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SMYD2_MOUSE
ID   SMYD2_MOUSE             Reviewed;         433 AA.
AC   Q8R5A0; Q3UBQ2;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=N-lysine methyltransferase SMYD2;
DE            EC=2.1.1.- {ECO:0000250|UniProtKB:Q9NRG4};
DE   AltName: Full=Histone methyltransferase SMYD2;
DE            EC=2.1.1.354 {ECO:0000250|UniProtKB:Q9NRG4};
DE   AltName: Full=SET and MYND domain-containing protein 2;
GN   Name=Smyd2;
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-240, AND INTERACTION
RP   WITH SIN3A AND HDAC1.
RX   PubMed=16805913; DOI=10.1186/1476-4598-5-26;
RA   Brown M.A., Sims R.J. III, Gottlieb P.D., Tucker P.W.;
RT   "Identification and characterization of Smyd2: a split SET/MYND domain-
RT   containing histone H3 lysine 36-specific methyltransferase that interacts
RT   with the Sin3 histone deacetylase complex.";
RL   Mol. Cancer 5:26-26(2006).
RN   [4]
RP   CAUTION.
RX   PubMed=18065756; DOI=10.1074/mcp.m700271-mcp200;
RA   Abu-Farha M., Lambert J.P., Al-Madhoun A.S., Elisma F., Skerjanc I.S.,
RA   Figeys D.;
RT   "The tale of two domains: proteomics and genomics analysis of SMYD2, a new
RT   histone methyltransferase.";
RL   Mol. Cell. Proteomics 7:560-572(2008).
RN   [5]
RP   TISSUE SPECIFICITY, INTERACTION WITH RNA POLYMERASE II AND HELZ, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=20305823; DOI=10.1371/journal.pone.0009748;
RA   Diehl F., Brown M.A., van Amerongen M.J., Novoyatleva T., Wietelmann A.,
RA   Harriss J., Ferrazzi F., Bottger T., Harvey R.P., Tucker P.W., Engel F.B.;
RT   "Cardiac deletion of Smyd2 is dispensable for mouse heart development.";
RL   PLoS ONE 5:E9748-E9748(2010).
CC   -!- FUNCTION: Protein-lysine N-methyltransferase that methylates both
CC       histones and non-histone proteins, including p53/TP53 and RB1.
CC       Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The
CC       activity requires interaction with HSP90alpha. Shows even higher
CC       methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of
CC       p53/TP53, leading to decreased DNA-binding activity and subsequent
CC       transcriptional regulation activity of p53/TP53. Monomethylates RB1 at
CC       'Lys-860'. {ECO:0000250|UniProtKB:Q9NRG4, ECO:0000269|PubMed:16805913}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) +
CC         N(6),N(6),N(6)-trimethyl-L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:60260, Rhea:RHEA-COMP:15537, Rhea:RHEA-
CC         COMP:15547, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61961; EC=2.1.1.354;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRG4};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N(6)-
CC         methyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:51736, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:13053,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789, ChEBI:CHEBI:61929;
CC         Evidence={ECO:0000250|UniProtKB:Q9NRG4};
CC   -!- SUBUNIT: Interacts (via MYND-type zinc finger) with EPB41L3. Interacts
CC       (via SET domain) with p53/TP53. Interacts with RB1 and HSP90AA1 (By
CC       similarity). Interacts with RNA polymerase II and HELZ. Interacts with
CC       SIN3A and HDAC1. {ECO:0000250, ECO:0000269|PubMed:16805913,
CC       ECO:0000269|PubMed:20305823}.
CC   -!- INTERACTION:
CC       Q8R5A0; P04637: TP53; Xeno; NbExp=3; IntAct=EBI-15612527, EBI-366083;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Nucleus.
CC   -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC       brain tissue. During cardiac development, it is differentially
CC       expressed with highest expression in the neonatal heart while very low
CC       expression is detected at 12.5 dpc and adult. Specifically expressed in
CC       cardiomyocytes (at protein level). {ECO:0000269|PubMed:20305823}.
CC   -!- MISCELLANEOUS: Although specifically expressed in cardiomyocytes, a
CC       conditional deletion in heart does not lead to any visible phenotype.
CC       {ECO:0000305|PubMed:20305823}.
CC   -!- SIMILARITY: Belongs to the class V-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000255|PROSITE-ProRule:PRU00190}.
CC   -!- CAUTION: The protein was previously thought to dimethylate histone 3
CC       'Lys-36', but this is now known not to take place in vivo.
CC       {ECO:0000269|PubMed:18065756}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE29912.1; Type=Miscellaneous discrepancy; Note=Deletion within an exon that does not correspond to an intron.; Evidence={ECO:0000305};
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DR   EMBL; AK150857; BAE29912.1; ALT_SEQ; mRNA.
DR   EMBL; BC023119; AAH23119.1; -; mRNA.
DR   CCDS; CCDS35821.1; -.
DR   RefSeq; NP_081072.1; NM_026796.1.
DR   PDB; 3QWV; X-ray; 2.03 A; A=1-433.
DR   PDB; 3QWW; X-ray; 1.80 A; A=1-433.
DR   PDBsum; 3QWV; -.
DR   PDBsum; 3QWW; -.
DR   AlphaFoldDB; Q8R5A0; -.
DR   SMR; Q8R5A0; -.
DR   BioGRID; 230559; 4.
DR   DIP; DIP-60503N; -.
DR   IntAct; Q8R5A0; 1.
DR   STRING; 10090.ENSMUSP00000027897; -.
DR   iPTMnet; Q8R5A0; -.
DR   PhosphoSitePlus; Q8R5A0; -.
