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Q54HS3 (SET1_DICDI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone-lysine N-methyltransferase set1

EC=2.1.1.43
Alternative name(s):
Histone H3 lysine 4 methyltransferase
SET domain-containing protein 1
Gene names
Name:set1
Synonyms:H3K4
ORF Names:DDB_G0289257
OrganismDictyostelium discoideum (Slime mold) [Reference proteome]
Taxonomic identifier44689 [NCBI]
Taxonomic lineageEukaryotaAmoebozoaMycetozoaDictyosteliidaDictyostelium

Protein attributes

Sequence length1486 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Histone methyltransferase that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3. May act to regulate chromatin-mediated events. Ref.2

Catalytic activity

S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].

Subcellular location

Nucleus. Chromosome Probable Ref.2.

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. Ref.2

Sequence similarities

Belongs to the class V-like SAM-binding methyltransferase superfamily.

Contains 1 post-SET domain.

Contains 1 SET domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14861486Histone-lysine N-methyltransferase set1
PRO_0000379483

Regions

Domain1347 – 1464118SET
Domain1470 – 148617Post-SET
Coiled coil359 – 40042 Potential
Coiled coil717 – 74428 Potential
Coiled coil1177 – 125579 Potential
Compositional bias30 – 4415Poly-Asn
Compositional bias45 – 506Poly-Thr
Compositional bias116 – 14025Thr-rich
Compositional bias143 – 1486Poly-Asn
Compositional bias225 – 23713Poly-Thr
Compositional bias321 – 33212Poly-Pro
Compositional bias335 – 3406Poly-Pro
Compositional bias360 – 39233Poly-Gln
Compositional bias455 – 54288Arg-rich
Compositional bias553 – 58533Thr-rich
Compositional bias619 – 6257Poly-Ser
Compositional bias627 – 66236Poly-Asn
Compositional bias884 – 8896Poly-Gln
Compositional bias912 – 9154Poly-Asn
Compositional bias916 – 93015Poly-Asp
Compositional bias958 – 9625Poly-Asp
Compositional bias963 – 97917Poly-His
Compositional bias1066 – 107611Poly-Thr
Compositional bias1219 – 12235Poly-Asn
Compositional bias1295 – 130713Poly-Ser

Experimental info

Mutagenesis14251N → Q: Loss of catalytic activity; when associated with Ala-1474. Ref.2
Mutagenesis14741C → A: Loss of catalytic activity; when associated with Gln-1425. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q54HS3 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: F46F71F1A5DFBFFC

FASTA1,486170,527
        10         20         30         40         50         60 
MENETIVDNS LNNKSNVNNS NNDINNSKSN NNNTNTNYNN NHNNTTTTTT INKTEEKQND 

        70         80         90        100        110        120 
SPKDSEFEFL DELKGVDDQH HVFSSEDESY TNGNKKRKQT DTPLSPNQDL KKRSITSPTT 

       130        140        150        160        170        180 
SPTTSTSTST STSTSTSTST IINNNNNNLK DKTKEEIEFI KHIRSQLVKP KFLKDKPNFP 

       190        200        210        220        230        240 
LRSSGGNWIF VGKLPSLQST TTDNTTLMSP NNATTTNGSS SNISTTTTTT TTTTPTTKIL 

       250        260        270        280        290        300 
YRVNGFLSDN ETIDSIEINF GDPRDRYEIE RLHSSRINNP FELPCVSFKN PLFIKSNIAK 

       310        320        330        340        350        360 
DIGISNEYGG MNDSFEFSNQ PPPPSPPPPP PPTLPPPPPP TLPPQHSLEQ QSTKQQIFTQ 

       370        380        390        400        410        420 
QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQQ QQIPKINQQH YSTQPSVLID DIYDPSNPTE 

       430        440        450        460        470        480 
PISPHQDHYP NFIFSKLQRY EHLPTRNPIS QYDYRDRPRD WERDRDRDWE RDRDWERDRD 

       490        500        510        520        530        540 
RERDRDRDRD WERDRDWERD RDWERDRDRD RDWERDRDRD WERDRDRDWE RDRERDRDRY 

       550        560        570        580        590        600 
DRQTNFSPAP QSTTTSASTS STTSSTDKNS NNTTSTSVSA TTSTTKRKSK FSEPIEPSPF 

       610        620        630        640        650        660 
AIQIPRDNIK INGNLINNSS SSSSSGNNNN NNNNNNNNNN NNNNNNNNNN NNNNNSNNNN 

