PROSITE; PS51565; SAM_MT43_SETD3; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Actin-binding; Alternative splicing; Complete proteome;
KW   Cytoplasm; Methyltransferase; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Ubl conjugation.
FT   CHAIN         1    594       Actin-histidine N-methyltransferase.
FT                                /FTId=PRO_0000254175.
FT   DOMAIN       94    314       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      104    106       S-adenosyl-L-methionine binding.
FT                                {ECO:0000244|PDB:3SMT,
FT                                ECO:0000244|PDB:6MBJ,
FT                                ECO:0000244|PDB:6MBK,
FT                                ECO:0000244|PDB:6MBL,
FT                                ECO:0000269|PubMed:30626964,
FT                                ECO:0000269|Ref.12}.
FT   REGION      275    279       S-adenosyl-L-methionine binding.
FT                                {ECO:0000244|PDB:3SMT,
FT                                ECO:0000244|PDB:6MBJ,
FT                                ECO:0000244|PDB:6MBK,
FT                                ECO:0000244|PDB:6MBL,
FT                                ECO:0000269|PubMed:30626964,
FT                                ECO:0000269|Ref.12}.
FT   REGION      325    327       S-adenosyl-L-methionine binding.
FT                                {ECO:0000244|PDB:3SMT,
FT                                ECO:0000244|PDB:6MBJ,
FT                                ECO:0000244|PDB:6MBK,
FT                                ECO:0000244|PDB:6MBL,
FT                                ECO:0000269|PubMed:30626964,
FT                                ECO:0000269|Ref.12}.
FT   BINDING      75     75       S-adenosyl-L-methionine.
FT                                {ECO:0000244|PDB:3SMT,
FT                                ECO:0000244|PDB:6MBJ,
FT                                ECO:0000244|PDB:6MBK,
FT                                ECO:0000244|PDB:6MBL,
FT                                ECO:0000269|PubMed:30626964,
FT                                ECO:0000269|Ref.12}.
FT   BINDING     254    254       S-adenosyl-L-methionine.
FT                                {ECO:0000244|PDB:3SMT,
FT                                ECO:0000244|PDB:6MBJ,
FT                                ECO:0000244|PDB:6MBK,
FT                                ECO:0000244|PDB:6MBL,
FT                                ECO:0000269|PubMed:30626964,
FT                                ECO:0000269|Ref.12}.
FT   MOD_RES     513    513       Phosphoserine.
FT                                {ECO:0000244|PubMed:18669648,
FT                                ECO:0000244|PubMed:23186163}.
FT   VAR_SEQ     284    296       ITTGYNLEDDRCE -> TPEDSFALAVASA (in
FT                                isoform 2). {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.1}.
FT                                /FTId=VSP_021190.
FT   VAR_SEQ     284    284       I -> V (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021191.
FT   VAR_SEQ     285    594       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021192.
FT   VAR_SEQ     297    594       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.1}.
FT                                /FTId=VSP_021193.
FT   VARIANT     278    278       N -> D (in dbSNP:rs1740231).
FT                                /FTId=VAR_028830.
FT   MUTAGEN      37     42       SSPAPG->ASPAPA: Does not affect
FT                                ubiquitination and degradation by the
FT                                SCF(FBXW7) complex.
FT                                {ECO:0000269|PubMed:28442573}.
FT   MUTAGEN     181    185       SEYDT->AEYDA: Decreased ubiquitination
FT                                and degradation by the SCF(FBXW7)
FT                                complex. {ECO:0000269|PubMed:28442573}.
FT   MUTAGEN     260    264       TEDGS->AEDGA: Does not affect
FT                                ubiquitination and degradation by the
FT                                SCF(FBXW7) complex.
FT                                {ECO:0000269|PubMed:28442573}.
FT   MUTAGEN     313    313       Y->A: Abolished arotein-histidine N-
FT                                methyltransferase activity.
FT                                {ECO:0000269|PubMed:30626964}.
FT   MUTAGEN     373    378       TEPPIS->AEPPIA: Strongly decreased
FT                                ubiquitination and degradation by the
FT                                SCF(FBXW7) complex.
FT                                {ECO:0000269|PubMed:28442573}.
FT   MUTAGEN     512    517       SSVGDS->ASVGDA: Does not affect
FT                                ubiquitination and degradation by the
FT                                SCF(FBXW7) complex.
FT                                {ECO:0000269|PubMed:28442573}.
FT   MUTAGEN     565    569       SENES->AENEA: Does not affect
FT                                ubiquitination and degradation by the
FT                                SCF(FBXW7) complex.
FT                                {ECO:0000269|PubMed:28442573}.
FT   CONFLICT    415    415       E -> K (in Ref. 5; AAI42996).
FT                                {ECO:0000305}.
FT   HELIX        22     36       {ECO:0000244|PDB:6MBK}.
