ID   C9JKQ0_HUMAN            Unreviewed;       299 AA.
AC   C9JKQ0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   16-JAN-2019, entry version 75.
DE   RecName: Full=Histone-lysine N-methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00904};
DE            EC=2.1.1.43 {ECO:0000256|PROSITE-ProRule:PRU00904};
DE   Flags: Fragment;
GN   Name=KMT5A {ECO:0000313|Ensembl:ENSP00000413811};
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 {ECO:0000313|Ensembl:ENSP00000413811, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000413811, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RG   Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A., null.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [2] {ECO:0000213|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [3] {ECO:0000213|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [4] {ECO:0000313|Ensembl:ENSP00000413811}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [5] {ECO:0000213|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
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:0000256|PROSITE-ProRule:PRU00904};
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. PR/SET subfamily. {ECO:0000256|PROSITE-ProRule:PRU00904}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AC137767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC145423; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   ProteinModelPortal; C9JKQ0; -.
DR   jPOST; C9JKQ0; -.
DR   MaxQB; C9JKQ0; -.
DR   PeptideAtlas; C9JKQ0; -.
DR   PRIDE; C9JKQ0; -.
DR   Ensembl; ENST00000437502; ENSP00000413811; ENSG00000183955.
DR   UCSC; uc058utd.1; human.
DR   EuPathDB; HostDB:ENSG00000183955.12; -.
DR   HGNC; HGNC:29489; KMT5A.
DR   OpenTargets; ENSG00000183955; -.
DR   eggNOG; KOG1085; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000160030; -.
DR   HOGENOM; HOG000020818; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000183955; Expressed in 148 organ(s), highest expression level in esophagus mucosa.
DR   ExpressionAtlas; C9JKQ0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:HPA.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   InterPro; IPR016858; Hist_H4-K20_MeTrfase.
DR   InterPro; IPR001214; SET_dom.
DR   Pfam; PF00856; SET; 1.
DR   PIRSF; PIRSF027717; Histone_H4-K20_mtfrase; 1.
DR   PROSITE; PS51571; SAM_MT43_PR_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   Complete proteome {ECO:0000313|Proteomes:UP000005640};
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00904};
KW   Proteomics identification {ECO:0000213|EPD:C9JKQ0,
KW   ECO:0000213|MaxQB:C9JKQ0, ECO:0000213|PeptideAtlas:C9JKQ0};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00904};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00904}.
FT   SIGNAL        1     16       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        17    299       Histone-lysine N-methyltransferase.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002997241.
FT   DOMAIN      207    299       SET. {ECO:0000259|PROSITE:PS50280}.
FT   REGION      217    219       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR027717-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00904}.
FT   REGION      289    290       S-adenosyl-L-methionine binding.
FT                                {ECO:0000256|PIRSR:PIRSR027717-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00904}.
FT   BINDING     262    262       S-adenosyl-L-methionine.
FT                                {ECO:0000256|PIRSR:PIRSR027717-1,
FT                                ECO:0000256|PROSITE-ProRule:PRU00904}.
FT   NON_TER     299    299       {ECO:0000313|Ensembl:ENSP00000413811}.
SQ   SEQUENCE   299 AA;  34025 MW;  5DC403FBF52D3E75 CRC64;
     MRWLWLLLFP DSPVTLREVL PSQPWRLRGC SDLRGENVFT GQSKIYSYMS PNKCSGMRFP
     LQEENSVTHH EVKCQGKPLA GIYRKREEKR NAGNAVRSAM KSEEQKIKDA RKGPLVPFPN
     QKSEAAEPPK TPPSSCDSTN AAIAKQALKK PIKGKQAPRK KAQGKTQQNR KLTDFYPVRR
     SSRKSKAELQ SEERKRIDEL IESGKEEGMK IDLIDGKGRG VIATKQFSRG DFVVEYHGDL
     IEITDAKKRE ALYAQDPSTG CYMYYFQYLS KTYCVDATRE TNRLGRLINH SKCGNCQTK
//