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Database: UniProt
Entry: Q9U263
LinkDB: Q9U263
Original site: Q9U263 
ID   SET26_CAEEL             Reviewed;        1645 AA.
AC   Q9U263;
DT   15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 3.
DT   16-JAN-2019, entry version 136.
DE   RecName: Full=Histone-lysine N-methyltransferase set-26 {ECO:0000305};
DE            EC=2.1.1.43 {ECO:0000269|PubMed:24685137};
GN   Name=set-26 {ECO:0000312|WormBase:Y51H4A.12};
GN   ORFNames=Y51H4A.12 {ECO:0000312|WormBase:Y51H4A.12};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=22212395; DOI=10.1111/j.1474-9726.2011.00785.x;
RA   Ni Z., Ebata A., Alipanahiramandi E., Lee S.S.;
RT   "Two SET domain containing genes link epigenetic changes and aging in
RT   Caenorhabditis elegans.";
RL   Aging Cell 11:315-325(2012).
RN   [3] {ECO:0000305}
RP   FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=24685137; DOI=10.1016/j.celrep.2014.02.044;
RA   Greer E.L., Beese-Sims S.E., Brookes E., Spadafora R., Zhu Y.,
RA   Rothbart S.B., Aristizabal-Corrales D., Chen S., Badeaux A.I., Jin Q.,
RA   Wang W., Strahl B.D., Colaiacovo M.P., Shi Y.;
RT   "A histone methylation network regulates transgenerational epigenetic
RT   memory in C. elegans.";
RL   Cell Rep. 7:113-126(2014).
RN   [4]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DOMAIN, AND
RP   DISRUPTION PHENOTYPE.
RX   PubMed=29714684; DOI=10.7554/eLife.34970;
RA   Wang W., Chaturbedi A., Wang M., An S., Santhi S., Lee S.S.;
RT   "SET-9 and SET-26 are H3K4me3 readers and play critical roles in
RT   germline development and longevity.";
RL   Elife 7:0-0(2018).
CC   -!- FUNCTION: Histone methyltransferase that mediates trimethylation
CC       of 'Lys-9' of histone H3 in vitro (PubMed:24685137). Involved in
CC       transcriptional regulation (PubMed:29714684). Plays a role in the
CC       negative regulation of lifespan and in heat resistance
CC       (PubMed:29714684). Together with set-9, negatively regulates
CC       lifespan in a germline-independent, partially daf-16-dependent
CC       fashion (PubMed:22212395, PubMed:29714684). Together with set-9,
CC       plays a role in germline development and maintenance and might
CC       play a role in the restriction of the trimethylation mark on
CC       histone H3 'Lys-4'(H3K4me3) to target genes specifically in the
CC       germline (PubMed:29714684). Together with spr-5, required for
CC       transgenerational fertility (PubMed:24685137).
CC       {ECO:0000269|PubMed:22212395, ECO:0000269|PubMed:24685137,
CC       ECO:0000269|PubMed:29714684}.
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         Evidence={ECO:0000269|PubMed:24685137};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22212395,
CC       ECO:0000269|PubMed:29714684}.
CC   -!- TISSUE SPECIFICITY: Expressed both in the germline and in somatic
CC       tissues. {ECO:0000269|PubMed:22212395,
CC       ECO:0000269|PubMed:29714684}.
CC   -!- DOMAIN: The PHD-type domain binds histone H3 when trimethylated at
CC       'Lys-4' (H3K4me3) in combination with a nearby acetylation (K9ac,
CC       K14ac and/or K18ac), but not H3K4me3 alone.
CC       {ECO:0000269|PubMed:29714684}.