       670        680        690        700        710        720 
NNSDVKDIKD KLLKQFKIYD PVNVYMDESY WYIDFRSSES RERAIQVLNG SFIDTWKLNV 

       730        740        750        760        770        780 
DNKKTNTINE ELQKQKQLEN DSNNNKPNNF NLLENERSLK EICKLLVATE LLSTSSKDIS 

       790        800        810        820        830        840 
KNFIEAEILK TIKLLDSQRI DPLTQNSTII NNTTNTTTSN INNTSNNTTV TPIVTPKSII 

       850        860        870        880        890        900 
SAPTSRDSPR GGRSSSTTTK KPSKLDLNGS GVPPTLKKLD TIKQQQQPQP PLSPLKRPPK 

       910        920        930        940        950        960 
SHFYSDSEDD GNNNNDDDDD DDDDEDDDFD QELSPLHSSR DSKKNIKSII KKKPIYSDDD 

       970        980        990       1000       1010       1020 
DDHYHHHNHH HNHHHHHHHD RSEVELYNES DLQVDVLDSD NENQDESDYH KSSDNFGHVE 

      1030       1040       1050       1060       1070       1080 
LSDDDNEFDS LDTDQDLYDT EENDNGKKSN KRPRKSKFNG KSKKPTTTTS TTTTATKSKG 

      1090       1100       1110       1120       1130       1140 
RSKKTTITTP THNIPVLDEI QSNLDDEDAS YVSMVMAADK DIKLLFSTKS EEGFEDSSQE 

      1150       1160       1170       1180       1190       1200 
ILSTPTRTKP SRNRKERNLP FLDEEDDESF KQLPQPQQKQ EKQEKHEHKL KNKELKQKNN 

      1210       1220       1230       1240       1250       1260 
EVIINKTEEH FSENLNGDNN NNNDKSENEN ENENENKNEN ENDNNNLNTS IDNINGVERR 

      1270       1280       1290       1300       1310       1320 
SITGCARSEG YTRSDIQKLF KRKQVAPTGK RGAASSASSG SNSSSSSTAE SFETGGNLSK 

      1330       1340       1350       1360       1370       1380 
SARSSRFDNR GFGSDPITLA SLKSRRKRIK FERSDIHDWG LFAMETISAK DMVIEYIGEV 

      1390       1400       1410       1420       1430       1440 
IRQKVADERE KRYVKKGIGS SYLFRVDDDT IIDATFKGNL ARFINHCCDP NCIAKVLTIG 

      1450       1460       1470       1480 
NQKKIIIYAK RDINIGEEIT YDYKFPIEDV KIPCLCKSPK CRQTLN 

« Hide

References

« Hide 'large scale' references
[1]"The genome of the social amoeba Dictyostelium discoideum."
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. expand/collapse author list , 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.
Nature 435:43-57(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AX4.
[2]"Developmental timing in Dictyostelium is regulated by the Set1 histone methyltransferase."
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.
Dev. Biol. 292:519-532(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION, MUTAGENESIS OF ASN-1425 AND CYS-1474, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAFI02000132 Genomic DNA. Translation: EAL62816.1.

3D structure databases

ProteinModelPortalQ54HS3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING44689.DDB_0233375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblProtistsDDB0233375; DDB0233375; DDB_G0289257.
KEGGddi:DDB_G0289257.

Organism-specific databases

dictyBaseDDB_G0289257. set1.

Phylogenomic databases

eggNOGCOG2940.
InParanoidQ54HS3.
KOK11422.
OMAWERDRDW.

Family and domain databases

InterProIPR015722. Histone-lysine_MeTfrase.
IPR003616. Post-SET_dom.
IPR001214. SET_dom.
[Graphical view]
PANTHERPTHR22884:SF10. PTHR22884:SF10. 1 hit.
PfamPF00856. SET. 1 hit.
[Graphical view]
SMARTSM00508. PostSET. 1 hit.
SM00317. SET. 1 hit.
[Graphical view]
PROSITEPS50868. POST_SET. 1 hit.
PS50280. SET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROQ54HS3.

Entry information

Entry nameSET1_DICDI
AccessionPrimary (citable) accession number: Q54HS3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: May 24, 2005
Last modified: April 16, 2014
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Dictyostelium discoideum

Dictyostelium discoideum: entries, gene names and cross-references to dictyBase