ID H9FTE9_MACMU Unreviewed; 2565 AA.
AC H9FTE9;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 24-JAN-2024, entry version 73.
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|EMBL:AFE77908.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:AFE77908.1};
RN [1] {ECO:0000313|EMBL:AFE77908.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Caudate {ECO:0000313|EMBL:AFE77908.1};
RX PubMed=25319552; DOI=10.1186/1745-6150-9-20;
RA Zimin A.V., Cornish A.S., Maudhoo M.D., Gibbs R.M., Zhang X., Pandey S.,
RA Meehan D.T., Wipfler K., Bosinger S.E., Johnson Z.P., Tharp G.K.,
RA Marcais G., Roberts M., Ferguson B., Fox H.S., Treangen T., Salzberg S.L.,
RA Yorke J.A., Norgren R.B.Jr.;
RT "A new rhesus macaque assembly and annotation for next-generation
RT sequencing analyses.";
RL Biol. Direct 9:20-20(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JU334153; AFE77908.1; -; mRNA.
DR RefSeq; XP_001113652.2; XM_001113652.3.
DR HOGENOM; CLU_000810_1_0_1; -.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
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 2: Evidence at transcript level;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AFE77908.1}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transcription {ECO:0000256|ARBA:ARBA00023015};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AFE77908.1}.
FT DOMAIN 1495..1549
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1551..1668
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1675..1691
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 2390..2423
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..996
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1133..1235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1394..1426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1832..1873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..2148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2440..2466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 968..994
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1095
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1096..1111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1141..1155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1297
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1832..1868
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1925..1950
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1953..1972
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2012..2047
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2056..2081
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2091..2131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2132..2148
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2450..2466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2565 AA; 287912 MW; 113C17930BC00C75 CRC64;
