GenomeNet

Database: UniProt
Entry: Q8BVE8
LinkDB: Q8BVE8
Original site: Q8BVE8 
ID   NSD2_MOUSE              Reviewed;        1365 AA.
AC   Q8BVE8; B3VCH6; Q6ZPY1; Q7TSF5; Q811F0;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 2.
DT   10-APR-2019, entry version 145.
DE   RecName: Full=Histone-lysine N-methyltransferase NSD2;
DE            EC=2.1.1.43;
DE   AltName: Full=Multiple myeloma SET domain-containing protein;
DE            Short=MMSET;
DE   AltName: Full=Nuclear SET domain-containing protein 2;
DE   AltName: Full=Wolf-Hirschhorn syndrome candidate 1 protein homolog;
GN   Name=Nsd2; Synonyms=Kiaa1090, Whsc1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RE-IIBP), FUNCTION, CATALYTIC
RP   ACTIVITY, AND MUTAGENESIS OF ARG-1138 AND CYS-1144.
RX   PubMed=18172012; DOI=10.1128/MCB.02130-07;
RA   Kim J.Y., Kee H.J., Choe N.W., Kim S.M., Eom G.H., Baek H.J., Kook H.,
RA   Kook H., Seo S.B.;
RT   "Multiple-myeloma-related WHSC1/MMSET isoform RE-IIBP is a histone
RT   methyltransferase with transcriptional repression activity.";
RL   Mol. Cell. Biol. 28:2023-2034(2008).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC   TISSUE=Embryonic tail;
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene:
RT   III. The complete nucleotide sequences of 500 mouse KIAA-homologous
RT   cDNAs identified by screening of terminal sequences of cDNA clones
RT   randomly sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 446-1365 (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Adrenal gland;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 516-1365 (ISOFORM 2).
RC   STRAIN=FVB/N; TISSUE=Limb, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=9618163; DOI=10.1093/hmg/7.7.1071;
RA   Stec I., Wright T.J., van Ommen G.-J.B., de Boer P.A.,
RA   van Haeringen A., Moorman A.F.M., Altherr M.R., den Dunnen J.T.;
RT   "WHSC1, a 90 kb SET domain-containing gene, expressed in early
RT   development and homologous to a Drosophila dysmorphy gene maps in the
RT   Wolf-Hirschhorn syndrome critical region and is fused to IgH in
RT   t(4;14) multiple myeloma.";
RL   Hum. Mol. Genet. 7:1071-1082(1998).
RN   [7]
RP   ERRATUM.
RA   Stec I., Wright T.J., van Ommen G.-J.B., de Boer P.A.,
RA   van Haeringen A., Moorman A.F.M., Altherr M.R., den Dunnen J.T.;
RL   Hum. Mol. Genet. 7:1527-1527(1998).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-110 AND SER-121, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Histone methyltransferase with histone H3 'Lys-27'
CC       (H3K27me) methyltransferase activity.
CC       {ECO:0000269|PubMed:18172012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) +
CC         N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:10024, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:9846,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1.1.43;
CC         Evidence={ECO:0000269|PubMed:18172012};
CC   -!- INTERACTION:
CC       P42582:Nkx2-5; NbExp=2; IntAct=EBI-11518042, EBI-297021;
CC       Q8BX22:Sall4; NbExp=3; IntAct=EBI-11518042, EBI-2312582;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00267}. Chromosome {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BVE8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BVE8-2; Sequence=VSP_021426;
CC       Name=3;
CC         IsoId=Q8BVE8-3; Sequence=VSP_021424, VSP_021425, VSP_021426;
CC         Note=No experimental confirmation available.;
CC       Name=RE-IIBP;
CC         IsoId=Q8BVE8-4; Sequence=VSP_044420;
CC   -!- TISSUE SPECIFICITY: Expressed preferentially in rapidly growing
CC       embryonic tissues. {ECO:0000269|PubMed:9618163}.
CC   -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in early development.
CC       {ECO:0000269|PubMed:9618163}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding
CC       methyltransferase superfamily. Histone-lysine methyltransferase
CC       family. SET2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ACE75882.1; Type=Miscellaneous discrepancy; Note=Incorrectly indicated as originating from human.; Evidence={ECO:0000305};
CC       Sequence=BAC37342.1; Type=Frameshift; Positions=649, 759; Evidence={ECO:0000305};
CC       Sequence=BAC98097.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; EU733655; ACE75882.1; ALT_SEQ; mRNA.
DR   EMBL; AK129287; BAC98097.1; ALT_INIT; mRNA.
DR   EMBL; AC163329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK078622; BAC37342.1; ALT_FRAME; mRNA.
DR   EMBL; BC046473; AAH46473.1; -; mRNA.
DR   EMBL; BC053454; AAH53454.1; -; mRNA.
