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Histone-lysine N-methyltransferase set1 (EC 2.1.1.43) (Histone H3 lysine 4 methyltransferase) (SET domain-containing protein 1)

 SET1_DICDI              Reviewed;        1486 AA.
Q54HS3;
07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
24-MAY-2005, sequence version 1.
25-OCT-2017, entry version 96.
RecName: Full=Histone-lysine N-methyltransferase set1;
EC=2.1.1.43;
AltName: Full=Histone H3 lysine 4 methyltransferase;
AltName: Full=SET domain-containing protein 1;
Name=set1; Synonyms=H3K4; ORFNames=DDB_G0289257;
Dictyostelium discoideum (Slime mold).
Eukaryota; Amoebozoa; Mycetozoa; Dictyosteliida; Dictyostelium.
NCBI_TaxID=44689;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AX4;
PubMed=15875012; DOI=10.1038/nature03481;
Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A.,
Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
Knights A., Loulseged H., Mungall K.L., Oliver K., Price C.,
Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
Kuspa A.;
"The genome of the social amoeba Dictyostelium discoideum.";
Nature 435:43-57(2005).
[2]
DISRUPTION PHENOTYPE, FUNCTION, MUTAGENESIS OF ASN-1425 AND CYS-1474,
AND SUBCELLULAR LOCATION.
PubMed=16469305; DOI=10.1016/j.ydbio.2005.12.054;
Chubb J.R., Bloomfield G., Xu Q., Kaller M., Ivens A., Skelton J.,
Turner B.M., Nellen W., Shaulsky G., Kay R.R., Bickmore W.A.,
Singer R.H.;
"Developmental timing in Dictyostelium is regulated by the Set1
histone methyltransferase.";
Dev. Biol. 292:519-532(2006).
-!- FUNCTION: Histone methyltransferase that specifically mono-,
di- and trimethylates histone H3 to form H3K4me1/2/3. May act to
regulate chromatin-mediated events. {ECO:0000269|PubMed:16469305}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16469305}.
Chromosome {ECO:0000305|PubMed:16469305}.
-!- DISRUPTION PHENOTYPE: Cells display unusually rapid development,
characterized by precocious aggregation into multicellular
aggregates, and completely lack mono-, di- and trimethylation of
H3K4 ('Lys-5' of histone 3). Cells also induce premature
differentiation. {ECO:0000269|PubMed:16469305}.
-!- SIMILARITY: Belongs to the class V-like SAM-binding
methyltransferase superfamily. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
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EMBL; AAFI02000132; EAL62816.1; -; Genomic_DNA.
RefSeq; XP_636258.1; XM_631166.1.
ProteinModelPortal; Q54HS3; -.
SMR; Q54HS3; -.
STRING; 44689.DDB0233375; -.
iPTMnet; Q54HS3; -.
PaxDb; Q54HS3; -.
EnsemblProtists; EAL62816; EAL62816; DDB_G0289257.
GeneID; 8627040; -.
KEGG; ddi:DDB_G0289257; -.
dictyBase; DDB_G0289257; set1.
eggNOG; KOG1080; Eukaryota.
eggNOG; COG2940; LUCA.
InParanoid; Q54HS3; -.
KO; K11422; -.
OMA; WERDRDW; -.
Reactome; R-DDI-3214841; PKMTs methylate histone lysines.
PRO; PR:Q54HS3; -.
Proteomes; UP000002195; Chromosome 5.
Proteomes; UP000002195; Unassembled WGS sequence.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IC:dictyBase.
GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IMP:dictyBase.
GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
GO; GO:0016571; P:histone methylation; IMP:dictyBase.
GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:dictyBase.
InterPro; IPR003616; Post-SET_dom.
InterPro; IPR035979; RBD_domain_sf.
InterPro; IPR001214; SET_dom.
Pfam; PF00856; SET; 1.
SMART; SM00508; PostSET; 1.
SMART; SM00317; SET; 1.
SUPFAM; SSF54928; SSF54928; 1.
PROSITE; PS50868; POST_SET; 1.
PROSITE; PS50280; SET; 1.
1: Evidence at protein level;
Activator; Chromatin regulator; Chromosome; Coiled coil;
Complete proteome; Methyltransferase; Nucleus; Reference proteome;
S-adenosyl-L-methionine; Transferase.
CHAIN 1 1486 Histone-lysine N-methyltransferase set1.
/FTId=PRO_0000379483.
DOMAIN 1347 1464 SET. {ECO:0000255|PROSITE-
ProRule:PRU00190}.
DOMAIN 1470 1486 Post-SET. {ECO:0000255|PROSITE-
ProRule:PRU00155}.
COILED 359 400 {ECO:0000255}.
COILED 717 744 {ECO:0000255}.
COILED 1177 1255 {ECO:0000255}.
COMPBIAS 30 44 Poly-Asn.
COMPBIAS 45 50 Poly-Thr.
