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
//