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Database: UniProt
Entry: A0A0G2JZM5_RAT
LinkDB: A0A0G2JZM5_RAT
Original site: A0A0G2JZM5_RAT 
ID   A0A0G2JZM5_RAT          Unreviewed;      1206 AA.
AC   A0A0G2JZM5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Euchromatic histone lysine methyltransferase 2 {ECO:0000313|Ensembl:ENSRNOP00000071106.1};
GN   Name=Ehmt2 {ECO:0000313|Ensembl:ENSRNOP00000071106.1,
GN   ECO:0000313|RGD:1302972};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000071106.1, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000071106.1, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000071106.1,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0007829|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
RN   [3] {ECO:0000313|Ensembl:ENSRNOP00000071106.1}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000071106.1};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_006256020.1; XM_006255958.2.
DR   AlphaFoldDB; A0A0G2JZM5; -.
DR   SMR; A0A0G2JZM5; -.
DR   Ensembl; ENSRNOT00000081456.2; ENSRNOP00000071106.1; ENSRNOG00000030630.6.
DR   GeneID; 361798; -.
DR   AGR; RGD:1302972; -.
DR   CTD; 10919; -.
DR   RGD; 1302972; Ehmt2.
DR   GeneTree; ENSGT00940000159459; -.
DR   OrthoDB; 5481936at2759; -.
DR   Proteomes; UP000002494; Chromosome 20.
DR   Bgee; ENSRNOG00000030630; Expressed in frontal cortex and 19 other cell types or tissues.
DR   ExpressionAtlas; A0A0G2JZM5; baseline and differential.
DR   GO; GO:0000785; C:chromatin; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0070742; F:C2H2 zinc finger domain binding; ISO:RGD.
DR   GO; GO:0046976; F:histone H3K27 methyltransferase activity; ISO:RGD.
DR   GO; GO:0140759; F:histone H3K56 methyltransferase activity; ISO:RGD.
DR   GO; GO:0046974; F:histone H3K9 methyltransferase activity; ISO:RGD.
DR   GO; GO:0002039; F:p53 binding; ISO:RGD.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; ISO:RGD.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISO:RGD.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0001222; F:transcription corepressor binding; ISO:RGD.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0048148; P:behavioral response to cocaine; ISO:RGD.
DR   GO; GO:0071314; P:cellular response to cocaine; ISO:RGD.
DR   GO; GO:0009267; P:cellular response to starvation; ISO:RGD.
DR   GO; GO:0071466; P:cellular response to xenobiotic stimulus; IDA:RGD.
DR   GO; GO:0006306; P:DNA methylation; ISO:RGD.
DR   GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; ISO:RGD.
DR   GO; GO:0009566; P:fertilization; ISO:RGD.
DR   GO; GO:0007616; P:long-term memory; IMP:RGD.
DR   GO; GO:1902902; P:negative regulation of autophagosome assembly; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0048665; P:neuron fate specification; ISO:RGD.
DR   GO; GO:0048599; P:oocyte development; ISO:RGD.
DR   GO; GO:0035265; P:organ growth; ISO:RGD.
DR   GO; GO:0036166; P:phenotypic switching; ISO:RGD.
DR   GO; GO:0044030; P:regulation of DNA methylation; IDA:RGD.
DR   GO; GO:0006275; P:regulation of DNA replication; ISO:RGD.
DR   GO; GO:0031399; P:regulation of protein modification process; IMP:RGD.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR   GO; GO:0060992; P:response to fungicide; IEP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0007286; P:spermatid development; ISO:RGD.
DR   GO; GO:0007130; P:synaptonemal complex assembly; ISO:RGD.
DR   CDD; cd20905; EHMT_ZBD; 1.
DR   CDD; cd10533; SET_EHMT2; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR043550; EHMT1/EHMT2.
DR   InterPro; IPR047762; EHMT_CRR.
DR   InterPro; IPR007728; Pre-SET_dom.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR038034; SET_EHMT2.
