SET1B_CHICK
ID SET1B_CHICK Reviewed; 2008 AA.
AC Q5F3P8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 106.
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; ORFNames=RCJMB04_10j6;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
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; AJ851602; CAH65236.1; -; mRNA.
DR RefSeq; NP_001025832.1; NM_001030661.1.
DR AlphaFoldDB; Q5F3P8; -.
DR SMR; Q5F3P8; -.
DR STRING; 9031.ENSGALP00000038427; -.
DR PaxDb; Q5F3P8; -.
DR GeneID; 416851; -.
DR KEGG; gga:416851; -.
DR CTD; 9739; -.
DR VEuPathDB; HostDB:geneid_416851; -.
DR eggNOG; KOG1080; Eukaryota.
DR InParanoid; Q5F3P8; -.
DR OrthoDB; 1234689at2759; -.
DR PhylomeDB; Q5F3P8; -.
DR PRO; PR:Q5F3P8; -.
DR Proteomes; UP000000539; 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..2008
FT /note="Histone-lysine N-methyltransferase SETD1B"
FT /id="PRO_0000316995"
FT DOMAIN 111..199
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 1869..1986
FT /note="SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT DOMAIN 1992..2008
FT /note="Post-SET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00155"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..652
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 682..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 950..1172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1345..1461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1563..1600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1674..1712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1814..1842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..390
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 579..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1012
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1013..1036
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1093
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1108..1149
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1150..1172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1397..1447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1578
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2008 AA; 223085 MW; 3A1CD3C9279D614C CRC64;
MSFREIKAGE KAKHPEDHGK KQSSSWINGM ENSTQASTSV EKRNHHWRSY KLIIDPALKK
GQHKLYRYDG QHFSMPNSGI APVDCVRDPR IGRIWTKTKE LELSVPKFKI DEFYVGPVPP
KQVTFAKLND NIRENFLTDM CKKYGEVEEV EILYNPKNKK HLGIAKVIFA TVKGAREAVQ
HLHNTSVMGN IIHVELDTKG ETRMRFYELL VNGLYTPQTL PVGTEQDASP TVNETLQLTD
SLKRLKDSNL SSVGSSVTPN SSTPFSHDTA YSSCRQDTPN SFSQFTPQSQ GTPHTPRLGT
PFSQDSTYSS RQTTPVYHFG QDSGYKHRRH ETKFTDAYNR RPGGHHYVHN SPGVFRGTEH
QFSTFKSHQQ EPVQFSHTPP LSHSSSSSYK SAFSPYQAPA VFPQSEEQPF AQTSREAEYR
RPAPPPAEMV VESSAATSAD FAPVKEKPEE PPPLPDSNSA PEPSAPSFSQ TPERSETPGT
PTMESEMQHN SLDSRIEMLL KEQRTKLPFL NEHDSDNEVR MEGSPISSSS SQLSPIPMYG
SNSQPGYRAQ TPSSRPSSTG LEDISPTPLP DSDDDEPIPG TASLNQNSRG TSEASMTPID
QLNRASKVET LEVKEMVPGD QTPTSEKMDE SQHSSGEDME ISDDEMNSAP ITSAECAKTI
VVNSSVSNAA VMAPSIPPLP PPPGFPPLPP PPPPPPQPAF PMPPPLPPPP PPTHPAVTVP
PPPLPAPPGV PPPHILPPLP PFHPGMFPVM QVDMISVLGN HWGGMPMSFQ MQTQMLSRMM
QAQNTYQYPP FMGGRMQFVN LPPYRPFSMG AARGRGQQWP PLPKFDPSVP PPGYEPKKED
PHKATVDGVL LVIVKELKAI MKRDLNRKMV EVVAFRAFDD WWDKKERLAK ASLTPVKSGG
ELEEKPKPKD RITSCLLENW NKGEGLGYEG IGLGIGLRGA IRLPSFKVKR KEPPEAASAG
DQKRIRPSTS VDDEDEESER DRDASDTTSD LSKKDAEAVG LRRRPARPLE LDSEGEEGDE
TSGKEEESSS EKEEEQEEEG GLVKAAPGKE EEEDEDDEED EDDDEDEEDE EDYEETGVET
SDKEEEQDSE EEDAASPSSS KAEVESSDES EDSSEFESSS DSDEDDDEEE EEEEDEEEEE
EEEVAEDQDR EAMVAETEHE PASHELPDDK RETILELYPV DYMDATGLGL SEPALVEKDE
GMEEVKAEES ECDQVPEESI AAETLKQLVM ERDQETKLAL SPICRPVEEP EPIVMLEPEV
QECPKPESQD EAGTVCLSTP VAVFGEARPS KSSFFSKSDD SCLETHVKTK LPSAVEEEDR
LPRTPGREVV VHSETDILLL PAHKVPSSTV PLPSTPGKEE SVVPPEKFPE QLMVTKTSIE
EEIPRTPGRD ILAKSSHPLG KSQSTDTVPA TPGSDAPLTG SSLTLSSPQV PGSPFSYPSQ
SPGINSGIPR TPGRDFNFTP TFPEAGATIP CLLSGKKQSE DDLDEKPFKE PLGASLTISM
NSVPSPIPFA SPTQADFRTD MGLPPNEPIP IAALPCIPGD GRMPIEECKA EVKSVLLSPE
APVGASILPP PPPHSVLPKR RPGRPRRSPP SVLSLDMYSG KTIEPPPVPV ALVESAMSKE
LLSAHPDAFY GLKDPEAVTL DFRNDSFHEK IAAETVAEKL PFKELENQWN EDFKEEEAHA
KPKRQWRRQK KSPEHLPVIP SPEYSPPQPQ FRPRSEFEEM TILYDIWNGG IDEEDIKFMC
ITYDRLLQQD NGMDWLNDTL WVFHPSTSFS TPKKKKRDDG MREHVTGCAR SEGYYKIDKK
DKLKYLNNSR AFAEEPPADT QGMSIPAQPH ASTRAGSERR SEQRRLLSSF TGSCDSDLLK
FNQLKFRKKK LKFCKSHIHD WGLFAMEPIA ADEMVIEYVG QNIRQVIADM REKRYEDEGI
GSSYMFRVDH DTIIDATKCG NFARFINHSC NPNCYAKVIT VESQKKIVIY SKQHINVNEE
ITYDYKFPIE DVKIPCLCGS ENCRGTLN
