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Database: UniProt
Entry: Q6GP17
LinkDB: Q6GP17
Original site: Q6GP17 
ID   KT5BA_XENLA             Reviewed;         855 AA.
AC   Q6GP17;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JAN-2019, entry version 63.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5B-A {ECO:0000305};
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine-specific methyltransferase 5B-A {ECO:0000250|UniProtKB:Q4FZB7};
DE   AltName: Full=Suppressor of variegation 4-20 homolog 1-A;
DE            Short=Su(var)4-20 homolog 1-A;
DE            Short=Suv4-20h1-A;
GN   Name=kmt5b-a {ECO:0000250|UniProtKB:Q4FZB7}; Synonyms=suv420h1-a;
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=Spleen;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-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; BC073331; AAH73331.1; -; mRNA.
DR   RefSeq; NP_001085777.1; NM_001092308.1.
DR   UniGene; Xl.1754; -.
DR   ProteinModelPortal; Q6GP17; -.
DR   SMR; Q6GP17; -.
DR   PRIDE; Q6GP17; -.
DR   GeneID; 444204; -.
DR   KEGG; xla:444204; -.
DR   CTD; 444204; -.
DR   Xenbase; XB-GENE-866439; 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    855       Histone-lysine N-methyltransferase KMT5B-
FT                                A.
FT                                /FTId=PRO_0000281791.
FT   DOMAIN      169    284       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
SQ   SEQUENCE   855 AA;  97594 MW;  802E90B1A617D183 CRC64;
     MKWLGESKNM VVNGRRNGNR LSAELRQNQP KLHSPGRENL RTSKNVPDRR SGRFGNVAFE
     AQSRYVPSSG MSAKELSEND DLATSLVLDP YLGFQTHKMN ARFRPIKGRQ EELKEVIENF
     KKKEHLEKTF KNLVAGDWSR HYFLNKTKMQ EKHFKEHVFI YLRMFATSSG FEILPCNRYS
     SERNGAKIVA TKEWKRNDKI ELLVGCIAEL SEAEENMLLR HGENDFSVMY STRKNCAQLW
     LGPAAFINHD CRPNCKFVST GRDTACVKAL RDIEPGEEIS CYYGDGFFGE NNEFCECYTC
     ERRATGAFKS RVGLNEPGPL INSKYGLRET DKRLNRLKKL GDSGKNSDSQ SVSSNTDADT
     SQEKDMSNRK SNGMRKRSKS RTLRRRSMSR IPVSSSSTSS KLPHINNSRV PKRLRKPPKP
     FHSKLKIRCH RKKVEQKKAS KKLEVSNLVL KEPKVVLYKN LAIKKDRESQ GAVPVTETTG
     CLTRHAAREY KLNSLKGAHS HGESSSCTYI TRSSLRTRFK SNDMSEAKLQ HNSVDGYRSS
     HGTVLQVDKS EPLCQSTCKN ELLQETPRQT IRFHRNNFNT STRNSRQNRY IKQASKVEDS
     VSSVYDQSSK DHALPDLGNS HCDLGEGNAL IQTSPDYKSF ESSADEYPLV TSEITKTKKN
     NRTAKNKKSR RITRYDAQLI LENSTGIPKL TLRRRHDSNS SKTNEKENEG MSSSKISIKL
     SKDHEKDNGL YVAKLNNGFN SGSGSTSTKL KIQLKRDEEN RTAFPNENGM YCNDTLSLLE
     TRMKVDGYDH YEEESVEESS TEEDEEEEDE YDDEFEDDFI PLPPAKRLRL IVGKDSIDID
     ISSRRREDQS LRLNA
//
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