DR   PANTHER; PTHR46307; G9A, ISOFORM B; 1.
DR   PANTHER; PTHR46307:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE EHMT2; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF21533; EHMT1-2_CRR; 1.
DR   Pfam; PF05033; Pre-SET; 1.
DR   Pfam; PF00856; SET; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00468; PreSET; 1.
DR   SMART; SM00317; SET; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS50867; PRE_SET; 1.
DR   PROSITE; PS50280; SET; 1.
PE   1: Evidence at protein level;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Proteomics identification {ECO:0007829|PeptideAtlas:A0A0G2JZM5};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494}.
FT   REPEAT          680..712
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          713..745
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          746..770
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          780..812
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          846..878
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          968..1031
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50867"
FT   DOMAIN          1034..1151
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..257
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..382
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..229
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..290
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..324
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..361
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1206 AA;  131833 MW;  AFE2A6D0A5084770 CRC64;
     MAAAAGAAAA AAAEGEAPAE MGALLLEKEP RGAAERVHGS LGDTSHSEET LPKANPDSLE
     PTGPSSPASV TVTVGDEGAD TPVGATPLIG EEPENLEGDG GRILLGHATK SFPSSPSKGG
     ACPSRAKMSM TGAGKSPPSV QSLAMRLLSM PGAQGAATAG PEPPPATTAG QEGQPKVHRA
     RKTMSKPSNG QPPVPEKRPP EVQHFRMSDD MHLGKVTSDV AKRRKLTSGS LSEDLGSAGG
     SGEVILEKGE PRPLEEWETV VGDDFSLYYD AYSVDERVDS DSKSEVEALA EQLSEEEEEE
     EEEEEEEEEE EEEEEEEEED EESGNQSDRS GSSGRRKAKK KWRKDSPWVK PSRKRRKREP
     PRAKEPRGVN GVGSSGPSEY MEVPLGSLEL PSEGTLSPNH AGVSNDTSSL ETERGFEELP
     LCSCRMEAPK IDRISERAGH KCMATESVDG ELLGCNAAIL KRETMRPSSR VALMVLCEAH
     RARMVKHHCC PGCGYFCTAG TFLECHPDFR VAHRFHKACV SQLNGMVFCP HCGEDASEAQ
     EVTIPRGDGG TPPVGTVAPA PPPLAHDAPG RADTSQPSAR MRGHGEPRRP PCDPLADTID
     SSGPSLTLPN GGCLSAVGLP PGPGREALEK ALVIQESERR KKLRFHPRQL YLSVKQGELQ
     KVILMLLDNL DPNFQSDQQS KRTPLHAAAQ KGSVEICHVL LQAGANINAV DKQQRTPLME
     AVVNNHLEVA RYMVQLGGCV YSKEEDGSTC LHHAAKIGNL EMVSLLLSTG QVDVNAQDSG
     GWTPIIWAAE HKHIDVIRML LTRGADVTLT DNEENICLHW ASFTGSAAIA EVLLNAQCDL
     HAVNYHGDTP LHIAARESYH DCVLLFLSRG ANPELRNKEG DTAWDLTPER SDVWFALQLN
     RKLRLGVGNR AVRTEKIICR DVARGYENVP IPCVNGVDGE PCPEDYKYIS ENCETSTMNI
     DRNITHLQHC TCVDDCSSSN CLCGQLSIRC WYDKDGRLLQ EFNKIEPPLI FECNQACSCW
     RSCKNRVVQS GIKVRLQLYR TAKMGWGVRA LQTIPQGTFI CEYVGELISD AEADVREDDS
     YLFDLDNKDG EVYCIDARYY GNISRFINHL CDPNIIPVRV FMLHQDLRFP RIAFFSSRDI
     RTGEELGFDY GDRFWDIKSK YFTCQCGSEK CKHSAEAIAL EQSRLARLDP HPELLPDLSS
     LPPINT
//
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