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ST18_MOUSE
ID   ST18_MOUSE              Reviewed;        1045 AA.
AC   Q80TY4; Q3UH00; Q3URH9; Q3UVB9; Q3UZN9; Q811B4; Q8K098;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 2.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=Suppression of tumorigenicity 18 protein;
GN   Name=St18; Synonyms=Kiaa0535;
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].
RC   STRAIN=C57BL/6J;
RA   Jandrig B., Seitz S., Hinzmann B., Arnold W.;
RT   "ST18 is a breast cancer candidate tumor suppressor gene.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J;
RC   TISSUE=Brain, Cerebellum, Embryo, and Embryonic spinal cord;
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 MRNA] OF 289-1045.
RC   TISSUE=Eye;
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).
CC   -!- FUNCTION: Repressor that binds to DNA sequences containing a bipartite
CC       element consisting of a direct repeat of the sequence 5'-AAAGTTT-3'
CC       separated by 2-9 nucleotides. Represses basal transcription activity
CC       from target promoters (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the MYT1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH32273.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC65585.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AJ536155; CAD60089.1; -; mRNA.
DR   EMBL; AK122303; BAC65585.1; ALT_INIT; mRNA.
DR   EMBL; AK133743; BAE21817.1; -; mRNA.
DR   EMBL; AK137440; BAE23351.1; -; mRNA.
DR   EMBL; AK141513; BAE24709.1; -; mRNA.
DR   EMBL; AK147320; BAE27844.1; -; mRNA.
DR   EMBL; AK147664; BAE28057.1; -; mRNA.
DR   EMBL; BC032273; AAH32273.1; ALT_INIT; mRNA.
DR   CCDS; CCDS14810.1; -.
DR   RefSeq; NP_001231621.1; NM_001244692.1.
DR   RefSeq; NP_001231622.1; NM_001244693.1.
DR   RefSeq; NP_776293.1; NM_173868.2.
DR   RefSeq; XP_006495564.1; XM_006495501.3.
DR   RefSeq; XP_006495565.1; XM_006495502.3.
DR   RefSeq; XP_006495566.1; XM_006495503.3.
DR   RefSeq; XP_006495567.1; XM_006495504.3.
DR   RefSeq; XP_011236672.1; XM_011238370.1.
DR   RefSeq; XP_011236673.1; XM_011238371.2.
DR   RefSeq; XP_011236674.1; XM_011238372.2.
DR   RefSeq; XP_011236675.1; XM_011238373.2.
DR   AlphaFoldDB; Q80TY4; -.
DR   SMR; Q80TY4; -.
DR   BioGRID; 232229; 6.
DR   STRING; 10090.ENSMUSP00000120298; -.
DR   iPTMnet; Q80TY4; -.
DR   PhosphoSitePlus; Q80TY4; -.
DR   MaxQB; Q80TY4; -.
DR   PaxDb; Q80TY4; -.
DR   PRIDE; Q80TY4; -.
DR   ProteomicsDB; 258630; -.
DR   Antibodypedia; 24412; 234 antibodies from 26 providers.
DR   DNASU; 240690; -.
DR   Ensembl; ENSMUST00000043578; ENSMUSP00000042056; ENSMUSG00000033740.
DR   Ensembl; ENSMUST00000131494; ENSMUSP00000117789; ENSMUSG00000033740.
DR   Ensembl; ENSMUST00000140079; ENSMUSP00000118322; ENSMUSG00000033740.
DR   Ensembl; ENSMUST00000150761; ENSMUSP00000120298; ENSMUSG00000033740.
DR   Ensembl; ENSMUST00000151281; ENSMUSP00000122055; ENSMUSG00000033740.
DR   Ensembl; ENSMUST00000163727; ENSMUSP00000131417; ENSMUSG00000033740.
DR   GeneID; 240690; -.
DR   KEGG; mmu:240690; -.
DR   UCSC; uc007afw.1; mouse.
DR   CTD; 9705; -.
DR   MGI; MGI:2446700; St18.
DR   VEuPathDB; HostDB:ENSMUSG00000033740; -.
DR   eggNOG; KOG3803; Eukaryota.
DR   GeneTree; ENSGT00940000159905; -.
DR   HOGENOM; CLU_007226_0_0_1; -.
DR   InParanoid; Q80TY4; -.
DR   OMA; DECYLIS; -.
DR   OrthoDB; 116799at2759; -.
DR   PhylomeDB; Q80TY4; -.
DR   TreeFam; TF317299; -.
DR   BioGRID-ORCS; 240690; 0 hits in 71 CRISPR screens.
DR   ChiTaRS; St18; mouse.
DR   PRO; PR:Q80TY4; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q80TY4; protein.
DR   Bgee; ENSMUSG00000033740; Expressed in cerebellum lobe and 120 other tissues.
