ID A0A452F675_CAPHI Unreviewed; 2556 AA.
AC A0A452F675;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=[histone H3]-lysine(36) N-trimethyltransferase {ECO:0000256|ARBA:ARBA00012178};
DE EC=2.1.1.359 {ECO:0000256|ARBA:ARBA00012178};
DE AltName: Full=SET domain-containing protein 2 {ECO:0000256|ARBA:ARBA00030091};
GN Name=SETD2 {ECO:0000313|Ensembl:ENSCHIP00000019636.1};
OS Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925 {ECO:0000313|Ensembl:ENSCHIP00000019636.1, ECO:0000313|Proteomes:UP000291000};
RN [1] {ECO:0000313|Ensembl:ENSCHIP00000019636.1, ECO:0000313|Proteomes:UP000291000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bickhart D.M., Koren S., Rosen B., Hastie A., Liachko I., Sullivan S.T.,
RA Burton J., Sayre B.L., Huson H.J., Lee J., Lam E., Kelley C.M.,
RA Hutchison J.L., Zhou Y., Sun J., Crisa A., Schwartz J.C., Hammond J.A.,
RA Schroeder S.G., Liu G.E., Dunham M., Shendure J., Sonstegard T.S.,
RA Phillippy A.M., Van Tassell C.P., Smith T.P.;
RT "Polished mammalian reference genomes with single-molecule sequencing and
RT chromosome conformation capture applied to the Capra hircus genome.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSCHIP00000019636.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+)
CC + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60324, Rhea:RHEA-COMP:9785, Rhea:RHEA-
CC COMP:15536, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.359;
CC Evidence={ECO:0000256|ARBA:ARBA00000317};
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000256|ARBA:ARBA00004286}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LWLT01000024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9925.ENSCHIP00000019636; -.
DR Ensembl; ENSCHIT00000027452.1; ENSCHIP00000019636.1; ENSCHIG00000018558.1.
DR GeneTree; ENSGT00940000160086; -.
DR Proteomes; UP000291000; Chromosome 22.
DR Bgee; ENSCHIG00000018558; Expressed in uterus and 17 other cell types or tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043014; F:alpha-tubulin binding; IEA:Ensembl.
DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0035441; P:cell migration involved in vasculogenesis; IEA:Ensembl.
DR GO; GO:0060977; P:coronary vasculature morphogenesis; IEA:Ensembl.
DR GO; GO:0051607; P:defense response to virus; IEA:Ensembl.
DR GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
DR GO; GO:0060669; P:embryonic placenta morphogenesis; IEA:Ensembl.
DR GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0048332; P:mesoderm morphogenesis; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:1902850; P:microtubule cytoskeleton organization involved in mitosis; IEA:Ensembl.
DR GO; GO:0006298; P:mismatch repair; IEA:Ensembl.
DR GO; GO:0001763; P:morphogenesis of a branching structure; IEA:Ensembl.
DR GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR GO; GO:0034728; P:nucleosome organization; IEA:Ensembl.
DR GO; GO:0060039; P:pericardium development; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0032727; P:positive regulation of interferon-alpha production; IEA:Ensembl.
DR GO; GO:0032465; P:regulation of cytokinesis; IEA:Ensembl.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR GO; GO:0010793; P:regulation of mRNA export from nucleus; IEA:Ensembl.
DR GO; GO:1905634; P:regulation of protein localization to chromatin; IEA:Ensembl.
DR GO; GO:0034340; P:response to type I interferon; IEA:Ensembl.
DR GO; GO:0048864; P:stem cell development; IEA:Ensembl.
DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:Ensembl.
DR CDD; cd19172; SET_SETD2; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.20.930.10; Conserved domain common to transcription factors TFIIS, elongin A, CRSP70; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 1.10.1740.100; Set2, Rpb1 interacting domain; 1.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR044437; SETD2/Set2_SET.
DR InterPro; IPR042294; SETD2_animal.
DR InterPro; IPR013257; SRI.
DR InterPro; IPR038190; SRI_sf.
DR InterPro; IPR035441; TFIIS/LEDGF_dom_sf.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR46711; HISTONE-LYSINE N-METHYLTRANSFERASE SETD2; 1.
DR PANTHER; PTHR46711:SF1; HISTONE-LYSINE N-METHYLTRANSFERASE SETD2; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF00856; SET; 1.