DR   CCDS; CCDS51467.1; -. [Q8BVE8-2]
DR   CCDS; CCDS51468.1; -. [Q8BVE8-1]
DR   RefSeq; NP_001074571.2; NM_001081102.2. [Q8BVE8-2]
DR   RefSeq; NP_780440.2; NM_175231.2. [Q8BVE8-1]
DR   RefSeq; XP_006503721.1; XM_006503658.3. [Q8BVE8-2]
DR   RefSeq; XP_006503722.1; XM_006503659.3. [Q8BVE8-2]
DR   RefSeq; XP_006503723.1; XM_006503660.3. [Q8BVE8-1]
DR   RefSeq; XP_017176079.1; XM_017320590.1. [Q8BVE8-2]
DR   UniGene; Mm.19892; -.
DR   UniGene; Mm.332320; -.
DR   UniGene; Mm.491382; -.
DR   ProteinModelPortal; Q8BVE8; -.
DR   SMR; Q8BVE8; -.
DR   BioGrid; 223605; 13.
DR   DIP; DIP-60452N; -.
DR   IntAct; Q8BVE8; 14.
DR   MINT; Q8BVE8; -.
DR   STRING; 10090.ENSMUSP00000058940; -.
DR   iPTMnet; Q8BVE8; -.
DR   PhosphoSitePlus; Q8BVE8; -.
DR   SwissPalm; Q8BVE8; -.
DR   jPOST; Q8BVE8; -.
DR   PaxDb; Q8BVE8; -.
DR   PeptideAtlas; Q8BVE8; -.
DR   PRIDE; Q8BVE8; -.
DR   Ensembl; ENSMUST00000058096; ENSMUSP00000058940; ENSMUSG00000057406. [Q8BVE8-1]
DR   Ensembl; ENSMUST00000066854; ENSMUSP00000067205; ENSMUSG00000057406. [Q8BVE8-2]
DR   Ensembl; ENSMUST00000075812; ENSMUSP00000075210; ENSMUSG00000057406. [Q8BVE8-2]
DR   GeneID; 107823; -.
DR   KEGG; mmu:107823; -.
DR   UCSC; uc008xbm.2; mouse. [Q8BVE8-1]
DR   UCSC; uc012duw.1; mouse. [Q8BVE8-2]
DR   CTD; 7468; -.
DR   MGI; MGI:1276574; Nsd2.
DR   eggNOG; KOG1081; Eukaryota.
DR   eggNOG; COG2940; LUCA.
DR   GeneTree; ENSGT00940000157429; -.
DR   HOGENOM; HOG000230893; -.
DR   HOVERGEN; HBG079979; -.
DR   InParanoid; Q8BVE8; -.
DR   KO; K11424; -.
DR   OMA; EYVMVHR; -.
DR   OrthoDB; 507784at2759; -.
DR   PhylomeDB; Q8BVE8; -.
DR   TreeFam; TF329088; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-MMU-5693571; Nonhomologous End-Joining (NHEJ).
DR   Reactome; R-MMU-5693607; Processing of DNA double-strand break ends.
DR   Reactome; R-MMU-69473; G2/M DNA damage checkpoint.
DR   ChiTaRS; Whsc1; mouse.
DR   PRO; PR:Q8BVE8; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   Bgee; ENSMUSG00000057406; Expressed in 264 organ(s), highest expression level in ear vesicle.
DR   ExpressionAtlas; Q8BVE8; baseline and differential.
DR   Genevisible; Q8BVE8; MM.
DR   GO; GO:0000785; C:chromatin; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IBA:GO_Central.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IDA:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0003289; P:atrial septum primum morphogenesis; IMP:MGI.
DR   GO; GO:0003290; P:atrial septum secundum morphogenesis; IMP:MGI.
DR   GO; GO:0060348; P:bone development; IMP:MGI.
DR   GO; GO:0010452; P:histone H3-K36 methylation; IDA:MGI.
DR   GO; GO:0034770; P:histone H4-K20 methylation; IDA:MGI.
DR   GO; GO:0003149; P:membranous septum morphogenesis; IMP:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR   GO; GO:0048298; P:positive regulation of isotype switching to IgA isotypes; IMP:MGI.
DR   GO; GO:2001032; P:regulation of double-strand break repair via nonhomologous end joining; IMP:MGI.
DR   GO; GO:0070201; P:regulation of establishment of protein localization; IMP:MGI.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
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; PF17907; AWS; 1.
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.
PE   1: Evidence at protein level;
KW   Alternative splicing; Chromatin regulator; Chromosome;
KW   Complete proteome; DNA-binding; Metal-binding; Methyltransferase;
KW   Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1   1365       Histone-lysine N-methyltransferase NSD2.
FT                                /FTId=PRO_0000259520.
FT   DOMAIN      222    286       PWWP 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN      880    942       PWWP 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00162}.
FT   DOMAIN     1011   1061       AWS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00562}.
FT   DOMAIN     1063   1180       SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00190}.
FT   DOMAIN     1187   1203       Post-SET. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00155}.
FT   DNA_BIND    453    521       HMG box. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00267}.
FT   ZN_FING     667    713       PHD-type 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     714    770       PHD-type 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING     831    875       PHD-type 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00146}.
FT   ZN_FING    1239   1286       PHD-type 4; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00146}.
