ID A0A2K6KLE1_RHIBE Unreviewed; 1853 AA.
AC A0A2K6KLE1;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Lysine methyltransferase 2E (inactive) {ECO:0000313|Ensembl:ENSRBIP00000012089.1};
GN Name=KMT2E {ECO:0000313|Ensembl:ENSRBIP00000012089.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000012089.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000012089.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000012089.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSRBIT00000035781.1; ENSRBIP00000012089.1; ENSRBIG00000029943.1.
DR GeneTree; ENSGT00940000157862; -.
DR OMA; GYFFKPY; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR CDD; cd15550; PHD_MLL5; 1.
DR CDD; cd19182; SET_KMT2E; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR044434; KMT2E_SET.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46462:SF2; INACTIVE HISTONE-LYSINE N-METHYLTRANSFERASE 2E; 1.
DR PANTHER; PTHR46462; UPSET, ISOFORM A; 1.
DR Pfam; PF20826; PHD_5; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 118..166
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 334..451
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT REGION 478..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1054
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1577..1835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 578..615
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 487..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..671
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1171..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1281..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1373..1429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1433..1447
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1448..1535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1536..1551
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1577..1598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1636
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1674..1690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1707..1721
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1739..1753
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1758..1772
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1853 AA; 204426 MW; 1B3503A9BA3CE2B6 CRC64;
MSIVIPLGVD TAETSYLEMA AGSEPESVEA SPVVVEKSNS YPHQLYTSSS HHSHSYIGLP
YADHNYGARP PPTPPASPPP SVLISKNEVG IFTTPNFDET SSATTISTSE DGSYGTDVTR
CICGFTHDDG YMICCDKCSV WQHIDCMGID RQHIPDTYLC ERCQPRNLDK ERAVLLQRRK
RENMSDGDTS ATESGDEVPV ELYTAFQHTP TSITLTASRV SKVNDKRRKK SGEKEQHISK
CKRYILLAFR EGSRKSSRVK GSAPEIDPSS DGSNFGWETK IKAWMDRYEE ANNNQYSEGV
QREAQRIALR LGNGNDKKEM NKSDLNTNSL LFKPPVESHI QKNKKILKSA KDLPPDALII
EYRGKFMLRE QFEANGYFFK RPYPFVLFYS KFHGLEMCVD ARTFGNEARF IRRSCTPNAE
VRHEIQDGTI HLYIYSIQSI PKGTEITIAF DFDYGNCKYK VDCACLKENP ECPVLKRSSE
SMENISSGYE TRRKKGKKDK DISKEKDTQN QNITLDCEGT TNKMKSPETK QRKLSPLRLS
VSNNQEPDFI DDIEEKTPVS NEVEMESEEQ IAERKRKMTR EERKMEAILQ AFARLEKREK
RREQALERIS TAKTEVKTEC KDTQIVSDAE VIQEQAKEEN ASKPTPAKVN RTKQRKSFSR
SRTHIGQQRR RHRTVSMCSD IQPSSPDIEV TSQQNDIENT VLTIEPETET ALAEIITETE
VPALNKCPTK YPKTKKHLVN EWLSEKNEKT GKPSDSLSER PLRITTDPEV LATQLNSLPG
LTYSPHVYST PKHYIRFTSP FLSEKRRRKE PTENISGSCK KRWLKQALEE ENSAILHRFN
SPFNGENKSP LLLNDSCSLP DLTTPLKKRR FYQLLDSVYS ETSTPTPSPY ATPTHTDITP
MDPSFATPPR IKSDDETCRN GYKPIYSPVT PVTPGTPGNT MHFENISSPE SSPEIKRRTY
SQEGYDRSST MLTLGPFRNS NLTELGLQEI KTIGYMSPRS RTEVNRQCPG EKEPMSDLQL
GLDAVEPTAL HKTLETPAHD RAEPNSQLDS THSGRGTIYS SWVKSPDRTG VNFSVNSNLR
DLTPSHQLEV GGGFRISESK CLMQDDTRGM FMETTVFCTS EDGLVSGFGR TVNDNLIDGS
CTPQNPPQKK KVSLLEYRKR QREARKSGSK TENFPLISVS PHASGSLSNN GDGCASSNEN
GEQVEHTASL PLPTPATVYN ATSEETSNNC PVKDATASEK NEPEVQWTAS TSVEQVRERS
YQRALLLSDH RKDKDSGGES PCVSCSPSHV QSSPSSHSNH IPQLQAKGPV PSFSELMEDP
DPENPEPTTT SECPSPDTSQ NTCKSPSKMS KPGSPGSVIP AQAHGKIFTK PDPQWDSTVT
ASEAENGVHL KTELQQKQLS NNSQALSKNH PPQTHVRNSS EQLSQKLPSA PTKLHCPPSP
HLENPPKSST PHTPAQHGYL SPKPPSQQLG SPYRPHHSQS PQVGTPQREP QRNFYPAAQN
LQANTQQATS GTLFTQTPSG QSAATYSQFN QQSLNSTAPP PPPPPPPSSS SYYQNQQPSA
TFQNYNQLKG SLSQQTVFTS GPNQALPGTT SQQTVPGHHV TPGHFLPSQN PTIHHQTAAA
VVPPPPPPPP APGPHLVQQP NSHQQHSVAH VVGPVHAVTP GSHIHSQTAG HHLPHPTPPG
PAPHHHPPPH PSTGLQGLQA QHQHVVNSAP PPPPPPPPSS VLASGHHTTS AQALHHPPHQ
GPPLFPSSAH PAVPPYPSQA THHTTLGPGP QHQPSGTGPH CPLPVTGPHL QPQGPNSIPT
PTASGFCPHP GSVALPHGVQ GPQQASPVPG QIPIHRAQVP PTFQNNYHGS GWH
//
