ID A0A493TDD3_ANAPP Unreviewed; 1394 AA.
AC A0A493TDD3;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Nuclear receptor binding SET domain protein 2 {ECO:0000313|Ensembl:ENSAPLP00000023665.1};
GN Name=NSD2 {ECO:0000313|Ensembl:ENSAPLP00000023665.1};
OS Anas platyrhynchos platyrhynchos (Northern mallard).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Anseriformes; Anatidae;
OC Anatinae; Anas.
OX NCBI_TaxID=8840 {ECO:0000313|Ensembl:ENSAPLP00000023665.1, ECO:0000313|Proteomes:UP000016666};
RN [1] {ECO:0000313|Ensembl:ENSAPLP00000023665.1, ECO:0000313|Proteomes:UP000016666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hou Z.-C., Zhou Z.-K., Zhu F., Hou S.-S.;
RT "A new Pekin duck reference genome.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSAPLP00000023665.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR STRING; 8840.ENSAPLP00000023665; -.
DR Ensembl; ENSAPLT00000040197.1; ENSAPLP00000023665.1; ENSAPLG00000003770.2.
DR GeneTree; ENSGT00940000157429; -.
DR Proteomes; UP000016666; Chromosome 4.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140955; F:histone H3K36 trimethyltransferase activity; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:Ensembl.
DR GO; GO:0003289; P:atrial septum primum morphogenesis; IEA:Ensembl.
DR GO; GO:0003290; P:atrial septum secundum morphogenesis; IEA:Ensembl.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0003149; P:membranous septum morphogenesis; IEA:Ensembl.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IEA:Ensembl.
DR GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IEA:Ensembl.
DR GO; GO:0070201; P:regulation of establishment of protein localization; IEA:Ensembl.
DR CDD; cd21991; HMG-box_NSD2; 1.
DR CDD; cd15651; PHD2_NSD2; 1.
DR CDD; cd15654; PHD3_NSD2; 1.
DR CDD; cd15657; PHD4_NSD2; 1.
DR CDD; cd15660; PHD5_NSD2; 1.
DR CDD; cd20162; PWWP_NSD2_rpt1; 1.
DR CDD; cd20165; PWWP_NSD2_rpt2; 1.
DR CDD; cd19211; SET_NSD2; 1.
DR Gene3D; 2.30.30.140; -; 2.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 2.170.270.10; SET domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 4.
DR InterPro; IPR006560; AWS_dom.
DR InterPro; IPR041306; C5HCH.
DR InterPro; IPR047443; HMG-box_NSD2.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR047439; PHD2_NSD2.
DR InterPro; IPR047441; PHD3_NSD2.
DR InterPro; IPR047442; PHD5_NSD2.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR047434; PWWP_NSD2_rpt1.
DR InterPro; IPR047435; PWWP_NSD2_rpt2.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR047437; SET_NSD2.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22884:SF293; HISTONE-LYSINE N-METHYLTRANSFERASE NSD2; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF17982; C5HCH; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF00855; PWWP; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00398; HMG; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00293; PWWP; 2.
DR SMART; SM00184; RING; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 2.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000016666};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 223..288
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 457..506
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 697..743
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 747..793
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 861..905
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 910..972
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1041..1091
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1093..1210
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1217..1233
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DNA_BIND 457..506
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 144..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 524..546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 674..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1388
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 157407 MW; B83B09C6D718456F CRC64;
MDFSIKRSSQ LLTRKINYIK MKQVPEILGN TNGKTQNCEV NRECSVYLGK AQLSATIQEG
VMQKYNGHDA LPFIPADKLK DLTSRVFNGE SGAQDAKLRF EPQEIKGVGT PPNTTPIKNG
SPEIKLKITK TYMNGKPLFE SSICGDNGAD VSQSEENEQK PANKERRNRK RSIKYDSLLE
QGLVEAALVS KTSSSPEKKA PAKKDLTQST IKEDKVHLLK YNIGDLVWSK VSGFPWWPCM
VSADPVLHAY TKLKGQKKSF RQYHVQFFGD APERAWIFEK SLVPFKEKDQ FEQLCQESAK
QALTKAEKIK MLKPVSGKLR PQWEMGVKQA SEAVSMTVEE RKAKYTFIYI RDRPHLNPRV
AKEVGIAVEP LEEIDESSYS NEETTENLKS MKESGIPNKR RRRTSKLSAA DDTQESSQSG
TKNTTPQKSS DQAESKRGIG SPLNRKKTPA STPRSRKGDA VSQFLVFCQK HRDEVVAEHP
DASSEEIEEL LESQWNMLSE KQKARYNTKF AIVTSPKSEE DSGSSLKNIG EAKRKVFQDS
PKRRSRSRSN LHGNKRNQKK RTKEPTEDFE VQEAPRKRLR MDKQNNRKRE TSNDKTAKTN
STKVTETSSS QKNQSATKNL SDACKPLKKR NRASAAESST LAFSKSSSPS ASLTENEISD
GQGDERSESP YESADETQTE VSISSKKSER GAGTKKEYVC QLCEKTGDLL LCEGLCYRAF
HVSCLGLSGR PAGKFICSEC TSGVHTCFVC KERKADLKRC VVSHCGKFYH EACVKKFHLT
VFENRGFRCP LHSCLSCHVS NPSHPRISKG KMMRCVRCPV AYHAGDVCIA AGCAVIASNS
IVCTNHFTAM KGKSHHAHVN VSWCFVCSKG GSLLCCESCP AAFHPDCLNI EMPDGSWYCN
DCRAGKKLHF QDIIWVKLGN YRWWPAEVCH PKNVPPNIQK MKHEIGEFPV FFFGSKDYFW
THQARVFPYM EGDRGSRYQG IKGIGKVFKN ALQEAEARFR EIKLQREAKE TQESERKPPP
YKHIKVNKPC GKVQIYTADI SEIPKCNCKP TDENPCGFDS ECLNRMLMYE CHPQVCPAGE
RCQNQCFTKR QYPETKIIKT DGKGWGLVAK RDIKKGEFVN EYVGELIDEE ECMARIKYAH
ENDITHFYML TIDKDRIIDA GPKGNYSRFM NHSCQPNCET LKWTVNGDTR VGLFAVCDIP
AGTELTFNYN LDCLGNEKTV CKCGAPNCSG FLGDRPKNSS TNASEEKGKK TKKRTRRRRT
KNEGKKESED DCFRCGDGGQ LVLCDRKSCT KAYHLSCLGL VKRPFGKWEC PWHHCDVCGK
PSVSFCHFCP NSFCKEHQDG TVLNSTLNGQ LCCSEHVLGV DSVETQKTEK PRKKLNKLKP
KRKQRNRWMR AECK
//
