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Database: UniProt/TrEMBL
Entry: A0A1S3JUZ0_LINUN
LinkDB: A0A1S3JUZ0_LINUN
Original site: A0A1S3JUZ0_LINUN 
ID   A0A1S3JUZ0_LINUN        Unreviewed;      1380 AA.
AC   A0A1S3JUZ0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   23-MAY-2018, entry version 12.
DE   SubName: Full=histone-lysine N-methyltransferase NSD2 {ECO:0000313|RefSeq:XP_013414143.1, ECO:0000313|RefSeq:XP_013414144.1};
GN   Name=LOC106176349 {ECO:0000313|RefSeq:XP_013414143.1,
GN   ECO:0000313|RefSeq:XP_013414144.1};
OS   Lingula unguis.
OC   Eukaryota; Metazoa; Lophotrochozoa; Brachiopoda; Linguliformea;
OC   Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX   NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013414143.1};
RN   [1] {ECO:0000313|RefSeq:XP_013414143.1, ECO:0000313|RefSeq:XP_013414144.1}
RP   IDENTIFICATION.
RC   TISSUE=Gonads {ECO:0000313|RefSeq:XP_013414143.1,
RC   ECO:0000313|RefSeq:XP_013414144.1};
RG   RefSeq;
RL   Submitted (APR-2018) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] =
CC       S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
CC       {ECO:0000256|SAAS:SAAS00591578}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|SAAS:SAAS00574581}.
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DR   RefSeq; XP_013414143.1; XM_013558689.1.
DR   RefSeq; XP_013414144.1; XM_013558690.1.
DR   EnsemblMetazoa; g17700.t1; g17700.t1; g17700.
DR   GeneID; 106176349; -.
DR   KEGG; lak:106176349; -.
DR   KO; K11424; -.
DR   OMA; CMARIKY; -.
DR   Proteomes; UP000085678; Genome assembly.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 3.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR003616; Post-SET_dom.
DR   InterPro; IPR000313; PWWP_dom.
DR   InterPro; IPR001214; SET_dom.
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; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00628; PHD; 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; SSF47095; SSF47095; 1.
DR   SUPFAM; SSF57903; SSF57903; 3.
DR   PROSITE; PS51215; AWS; 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.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000085678};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01011399};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS00590675,
KW   ECO:0000313|RefSeq:XP_013414143.1, ECO:0000313|RefSeq:XP_013414144.1};
KW   Nucleus {ECO:0000256|SAAS:SAAS00574642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW   S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00591079};
KW   Transferase {ECO:0000256|SAAS:SAAS00591533,
KW   ECO:0000313|RefSeq:XP_013414143.1, ECO:0000313|RefSeq:XP_013414144.1};
KW   Zinc {ECO:0000256|SAAS:SAAS01006535};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00146,
KW   ECO:0000256|SAAS:SAAS01007077}.
FT   DOMAIN      215    277       PWWP. {ECO:0000259|PROSITE:PS50812}.
FT   DOMAIN      608    657       PHD-type. {ECO:0000259|PROSITE:PS50016}.
FT   DOMAIN      775    819       PHD-type. {ECO:0000259|PROSITE:PS50016}.
FT   DOMAIN      824    886       PWWP. {ECO:0000259|PROSITE:PS50812}.
FT   DOMAIN      959   1009       AWS. {ECO:0000259|PROSITE:PS51215}.
FT   DOMAIN     1011   1128       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN     1135   1151       Post-SET. {ECO:0000259|PROSITE:PS50868}.
FT   COILED     1157   1177       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1380 AA;  153365 MW;  0D94E0A1DA3016C5 CRC64;
     MEEQQQSASR SSKPAVPVVH RHLPQIAPMS HNPKIAQSKA SAKQTYADAE PAILPGPIPS
     DTAAFPNIVA NIEAKVNEEE KVSNATPSLP NGNVSISDHA IGDTSDGNEN GGEKKVKSRV
     ASPAKMRIKK GTKVNSGDSI PDNLPAESVA KAAPTEASAN GIADNSGKRR RKKKDLDKED
     ETLSGSVKST PPSTPPKLSK PIQQLEAERP PKWLVGEMVW SKVSGHPWWP CMVTYDPLEG
     VYTKFQGVTR KYHMQFFGEV AERGWVTETS TLPYEGKAAF DKYIQDKMAA APNKTAKAQI
     AHKFEVSSRR KFARDFAVEC AEEAFQMPRN ERKHKYTFVY EDLKPNDQSQ GADGATEKPG
     SDLPNGVIKP KRPYNKRKLS NKESVSSSPV AKKSRTGPEM HTNSEEASPK KTSRALKEKS
     PGQFLVFCEK HRDQVKSEHN EFDEAMVEAY LKQQWNAMND KQRGRYTSKF QSNSEGPDEE
     EGAGTTEERG VKTSSRLPKP SKKVLEAHTA KHARRKKLKK RGRKPKTDGQ PGSGSSLDDV
     INSVVAGCGK PKSYKHAAVS RKTSVATEED EQEPGTRKMT LEERRIQEGQ EYELEIFKLV
     ANGTQKKENI CVICEESHAL GELIQCEGPC SGSFHLSCLG LTAAPAGVFK CDECTSGCHT
     CFACKKAGKD LKKCSVPLCG KFYHEHCASQ FLLSKFEAKG LVCPLHVCTN CAEGNPKNPK
     ATKGRLYRCV RCPTAYHAGD LCVAAGSVNL AGYNIVCSKH FQPVKAHKHH SHVNVSWCFI
     CNKGGTLLCC ESCPAAFHPE CLKILFPDDS WFCRDCAVGK TPLYGDIIWV KLGIYRWWPG
     EICHPRHVPL NIQEKDHQVG EFPVRFFGSH DYFWTHKRRV FLFQEGDKGS RDYTNCKGLA
     KVFRLAVAEA TEAFKVWKSY KDTKEQQEIE RNDKKPAPFK FIKTNIPYGS VQLYKPDLSE
     LPRCECKPSS EHPCGSDSEC YNRMLQYECH PSVCPAGEKC ENQRFQKRLY VESESFRTSS
     RGWGLRALRD VKKGEFVNEY CGELVDEEEC KRRIQKAHDE NISNFYMLTI DKNRIIDAGP
     KGNLSRFINH SCQPNLETQK WTVNGNIRVG LFASDDIPAG TEFTFNYNLD CLGNEKTVCQ
     CGSPNCSGFL GVRPKTAAAA ANEKKAKEAK KRKKRRNKPD VKKEHEDWCF RCGEGGELVM
     CDRTKCPKAY HLGCLGLNKP PHGKWDCPWH HCDDCGKPAV KLCTECPNSF CQAHIEKNVI
     LDLADGTVLC SDHDELVDSM KNSSSGTDSE SSSQVASDVT QTSTSAVPTE QGTDQDKTKA
     IKRRKAAESN RTAASKKIQK RAKTSSKQPS QGNEMKIETE DPGSESDDGD GKLVMDVPVL
//
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