GenomeNet

Database: UniProt/TrEMBL
Entry: D4A9J4_RAT
LinkDB: D4A9J4_RAT
Original site: D4A9J4_RAT 
ID   D4A9J4_RAT              Unreviewed;      1346 AA.
AC   D4A9J4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 2.
DT   25-APR-2018, entry version 81.
DE   SubName: Full=Nuclear receptor-binding SET domain protein 2 {ECO:0000313|Ensembl:ENSRNOP00000021952};
GN   Name=Nsd2 {ECO:0000313|Ensembl:ENSRNOP00000021952,
GN   ECO:0000313|RGD:1307955}; Synonyms=Whsc1 {ECO:0000313|RGD:1307955};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|Ensembl:ENSRNOP00000021952, ECO:0000313|Proteomes:UP000002494};
RN   [1] {ECO:0000313|Ensembl:ENSRNOP00000021952, ECO:0000313|Proteomes:UP000002494}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000021952,
RC   ECO:0000313|Proteomes:UP000002494};
RX   PubMed=15057822; DOI=10.1038/nature02426;
RG   Rat Genome Sequencing Project Consortium;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
RA   Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
RA   Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
RA   Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
RA   Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
RA   Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
RA   Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
RA   Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
RA   Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
RA   D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
RA   Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
RA   Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
RA   Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
RA   Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
RA   Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
RA   Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
RA   Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
RA   Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
RA   Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
RA   Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
RA   Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
RA   Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
RA   Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
RA   Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
RA   Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
RA   Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
RA   Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
RA   Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
RA   Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
RA   Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
RA   Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
RA   Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
RA   Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
RA   Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
RA   Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into
RT   mammalian evolution.";
RL   Nature 428:493-521(2004).
RN   [2] {ECO:0000313|Ensembl:ENSRNOP00000021952}
RP   IDENTIFICATION.
RC   STRAIN=Brown Norway {ECO:0000313|Ensembl:ENSRNOP00000021952};
RG   Ensembl;
RL   Submitted (JUL-2011) to UniProtKB.
RN   [3] {ECO:0000213|PubMed:22673903}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   EMBL; AABR07072416; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC133613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001178481.1; NM_001191552.1.
DR   UniGene; Rn.53029; -.
DR   STRING; 10116.ENSRNOP00000021952; -.
DR   PaxDb; D4A9J4; -.
DR   Ensembl; ENSRNOT00000021952; ENSRNOP00000021952; ENSRNOG00000038140.
DR   GeneID; 680537; -.
DR   KEGG; rno:680537; -.
DR   CTD; 7468; -.
DR   RGD; 1307955; Nsd2.
DR   eggNOG; KOG1081; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00780000121845; -.
DR   InParanoid; D4A9J4; -.
DR   KO; K11424; -.
DR   OMA; CMARIKY; -.
DR   OrthoDB; EOG091G00XD; -.
DR   TreeFam; TF329088; -.
DR   Reactome; R-RNO-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-RNO-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR   Reactome; R-RNO-69473; G2/M DNA damage checkpoint.
DR   Proteomes; UP000002494; Chromosome 14.
DR   Bgee; ENSRNOG00000038140; -.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0003682; F:chromatin binding; ISO:RGD.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR   GO; GO:0003289; P:atrial septum primum morphogenesis; ISO:RGD.
DR   GO; GO:0003290; P:atrial septum secundum morphogenesis; ISO:RGD.
DR   GO; GO:0060348; P:bone development; ISO:RGD.
DR   GO; GO:0010452; P:histone H3-K36 methylation; ISO:RGD.
DR   GO; GO:0034770; P:histone H4-K20 methylation; ISO:RGD.
DR   GO; GO:0003149; P:membranous septum morphogenesis; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; ISO:RGD.
DR   GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; ISO:RGD.
DR   GO; GO:0070201; P:regulation of establishment of protein localization; ISO:RGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR   Gene3D; 1.10.30.10; -; 1.
DR   Gene3D; 3.30.40.10; -; 4.
DR   InterPro; IPR006560; AWS_dom.
DR   InterPro; IPR009071; HMG_box_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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF00505; HMG_box; 1.
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; SM00317; SET; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   SUPFAM; SSF57903; SSF57903; 3.
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; 2.
DR   PROSITE; PS50016; ZF_PHD_2; 2.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   1: Evidence at protein level;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002494};
KW   DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267,
KW   ECO:0000256|SAAS:SAAS00879239};
KW   Metal-binding {ECO:0000256|SAAS:SAAS01011399};
KW   Methyltransferase {ECO:0000256|SAAS:SAAS00590675};
KW   Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267,
KW   ECO:0000256|SAAS:SAAS00574642};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002494};
KW   S-adenosyl-L-methionine {ECO:0000256|SAAS:SAAS00591079};
KW   Transferase {ECO:0000256|SAAS:SAAS00591533};
KW   Zinc {ECO:0000256|SAAS:SAAS01006535};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00146,
KW   ECO:0000256|SAAS:SAAS01007077}.
