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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}.
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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
 
 
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