SET1B_XENTR
ID SET1B_XENTR Reviewed; 1956 AA.
AC Q08D57;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (SEP-2006) 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; BC123932; AAI23933.1; -; mRNA.
DR RefSeq; NP_001072649.1; NM_001079181.1.
DR AlphaFoldDB; Q08D57; -.
DR SMR; Q08D57; -.
DR STRING; 8364.ENSXETP00000008143; -.
DR PaxDb; Q08D57; -.
DR GeneID; 780106; -.
DR KEGG; xtr:780106; -.
DR CTD; 23067; -.
DR Xenbase; XB-GENE-5842344; setd1b.
DR eggNOG; KOG1080; Eukaryota.
DR InParanoid; Q08D57; -.
DR OrthoDB; 1234689at2759; -.
DR Reactome; R-XTR-3214841; PKMTs methylate histone lysines.
DR Reactome; R-XTR-8936459; RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
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; IBA:GO_Central.
DR GO; GO:0042800; F:histone methyltransferase activity (H3-K4 specific); IBA:GO_Central.
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; IBA:GO_Central.
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..1956
FT /note="Histone-lysine N-methyltransferase SETD1B"
FT /id="PRO_0000316998"
FT DOMAIN 111..199
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 1817..1934
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1940..1956
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..637
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..696
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1766..1790
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 248..316
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 349..365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..627
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..987
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1003
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1055
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1118
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1356..1386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1528..1550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1766..1784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1956 AA; 218069 MW; 9AFF263E87E53DCD CRC64;
MSFKEAKPGE RGKNPEDHGR KQTASWINGM EAGNQPSTSG EKKSHHWRSY KLIIDPALRK
GQHKLYRYDG LSFSMPNSGV PPVDSVRDPR IGRIWTKTKE LDLPVPKLKI DEFYVGPVPP
KQVTFAKLND NIRENFLGDM CKKYGEVEEV EILYNPKNKK HLGIAKVIFA SVKGARDAVK
HLHNTSVMGN IIHVELDTKG ETRMRFYDLL VNGFYTPQTL PVGSDLDASP TVNETPQVVE
SVKRTKETAI GPSVTPNSST PFSHDTAYSS SRQGTPNSYS QFTPQSQGTP HTPRLGTPFS
QDSSYSSRQT TPAFHYGQDS GFKPRRHENK FTDAYNRRPG HHYVHSSGSY RGTEHTFNVT
RPQPEPVQVP RTPPLSHSSG NYKSAFSPYQ GNTVFPQTDE SQYPQTSRDM EYRRTGPQTS
DSYSDAGCNS ASLELKPVKE KPEEPPPPEP DSTTEQKASF SQTPERCETP GTPTLEAELQ
HNSLDTRIAM LLKEQRTQLH LIAGDQNSDN EIRMEGSPIS SSSSQLSPIP PYSSGSRYQD
VTPSSRPSST GLEDISPTPL PDSDDDDEPI PGTASLCQNS RSASPIDQIN QSGRKTESLD
KKELVAGDET PTSEKMDEGH PSSGEDMEIS DDEVTPSPIT SAECAITSSS VISSVIPIPP
PGFPPLPPPP PPQPGFPMPP PLPPPPPPTH PSVTVPPPPL PAPPGVPPHH ILHHPPPYHH
FPVMQGEMMN VLGNHWGGMT MSFQMQTQML SRMMQGQGSY PYHHFMGGSM QFGNQHPYRP
FAISAHLTRG QPWPPFPKFD PSVPPPGYEH KKEDPHKATV DGVLQVIVKE LKAIMKRDLN
RKMVEVVAFR AFDEWWDKKE RLAKQSLTPV KSGESKEEDK QKTKEHITSS LLESWNKGEG
LGFEGIGLGI GLRGAIRLPS FKVKRKEPPD AALAGDQKRI RPSHSVDDED EESERDRDIS
STASDLSKKD ADAVNNRRRP ARPLDSEGEE EVESEGDDGE TSDKEDSSSE KEDQDDGSVS
ALSSKKQLYG DKEGDDEDDD TQSSGKEEDL VSEEEDTTSV ASSRAEMDSS DESEESSEYE
SSSDSDEKEE EDDEEEELVF GDDQSEDQDL GQEYEVETDR EEDFFRENLS ECSSLPKAGD
VELEDEMQKV EEDVARQTTQ ETLHLRKKNL DVPLVESKEC KQDTLDKVEK LFAVPMQEEV
FKEHEKAPSP MNEEEEYIEL QLEPVPLVPE GAAPAAQEPV IIRPLTPTGA FGETGPVLKL
EEPKLQVNLT QFATEDEELY PRTPGRDTAA HSDTEVTFQP GLKVAPSSLP FLPSHNKEEE
CLLPPEKHAG HLTVTKMLSE EDLPRTPGRD IVVKSSHLGK SQSTETVPAT PGSDAPLTGS
SLTLTSPHIP GSPFSYLSQS PGIINSGIPR TPGRDFNFTP TFPESNSIFP CHPSGKKPSV
DEPDEKSFKE PTSASLTMNS VPSPIPFASP PRGLPHMDIR LGADDLESSD TPAYLSDKLL
SEESECEFTK VHLTSTDESA PSPPLPPAEK RKGDRSKKPL SAHEFETEKN YETSSAVAMS
EGALGKQMFI GQPDAVSGIK DPAAVPLDFR NDSLSENTVH EPIIQKVPLK ELENQWNEVL
KEEEDITKHK KSRNSRHNNR YDEFSTVPSP EFSPPRAMFK PRSEFEEMTI LYDIWNGGID
DEDIKYMCIT YDRLLQQDNG MDWLNDTLWV YHPSTSVYSP KKKKRDDGLR EHVTGCARSE
GYYKIDKKDK LKYLINNRSL TEELPIDTQG KSIPAQPQAS TRAGSERRSE QRRLLSSFTG
SCDSDLLKFN QLKFRKKKLR FCKSHIHDWG LFAMEPIIAD EMVIEYVGQN IRQVIADMRE
KRYEDEGIGS SYMFRVDHDT IIDATKCGNF ARFINHSCNP NCYAKVITVE SQKKIVIYSK
QYINVNEEIT YDYKFPIEDV KIPCLCGAEN CRGTLN