FT   DOMAIN      202    266       PWWP. {ECO:0000259|PROSITE:PS50812}.
FT   DOMAIN      433    482       HMG box. {ECO:0000259|PROSITE:PS50118}.
FT   DOMAIN      648    694       PHD-type. {ECO:0000259|PROSITE:PS50016}.
FT   DOMAIN      698    744       RING-type. {ECO:0000259|PROSITE:PS50089}.
FT   DOMAIN      812    856       PHD-type. {ECO:0000259|PROSITE:PS50016}.
FT   DOMAIN      861    923       PWWP. {ECO:0000259|PROSITE:PS50812}.
FT   DOMAIN      992   1042       AWS. {ECO:0000259|PROSITE:PS51215}.
FT   DOMAIN     1044   1161       SET. {ECO:0000259|PROSITE:PS50280}.
FT   DOMAIN     1168   1184       Post-SET. {ECO:0000259|PROSITE:PS50868}.
FT   DNA_BIND    433    482       HMG box. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00267}.
FT   COILED      526    546       {ECO:0000256|SAM:Coils}.
FT   COILED      943    963       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   1346 AA;  150411 MW;  846CEA7217199815 CRC64;
     MKQAPEILGS ANGKTQNCEV NHECSVFLSK AQLSNSLQEG VMQKFNGHDA LPFLPAEKLK
     DLTSCVFNGE PGAHDTKLCF ETQEVKGIGT PPNTTPIKNG SPEIKLKITK TYMNGKPLFE
     SSICGDGAAD MSQSEENGQK SDNKTRRNRK RSIKYDSLLE QGLVEAALVS KISSPEDKKI
     PVKKESCPNS GRDRDLLLKY NVGDLVWSKV SGYPWWPCMV SADPLLHNHT KLKGQKKSAR
     QYHVQFFGDA PERAWIFEKS LVAFEGEEQF EKLCQESAKQ APTKAEKIKL LKPISGRLRA
     QWEMGIVQAE EAASMSVEER KAKFTFLYVG DQLRLNPQVA KEAGIATEPL GEMVDSSVAN
     EEAAVDPGTM REEDIPVKRR RRAKRSSSAE NQEGDPGTEK STPPKMADAE PKRGVGSPAG
     RKRSTGSASR SRKGDSAAQF LVFCQKHRDE VVAEHPDASE EEIEELLGSQ WSMLNEKQKA
     RYNTKFSLMI SAQSEEDSGN TSGKKRTHTK RTDDPPEDVD VEDAPRKRLR TDKHSLRKQR
     ETITDKTART SSYKAIEAAS SLKSQAATKN LSDACKPLKK RNRASATASS ALGFNKSSSP
     SASLTENEVS DNPGDEPSES PYESADETQT EASVSSKKSE RGMAAKKEYV CQLCEKTGSL
     LLCEGPCCGA FHLACLGLSQ RPEGRFTCTE CASGIHSCFV CKESKMEVKR CMVNQCGKFY
     HEACVKKYPL TVFESRGFRC PLHSCMSCHA SNPSNPRPSK GKMMRCVRCP VAYHGGDACL
     AAGCSVIASN SIICTGHFTA RKGKRHHTHV NVSWCFVCSK GGSLLCCEAC PAAFHPDCLS
     IEMPDGSWFC NDCRAGKKLH FQDIIWVKLG NYRWWPAEVC HPKNVPPNIQ KMKHEIGEFP
     VFFFGSKDYY WTHQARVFPY MEGDRGSRYQ GVRGIGRVFK NALQEAEARF NEIKLQREAR
     ETQESERKPP PYKHIKVNKP YGKVQIYTAD ISEIPKCNCK PTDENPCGSD SECLNRMLMF
     ECHPQVCPAG EYCQNQCFTK RQYPETKIIK TDGKGWGLVA KRDIRKGEFV NEYVGELIDE
     EECMARIKYA HENDITHFYM LTIDKDRIID AGPKGNYSRF MNHSCQPNCE TLKWTVNGDT
     RVGLFAVCDI PAGTELTFNY NLDCLGNEKT VCRCGASNCS GFLGDRPKTS TSLSSEEKSK
     KAKKKTRRRR AKGEGKRQSE DECFRCGDGG QLVLCDRKFC TKAYHLSCLG LGKRPFGKWE
     CPWHHCDVCG KPSTSFCHLC PNSFCKEHQD GTAFRSTQDG QSYCCEHDLR ADSANNTKTE
     KPFLDSLKAK GKRKKRRCWR RVTDGK
//
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