GenomeNet

Database: UniProt/SWISS-PROT
Entry: KMT5C_HUMAN
LinkDB: KMT5C_HUMAN
Original site: KMT5C_HUMAN 
ID   KMT5C_HUMAN             Reviewed;         462 AA.
AC   Q86Y97; Q8WZ10; Q9BRZ6;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   13-FEB-2019, entry version 135.
DE   RecName: Full=Histone-lysine N-methyltransferase KMT5C {ECO:0000305};
DE            EC=2.1.1.43;
DE   AltName: Full=Lysine N-methyltransferase 5C;
DE   AltName: Full=Lysine-specific methyltransferase 5C {ECO:0000312|HGNC:HGNC:28405};
DE   AltName: Full=Suppressor of variegation 4-20 homolog 2;
DE            Short=Su(var)4-20 homolog 2;
DE            Short=Suv4-20h2;
GN   Name=KMT5C {ECO:0000312|HGNC:HGNC:28405}; Synonyms=SUV420H2;
GN   ORFNames=PP7130;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Cervix;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-129 (ISOFORM 1).
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H.,
RA   Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y.,
RA   Shu H., Chen X., Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S.,
RA   Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-416, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-416 AND THR-422, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA   Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full
RT   phosphorylation site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
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. KMT5C is targeted
CC       to histone H3 via its interaction with RB1 family proteins (RB1,
CC       RBL1 and RBL2) (By 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   -!- SUBUNIT: Interacts with HP1 proteins CBX1, CBX3 and CBX5.
CC       Interacts with RB1 family proteins RB1, RBL1 and RBL2 (By
CC       similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q13185:CBX3; NbExp=2; IntAct=EBI-7960569, EBI-78176;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome {ECO:0000250}.
CC       Note=Associated with pericentric heterochromatin. CBX1 and CBX5
CC       are required for the localization to pericentric heterochromatin
CC       (By similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q86Y97-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q86Y97-2; Sequence=VSP_043947, VSP_043948;
CC         Note=No experimental confirmation available. May be produced at
CC         very low levels due to a premature stop codon in the mRNA,
CC         leading to nonsense-mediated mRNA decay.;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH05842.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC       Sequence=AAL55766.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
DR   EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005842; AAH05842.1; ALT_SEQ; mRNA.
DR   EMBL; BC019313; AAH19313.1; -; mRNA.
DR   EMBL; BC044889; AAH44889.1; -; mRNA.
DR   EMBL; AF289582; AAL55766.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS12922.1; -. [Q86Y97-1]
DR   RefSeq; NP_116090.2; NM_032701.3. [Q86Y97-1]
DR   RefSeq; XP_005259395.1; XM_005259338.3.
DR   RefSeq; XP_006723505.1; XM_006723442.3.
DR   RefSeq; XP_011525717.1; XM_011527415.2. [Q86Y97-1]
DR   UniGene; Hs.590982; -.
DR   PDB; 3RQ4; X-ray; 1.80 A; A=2-248.
DR   PDBsum; 3RQ4; -.
DR   ProteinModelPortal; Q86Y97; -.
DR   SMR; Q86Y97; -.
DR   BioGrid; 124257; 11.
DR   IntAct; Q86Y97; 5.
DR   MINT; Q86Y97; -.
DR   STRING; 9606.ENSP00000255613; -.
DR   BindingDB; Q86Y97; -.
DR   ChEMBL; CHEMBL2321644; -.
DR   GuidetoPHARMACOLOGY; 2718; -.
DR   iPTMnet; Q86Y97; -.
DR   PhosphoSitePlus; Q86Y97; -.
DR   BioMuta; KMT5C; -.
DR   DMDM; 74727906; -.
DR   EPD; Q86Y97; -.
DR   jPOST; Q86Y97; -.
DR   MaxQB; Q86Y97; -.
DR   PaxDb; Q86Y97; -.
DR   PeptideAtlas; Q86Y97; -.
DR   PRIDE; Q86Y97; -.
DR   ProteomicsDB; 70387; -.
DR   ProteomicsDB; 70388; -. [Q86Y97-2]
DR   Ensembl; ENST00000255613; ENSP00000255613; ENSG00000133247. [Q86Y97-1]
DR   Ensembl; ENST00000445196; ENSP00000397296; ENSG00000133247. [Q86Y97-2]
DR   Ensembl; ENST00000592631; ENSP00000467499; ENSG00000133247. [Q86Y97-2]
DR   GeneID; 84787; -.
DR   KEGG; hsa:84787; -.
DR   UCSC; uc002qkj.5; human. [Q86Y97-1]
DR   CTD; 84787; -.
DR   DisGeNET; 84787; -.
DR   EuPathDB; HostDB:ENSG00000133247.13; -.
DR   GeneCards; KMT5C; -.
DR   H-InvDB; HIX0174420; -.
DR   HGNC; HGNC:28405; KMT5C.
DR   HPA; HPA052294; -.
DR   MIM; 613198; gene.
DR   neXtProt; NX_Q86Y97; -.
DR   OpenTargets; ENSG00000133247; -.
DR   PharmGKB; PA134934307; -.
DR   eggNOG; KOG2589; Eukaryota.
DR   eggNOG; ENOG410XPH8; LUCA.
DR   GeneTree; ENSGT00940000161700; -.