FT   HELIX        43     45       {ECO:0000244|PDB:6MBK}.
FT   HELIX        46     62       {ECO:0000244|PDB:6MBK}.
FT   HELIX        75     78       {ECO:0000244|PDB:6MBK}.
FT   HELIX        79     88       {ECO:0000244|PDB:6MBK}.
FT   STRAND       94    101       {ECO:0000244|PDB:6MBK}.
FT   TURN        102    104       {ECO:0000244|PDB:6MBK}.
FT   STRAND      105    112       {ECO:0000244|PDB:6MBK}.
FT   STRAND      119    124       {ECO:0000244|PDB:6MBK}.
FT   HELIX       125    127       {ECO:0000244|PDB:6MBK}.
FT   HELIX       131    135       {ECO:0000244|PDB:6MBK}.
FT   HELIX       140    143       {ECO:0000244|PDB:6MBK}.
FT   HELIX       147    151       {ECO:0000244|PDB:6MBK}.
FT   HELIX       153    165       {ECO:0000244|PDB:6MBK}.
FT   HELIX       173    176       {ECO:0000244|PDB:6MBK}.
FT   HELIX       186    188       {ECO:0000244|PDB:6MBK}.
FT   HELIX       191    195       {ECO:0000244|PDB:6MBK}.
FT   TURN        196    199       {ECO:0000244|PDB:6MBK}.
FT   HELIX       203    226       {ECO:0000244|PDB:6MBK}.
FT   HELIX       228    230       {ECO:0000244|PDB:6MBK}.
FT   HELIX       234    236       {ECO:0000244|PDB:6MBJ}.
FT   HELIX       241    254       {ECO:0000244|PDB:6MBK}.
FT   STRAND      256    259       {ECO:0000244|PDB:6MBK}.
FT   STRAND      263    270       {ECO:0000244|PDB:6MBK}.
FT   HELIX       274    276       {ECO:0000244|PDB:6MBK}.
FT   STRAND      286    289       {ECO:0000244|PDB:6MBK}.
FT   TURN        290    293       {ECO:0000244|PDB:6MBK}.
FT   STRAND      294    298       {ECO:0000244|PDB:6MBK}.
FT   STRAND      307    311       {ECO:0000244|PDB:6MBK}.
FT   HELIX       318    325       {ECO:0000244|PDB:6MBK}.
FT   STRAND      336    342       {ECO:0000244|PDB:6MBK}.
FT   HELIX       350    359       {ECO:0000244|PDB:6MBK}.
FT   STRAND      364    377       {ECO:0000244|PDB:6MBK}.
FT   HELIX       379    388       {ECO:0000244|PDB:6MBK}.
FT   HELIX       392    399       {ECO:0000244|PDB:6MBK}.
FT   HELIX       404    409       {ECO:0000244|PDB:6MBK}.
FT   TURN        410    412       {ECO:0000244|PDB:6MBK}.
FT   HELIX       420    438       {ECO:0000244|PDB:6MBK}.
FT   STRAND      441    443       {ECO:0000244|PDB:6MBK}.
FT   HELIX       445    454       {ECO:0000244|PDB:6MBK}.
FT   HELIX       459    495       {ECO:0000244|PDB:6MBK}.
SQ   SEQUENCE   594 AA;  67257 MW;  DF27C8B133A19E16 CRC64;
     MGKKSRVKTQ KSGTGATATV SPKEILNLTS ELLQKCSSPA PGPGKEWEEY VQIRTLVEKI
     RKKQKGLSVT FDGKREDYFP DLMKWASENG ASVEGFEMVN FKEEGFGLRA TRDIKAEELF
     LWVPRKLLMT VESAKNSVLG PLYSQDRILQ AMGNIALAFH LLCERASPNS FWQPYIQTLP
     SEYDTPLYFE EDEVRYLQST QAIHDVFSQY KNTARQYAYF YKVIQTHPHA NKLPLKDSFT
     YEDYRWAVSS VMTRQNQIPT EDGSRVTLAL IPLWDMCNHT NGLITTGYNL EDDRCECVAL
     QDFRAGEQIY IFYGTRSNAE FVIHSGFFFD NNSHDRVKIK LGVSKSDRLY AMKAEVLARA
     GIPTSSVFAL HFTEPPISAQ LLAFLRVFCM TEEELKEHLL GDSAIDRIFT LGNSEFPVSW
     DNEVKLWTFL EDRASLLLKT YKTTIEEDKS VLKNHDLSVR AKMAIKLRLG EKEILEKAVK
     SAAVNREYYR QQMEEKAPLP KYEESNLGLL ESSVGDSRLP LVLRNLEEEA GVQDALNIRE
     AISKAKATEN GLVNGENSIP NGTRSENESL NQESKRAVED AKGSSSDSTA GVKE
//
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