FT   MOD_RES     110    110       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     114    114       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O96028}.
FT   MOD_RES     121    121       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     172    172       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O96028}.
FT   MOD_RES     376    376       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O96028}.
FT   MOD_RES     422    422       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:O96028}.
FT   VAR_SEQ       1    661       Missing (in isoform RE-IIBP).
FT                                {ECO:0000303|PubMed:18172012}.
FT                                /FTId=VSP_044420.
FT   VAR_SEQ       1    519       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:14621295}.
FT                                /FTId=VSP_021424.
FT   VAR_SEQ     520    522       NGN -> MGM (in isoform 3).
FT                                {ECO:0000303|PubMed:14621295}.
FT                                /FTId=VSP_021425.
FT   VAR_SEQ     558    558       K -> KQ (in isoform 2 and isoform 3).
FT                                {ECO:0000303|PubMed:14621295,
FT                                ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_021426.
FT   MUTAGEN    1138   1138       R->A: No methyltransferase activity.
FT                                {ECO:0000269|PubMed:18172012}.
FT   MUTAGEN    1144   1144       C->A: No methyltransferase activity.
FT                                {ECO:0000269|PubMed:18172012}.
FT   CONFLICT    757    757       F -> L (in Ref. 4; BAC37342).
FT                                {ECO:0000305}.
FT   CONFLICT   1019   1019       K -> T (in Ref. 1; ACE75882).
FT                                {ECO:0000305}.
FT   CONFLICT   1345   1345       S -> L (in Ref. 5; AAH53454).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1365 AA;  152253 MW;  D8DC3F687D3EA2C2 CRC64;
     MEFSIRKSPL SVQKVVKCMK MKQTPEILGS ANGKTQNCEV NHECSVFLSK AQLSNSLQEG
     VMQKFNGHDA LPFLPAEKLK DLTSCVFNGE PGAHDTKLCF EAQEVKGIGT PPNTTPIKNG
     SPEIKLKITK TYMNGKPLFE SSICGDGAAD VSQSEENEQK SDNKTRRNRK RSIKYDSLLE
     QGLVEAALVS KISSPADKKI PVKKESCPNT GRDRDLLLKY NVGDLVWSKV SGYPWWPCMV
     SADPLLHNHT KLKGQKKSAR QYHVQFFGDA PERAWIFEKS LVAFEGEEQF EKLCQESAKQ
     APTKAEKIKL LKPISGRLRA QWEMGIVQAE EAASMSIEER KAKFTFLYVG DQLHLNPQVA
     KEAGIVTEPL GEMVDSSGAS EEAAVDPGSV REEDIPTKRR RRTKRSSSAE NQEGDPGTDK
     STPPKMAEAE PKRGVGSPAG RKKSTGSAPR SRKGDSAAQF LVFCQKHRDE VVAEHPDASG
     EEIEELLGSQ WSMLNEKQKA RYNTKFSLMI SAQSEEDSGN GNGKKRSHTK RADDPAEDVD
     VEDAPRKRLR ADKHSLRKRE TITDKTARTS SYKAIEAASS LKSQAATKNL SDACKPLKKR
     NRASATASSA LGFNKSSSPS ASLTEHEVSD SPGDEPSESP YESADETQTE ASVSSKKSER
     GMAAKKEYVC QLCEKTGSLL LCEGPCCGAF HLACLGLSRR PEGRFTCTEC ASGIHSCFVC
     KESKMEVKRC VVNQCGKFYH EACVKKYPLT VFESRGFRCP LHSCMSCHAS NPSNPRPSKG
     KMMRCVRCPV AYHGGDACLA AGCSVIASNS IICTGHFTAR KGKRHHTHVN VSWCFVCSKG
     GSLLCCEACP AAFHPDCLNI EMPDGSWFCN DCRAGKKLHF QDIIWVKLGN YRWWPAEVCH
     PKNVPPNIQK MKHEIGEFPV FFFGSKDYYW THQARVFPYM EGDRGSRYQG VRGIGRVFKN
     ALQEAEARFN EVKLQREARE TQESERKPPP YKHIKVNKPY GKVQIYTADI SEIPKCNCKP
     TDENPCGSDS ECLNRMLMFE CHPQVCPAGE YCQNQCFTKR QYPETKIIKT DGKGWGLVAK
     RDIRKGEFVN EYVGELIDEE ECMARIKYAH ENDITHFYML TIDKDRIIDA GPKGNYSRFM
     NHSCQPNCET LKWTVNGDTR VGLFAVCDIP AGTELTFNYN LDCLGNEKTV CRCGASNCSG
     FLGDRPKTSA SLSSEEKGKK AKKKTRRRRA KGEGKRQSED ECFRCGDGGQ LVLCDRKFCT
     KAYHLSCLGL GKRPFGKWEC PWHHCDVCGK PSTSFCHLCP NSFCKEHQDG TAFRSTQDGQ
     SYCCEHDLRA DSSSSTKTEK PFPESLKSKG KRKKRRCWRR VTDGK
//
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