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EOMES_MOUSE
ID   EOMES_MOUSE             Reviewed;         707 AA.
AC   O54839; Q3UPL1; Q52KJ1; Q8BN22; Q9JJL1; Q9QYG7;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   23-MAR-2010, sequence version 3.
DT   03-AUG-2022, entry version 165.
DE   RecName: Full=Eomesodermin homolog;
DE   AltName: Full=T-box brain protein 2;
DE            Short=T-brain-2;
DE            Short=TBR-2;
GN   Name=Eomes; Synonyms=Tbr2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
RX   PubMed=10407135; DOI=10.1016/s0165-3806(99)00064-4;
RA   Kimura N., Nakashima K., Ueno M., Taga T.;
RT   "A novel mammalian T-box-containing gene, Tbr2, expressed in mouse
RT   developing brain.";
RL   Brain Res. Dev. Brain Res. 115:183-193(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 2).
RC   STRAIN=129/Sv; TISSUE=Liver;
RX   PubMed=10974533; DOI=10.1016/s0378-1119(00)00290-0;
RA   Ueno M., Kimura N., Nakashima K., Saito-Ohara F., Inazawa J., Taga T.;
RT   "Genomic organization, sequence and chromosomal localization of the mouse
RT   Tbr2 gene and a comparative study with Tbr1.";
RL   Gene 254:29-35(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Olfactory bulb, and Spleen;
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., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., 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., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
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., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 278-457.
RX   PubMed=9503012; DOI=10.1006/geno.1997.5150;
RA   Wattler S., Russ A., Evans M., Nehls M.;
RT   "A combined analysis of genomic and primary protein structure defines the
RT   phylogenetic relationship of new members of the T-box family.";
RL   Genomics 48:24-33(1998).
RN   [7]
RP   FUNCTION IN TROPHOBLAST DIFFERENTIATION, FUNCTION IN GASTRULATION,
RP   DISRUPTION PHENOTYPE, AND DEVELOPMENTAL STAGE.
RX   PubMed=10716450; DOI=10.1038/35003601;
RA   Russ A.P., Wattler S., Colledge W.H., Aparicio S.A.J.R., Carlton M.B.L.,
RA   Pearce J.J., Barton S.C., Surani M.A., Ryan K., Nehls M.C., Wilson V.,
RA   Evans M.J.;
RT   "Eomesodermin is required for mouse trophoblast development and mesoderm
RT   formation.";
RL   Nature 404:95-99(2000).
RN   [8]
RP   FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=14605368; DOI=10.1126/science.1090148;
RA   Pearce E.L., Mullen A.C., Martins G.A., Krawczyk C.M., Hutchins A.S.,
RA   Zediak V.P., Banica M., DiCioccio C.B., Gross D.A., Mao C.-A., Shen H.,
RA   Cereb N., Yang S.Y., Lindsten T., Rossant J., Hunter C.A., Reiner S.L.;
RT   "Control of effector CD8+ T cell function by the transcription factor
RT   Eomesodermin.";
RL   Science 302:1041-1043(2003).
RN   [9]
RP   FUNCTION IN GASTRULATION.
RX   PubMed=18171685; DOI=10.1242/dev.014357;
RA   Arnold S.J., Hofmann U.K., Bikoff E.K., Robertson E.J.;
RT   "Pivotal roles for eomesodermin during axis formation, epithelium-to-
RT   mesenchyme transition and endoderm specification in the mouse.";
RL   Development 135:501-511(2008).
RN   [10]
RP   FUNCTION, AND DEVELOPMENTAL STAGE.
RX   PubMed=18940588; DOI=10.1016/j.neuron.2008.09.028;
RA   Sessa A., Mao C.-A., Hadjantonakis A.-K., Klein W.H., Broccoli V.;
RT   "Tbr2 directs conversion of radial glia into basal precursors and guides
RT   neuronal amplification by indirect neurogenesis in the developing
RT   neocortex.";
RL   Neuron 60:56-69(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117 AND THR-473, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Spleen;
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 expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Functions as a transcriptional activator playing a crucial
CC       role during development. Functions in trophoblast differentiation and
CC       later in gastrulation, regulating both mesoderm delamination and
CC       endoderm specification. Plays a role in brain development being
CC       required for the specification and the proliferation of the
CC       intermediate progenitor cells and their progeny in the cerebral cortex.
CC       Also involved in the differentiation of CD8+ T-cells during immune
CC       response regulating the expression of lytic effector genes.
CC       {ECO:0000269|PubMed:10716450, ECO:0000269|PubMed:14605368,
CC       ECO:0000269|PubMed:18171685, ECO:0000269|PubMed:18940588}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O54839-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O54839-2; Sequence=VSP_038806;
CC   -!- TISSUE SPECIFICITY: Expressed in CD8+ T-cells.
CC       {ECO:0000269|PubMed:14605368}.
