SET1B_XENLA
ID SET1B_XENLA Reviewed; 1938 AA.
AC Q66J90;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Histone-lysine N-methyltransferase SETD1B;
DE EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9UPS6};
DE AltName: Full=SET domain-containing protein 1B;
GN Name=setd1b;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Histone methyltransferase that specifically methylates 'Lys-
CC 4' of histone H3, when part of the SET1 histone methyltransferase (HMT)
CC complex, but not if the neighboring 'Lys-9' residue is already
CC methylated. H3 'Lys-4' methylation represents a specific tag for
CC epigenetic transcriptional activation. {ECO:0000250|UniProtKB:O15047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC Evidence={ECO:0000250|UniProtKB:Q9UPS6};
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250}. Chromosome
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
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DR EMBL; BC081016; AAH81016.1; -; mRNA.
DR RefSeq; NP_001087630.1; NM_001094161.1.
DR AlphaFoldDB; Q66J90; -.
DR SMR; Q66J90; -.
DR PRIDE; Q66J90; -.
DR DNASU; 447454; -.
DR GeneID; 447454; -.
DR KEGG; xla:447454; -.
DR CTD; 447454; -.
DR Xenbase; XB-GENE-5842376; setd1b.S.
DR OMA; RMPIEEC; -.
DR OrthoDB; 1234689at2759; -.
DR Proteomes; UP000186698; Chromosome 1S.
DR Bgee; 447454; Expressed in egg cell and 13 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IEA:InterPro.
DR CDD; cd12549; RRM_Set1B; 1.
DR Gene3D; 2.170.270.10; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR024657; COMPASS_Set1_N-SET.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR044570; Set1-like.
DR InterPro; IPR034468; Set1B_RRM.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR037842; SETD1B.
DR PANTHER; PTHR45814; PTHR45814; 1.
DR PANTHER; PTHR45814:SF1; PTHR45814:SF1; 1.
DR Pfam; PF11764; N-SET; 1.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF00856; SET; 1.
DR SMART; SM01291; N-SET; 1.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR SUPFAM; SSF82199; SSF82199; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50280; SET; 1.
PE 2: Evidence at transcript level;
KW Activator; Chromatin regulator; Chromosome; Methyltransferase; Nucleus;
KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transcription;
KW Transcription regulation; Transferase.
FT CHAIN 1..1938
FT /note="Histone-lysine N-methyltransferase SETD1B"
FT /id="PRO_0000316997"
FT DOMAIN 111..199
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 1799..1916
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1922..1938
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 496..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 916..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1327..1373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1413..1468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1496..1528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..1772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..340
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 567..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1023..1041
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1110
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1111..1125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1174
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1347..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1938 AA; 216257 MW; B8DD492A64888086 CRC64;
MSFKEAKPGE RGKNPEDHGR KQAASWMNGM EAANQPSTSA EKKSHHWRSY KLIIDPALRK
GQQKLYRYDG LSFSMPNSGA PPVDSVRDPR IGRIWTKTKE LDLPVPKLKI DEFYVGPVPP
KQVTFAKLND NIRENFLGDM CKKYGEVEEV EILYNPKNKK HLGIAKVIFA TVKGAKDAVK
HLHNTSVMGN IIHAELDTKG ETRMRFYELL VNGYYTPQTL PVGSDLDASP TVNETPQVVE
PVKRTKETAV GASVTPNSST PFSHDTAYSS SRQGTPNSYS QFTPQSQGTP HTPRLGTPFS
QDSSYSSRQT TPAFHYGQDS SFKPRRHENK FTDAYNRRPG HHYVHSSGSY RGPENTFNVT
RPQAETVQFP RTPPLSHSSG NNKSAFSPYQ GSTVFPQTDD NQYPQTSRDM EYRRTGPPTS
DSYSDGSLEL KLVKEKPEEP PPPEPDSTTE QKASFAQTPE RCATPGTPTL EAEMQHDSLD
TRIAMLLKEQ RTQLHLISSD QNSDSEIRME GSPISSSSSQ LSPIPPYSSS SHYQDVTPSS
RPSSTGLEDI SPTPLPDSDD DEPIPGTASL CQNSRSASPI DQINQPVRKM ETLDNKELVV
GDETPTSEKM DEGHPSSGED MEISDDEVTP SPITSAECAI TSSSVIPILP PGFPPLPPPP
PPQSGFPMPP PLPPPPPPTH PSVTVPPPPL PAPPGVPPHH ILHHPPPYHH FPVMQGEMMN
VLGNHWGGMT MSFQMQTQML SRMMQGQGSY PYHHFMGGSM QFGNQLPYRP FALSAHLSRG
QPWPPLPKFD PSVPPPGYEP KKEDPHKATV DGVLQVIVKE LKAIMKRDLN RKMVEVVAFR
AFDEWWDKKE RLAKQSLTPV KSGESKDEDK QKTKEHITSS LLESWNKGEG LGFEGIGLGI
GLRGAIRLPS FKVKRKEPPD AALAGDQKRI RPSHSVDDED EESERDRDIS GTASDLSKKD
ADAVNIRRRP ARPLDSEGEE EVESEGDDGE TSDKEAFEKE DQDAGSVSAL SSKKRLYGEK
EDEEDETQSS GKEEDLVSEE EDITSVASSR AEMDSSDESD ESSEYESSSD SDDEIEEEDD
DDEEEELVFE DDQSEELDLG QEDYIETDRE EDFFKEDVSE CSSPVKAEAD MELEDDDVQK
LEQDVAHQTA QDTSHLRKKD LDVPLVESKE HKQDTFDKME RLSAVPMQQN VFKEHEKAPS
PMNEEEEYIE LRLEPVPLVP DNAPPAVQEP MIIRPLTPTG AFGESGPVLK LEEPKLQVNL
AHFVAEDEDL YPRTPGRDTA AHSDTEVTFQ PGLKVAPSSL PLLQSHNKEE ECLLPPEKHT
GHLKVTKTLS EEELPRTPGR DILVKSSHLG KSQSTETIPA TPGSDAPLTG NSLTLTSPHI
PGSPFSYLSQ SPGIINSGIP RTPGRDFNFT PIFPESNSIF PSHPSGKKSS VDEPDEKSFK
EPTSASLTMN SVPSPIPFAS PPRGVPHMDI RLETDDLESS DTQAYLSDKL LSEESECEFT
KGQLPSTDES APSPPFPPTD KRKGPKKPLA AHEFEACVAL SEGALGKQLF IGQPDSVSGI
KDPAAVPLDF RNDGLSENTV HDPIIQKVPL KELENQWNEV LKEEEEDISK HKKSRNSRLN
KLYDEFSTLP SPEYSPPRAM FKPRSEFEEM TILYDIWNGG IDDEDMKYMC ITYDRLLQQD
NGMDWLNDTL WVYHPPTSVY SPKKKKRDDG LREHVTGCAR SEGYYKIDKK DKLKYLINNR
SLADEPPIDT QGKSIPAQPQ ASTRAGSERR SEQRRLLSSF TGSCDSDLLK FNQLKFRKKK
IRFCKSHIHD WGLFAMEPIV ADEMVIEYVG QNIRQVIADM REKRYEDEGI GSSYMFRVDH
DTIIDATKCG NFARFINHSC NPNCYAKVVT VESQKKIVIY SKQYINVNEE ITYDYKFPIE
DVKIPCLCGA ENCRGTLN