DR Pfam; PF08236; SRI; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00317; SET; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000291000};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..2556
FT /note="[histone H3]-lysine(36) N-trimethyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019280064"
FT DOMAIN 1486..1540
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1542..1659
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1666..1682
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 2381..2414
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 109..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 590..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..982
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1024..1088
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1138..1278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1384..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1827..1864
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1928..1999
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2011..2146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2431..2457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..459
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..515
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1083
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1154..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1247..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1944..1963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2011..2038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2047..2072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2082..2122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2123..2141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2441..2457
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2556 AA; 286275 MW; DD4F934ADC1DBE85 CRC64;
MIYFLFFCML SWLDDNREEE NEAKIENVPK TGFIKGPMFK GVASSRFLPK GTKTKVNLEE
QGRQKVSFSF SLTKKTLQNR FLTALGNEKQ NDTPNSPVVP LQVDSTPKVK TDIGDTLSTT
EESSPPKSRV ELGKIHFKKH LLHVTSRPLL TATTAVASLS PPMAPLPAVI AESTTVDSPP
SSPPPPPPPP QATTPSSPAP VTEPVALPHT PVTVLMTAPV DVAARALKEP PVTVVPESSE
VDTKQDPVSN SSEEHITHSL NEQADIPSQK EDSHIGKEEE TPDSSKSSLG SKRTGSKKKS
SQSEGTFLGS ESDEDSVRTS SSQRSHDLKF SANTDRERDS KKSLATFKSE DLGKSSRSKT
ERDDKYFSYS KLERDTRYIS SRCRERERRR SRSRSRSDRG SRTSLSYSRS ERSHYYDSDR
RYHRSSPYRE RTRYSRAYTD SRARESSDSE DEYKKTYSRR TSSHSSSYRD LRTSSSYSKS
DRDCKTESSY LEIEKRGKYS SKLERESKRT SESEAMKRCC SPPNELGFRR GSSYSKHDNN
ASRYKSAPSK PVSKSDKFKN SFCCTELNEE TRQSHSFSLQ TPCSKGSELR VISKIPEREK
TRSPSPSNRL NDSPTFKKLD GSPVFKSEFI GHDSHDSIKE VDSLCKVKND QLRSYCPTEL
NINGSPGAES DLAAFCTSKH DTVLMSSDDS VTGSEVSPSV KTCMLSSNGF QNTNRCKEKD
LDDTCMKHSK SESASRETEP LVSPHQDQLI SLPVITIDYS KTVVKEPVEV RVSCCKTKDS
DIYCTSNDNH TSSCHSGAEN TEPLVSKMSS NSFMNVHLKS KTVICDHGNL TDQRSKFACG
EYKQSVGSTS SASVNHFDDL YQTPGSSCIA SSLQSLPPGM KVNSLTLLQR GENISPVLDA
VLKSKNSEFL KHAEKETVIE VGGDLPDSGR GFASWDSRHN NGLSEKCVQE AHEEGNSLLP
DRRGRPEISL DEEGGRGHTH ISDDSEVVFS SCDLNLTMED SDGVTYTLKC DSSGHASEIV
STVHEDYSGS SESSSDESDS EDTDSDDSSI PRNRLQSVVV VPKNSTLTME ETSPCSSRSS
QSYRHYSDHW EDERLEPRRH SYEEKFESIT TKSCPQTEKF FFHKAAEKNS EISFIQPSRK
QIDNHLPEIA HPQSDGVDST SHPDIKSDPL GHSNSEETVK TKIASQQQEE LPVYSPDDFE
DVSSKSRQQT AFPIRADSRL GKTDSSFSSS CEISRVDGVR SSEELRNLGW DFSQQEKPTS
TYQQPDSSYG ACGGHKHQQS AEQCSGVRSY WQGNGYWDPR LASRPPGAGL VYDRIQGQVP
DSLTDDREEE ENWDQRGGSH FSSQSSKFFL SLQKDKGSVQ APEISSNSIK DSLAVNEKKD
LLKNLDRNDM KDRGPLKKRR QELESDSESD GELQDRKKVR VEIEQGETAV PLGSALVGPS
CVMEDFRDPQ RWKEYAKQGK MPCYFDLIEE NVYLTERKKN KSHRDIKRMQ CECTPLSKDE
RAQGEIACGE DCLNRLLMIE CSSRCPNGDY CSNRRFQRKQ HADVEVILTE KKGWGLRAAK
DLPSNTFVLE YCGEVLDHKE FKARVKEYAR NKNIHYYFMA LKNDEIIDAT QKGNCSRFMN
HSCEPNCETQ KWTVNGQLRV GFFTTKLVPS GSELTFDYQF QRYGKEAQKC FCGSANCRGY
LGGENRVSIR AAGGKMKKER SRKKDSVDGE LEALMENGEG LSDKNQVLSL SRLMVRIETL
EQKLTCLKLI QNTHSQSCLK SFLERHGLSL LWIWMAELGD GRESNQKLQE EIIKTLEHLP
IPTKNMLEES KVLPIIQRWS QTKTAIPQLS EGDGYSSENT SRAHTPLNTP DPSTKLNAEA
DTDTPKKLMF RRLKIISENS MDSAISDATS ELEGKDGKED LDQLENVPIE EEEEPQPQQL
LVQQLPEPKV DSDIAAEASK LPASELEADA EIEHKESSGA KLDEPIAEET PSQDEEEGVS
DVESERSQEP PDKTVDISDL ATKLLDSWKD LKEVYRIPKK SQTEKESTIT ERGRDAVGFR
DQTVAPKTPN RSRERDPDKQ TQIKEKRKRR GSLSPPSSAY ERGTKRPDDR YDTPTSKKKV
RIKDRNKLST EERRKLFEQE VAQREAQKQQ QQMQNLGMTS PLPYDSLGYN APHHPFAGYP
PGYPMQAYVD PSNPNAGKVL LPTPSMDPVC SPAAYDHSQP LVGHSTEPLA APPPVPVVPH
VAAPVEVSSS QYVAQSDAVV HQDSSVTVLP VPAPGPVQGQ NYSVWDSNQQ SVSVQQQYSP
AQSQTTIYYQ GQACPTVYGV TSPYSQTTPP IVQSYAQPSL QYIQGQQIFT AHPQGVVVQP
TAAVTTIVAP GQPQPLQPPE MVVTNNLLDL PPPSPPKPKT IVLPPNWKTA RDPEGKIYYY
HVVTRQTQWD PPTWESPGDD ASLEHEAEMD LGTPTYDENP MKTSKKPKTA EADTSSELAK
KSKEVFRKEM SQFIVQCLNP YRKPDCKVGR ITTTEDFKHL ARKLTHGVMN KELKYCKNPE
DLECNENVKH KTKEYIKKYM QKFGAVYKPK EDTELE
//
