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Database: UniProt
Entry: Q5RJX8
LinkDB: Q5RJX8
Original site: Q5RJX8 
ID   KT5BB_XENLA             Reviewed;         785 AA.
AC   Q5RJX8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   16-JAN-2019, entry version 59.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5B-B {ECO:0000305};
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine-specific methyltransferase 5B-B {ECO:0000250|UniProtKB:Q4FZB7};
DE   AltName: Full=Suppressor of variegation 4-20 homolog 1-B;
DE            Short=Su(var)4-20 homolog 1-B;
DE            Short=Suv4-20h1-B;
GN   Name=kmt5b-b {ECO:0000250|UniProtKB:Q4FZB7}; Synonyms=suv420h1-b;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
OC   Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Histone methyltransferase that specifically
CC       trimethylates 'Lys-20' of histone H4. H4 'Lys-20' trimethylation
CC       represents a specific tag for epigenetic transcriptional
CC       repression. Mainly functions in pericentric heterochromatin
CC       regions, thereby playing a central role in the establishment of
CC       constitutive heterochromatin in these regions. Plays a role in
CC       myogenesis by regulating the expression of target genes (By
CC       similarity). {ECO:0000250}.
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:0000255|PROSITE-ProRule:PRU00903};
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}.
CC       Note=Associated with pericentric heterochromatin. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. Suvar4-20 subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU00903}.
DR   EMBL; BC086459; AAH86459.1; -; mRNA.
DR   RefSeq; NP_001088653.1; NM_001095184.1.
DR   UniGene; Xl.71915; -.
DR   ProteinModelPortal; Q5RJX8; -.
DR   SMR; Q5RJX8; -.
DR   PRIDE; Q5RJX8; -.
DR   GeneID; 495826; -.
DR   KEGG; xla:495826; -.
DR   CTD; 495826; -.
DR   Xenbase; XB-GENE-6253211; kmt5b.
DR   HOVERGEN; HBG105761; -.
DR   KO; K11429; -.
DR   OrthoDB; 236983at2759; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IEA:InterPro.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:InterPro.
DR   GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR   InterPro; IPR025790; Hist-Lys_N-MTase_Suvar4-20.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   SMART; SM00317; SET; 1.
DR   PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR   PROSITE; PS50280; SET; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator; Chromosome; Methyltransferase; Myogenesis;
KW   Nucleus; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    785       Histone-lysine N-methyltransferase KMT5B-
FT                                B.
FT                                /FTId=PRO_0000281792.
FT   DOMAIN       99    214       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
SQ   SEQUENCE   785 AA;  89547 MW;  44C18929602CC834 CRC64;
     MSAKELCEND DLATSLVLDP YLGFQTHKMN TRFRPIKGRQ EELKEVIENF KKNEQLEKTF
     KNLVAGDWAR HYFLHKNKMQ ETHFKAHVFI YLRMFATSSG FEILPCCRYS SERNGAKIVA
     TKDWKRNDKI ELLVGCIAEL SEAEENMLLR HGENDFSVMY STRKNCAQLW LGPAAFINHD
     CRPNCKFVST GRDTACVKAL RDIEPGEEIS CYYGDGFFGE NNEFCECYTC ERRATGAFKS
     RVGLNEPGPV INSKYGLRET DKRLNRLKKL GDNGKNSDSQ SVSSNTDADT SQEKNTANRK
     SNGLRKKSKS RTLRRQSMSR IPISSSSTSS KLPHINNSRV PKRLRKTAKP LHSKLKIRCH
     RKKVEQKKTS KKLDVSNLVL KEPKVVLYKN LAIKKDRESQ GAVQVTETTG CLTRHAAREY
     KLNSFKGAYA HGDTSPCTYI TRSSLRTRFN SKDMSEAKLQ PNSVDGYRSS HGTVIQLDTG
     DPLFQSTRKN ELLQETSRQS MRFQRNNFNT SRRNSRQNRY ITQASKVEDS VSIYNSSSID
     NSLPDLGNSH CDLGEGNALI HTSPDYKNIK SSTDEYPLVT SEITKSKKNI RTVKNKKRRR
     ITRYDAQLIL ENSTGIPKLT LRRRHDSNSS KTNEKENEGM GSSKISIKLS KDHEKDKNSL
     YVAKLNNGFN SGSGSTSTKL KIQLKRDEEN RMAFPNENGM YCSDTLSLLG TRMEVDGYDH
     YEEESVGESS TEEEEEEEDE FDDEFEDDFI PLPPAKRLRL IVGKDSIDID ISSRRREDQS
     LRLNA
//
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