LIN59_CAEEL
ID LIN59_CAEEL Reviewed; 1312 AA.
AC O44757;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Probable histone-lysine N-methyltransferase lin-59;
DE EC=2.1.1.-;
DE AltName: Full=Abnormal cell lineage protein 59;
GN Name=lin-59; ORFNames=T12F5.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=10648230; DOI=10.1242/dev.127.4.713;
RA Chamberlin H.M., Thomas J.H.;
RT "The bromodomain protein LIN-49 and trithorax-related protein LIN-59 affect
RT development and gene expression in Caenorhabditis elegans.";
RL Development 127:713-723(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
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 investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Probable histone methyltransferase (By similarity). Essential
CC protein required to maintain expression of homeotic genes egl-5 and
CC mab-5. May play an analogous role to the trithorax Group (trxG)
CC proteins. TrxG proteins form multiprotein complexes that are required
CC to maintain the transcriptionally active state of homeotic genes
CC throughout development. May act via a modification of chromatin.
CC {ECO:0000250, ECO:0000269|PubMed:10648230}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-
CC 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;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Widely expressed throughout embryonic development
CC and into adulthood. {ECO:0000269|PubMed:10648230}.
CC -!- DEVELOPMENTAL STAGE: Expressed from mid-blastula.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF163019; AAD49324.1; -; mRNA.
DR EMBL; FO081191; CCD69785.1; -; Genomic_DNA.
DR PIR; T32758; T32758.
DR RefSeq; NP_491206.1; NM_058805.5.
DR AlphaFoldDB; O44757; -.
DR SMR; O44757; -.
DR BioGRID; 57313; 7.
DR IntAct; O44757; 3.
DR MINT; O44757; -.
DR STRING; 6239.T12F5.4; -.
DR EPD; O44757; -.
DR PaxDb; O44757; -.
DR EnsemblMetazoa; T12F5.4.1; T12F5.4.1; WBGene00003040.
DR GeneID; 266825; -.
DR KEGG; cel:CELE_T12F5.4; -.
DR UCSC; T12F5.4; c. elegans.
DR CTD; 266825; -.
DR WormBase; T12F5.4; CE13601; WBGene00003040; lin-59.
DR eggNOG; KOG1083; Eukaryota.
DR HOGENOM; CLU_006192_0_0_1; -.
DR InParanoid; O44757; -.
DR OMA; GACTSDM; -.
DR OrthoDB; 290101at2759; -.
DR PhylomeDB; O44757; -.
DR PRO; PR:O44757; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00003040; Expressed in pharyngeal muscle cell (C elegans) and 9 other tissues.
DR GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0001715; P:ectodermal cell fate specification; IMP:WormBase.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:WormBase.
DR GO; GO:0040011; P:locomotion; IMP:WormBase.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0045138; P:nematode male tail tip morphogenesis; IMP:WormBase.
DR GO; GO:0018991; P:oviposition; IMP:WormBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:WormBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
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; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW Activator; Chromatin regulator; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..1312
FT /note="Probable histone-lysine N-methyltransferase lin-59"
FT /id="PRO_0000084431"
FT DOMAIN 590..635
FT /note="AWS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00562"
FT DOMAIN 638..750
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1100..1223
FT /note="BAH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00370"
FT ZN_FING 967..1027
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 154..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 913..934
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1248..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 154..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..212
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1286
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1312 AA; 147583 MW; 9DC16CEF07E65163 CRC64;
MHGAGEQQQR YRYNARSDEQ HHHPSTSSHQ YQQQGARQMH QMHPIQATLM CTPTTTSAAA
STSSSGGSNS SGGSGGHRQQ GNILRIGNSI KIGDNILEPA GTLVFSQADG TPWTGQRIVV
NGSTHAVVKA NLFPIGTTPP VLNMQSNQNW YMNQPSGTVP MSSNAPATTS SATPDSGIQS
VPTSPPSPSY AMMNDVDIGD HDDEEDDDGP ADFTDMPLLK PVDEDDDCYD VPCTSEGPPP
NNSNPAITTI PSSCSTPAPP KESLPTGMNV EEWGSFLIAS NMDREEIVRR LMAHDPEMAK
AIAMRIRELS AEESKKKKDM EAEVSSTTPT TPRARGTRTR NKCATRSTNS PDVTTSNLPE
EPSTSTMGLV KENEDVEKVE GKRRGRKPKK RRGFHKESFE DLESDAKKSK AEQHEDHLPE
ASCSSRPESV IPPPVDPIQF RLKVREMMER KLEQLTQKMS EDMTELRLSH LTSSKMVNGE
RGKRRESFLR QLNEQSKKLR KGGMLGRKRL RMFMTESDIL EENKDNIKKE VKEESTPPPT
KLRGRLPSRR TREPSEIVNP EPVEKKFNGE YFEITKSVPS SDDIIPLWMA PSLTCGCTKG
ACTSDMDCLN RALRVQCSSD CSVPYCSNRR FWKEDCGNKL CVSNGPRSKR VLKTKIARRA
GEFLCEYAGE VITREQAQEK FAQDRDPRII AIAAHLFVDA TKRSNIARFI KHSCKPNSRL
EVWSVNGFYR AGVFALSDLN PNAEITVDKS DLLPFDMACN CGATECKRVI RGVRWRCADP
NEKIVTRRFV IRNRRKTIER SSHSGLPAIL QTPMDENSSI RLKMKQVLAA FAFRVRKIDG
SMSRTMLPHY TLIIKFLKTK GNNPNPVEFV SLFRKWLEAI DDDDLERAFV AIESHYMSSS
ILSSSLQSKK AKDNAPRARA LSTSCPSPVP SKRGDADLSY LESLYPIGSY DPDDAWESYS
TNKKGNAVRC ICGALDEEGT MVQCDTCHFW LHVDCCQYVV RSNEKAQKSK NPPSDDGEYI
CDFCTNKQNG LRPSADVKLT EQPDVRFENC DYYRSLINRR GIQVVLNETV YVNRVLPEDH
KAMLRNLREE KKGSKQKDTN KYRFPKAATS PLPIEKVDRK NARIFRVERL FVCPGNNRFV
FGSFYAWPHE TYADAGRVFS KKEVFATPYY ETLPLDEVIG RCLVLDTATW CKGRPKVPKF
KEDDVFLCEM QIGKTQRVFE KVPPKNRYPI NTNSYVFTEF THPKKVVRDF RPYDPSNPSP
KPPKTSSIPS TSSIDPPQSS SDGLPEVDTK KLSKRHIQRV LKRLVKNGSR RS