CC   -!- DISRUPTION PHENOTYPE: Exhibits prolonged lifespan, increased
CC       resistance to heat stress, reduced brood size and changes in gene
CC       expression (PubMed:29714684). In a glp-1(e2141) mutant background
CC       which lacks a germline, extended lifespan, increased H3 protein
CC       levels, decreased levels of trimethylated histone H3 'Lys-9'
CC       (H3K9me3) and 'Lys-27' (H3K27me3) and changes in gene expression
CC       (PubMed:22212395, PubMed:29714684). In spr-5 null mutants,
CC       accelerates the progressive sterility and accumulation of histone
CC       H3 'Lys-4' dimethylation (H3K4me2) over generations which is seen
CC       in spr-5 mutants (PubMed:24685137). Simultaneous RNAi-mediated
CC       knockdown of set-26 and set-9 results in extended lifespan
CC       (PubMed:22212395). {ECO:0000269|PubMed:22212395,
CC       ECO:0000269|PubMed:24685137, ECO:0000269|PubMed:29714684}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. {ECO:0000305}.
CC   -!- CAUTION: Contrary to other SET-domain containing
CC       methyltransferases, set-26 does not have the residues usually
CC       involved in cofactor binding: instead of the highly conserved
CC       XGXG, Y and NH motifs, set-26 displays AVEA (Ala-948-Ala-951), V
CC       (Val-967) and F (Phe-1063) and RR (Arg-1024-Arg-1025) motifs
CC       (PubMed:29714684). However, histone methyltransferase activity has
CC       been detected in vitro (PubMed:24685137).
CC       {ECO:0000269|PubMed:24685137, ECO:0000303|PubMed:29714684}.
DR   EMBL; BX284604; CAB63382.3; -; Genomic_DNA.
DR   RefSeq; NP_502971.3; NM_070570.3.
DR   UniGene; Cel.11947; -.
DR   ProteinModelPortal; Q9U263; -.
DR   STRING; 6239.Y51H4A.12; -.
DR   EPD; Q9U263; -.
DR   PaxDb; Q9U263; -.
DR   PeptideAtlas; Q9U263; -.
DR   EnsemblMetazoa; Y51H4A.12; Y51H4A.12; WBGene00013106.
DR   GeneID; 178463; -.
DR   KEGG; cel:CELE_Y51H4A.12; -.
DR   UCSC; Y51H4A.12; c. elegans.
DR   CTD; 178463; -.
DR   WormBase; Y51H4A.12; CE25361; WBGene00013106; set-26.
DR   eggNOG; ENOG410IMX8; Eukaryota.
DR   eggNOG; ENOG4111FV9; LUCA.
DR   GeneTree; ENSGT00940000168747; -.
DR   HOGENOM; HOG000020083; -.
DR   InParanoid; Q9U263; -.
DR   OMA; IHPQEGP; -.
DR   OrthoDB; 790990at2759; -.
DR   PRO; PR:Q9U263; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00013106; Expressed in 3 organ(s), highest expression level in multi-cellular organism.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR   GO; GO:0046974; F:histone methyltransferase activity (H3-K9 specific); IDA:WormBase.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0036124; P:histone H3-K9 trimethylation; IDA:WormBase.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR   InterPro; IPR011011; Znf_FYVE_PHD.
DR   InterPro; IPR001965; Znf_PHD.
DR   InterPro; IPR019787; Znf_PHD-finger.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 1.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00249; PHD; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF57903; SSF57903; 1.
DR   PROSITE; PS01359; ZF_PHD_1; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Complete proteome; Metal-binding; Methyltransferase;
KW   Nucleus; Reference proteome; S-adenosyl-L-methionine; Transferase;
KW   Zinc; Zinc-finger.
FT   CHAIN         1   1645       Histone-lysine N-methyltransferase set-
FT                                26.
FT                                /FTId=PRO_0000438927.
FT   DOMAIN      973   1064       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   ZN_FING     794    842       PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   COILED     1103   1217       {ECO:0000255}.
FT   COMPBIAS    508    606       Pro-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00015}.
FT   COMPBIAS   1069   1212       Glu-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00007}.
FT   COMPBIAS   1395   1469       Lys-rich. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00012}.