DR   EPD; Q8R5A0; -.
DR   MaxQB; Q8R5A0; -.
DR   PaxDb; Q8R5A0; -.
DR   PeptideAtlas; Q8R5A0; -.
DR   PRIDE; Q8R5A0; -.
DR   ProteomicsDB; 261589; -.
DR   Antibodypedia; 34617; 348 antibodies from 37 providers.
DR   DNASU; 226830; -.
DR   Ensembl; ENSMUST00000027897; ENSMUSP00000027897; ENSMUSG00000026603.
DR   GeneID; 226830; -.
DR   KEGG; mmu:226830; -.
DR   UCSC; uc007eax.1; mouse.
DR   CTD; 56950; -.
DR   MGI; MGI:1915889; Smyd2.
DR   VEuPathDB; HostDB:ENSMUSG00000026603; -.
DR   eggNOG; KOG2084; Eukaryota.
DR   GeneTree; ENSGT00940000157082; -.
DR   HOGENOM; CLU_018406_0_0_1; -.
DR   InParanoid; Q8R5A0; -.
DR   OMA; YSRHLEF; -.
DR   OrthoDB; 981799at2759; -.
DR   PhylomeDB; Q8R5A0; -.
DR   TreeFam; TF106487; -.
DR   Reactome; R-MMU-3214841; PKMTs methylate histone lysines.
DR   Reactome; R-MMU-6804760; Regulation of TP53 Activity through Methylation.
DR   BioGRID-ORCS; 226830; 3 hits in 77 CRISPR screens.
DR   ChiTaRS; Smyd2; mouse.
DR   EvolutionaryTrace; Q8R5A0; -.
DR   PRO; PR:Q8R5A0; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q8R5A0; protein.
DR   Bgee; ENSMUSG00000026603; Expressed in gastrocnemius and 263 other tissues.
DR   Genevisible; Q8R5A0; MM.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0046975; F:histone methyltransferase activity (H3-K36 specific); IDA:UniProtKB.
DR   GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0016279; F:protein-lysine N-methyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0000993; F:RNA polymerase II complex binding; IDA:UniProtKB.
DR   GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR   GO; GO:0007507; P:heart development; IEA:Ensembl.
DR   GO; GO:0034968; P:histone lysine methylation; IBA:GO_Central.
DR   GO; GO:0016571; P:histone methylation; IDA:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IDA:UniProtKB.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
DR   GO; GO:0018027; P:peptidyl-lysine dimethylation; IDA:UniProtKB.
DR   GO; GO:0018026; P:peptidyl-lysine monomethylation; ISS:UniProtKB.
DR   GO; GO:0043516; P:regulation of DNA damage response, signal transduction by p53 class mediator; ISS:UniProtKB.
DR   CDD; cd19202; SET_SMYD2; 1.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 2.170.270.10; -; 2.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR044419; SMYD2_SET.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF00856; SET; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF82199; SSF82199; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chromatin regulator; Cytoplasm; Metal-binding;
KW   Methyltransferase; Nucleus; Phosphoprotein; Reference proteome;
KW   S-adenosyl-L-methionine; Transcription; Transcription regulation;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..433
FT                   /note="N-lysine methyltransferase SMYD2"
FT                   /id="PRO_0000218310"
FT   DOMAIN          7..241
FT                   /note="SET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   ZN_FING         52..90
FT                   /note="MYND-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         17..19
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         52
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         55
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT   BINDING         137
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00190"
FT   BINDING         206..207
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         258..260
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NRG4"
FT   MUTAGEN         240
FT                   /note="Y->F: Abolishes methyltransferase activity."
FT                   /evidence="ECO:0000269|PubMed:16805913"
FT   STRAND          9..13
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          19..25
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          32..37
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          39..43
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   TURN            48..50
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   TURN            53..55
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   TURN            66..68
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           76..86
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   TURN            87..89
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           90..95
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           104..118
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           124..126
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           131..133
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           143..160
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   TURN            161..163
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           169..182
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          184..187
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          193..198
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           202..204
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          205..207
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          221..228
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   STRAND          235..238
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           247..258
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           265..269
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           273..276
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           288..308
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   TURN            309..311
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           314..328
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   TURN            329..331
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           337..352
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           356..373
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           379..394
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           398..415
FT                   /evidence="ECO:0007829|PDB:3QWW"
FT   HELIX           421..431
FT                   /evidence="ECO:0007829|PDB:3QWW"
SQ   SEQUENCE   433 AA;  49567 MW;  5978E9A3FC2CDCE4 CRC64;
     MRAEARGGLE RFCSAGKGRG LRALRPFHVG DLLFSCPAYA CVLTVGERGH HCECCFARKE
     GLSKCGRCKQ AFYCDVECQK EDWPLHKLEC SSMVVLGENW NPSETVRLTA RILAKQKIHP
     ERTPSEKLLA VREFESHLDK LDNEKKDLIQ SDIAALHQFY SKYLEFPDHS SLVVLFAQVN
     CNGFTIEDEE LSHLGSAIFP DVALMNHSCC PNVIVTYKGT LAEVRAVQEI HPGDEVFTSY
     IDLLYPTEDR NDRLRDSYFF TCECRECTTK DKDKAKVEVR KLSSPPQAEA IRDMVRYARN
     VIEEFRRAKH YKSPSELLEI CELSQEKMSS VFEDSNVYML HMMYQAMGVC LYMQDWEGAL
     KYGQKIIKPY SKHYPVYSLN VASMWLKLGR LYMGLENKAA GEKALKKAIA IMEVAHGKDH
     PYISEIKQEI ESH
 
 
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