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Database: UniProt
Entry: G3SCS1_GORGO
LinkDB: G3SCS1_GORGO
Original site: G3SCS1_GORGO 
ID   G3SCS1_GORGO            Unreviewed;      1244 AA.
AC   G3SCS1;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 2.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Euchromatic histone lysine methyltransferase 2 {ECO:0000313|Ensembl:ENSGGOP00000025899.2};
GN   Name=EHMT2 {ECO:0000313|Ensembl:ENSGGOP00000025899.2};
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:ENSGGOP00000025899.2, ECO:0000313|Proteomes:UP000001519};
RN   [1] {ECO:0000313|Ensembl:ENSGGOP00000025899.2, 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:ENSGGOP00000025899.2, 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:ENSGGOP00000025899.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; CABD030044211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030044212; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CABD030044213; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; G3SCS1; -.
DR   Ensembl; ENSGGOT00000031361.2; ENSGGOP00000025899.2; ENSGGOG00000026532.2.
DR   eggNOG; KOG1082; Eukaryota.
DR   GeneTree; ENSGT00940000159459; -.
DR   TreeFam; TF106443; -.
DR   Proteomes; UP000001519; Chromosome 6.
DR   Bgee; ENSGGOG00000026532; Expressed in cerebellum and 6 other cell types or tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:InterPro.
DR   GO; GO:0140938; F:histone H3 methyltransferase activity; IEA:UniProt.
DR   GO; GO:0002039; F:p53 binding; IEA:InterPro.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001519}.
FT   REPEAT          718..750
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          751..783
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          784..808
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          818..850
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          884..916
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          1006..1069
FT                   /note="Pre-SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50867"
FT   DOMAIN          1072..1189
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   REGION          1..319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..393
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        171..185
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..283
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..352
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..384
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1244 AA;  135689 MW;  A9940BC842C78614 CRC64;
     MRGLPRGRGL MRARGRGRAA PPGSRGRGRG GPHRGRGRPR SLLSLPRAQA SWTPQLSTGL
     TSPPVPCLPS QGEAPAEMGA LLLEKETRGA TERVHGSLGD TPRSEETLPK ATPDSLEPAG
     PSSPASVTVT VGDEGADTPV GATPLIGDES ENLEGDGDLR GGRILLGHAT KSFPSSPSKG
     GSCPSRAKMS MTGAGKSPPS VQSLAMRLLS MPGAQGAAAA GSEPPPATTS PEGQPKVHRA
     RKTMSKPGNG QPPVPEKRPP EVQHFRMSDD VHSLGKVTSD LAKRRKLNSG GGLSEELGSA
     RRSGEVTLTK GDPGSLEEWE TVVGDDFSLY YDSYSVDERV DSDSKSEVEA LTEQLSEEEE
     EEEEEEEEEE EEEEEEEEEE DEESGNQSDR VRDGARTLTL SVSVSGVNGV GSSGPSEYME
     VPLGSLELPS EGTLSPNHAG VSNDTSSLET ERGFEELPLC SCRMEAPKID RISERAGHKC
     MATESVDGEL SGCNAAILKR ETMRPSSRVA LMVLCETHRA RMVKHHCCPG CGYFCTAGTF
     LECHPDFRVA HRFHKACVSQ LNGMVFCPHC GEDASEAQEV TIPRGDGVTP PAGTAAPAPP
     PLSQDAPGRA DTSQPSARMR GHGEPRRPPC DPLADTIDSS GPSLTLPNGG CLSAVGLPLG
     PGREALEKAL VIQESERRKK LRFHPRQLYL SVKQGELQKV ILMLLDNLDP NFQSDQQSKR
     TPLHAAAQKG SVEICHVLLQ AGANINAVDK QQRTPLMEAV VNNHLEVARY MVQRGGCVYS
     KEEDGSTCLH HAAKIGNLEM VSLLLSTGQV DVNAQDSGGW TPIIWAAEHK HIEVIRMLLT
     RGADVTLTDN EENICLHWAS FTGSAAIAEV LLNARCDLHA VNYHGDTPLH IAARESYHDC
     VLLFLSRGAN PELRNKEGDT AWDLTPERSD VWFALQLNRK LRLGVGNRAI RTEKIICRDV
     ARGYENVPIP CVNGVDGEPC PEDYKYISEN CETSTMNIDR NITHLQHCTC VDDCSSSNCL
     CGQLSIRCWY DKDGRLLQEF NKIEPPLIFE CNQACSCWRN CKNRVVQSGI KVRLQLYRTA
     KMGWGVRALQ TIPQGTFICE YVGELISDAE ADVREDDSYL FDLDNKDGEV YCIDARYYGN
     ISRFINHLCD PNIIPVRVFM LHQDLRFPRI AFFSSRDIRT GEELGFDYGD RFWDIKSKYF
     TCQCGSEKCK HSAEAIALEQ SRLARLDPHP ELLPELGSLP PVNT
//
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