DR   HOGENOM; HOG000154453; -.
DR   HOVERGEN; HBG095676; -.
DR   InParanoid; Q86Y97; -.
DR   KO; K11429; -.
DR   OMA; PQQDWHW; -.
DR   OrthoDB; 236983at2759; -.
DR   PhylomeDB; Q86Y97; -.
DR   TreeFam; TF106433; -.
DR   Reactome; R-HSA-3214841; PKMTs methylate histone lysines.
DR   ChiTaRS; KMT5C; human.
DR   GenomeRNAi; 84787; -.
DR   PRO; PR:Q86Y97; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; ENSG00000133247; Expressed in 205 organ(s), highest expression level in islet of Langerhans.
DR   ExpressionAtlas; Q86Y97; baseline and differential.
DR   Genevisible; Q86Y97; HS.
DR   GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0005720; C:nuclear heterochromatin; IDA:BHF-UCL.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:BHF-UCL.
DR   GO; GO:0042799; F:histone methyltransferase activity (H4-K20 specific); IEA:Ensembl.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; TAS:Reactome.
DR   GO; GO:0034773; P:histone H4-K20 trimethylation; IEA:Ensembl.
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   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; Methyltransferase; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; S-adenosyl-L-methionine; Transcription;
KW   Transcription regulation; Transferase.
FT   CHAIN         1    462       Histone-lysine N-methyltransferase KMT5C.
FT                                /FTId=PRO_0000281793.
FT   DOMAIN      104    218       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   REGION      346    435       Required for heterochromatin
FT                                localization. {ECO:0000250}.
FT   MOD_RES     416    416       Phosphothreonine.
FT                                {ECO:0000244|PubMed:19690332,
FT                                ECO:0000244|PubMed:20068231}.
FT   MOD_RES     422    422       Phosphothreonine.
FT                                {ECO:0000244|PubMed:20068231}.
FT   VAR_SEQ      37     97       SPVPPLRRQQHLRSALETFLRQRDLEAAYRALTLGGWTARY
FT                                FQSRGPRQEAALKTHVYRYL -> RSIATSVPSCRKVALPS
FT                                CPARATPWRPTGPRSCPLVLGKRMRSWSCWWAALQSCGRQM
FT                                RGC (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043947.
FT   VAR_SEQ      98    462       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_043948.
FT   HELIX         8     27       {ECO:0000244|PDB:3RQ4}.
FT   HELIX        45     58       {ECO:0000244|PDB:3RQ4}.
FT   HELIX        61     69       {ECO:0000244|PDB:3RQ4}.
FT   TURN         70     78       {ECO:0000244|PDB:3RQ4}.
FT   HELIX        83     99       {ECO:0000244|PDB:3RQ4}.
FT   HELIX       102    104       {ECO:0000244|PDB:3RQ4}.
FT   STRAND      106    110       {ECO:0000244|PDB:3RQ4}.
FT   STRAND      121    127       {ECO:0000244|PDB:3RQ4}.
FT   STRAND      134    144       {ECO:0000244|PDB:3RQ4}.
FT   HELIX       147    152       {ECO:0000244|PDB:3RQ4}.
FT   TURN        155    157       {ECO:0000244|PDB:3RQ4}.
FT   STRAND      162    165       {ECO:0000244|PDB:3RQ4}.
FT   TURN        166    169       {ECO:0000244|PDB:3RQ4}.
FT   STRAND      170    176       {ECO:0000244|PDB:3RQ4}.
FT   HELIX       177    180       {ECO:0000244|PDB:3RQ4}.
FT   STRAND      188    194       {ECO:0000244|PDB:3RQ4}.
FT   TURN        195    197       {ECO:0000244|PDB:3RQ4}.
FT   STRAND      198    205       {ECO:0000244|PDB:3RQ4}.
FT   STRAND      221    223       {ECO:0000244|PDB:3RQ4}.
FT   HELIX       224    226       {ECO:0000244|PDB:3RQ4}.
FT   HELIX       232    237       {ECO:0000244|PDB:3RQ4}.
FT   HELIX       240    242       {ECO:0000244|PDB:3RQ4}.
SQ   SEQUENCE   462 AA;  52113 MW;  6814F7BDFA109070 CRC64;
     MGPDRVTARE LCENDDLATS LVLDPYLGFR THKMNVSPVP PLRRQQHLRS ALETFLRQRD
     LEAAYRALTL GGWTARYFQS RGPRQEAALK THVYRYLRAF LPESGFTILP CTRYSMETNG
     AKIVSTRAWK KNEKLELLVG CIAELREADE GLLRAGENDF SIMYSTRKRS AQLWLGPAAF
     INHDCKPNCK FVPADGNAAC VKVLRDIEPG DEVTCFYGEG FFGEKNEHCE CHTCERKGEG
     AFRTRPREPA LPPRPLDKYQ LRETKRRLQQ GLDSGSRQGL LGPRACVHPS PLRRDPFCAA
     CQPLRLPACS ARPDTSPLWL QWLPQPQPRV RPRKRRRPRP RRAPVLSTHH AARVSLHRWG
     GCGPHCRLRG EALVALGQPP HARWAPQQDW HWARRYGLPY VVRVDLRRLA PAPPATPAPA
     GTPGPILIPK QALAFAPFSP PKRLRLVVSH GSIDLDVGGE EL
//
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