MKQLQPQPPP KMGDFYDPEH PTPEEEENEA KIENVQKTGF IKGPMFKGVA SSRFLPKGTK
TKVNLEEQGR QKVSFSFSLT KKTLQNRFLT ALGNEKQSDT PNPPAVPLQV DSTPKMKMEI
GDTLSTAEES SPPKSRVELG KIHFKKHLLH VTSRPLLATT TAVASPPTHA APLPAVIAES
TTVDSPPSSP PPPPPPAQAT TPSSPAPITE PVALPHTPVT VLMAAPVPLP VDVAVRSLKE
PPIIIVPESL EADTKQDTVS NSSEEHITQI LNEQADISSK KEDSHIGKDE EIPDSSKISL
SCKKTGSKKK SSQSEGTFLG SESDEDSVRT SSSQRSHDLK FSASIERERD FKKSSAPLKS
EDLGKSSRSK TERDDKYFSY SKLERDTRYV SSRCRSERER RRSRSHSRSE RGPRTNLSYS
RSERSHYYDS DRRYHRSSPY RERTRYSRPY TDNRARESSD SEEEYKKTYS RRTSSHSSSY
RDLRTSSYSK SDRDCKTETS YLEMERRGKY SSKLERESKR TSENEAVKRC CSPPNELGFR
RGSSYSKHDS SASRYKSTLS KPIPKSDKFK NSFCCTELNE EIKQSHSFSL QTPCSKGSEL
RMINKNPERE KAGSPAPSNR LNDSPTLKKL DEFPIFKSEF ITHDSHDRIK ELDSLSKVRN
DQLRSFCPIE LNINGSPGAE SDLATFCTSK TDAVLMTSDD SVTGSEVSPL VKACMLSSNG
FQNISRCKGK DLDDTRMLHK KSESPFRETE PLVSPHQDKL MSLPVMTIDY SKTVVKEPVD
TRVSCCKTKD SDIYCTSNDS NNPSLCNSEA ENIEPSVMKI SSNSFMNVHL ESKPVICDSR
NLTDHSKFAC EEYKQSIGST SSASVNHFDD LYQPIGSSDI ASSLQSLPPG IKVDSLTLLK
CGENTSPVLD AVLKSRKSSE FLKHAGKETV VEVGSDLPDS GKGFASRENR RNNGLSGKCL
QEAQEEGNSI LPDRRGRPEI SLHERGEGGR VHTSDDSEVV FSSCDLNLTM EDSDGVTYAL
KCDSSGHAPE IVSTAHEDYS DSSESSSDES DSEDTDSDDS SIPRNRLQSV VVVPKNSTLP
VEETSPCSSR SSQSYRHYSD HWEDERLESR RHSYEEKFES IANKACPQTD KFFLHKGTEK
NPEISFTQSN RKQIDNHLPE LSHPQSDGVD STSHTDVKSD SLGHPNSEET VKAKISSRQQ
EELPIYSSDF EDVPNKSWQQ STFQNRPDSR LGKTELSFSS SCEISRVDGL HSSEELRNLG
WDFSQEKPST TYQQPDSSYG TCGGHKYQQN AEQYGGTRDY WQGNGYWDPR SGRPPGTGVV
YDRTQGQVPD SLTDDREEEE NWDQQDGSHF SDQSNKYLLS LQKDKGSVQA PEISSNSIKD
TLAVNEKKEF SKNLEKNDIK DRGPLKKRRQ EIESDSESDG ELQDRKKVRV EVEQGETSVP
PGSALVGPSC VMDDFRDPQR WKECAKQGKM PCYFDLIEEN VYLTERKKNK SHRDIKRMQC
ECTPLSKDER AQGEIACGED CLNRLLMIEC SSRCPNGDYC SNRRFQRKQH ADVEVILTEK
KGWGLRAAKD LPSNTFVLEY CGEVLDHKEF KARVKEYARN KNIHYYFMAL KNDEIIDATQ
KGNCSRFMNH SCEPNCETQK WTVNGQLRVG FFTTKLVPSG SELTFDYQFQ RYGKEAQKCF
CGSANCRGYL GGENRVSIRA AGGKMKKERS RKKDSVDGEL EALMENGEGL SDKNQVLSLC
RLMVRIETLE QKLTCLELIQ NTHSQSCLKS FLERHGLSLL WIWMAELGDG RESNQKLQEE
IIKTLEHLPI PTKNMLEESK VLPIIQRWSQ TKTAVPPLSE GDGYSSENTS RAHTPLNTPD
PSTKLSTEAD TDTPKKLMFR RLKIISENSM DSAISDATSE LEGKDGKEDL DQLENVPVEE
EEELQSQQLL PQQLPECKVE SETNIEASKL PTSEPEADTE IEPKESNGTK LEEPINEETP
SQDEEEGVSD VESERSQEQP DKTVDISDLA TKLLDSWKDL KEVYRIPKKS QTEKENTTAE
RGRDAVGFRD QTPAPKTPNR SRERDPEKQT QNKEKRKRRG SLSPPPSAYE RGTKRPDDRY
DTPTSKKKVR IKDRNKLSTE ERRKLFEQEV AQREAQKQQQ QMQNLGMTSP LPYDSLGYNA
PHHPFAGYPP GYPMQAYVDP SNPNAGKVLL PTPSMDPVCS PAPYDHAQPM VGHSTEPLSA
PPPVPVVPHV AASVEVSSSQ YVAQSEGVVH QDSSVAVLPV PAPGPVQGQN YSVWDSNQQS
VSVQQQYSPA QSQATIYYQG QTCPAVYGVT SPYSQTTPPI VQSYAQPSLQ YIQGQQIFTA
HPQGVVVQPA AAVTTIVAPG QPQPLQPSEM VVTNNLLDLP PPSPPKPKTI VLPPNWKTAR
DPEGKIYYYH VITRQTQWDP PTWESPGDDA SLEHEAEMDL GTPTYDENPM KTSKKPKTAE
ADTSSELAKK SKEVFRKEMS QFIVQCLNPY RKPDCKVGRI TTTEDFKHLA RKLTHGVMNK
ELKYCKNPED LECNENVKHK TKEYIKKYMQ KFGAVYKPKE DTELE
//