ID A0A2I2ZP50_GORGO Unreviewed; 885 AA.
AC A0A2I2ZP50;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=[histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B {ECO:0000256|ARBA:ARBA00031786};
DE EC=2.1.1.361 {ECO:0000256|ARBA:ARBA00012187};
DE EC=2.1.1.362 {ECO:0000256|ARBA:ARBA00012188};
DE AltName: Full=[histone H4]-lysine20 N-methyltransferase KMT5B {ECO:0000256|ARBA:ARBA00031835};
GN Name=KMT5B {ECO:0000313|Ensembl:ENSGGOP00000049068.1};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000049068.1, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000049068.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000049068.1, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000049068.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) +
CC N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:60344, Rhea:RHEA-COMP:15554, Rhea:RHEA-COMP:15555,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.361;
CC Evidence={ECO:0000256|ARBA:ARBA00023995};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60345;
CC Evidence={ECO:0000256|ARBA:ARBA00023995};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC methionine = H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(20)-[histone H4]
CC + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:61992, Rhea:RHEA-
CC COMP:15556, Rhea:RHEA-COMP:15998, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61961,
CC ChEBI:CHEBI:61976; Evidence={ECO:0000256|ARBA:ARBA00001543};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61993;
CC Evidence={ECO:0000256|ARBA:ARBA00001543};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine
CC = H(+) + N(6),N(6)-dimethyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60348, Rhea:RHEA-COMP:15555, Rhea:RHEA-
CC COMP:15556, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:61929, ChEBI:CHEBI:61976; EC=2.1.1.362;
CC Evidence={ECO:0000256|ARBA:ARBA00000167};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60349;
CC Evidence={ECO:0000256|ARBA:ARBA00000167};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CABD030079928; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030079929; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030079930; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_018892822.1; XM_019037277.1.
DR RefSeq; XP_018892823.1; XM_019037278.1.
DR AlphaFoldDB; A0A2I2ZP50; -.
DR STRING; 9593.ENSGGOP00000049068; -.
DR Ensembl; ENSGGOT00000057099.1; ENSGGOP00000049068.1; ENSGGOG00000004122.3.
DR GeneID; 101151252; -.
DR KEGG; ggo:101151252; -.
DR CTD; 51111; -.
DR GeneTree; ENSGT00940000156431; -.
DR InParanoid; A0A2I2ZP50; -.
DR OMA; NDHAQTK; -.
DR OrthoDB; 5396777at2759; -.
DR Proteomes; UP000001519; Chromosome 11.
DR Bgee; ENSGGOG00000004122; Expressed in testis and 5 other cell types or tissues.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0042799; F:histone H4K20 methyltransferase activity; IBA:GO_Central.
DR GO; GO:0140944; F:histone H4K20 monomethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0140941; F:histone H4K20me methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:Ensembl.
DR GO; GO:0006281; P:DNA repair; IEA:Ensembl.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0045830; P:positive regulation of isotype switching; IEA:Ensembl.
DR CDD; cd19184; SET_KMT5B; 1.
DR Gene3D; 1.10.10.1700; Histone-lysine N-methyltransferase; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR InterPro; IPR041938; Hist-Lys_N-MTase_N.
DR InterPro; IPR044424; KMT5B_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR039977; Suv4-20/Set9.
DR InterPro; IPR025790; Suv4-20_animal.
DR PANTHER; PTHR12977:SF12; HISTONE-LYSINE N-METHYLTRANSFERASE KMT5B; 1.
DR PANTHER; PTHR12977; SUPPRESSOR OF VARIEGATION 4-20-RELATED; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS51570; SAM_MT43_SUVAR420_2; 1.
DR PROSITE; PS50280; SET; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Myogenesis {ECO:0000256|ARBA:ARBA00022541};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 193..308
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 363..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..848
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 885 AA; 99196 MW; 9EDD43F297CCC7BB CRC64;
MKWLGESKNM VVNGRRNGGK LSNDHQQNQS KLQHTGKDTL KAGKNAVERR SNRCHGNSGF
EGQSRYVPSS GMSAKELCEN DDLATSLVLD PYLGFQTHKM NTSAFPSRSS RHFSKSDSFS
HNNPVRFRPI KGRQEELKEV IERFKKDEHL EKAFKCLTSG EWARHYFLNK NKMQEKLFKE
HVFIYLRMFA TDSGFEILPC NRYSSEQNGA KIVATKEWKR NDKIELLVGC IAELSEIEEN
MLLRHGENDF SVMYSTRKNC AQLWLGPAAF INHDCRPNCK FVSTGRDTAC VKALRDIEPG
EEISCYYGDG FFGENNEFCE CYTCERRGTG AFKSRVGLPA PAPVINSKYG LRETDKRLNR
LKKLGDSSKN SDSQSVSSNT DADTTQEKNN ATSNRKSSVG VKKNSKSRTL TRQSMSRIPA
SSNSTSSKLT HINNSRVPKK LKKPAKPLLS KIKLRNHCKR LEQKNASRKL EMGNLVLKEP
KVVLYKNLPI KKDKEPEGPA QAAVASGCLT RHAAREHRQN PVRGAHSQGE SSPCTYITRR
SVRTRTNLKE ASDIKLEPNT LDGYKSSVTE PCPDSGEQPQ PAPVLQEEEL AHETAQKGEA
KCHKSDTGMS KKKSRQGKLV KQFAKIEEST PVHDSPGKDD AVPDLMGPHS DQGEHSGTVG
VPVSYTDCAP SPVGCSVVTS DSFKTKDSFR TAKSKKKRRI TRYDAQLILE NNSGIPKLTL
RRRHDSSSKT NDQENDGMNS SKISIKLSKD HDNDNNLYVA KLNNGFNSGS GSSSTKLKIQ
LKRDEENRGS YTEGLHENGV CCSDPLSLLE SRMEVDDYSQ YEEESTDDSS SSEGDEEEDD
YDDDFEDDFI PLPPAKRLRL IVGKDSIDID ISSRRREDQS LRLNA
//