COMPBIAS 116 140 Thr-rich.
COMPBIAS 143 148 Poly-Asn.
COMPBIAS 225 237 Poly-Thr.
COMPBIAS 321 332 Poly-Pro.
COMPBIAS 335 340 Poly-Pro.
COMPBIAS 360 392 Poly-Gln.
COMPBIAS 455 542 Arg-rich.
COMPBIAS 553 585 Thr-rich.
COMPBIAS 619 625 Poly-Ser.
COMPBIAS 627 662 Poly-Asn.
COMPBIAS 884 889 Poly-Gln.
COMPBIAS 912 915 Poly-Asn.
COMPBIAS 916 930 Poly-Asp.
COMPBIAS 958 962 Poly-Asp.
COMPBIAS 963 979 Poly-His.
COMPBIAS 1066 1076 Poly-Thr.
COMPBIAS 1219 1223 Poly-Asn.
COMPBIAS 1295 1307 Poly-Ser.
MUTAGEN 1425 1425 N->Q: Loss of catalytic activity; when
associated with Ala-1474.
{ECO:0000269|PubMed:16469305}.
MUTAGEN 1474 1474 C->A: Loss of catalytic activity; when
associated with Gln-1425.
{ECO:0000269|PubMed:16469305}.
SEQUENCE 1486 AA; 170527 MW; F46F71F1A5DFBFFC CRC64;
MENETIVDNS LNNKSNVNNS NNDINNSKSN NNNTNTNYNN NHNNTTTTTT INKTEEKQND
SPKDSEFEFL DELKGVDDQH HVFSSEDESY TNGNKKRKQT DTPLSPNQDL KKRSITSPTT
SPTTSTSTST STSTSTSTST IINNNNNNLK DKTKEEIEFI KHIRSQLVKP KFLKDKPNFP
LRSSGGNWIF VGKLPSLQST TTDNTTLMSP NNATTTNGSS SNISTTTTTT TTTTPTTKIL
YRVNGFLSDN ETIDSIEINF GDPRDRYEIE RLHSSRINNP FELPCVSFKN PLFIKSNIAK
DIGISNEYGG MNDSFEFSNQ PPPPSPPPPP PPTLPPPPPP TLPPQHSLEQ QSTKQQIFTQ
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQIPKINQQH YSTQPSVLID DIYDPSNPTE
PISPHQDHYP NFIFSKLQRY EHLPTRNPIS QYDYRDRPRD WERDRDRDWE RDRDWERDRD
RERDRDRDRD WERDRDWERD RDWERDRDRD RDWERDRDRD WERDRDRDWE RDRERDRDRY
DRQTNFSPAP QSTTTSASTS STTSSTDKNS NNTTSTSVSA TTSTTKRKSK FSEPIEPSPF
AIQIPRDNIK INGNLINNSS SSSSSGNNNN NNNNNNNNNN NNNNNNNNNN NNNNNSNNNN
NNSDVKDIKD KLLKQFKIYD PVNVYMDESY WYIDFRSSES RERAIQVLNG SFIDTWKLNV
DNKKTNTINE ELQKQKQLEN DSNNNKPNNF NLLENERSLK EICKLLVATE LLSTSSKDIS
KNFIEAEILK TIKLLDSQRI DPLTQNSTII NNTTNTTTSN INNTSNNTTV TPIVTPKSII
SAPTSRDSPR GGRSSSTTTK KPSKLDLNGS GVPPTLKKLD TIKQQQQPQP PLSPLKRPPK
SHFYSDSEDD GNNNNDDDDD DDDDEDDDFD QELSPLHSSR DSKKNIKSII KKKPIYSDDD
DDHYHHHNHH HNHHHHHHHD RSEVELYNES DLQVDVLDSD NENQDESDYH KSSDNFGHVE
LSDDDNEFDS LDTDQDLYDT EENDNGKKSN KRPRKSKFNG KSKKPTTTTS TTTTATKSKG
RSKKTTITTP THNIPVLDEI QSNLDDEDAS YVSMVMAADK DIKLLFSTKS EEGFEDSSQE
ILSTPTRTKP SRNRKERNLP FLDEEDDESF KQLPQPQQKQ EKQEKHEHKL KNKELKQKNN
EVIINKTEEH FSENLNGDNN NNNDKSENEN ENENENKNEN ENDNNNLNTS IDNINGVERR
SITGCARSEG YTRSDIQKLF KRKQVAPTGK RGAASSASSG SNSSSSSTAE SFETGGNLSK
SARSSRFDNR GFGSDPITLA SLKSRRKRIK FERSDIHDWG LFAMETISAK DMVIEYIGEV
IRQKVADERE KRYVKKGIGS SYLFRVDDDT IIDATFKGNL ARFINHCCDP NCIAKVLTIG
NQKKIIIYAK RDINIGEEIT YDYKFPIEDV KIPCLCKSPK CRQTLN


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