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Database: UniProt
Entry: Q54HS3
LinkDB: Q54HS3
Original site: Q54HS3 
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   05-DEC-2018, entry version 102.
DE   RecName: Full=Histone-lysine N-methyltransferase set1;
DE            EC=2.1.1.43;
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; Mycetozoa; Dictyostelids; 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.,
RA   Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q.,
RA   Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F.,
RA   Bankier A.T., Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P.,
RA   Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P.,
RA   Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N.,
RA   Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M.,
RA   Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I.,
RA   Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R.,
RA   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.,
RA   Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D.,
RA   Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S.,
RA   Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T.,
RA   Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A.,
RA   Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M.,
RA   Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G.,
RA   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,
RP   AND 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.,
RA   Singer R.H.;
RT   "Developmental timing in Dictyostelium is regulated by the Set1
RT   histone methyltransferase.";
RL   Dev. Biol. 292:519-532(2006).
CC   -!- FUNCTION: Histone methyltransferase that specifically mono-,
CC       di- and trimethylates histone H3 to form H3K4me1/2/3. May act to
CC       regulate chromatin-mediated events. {ECO:0000269|PubMed:16469305}.
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16469305}.
CC       Chromosome {ECO:0000305|PubMed:16469305}.
CC   -!- DISRUPTION PHENOTYPE: Cells display unusually rapid development,
CC       characterized by precocious aggregation into multicellular
CC       aggregates, and completely lack mono-, di- and trimethylation of
CC       H3K4 ('Lys-5' of histone 3). Cells also induce premature
CC       differentiation. {ECO:0000269|PubMed:16469305}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00190}.
DR   EMBL; AAFI02000132; EAL62816.1; -; Genomic_DNA.
DR   RefSeq; XP_636258.1; XM_631166.1.
DR   ProteinModelPortal; Q54HS3; -.
DR   SMR; Q54HS3; -.
DR   STRING; 44689.DDB0233375; -.
DR   iPTMnet; Q54HS3; -.
DR   PaxDb; 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; COG2940; LUCA.
DR   InParanoid; Q54HS3; -.
DR   KO; K11422; -.
DR   OMA; NCIAKVL; -.
DR   Reactome; R-DDI-3214841; PKMTs methylate histone lysines.
DR   PRO; PR:Q54HS3; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   Proteomes; UP000002195; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IC:dictyBase.
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:0016571; P:histone methylation; IMP:dictyBase.
DR   GO; GO:0040029; P:regulation of gene expression, epigenetic; IMP:dictyBase.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR037861; SETD1-like.
DR   PANTHER; PTHR22884:SF464; PTHR22884:SF464; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00508; PostSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF54928; SSF54928; 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;
KW   Complete proteome; Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN         1   1486       Histone-lysine N-methyltransferase set1.
FT                                /FTId=PRO_0000379483.
FT   DOMAIN     1347   1464       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1470   1486       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   COILED      359    400       {ECO:0000255}.
FT   COILED      717    744       {ECO:0000255}.
FT   COILED     1177   1255       {ECO:0000255}.
FT   COMPBIAS     30     44       Poly-Asn.
FT   COMPBIAS     45     50       Poly-Thr.
FT   COMPBIAS    116    140       Thr-rich.
FT   COMPBIAS    143    148       Poly-Asn.
FT   COMPBIAS    225    237       Poly-Thr.
FT   COMPBIAS    321    332       Poly-Pro.
FT   COMPBIAS    335    340       Poly-Pro.
FT   COMPBIAS    360    392       Poly-Gln.
FT   COMPBIAS    455    542       Arg-rich.
FT   COMPBIAS    553    585       Thr-rich.
FT   COMPBIAS    619    625       Poly-Ser.
FT   COMPBIAS    627    662       Poly-Asn.
FT   COMPBIAS    884    889       Poly-Gln.
FT   COMPBIAS    912    915       Poly-Asn.
FT   COMPBIAS    916    930       Poly-Asp.
FT   COMPBIAS    958    962       Poly-Asp.
FT   COMPBIAS    963    979       Poly-His.
FT   COMPBIAS   1066   1076       Poly-Thr.
FT   COMPBIAS   1219   1223       Poly-Asn.
FT   COMPBIAS   1295   1307       Poly-Ser.
FT   MUTAGEN    1425   1425       N->Q: Loss of catalytic activity; when
FT                                associated with Ala-1474.
FT                                {ECO:0000269|PubMed:16469305}.
FT   MUTAGEN    1474   1474       C->A: Loss of catalytic activity; when
FT                                associated with Gln-1425.
FT                                {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
//
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