ID A0A1S3FYC2_DIPOR Unreviewed; 1440 AA.
AC A0A1S3FYC2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Histone-lysine N-methyltransferase NSD3 isoform X2 {ECO:0000313|RefSeq:XP_012880842.1};
GN Name=Whsc1l1 {ECO:0000313|RefSeq:XP_012880842.1};
OS Dipodomys ordii (Ord's kangaroo rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC Dipodomyinae; Dipodomys.
OX NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012880842.1};
RN [1] {ECO:0000313|RefSeq:XP_012880842.1}
RP IDENTIFICATION.
RC TISSUE=Kidney {ECO:0000313|RefSeq:XP_012880842.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR RefSeq; XP_012880842.1; XM_013025388.1.
DR STRING; 10020.ENSDORP00000006773; -.
DR GeneID; 105992508; -.
DR CTD; 54904; -.
DR InParanoid; A0A1S3FYC2; -.
DR OrthoDB; 950362at2759; -.
DR Proteomes; UP000081671; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042054; F:histone methyltransferase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15649; PHD1_NSD3; 1.
DR CDD; cd15652; PHD2_NSD3; 1.
DR CDD; cd15658; PHD4_NSD3; 1.
DR CDD; cd15661; PHD5_NSD3; 1.
DR CDD; cd20163; PWWP_NSD3_rpt1; 1.
DR CDD; cd20166; PWWP_NSD3_rpt2; 1.
DR CDD; cd19212; SET_NSD3; 1.
DR Gene3D; 2.30.30.140; -; 2.
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; IPR047456; PHD2_NSD3.
DR InterPro; IPR047458; PHD4_NSD3.
DR InterPro; IPR047527; PHD5_NSD3.
DR InterPro; IPR003616; Post-SET_dom.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR047451; PWWP_NSD3_rpt1.
DR InterPro; IPR047453; PWWP_NSD3_rpt2.
DR InterPro; IPR001214; SET_dom.
DR InterPro; IPR046341; SET_dom_sf.
DR InterPro; IPR047461; SET_NSD3.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22884:SF473; HISTONE-LYSINE N-METHYLTRANSFERASE NSD3; 1.
DR PANTHER; PTHR22884; SET DOMAIN PROTEINS; 1.
DR Pfam; PF17907; AWS; 1.
DR Pfam; PF17982; C5HCH; 1.
DR Pfam; PF00855; PWWP; 2.
DR Pfam; PF00856; SET; 1.
DR SMART; SM00570; AWS; 1.
DR SMART; SM00249; PHD; 4.
DR SMART; SM00508; PostSET; 1.
DR SMART; SM00293; PWWP; 2.
DR SMART; SM00317; SET; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 3.
DR SUPFAM; SSF82199; SET domain; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 2.
DR PROSITE; PS51215; AWS; 1.
DR PROSITE; PS50868; POST_SET; 1.
DR PROSITE; PS50812; PWWP; 2.
DR PROSITE; PS50280; SET; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000081671};
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:PRU00146}.
FT DOMAIN 270..333
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 700..747
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 960..1025
FT /note="PWWP"
FT /evidence="ECO:0000259|PROSITE:PS50812"
FT DOMAIN 1096..1146
FT /note="AWS"
FT /evidence="ECO:0000259|PROSITE:PS51215"
FT DOMAIN 1148..1265
FT /note="SET"
FT /evidence="ECO:0000259|PROSITE:PS50280"
FT DOMAIN 1272..1288
FT /note="Post-SET"
FT /evidence="ECO:0000259|PROSITE:PS50868"
FT DOMAIN 1324..1371
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 121..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 545..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1037..1064
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 124..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..466
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1440 AA; 161927 MW; AFF17D3869B5615F CRC64;
MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNNSDI VEDGGQTPYE ATLQQGFQYP
PTTEDLPPLT NGYPPSISMY DTQTKYQPYN QYPNGSANGF GAVRNFSPTD YYHSEIPNTR
PHEILEKPSP PQPPPPPSVP QTVIPKKTGS PEIKLKITKT IQNGRELFES SLCGDLLNEV
QASEHTKSKH ESRKEKRKKS NKHDSARSEE RKAHKIPKLE PEEQNRPNER LDPTPEKPRA
EPVIKETAPV QPILSSVSTT EVSTGIKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHTKI
NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHKQYEELL AEATKQASNH SEKQKIRKPR
PQRERAQWDI GIAHAEKALK MTREERIEQY TFIYIDKQPE ETLSQAKKNV TSKTDVKKPR
RPRSVLNTQP EQTNAGEVAS SQSSTEIRRQ SQRRHTSTEE EEPPPVKIAW KTAAARKSLP
ASITMHKGGL DLQKCNMSPV VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ
DRLIISSPNQ KSEKPTQNIS SPEATSCPTG SVEKKQQRRS IRTRSESEKS TEVVPKKKIK
KEQVETVPQA TVKTGLQKGA SEISDSCKPL KKRSRASTDV EMTSSAYRDT SDSDSRGLSD
LQVGFGKQVD SPSATADADM SDAQSMDSNL SRRGVGSRKD TVCQICESPG DSLTPCEGEC
CRHFHLECLG LTSVPEGKFI CTECNTGEHP CFSCKVSGKD VKRCSVGTCG KFYHEACVRK
FPTAIFESKG FRCPQHCCSA CCMEKDIHKA SKGRMMRCLR CPVAYHSGDA CIAAGSVSVT
SYILICSNHS KRANHTTAAI NVGFCFVCAR GLIVQDHSDP MFSSYAYKSH YLLNESNRAE
LMKLPMIPSS SASKKKCEKG GRLLCCESCP ASFHPECLSI DMPDGCWNCN DCKAGKKLHY
KQIVWVKLGN YRQVLWWPAE ICNPRSVPLN IQGLKHDLGD FPVFFFGSHD YYWVHQGRVF
PYVEGDKSFA EGQTSINKTF KKALEEAAKR FQELKAQRES KEALEIEKNS RKPPPYKHIK
ANKVIGKVQI QVADLSEIPR CNCKPADENP CGLESECLNR MLQYECHPQV CPAGDRCQNQ
CFTKRLYPDA EIIKTERRGW GLRTKRSIKK GEFVNEYVGE LIDEEECRLR IKRAHENSVT
NFYMLTVTKD RIIDAGPKGN YSRFMNHSCN PNCETQKWTV NGDVRVGLFA LCDIPAGMEL
TFNYNLDCLG NGRTACHCGA DNCSGFLGVR PKTACASTAE EKAKNAKLKQ KRRKIKTEPK
QMYEDYCFQC GDSGELVMCD KKDCPKAYHL LCLNLTQPPY GKWECPWHQC SKCGSAAISF
CEFCPRSFCK EHDKGALVPS ALEGHLCCSE HDPLSPVSSE YWSKIKCRWE SQDHGEEAGE
//
