SET1_DICDI
ID SET1_DICDI Reviewed; 1486 AA.
AC Q54HS3;
DT 07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Histone-lysine N-methyltransferase set1;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9UPS6};
DE AltName: Full=Histone H3 lysine 4 methyltransferase;
DE AltName: Full=SET domain-containing protein 1;
GN Name=set1; Synonyms=H3K4; ORFNames=DDB_G0289257;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP DISRUPTION PHENOTYPE, FUNCTION, MUTAGENESIS OF ASN-1425 AND CYS-1474, AND
RP SUBCELLULAR LOCATION.
RX PubMed=16469305; DOI=10.1016/j.ydbio.2005.12.054;
RA Chubb J.R., Bloomfield G., Xu Q., Kaller M., Ivens A., Skelton J.,
RA Turner B.M., Nellen W., Shaulsky G., Kay R.R., Bickmore W.A., Singer R.H.;
RT "Developmental timing in Dictyostelium is regulated by the Set1 histone
RT methyltransferase.";
RL Dev. Biol. 292:519-532(2006).
CC -!- FUNCTION: Histone methyltransferase that specifically mono-, di- and
CC trimethylates histone H3 to form H3K4me1/2/3. May act to regulate
CC chromatin-mediated events. {ECO:0000269|PubMed:16469305}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16469305}. Chromosome
CC {ECO:0000305|PubMed:16469305}.
CC -!- DISRUPTION PHENOTYPE: Cells display unusually rapid development,
CC characterized by precocious aggregation into multicellular aggregates,
CC and completely lack mono-, di- and trimethylation of H3K4 ('Lys-5' of
CC histone 3). Cells also induce premature differentiation.
CC {ECO:0000269|PubMed:16469305}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; AAFI02000132; EAL62816.1; -; Genomic_DNA.
DR RefSeq; XP_636258.1; XM_631166.1.
DR AlphaFoldDB; Q54HS3; -.
DR SMR; Q54HS3; -.
DR STRING; 44689.DDB0233375; -.
DR PaxDb; Q54HS3; -.
DR PRIDE; Q54HS3; -.
DR EnsemblProtists; EAL62816; EAL62816; DDB_G0289257.
DR GeneID; 8627040; -.
DR KEGG; ddi:DDB_G0289257; -.
DR dictyBase; DDB_G0289257; set1.
DR eggNOG; KOG1080; Eukaryota.
DR eggNOG; KOG2217; Eukaryota.
DR HOGENOM; CLU_249415_0_0_1; -.
DR InParanoid; Q54HS3; -.
DR OMA; NCIAKVL; -.
DR Reactome; R-DDI-3214841; PKMTs methylate histone lysines.
DR PRO; PR:Q54HS3; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IC:dictyBase.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IMP:dictyBase.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0031152; P:aggregation involved in sorocarp development; IMP:dictyBase.
DR GO; GO:0051568; P:histone H3-K4 methylation; IBA:GO_Central.
DR GO; GO:0016571; P:histone methylation; IMP:dictyBase.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:dictyBase.
DR Gene3D; 2.170.270.10; -; 1.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Chromosome; Coiled coil; Methyltransferase;
KW Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..1486
FT /note="Histone-lysine N-methyltransferase set1"
FT /id="PRO_0000379483"
FT DOMAIN 1347..1464
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1470..1486
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 83..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1130..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 359..400
FT /evidence="ECO:0000255"
FT COILED 717..744
FT /evidence="ECO:0000255"
FT COILED 1177..1255
FT /evidence="ECO:0000255"
FT COMPBIAS 1..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..345
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..865
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 910..931
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 951..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1024
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1025..1039
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1224..1240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1291..1327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 1425
FT /note="N->Q: Loss of catalytic activity; when associated
FT with Ala-1474."
FT /evidence="ECO:0000269|PubMed:16469305"
FT MUTAGEN 1474
FT /note="C->A: Loss of catalytic activity; when associated
FT with Gln-1425."
FT /evidence="ECO:0000269|PubMed:16469305"
SQ 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