CC   -!- DEVELOPMENTAL STAGE: Originally expressed in the trophoectoderm of the
CC       blastocyst and later in the extraembryonic ectoderm of the early post-
CC       implantation embryo. In the embryo proper, expressed in the posterior
CC       part of the epiblast. During gastrulation, extends distally into the
CC       primitive streak and nascent mesoderm. Also expressed in the developing
CC       forebrain and the olfactory lobes. Expressed at 12.5 dpc and 14.5 dpc
CC       in the forebrain. {ECO:0000269|PubMed:10716450,
CC       ECO:0000269|PubMed:18940588}.
CC   -!- INDUCTION: Up-regulated in CD8+ T-cells upon activation.
CC       {ECO:0000269|PubMed:14605368}.
CC   -!- DISRUPTION PHENOTYPE: Embryonic lethal due to peri-implantation
CC       defects. Mutant embryos arrest soon after implantation and fail to form
CC       organized embryonic or extraembryonic structures. Conditional mutants,
CC       with expression abrogated in the inner cell mass of embryos from early
CC       implantation stages onward, display gastrulation defects.
CC       {ECO:0000269|PubMed:10716450}.
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DR   EMBL; AB031037; BAA83416.1; -; mRNA.
DR   EMBL; AB032373; BAB07808.1; -; Genomic_DNA.
DR   EMBL; AK089817; BAC40968.1; -; mRNA.
DR   EMBL; AK143454; BAE25384.1; -; mRNA.
DR   EMBL; AC173340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC094319; AAH94319.1; -; mRNA.
DR   EMBL; AF013281; AAC16233.1; -; mRNA.
DR   CCDS; CCDS23603.1; -. [O54839-1]
DR   CCDS; CCDS52960.1; -. [O54839-2]
DR   RefSeq; NP_001158261.1; NM_001164789.1. [O54839-2]
DR   RefSeq; NP_034266.2; NM_010136.3. [O54839-1]
DR   AlphaFoldDB; O54839; -.
DR   SMR; O54839; -.
DR   BioGRID; 199457; 3.
DR   IntAct; O54839; 1.
DR   STRING; 10090.ENSMUSP00000035020; -.
DR   iPTMnet; O54839; -.
DR   PhosphoSitePlus; O54839; -.
DR   EPD; O54839; -.
DR   PaxDb; O54839; -.
DR   PeptideAtlas; O54839; -.
DR   PRIDE; O54839; -.
DR   ProteomicsDB; 277880; -. [O54839-1]
DR   ProteomicsDB; 277881; -. [O54839-2]
DR   Antibodypedia; 11523; 452 antibodies from 40 providers.
DR   DNASU; 13813; -.
DR   Ensembl; ENSMUST00000035020; ENSMUSP00000035020; ENSMUSG00000032446. [O54839-1]
DR   Ensembl; ENSMUST00000111763; ENSMUSP00000107393; ENSMUSG00000032446. [O54839-2]
DR   GeneID; 13813; -.
DR   KEGG; mmu:13813; -.
DR   UCSC; uc009rzo.2; mouse. [O54839-1]
DR   UCSC; uc009rzp.2; mouse. [O54839-2]
DR   CTD; 8320; -.
DR   MGI; MGI:1201683; Eomes.
DR   VEuPathDB; HostDB:ENSMUSG00000032446; -.
DR   eggNOG; KOG3585; Eukaryota.
DR   GeneTree; ENSGT00940000158728; -.
DR   HOGENOM; CLU_014430_8_1_1; -.
DR   InParanoid; O54839; -.
DR   OMA; YGPYPGT; -.
DR   OrthoDB; 374561at2759; -.
DR   PhylomeDB; O54839; -.
DR   TreeFam; TF106341; -.
DR   BioGRID-ORCS; 13813; 2 hits in 75 CRISPR screens.
DR   ChiTaRS; Eomes; mouse.
DR   PRO; PR:O54839; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; O54839; protein.
DR   Bgee; ENSMUSG00000032446; Expressed in ventricular zone and 98 other tissues.
DR   ExpressionAtlas; O54839; baseline and differential.
DR   Genevisible; O54839; MM.
DR   GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR   GO; GO:0031490; F:chromatin DNA binding; IDA:MGI.
DR   GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IC:NTNU_SB.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR   GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; IMP:MGI.
DR   GO; GO:0048708; P:astrocyte differentiation; IMP:MGI.
DR   GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR   GO; GO:0007420; P:brain development; ISO:MGI.
DR   GO; GO:0010002; P:cardioblast differentiation; IMP:MGI.
DR   GO; GO:0002302; P:CD8-positive, alpha-beta T cell differentiation involved in immune response; IDA:UniProtKB.
DR   GO; GO:0030154; P:cell differentiation; IMP:MGI.
DR   GO; GO:0060706; P:cell differentiation involved in embryonic placenta development; IMP:UniProtKB.
DR   GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR   GO; GO:0021987; P:cerebral cortex development; IMP:MGI.
DR   GO; GO:0021895; P:cerebral cortex neuron differentiation; IDA:UniProtKB.
