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Database: UniProt
Entry: O44757
LinkDB: O44757
Original site: O44757 
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   16-JAN-2019, entry version 134.
DE   RecName: Full=Probable histone-lysine N-methyltransferase lin-59;
DE            EC=2.1.1.43;
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;
RA   Chamberlin H.M., Thomas J.H.;
RT   "The bromodomain protein LIN-49 and trithorax-related protein LIN-59
RT   affect 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
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
CC   -!- FUNCTION: Probable histone methyltransferase (By similarity).
CC       Essential protein required to maintain expression of homeotic
CC       genes egl-5 and mab-5. May play an analogous role to the trithorax
CC       Group (trxG) proteins. TrxG proteins form multiprotein complexes
CC       that are required to maintain the transcriptionally active state
CC       of homeotic genes throughout development. May act via a
CC       modification of chromatin. {ECO:0000250,
CC       ECO:0000269|PubMed:10648230}.
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:0000305}.
CC   -!- TISSUE SPECIFICITY: Widely expressed throughout embryonic
CC       development and into adulthood. {ECO:0000269|PubMed:10648230}.
CC   -!- DEVELOPMENTAL STAGE: Expressed from mid-blastula.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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   UniGene; Cel.17896; -.
DR   ProteinModelPortal; O44757; -.
DR   BioGrid; 57313; 2.
DR   IntAct; O44757; 3.
DR   MINT; O44757; -.
DR   STRING; 6239.T12F5.4; -.
DR   EPD; O44757; -.
DR   PaxDb; O44757; -.
DR   PRIDE; O44757; -.
DR   EnsemblMetazoa; T12F5.4; T12F5.4; 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   eggNOG; COG2940; LUCA.
DR   InParanoid; O44757; -.
DR   KO; K06101; -.
DR   OMA; GACTSDM; -.
DR   OrthoDB; 290101at2759; -.
DR   PhylomeDB; O44757; -.
DR   PRO; PR:O44757; -.
DR   Proteomes; UP000001940; Chromosome I.
DR   Bgee; WBGene00003040; Expressed in 5 organ(s), highest expression level in pharyngeal muscle cell (C elegans).
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: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; 3.30.40.10; -; 1.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR001025; BAH_dom.
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; 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   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; Complete proteome; Metal-binding;
KW   Methyltransferase; Nucleus; Reference proteome;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1312       Probable histone-lysine N-
FT                                methyltransferase lin-59.
FT                                /FTId=PRO_0000084431.
FT   DOMAIN      590    635       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN      638    750       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1100   1223       BAH. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00370}.
FT   ZN_FING     967   1027       PHD-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   COMPBIAS    195    230       Asp-rich.
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
//
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