DR   ExpressionAtlas; Q80TY4; baseline and differential.
DR   Genevisible; Q80TY4; MM.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0032993; C:protein-DNA complex; ISO:MGI.
DR   GO; GO:0003677; F:DNA binding; ISO:MGI.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0070102; P:interleukin-6-mediated signaling pathway; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:2001269; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISO:MGI.
DR   InterPro; IPR013681; Myelin_TF.
DR   InterPro; IPR002515; Znf_C2H2C.
DR   InterPro; IPR036060; Znf_C2H2C_sf.
DR   Pfam; PF08474; MYT1; 1.
DR   Pfam; PF01530; zf-C2HC; 6.
DR   SUPFAM; SSF103637; SSF103637; 6.
DR   PROSITE; PS51802; ZF_CCHHC; 6.
PE   2: Evidence at transcript level;
KW   Coiled coil; DNA-binding; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Repressor; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..1045
FT                   /note="Suppression of tumorigenicity 18 protein"
FT                   /id="PRO_0000234031"
FT   ZN_FING         357..400
FT                   /note="CCHHC-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   ZN_FING         401..444
FT                   /note="CCHHC-type 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   ZN_FING         713..756
FT                   /note="CCHHC-type 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   ZN_FING         757..800
FT                   /note="CCHHC-type 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   ZN_FING         805..848
FT                   /note="CCHHC-type 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   ZN_FING         858..901
FT                   /note="CCHHC-type 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   REGION          38..90
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          158..228
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..364
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          918..987
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        65..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..212
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        213..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         366
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         371
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         410
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         415
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         428
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         434
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         722
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         727
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         740
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         746
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         766
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         771
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         784
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         790
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         814
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         819
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         832
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         838
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         867
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         872
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         885
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   BINDING         891
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01143"
FT   CONFLICT        198
FT                   /note="S -> R (in Ref. 3; BAE24709)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="D -> N (in Ref. 3; BAE27844/BAE28057)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        493
FT                   /note="E -> D (in Ref. 3; BAE23351)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        736
FT                   /note="N -> D (in Ref. 3; BAE23351)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1045 AA;  114750 MW;  B18FE57081BB0CFA CRC64;
     MDAEVEDKTL HTLSKGTEVP MDSLIPELRV PYDCSMAKKR RAEEQASGVP INKRKSLLMK
     PRHYSPDMGC KESPDNRNED DGLLETNDHA TADEIMVKSM DETLHLPAQD SSLQKKDQYT
     CYPELMVKSL VHLGKFEESE SVQTTCENLN GSSIQSLKAE SDEAHEGSMV HSDNGRDKVH
     HSQPPFCSSG DSESDSDSAE NGWGNGSNSS EDTDTHKGPK HKLTYNRKDL LEVPEIKAED
     DKFIPCENRC DSDTDGRDPQ NSHMEPLVVK AQPSFPEVEE GESLATVTEE PAEVEKAKGN
     LSLLEQAIAL QAERGSVFHH TYKELDRFFL DHLARERRQP RVTDANGRQI FTNKHSPRPE
     RREAKCPIPG CDGTGHVTGL YPHHRSLSGC PHKVRVPLEI LAMHENVLKC PTPGCTGRGH
     VNSNRNTHRS LSGCPIAAAE KLAMTQDKSQ LDSSQTGQCP EQAHRVNLVK QIEFNFRSHA
     ITSPRASASK EQEKFGKVPF DYASFDAQVF GKRPLLQTGQ GQKAPPFPES KHFSNPVKFP
     NGLPSAGAHT QSTVRASSYG HGQYSEDTHI AAAAAILNLS TRCREATDIL SNKPQSLRAK
     GAEIEVDENG TLDLSMKKNR IHDKSIPPTS SPTTITTPSS SPFNASSLLV NAAFYQALSD
     QEGWNVPINY SKSHGKTEEE KEKDPVNFLE NLEEKKFAGE ASIPSPKPKL HTRDLKKELI
     TCPTPGCDGS GHVTGNYASH RSVSGCPLAD KTLKSLMAAN SQELKCPTPG CDGSGHVTGN
     YASHRSLSGC PRARKGGIKM TPTKEEKEDS ELRCPVIGCD GQGHISGKYT SHRTASGCPL
     AAKRQKENPL NGAPLSWKLN KQELPHCPLP GCNGLGHVNN VFVTHRSLSG CPLNAQAIKK
     VKVSEELMTI KLKATGGIDG DEEIRHLDEE IKELNESNLK IEADMMKLQT QITSMESNLK
     TIEEENKLIE QSNESLLKEL AGLSQALISS LADIQLPQMG PINEQNFEAY VNTLTDMYSN
     LEQDYSPECK ALLESIKQAV KGIHV
 
 
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