DR   GO; GO:0021796; P:cerebral cortex regionalization; IMP:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR   GO; GO:0080111; P:DNA demethylation; IMP:MGI.
DR   GO; GO:0006306; P:DNA methylation; IMP:MGI.
DR   GO; GO:0007492; P:endoderm development; IMP:MGI.
DR   GO; GO:0001706; P:endoderm formation; IMP:UniProtKB.
DR   GO; GO:0001714; P:endodermal cell fate specification; IMP:MGI.
DR   GO; GO:0010467; P:gene expression; IMP:MGI.
DR   GO; GO:0016573; P:histone acetylation; IMP:MGI.
DR   GO; GO:0016575; P:histone deacetylation; IMP:MGI.
DR   GO; GO:0048382; P:mesendoderm development; IMP:MGI.
DR   GO; GO:0001707; P:mesoderm formation; IMP:UniProtKB.
DR   GO; GO:0060809; P:mesodermal to mesenchymal transition involved in gastrulation; IMP:UniProtKB.
DR   GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR   GO; GO:0022008; P:neurogenesis; IMP:MGI.
DR   GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR   GO; GO:0001764; P:neuron migration; IMP:MGI.
DR   GO; GO:0021772; P:olfactory bulb development; IMP:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR   GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR   GO; GO:0001829; P:trophectodermal cell differentiation; IDA:MGI.
DR   CDD; cd00182; TBOX; 1.
DR   Gene3D; 2.60.40.820; -; 1.
DR   InterPro; IPR008967; p53-like_TF_DNA-bd.
DR   InterPro; IPR032385; T-box_assoc.
DR   InterPro; IPR046360; T-box_DNA-bd.
DR   InterPro; IPR036960; T-box_sf.
DR   InterPro; IPR001699; TF_T-box.
DR   InterPro; IPR018186; TF_T-box_CS.
DR   PANTHER; PTHR11267; PTHR11267; 1.
DR   Pfam; PF00907; T-box; 1.
DR   Pfam; PF16176; T-box_assoc; 1.
DR   PRINTS; PR00937; TBOX.
DR   SMART; SM00425; TBOX; 1.
DR   SUPFAM; SSF49417; SSF49417; 1.
DR   PROSITE; PS01283; TBOX_1; 1.
DR   PROSITE; PS01264; TBOX_2; 1.
DR   PROSITE; PS50252; TBOX_3; 1.
PE   1: Evidence at protein level;
KW   Activator; Adaptive immunity; Alternative splicing; Developmental protein;
KW   Differentiation; DNA-binding; Gastrulation; Immunity; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..707
FT                   /note="Eomesodermin homolog"
FT                   /id="PRO_0000184460"
FT   DNA_BIND        278..458
FT                   /note="T-box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT   REGION          27..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..707
FT                   /note="Required for transcription activation"
FT                   /evidence="ECO:0000250"
FT   REGION          642..689
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..680
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         117
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         473
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         463..481
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10407135"
FT                   /id="VSP_038806"
FT   CONFLICT        144
FT                   /note="E -> D (in Ref. 3; BAC40968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="A -> T (in Ref. 3; BAC40968)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        178
FT                   /note="V -> G (in Ref. 1; BAA83416)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   707 AA;  74801 MW;  277AA462E214A927 CRC64;
     MQLGEQLLVS SVNLPGAHFY SLESARGGGG GGGGGGGGGG GSVSLLPGAA PSPQRLDLDK
     ASKKFPGSLP CQAGSAEPAG AGAGAPAAML SDADAGDTFG STSAVAKPGP PDGRKGSPCA
     EEELPSAATA AATARYSMDS LSSERYYLPS PGPQGSELAA PCSLFQYPAA AGAAHGPVYP
     ASNGARYPYG SMLPPGGFPA AVCPPARAQF GPAAGSGSGA GSSGGGAGGP GAYPYGQGSP
     LYGPYAGTSA AGSCGGLGGL GVPGSGFRAH VYLCNRPLWL KFHRHQTEMI ITKQGRRMFP
     FLSFNINGLN PTAHYNVFVE VVLADPNHWR FQGGKWVTCG KADNNMQGNK MYVHPESPNT
     GSHWMRQEIS FGKLKLTNNK GANNNNTQMI VLQSLHKYQP RLHIVEVTED GVEDLNEPSK
     TQTFTFSETQ FIAVTAYQNT DITQLKIDHN PFAKGFRDNY DSMYTASEND RLTPSPTDSP
     RSHQIVPGGR YGVQNFFPEP FVNTLPQARY YNGERTVPQT NGLLSPQQSE EVANPPQRWL
     VTPVQQPVTN KLDIGSYESE YTSSTLLPYG IKSLPLQTSH ALGYYPDPTF PAMAGWGGRG
     AYQRKMAAGL PWTSRMSPPV FPEDQLAKEK VKEEISSSWI ETPPSIKSLD SSDSGVYNSA
     CKRKRLSPST PSNGNSPPIK CEDINTEEYS KDTSKGMGAY YAFYTSP
 
 
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