SQ   SEQUENCE   1645 AA;  181666 MW;  74BF8830788BED57 CRC64;
     MADGEHTLPA DEELFEQPPL QQQQPEIAEP IVMAQEPIQG VSEDPQASEA THEAPDNYPV
     DHQMENQEFY QEPQIPEPQQ IPQIPVFQPA AYNPPNYVAP QQRANNFGEP AAAADSRPLT
     EEEQLAAERP TEDTVWIDSD DDTDVEEAIL RANFWLPYSD HNYDPPDPAD RIILPTEGPF
     PCIAGLDEDC NIVKQWMPED AVGPGSPGTQ YRRNQQTGGG LPSTSVAPQQ QQLPVRHNIQ
     NRPMVAAQPF SIGGNQVEYG GIGGMDSRMQ QRGVVRDGPQ YRVMNDFGNG LPMRGQLPPR
     NSPAANAINR VREQQQQMYH QAGARGSLQQ RVPAPAAPTP GSYQHIVNAV PVGGANPMRR
     VPPQARPGMI GGAANNNRAR PIHVTRPMDT QEFEHPVAPA AAAPPRRVVD VAPHRMTPEQ
     RQELQQMNRQ RAAPQFPAAA AQRSAEKIVI QQRPGASSSR APRPSMAQED LLRSPTRRLS
     ERVPQEHQTP VLEPRRFQVK VTDTYSTPIP KASDQLPAQL TEEDPPEESA AAAAPEDVPD
     AAPEDPPKGI LKPTPPHRMT QEEKNAHFAR LTTDKEKPTS SASILPQDAA PPHVPPPPPP
     PLVLRPHHQD ETLAMVQSVF ESKPRQPDTP KDKEAISKIA DLLRFSADEF TGQSGSSAAA
     RQRTVSGSAA RAQTYQMHHQ QQQQHHHQMP MDQRKRHSSG RYDALMGAMP LQQQPPPPPP
     SQFQHTDSIA HRPRGRPKGT RHPSVAVQPQ RSGGARTLPP RAQTVAMSAR NGANAKNSDS
     ESEGIDEAAE ESWTMRCHCG MDHGDGDTIE CEGCKTWQHM ACMGLTLKSN TSKYKCEMCL
     PRRLPVSKAE AAREQERILN RLRAAAKKQK RKSEPVEQKQ KSQPSTSRKS APMALQQQPA
     EPRVAQLNDY SKQASALLFG MEQTAGADTL LAESRLHKKA RRMFVEEAVE ALVTTDLVQI
     RQVILEVNGH VSMSNEVKRQ PGGGNCIFMY DGLMKGTAGE DMGDGQELVC IDTKRKGNDT
     KFTRRSCVPN CVLKHVLGSN ATLGIMIVAT KDITRNTEVT LPFDADWRES EVELECAEHM
     KELQACPFES ERRRFAAERH RAMDHKKREA EEARRADEER RRLEEEVRRE RAAKTKQMDE
     AEKARLEAEK AAEKEKKAKE REEAKERKKM EVEASAAAAP ESSNSITARE ERRIQQAEEM
     FRRQEEEGKR KEARRRSKSV TPGVLEAAGT AAREDAPEAS IPAPAPSPPA SRRSVSRTTQ
     PSTSSFATPT EPPAKNKRMR SVVPPKSEPA SSAKRVRATT VATPKDTTAS NDSRKRKSSA
     TGKTPVAKRS KNVVPTSFGL ALIEKELREQ ARDSTVLEMI LPDYIMKEKR SGLLAGQSPD
     FSEVRAQIEE ENRMKERFTK REAKKKAVEK AKEKEKKEHR KEPKKANEPG PAPKSEKAVE
     KAVEKVEKKP KSPQKPPAKP TAQKPPLKKT EEVDGIEREA SESSSKESSV APEEKKNPKK
     ITFAEYNSRR SQKREAGECS TPPAVTRRGF IPSTEGEDLV NVELSAIPLD DHPSSSNTAP
     TTTIAPSVGG APKPTSVVVK SPSTRSRTRG AASESVDDAP AEHSMSLQDR VFSMFGSTVD
     APAPPPPPPA SAETNSRRSR STRWN
//
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