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ZBTB9_HUMAN
ID   ZBTB9_HUMAN             Reviewed;         473 AA.
AC   Q96C00; A2AB19;
DT   26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 163.
DE   RecName: Full=Zinc finger and BTB domain-containing protein 9;
GN   Name=ZBTB9;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-286, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25218447; DOI=10.1038/nsmb.2890;
RA   Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA   Vertegaal A.C.;
RT   "Uncovering global SUMOylation signaling networks in a site-specific
RT   manner.";
RL   Nat. Struct. Mol. Biol. 21:927-936(2014).
RN   [7]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-286, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA   Impens F., Radoshevich L., Cossart P., Ribet D.;
RT   "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT   external stimuli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN   [8]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-286, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA   Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL   Cell Rep. 10:1778-1791(2015).
RN   [9]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-286, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA   Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA   Vertegaal A.C.;
RT   "System-wide analysis of SUMOylation dynamics in response to replication
RT   stress reveals novel small ubiquitin-like modified target proteins and
RT   acceptor lysines relevant for genome stability.";
RL   Mol. Cell. Proteomics 14:1419-1434(2015).
RN   [10]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-286; LYS-293; LYS-307 AND
RP   LYS-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
CC   -!- FUNCTION: May be involved in transcriptional regulation.
CC   -!- INTERACTION:
CC       Q96C00; Q7Z479: CAPN7; NbExp=3; IntAct=EBI-395708, EBI-10213454;
CC       Q96C00; Q9HC52: CBX8; NbExp=3; IntAct=EBI-395708, EBI-712912;
CC       Q96C00; Q8N8U2: CDYL2; NbExp=3; IntAct=EBI-395708, EBI-8467076;
CC       Q96C00; A0PJX0: CIB4; NbExp=3; IntAct=EBI-395708, EBI-12868028;
CC       Q96C00; P61024: CKS1B; NbExp=3; IntAct=EBI-395708, EBI-456371;
CC       Q96C00; O60941: DTNB; NbExp=5; IntAct=EBI-395708, EBI-740402;
CC       Q96C00; Q92630: DYRK2; NbExp=3; IntAct=EBI-395708, EBI-749432;
CC       Q96C00; Q08426: EHHADH; NbExp=6; IntAct=EBI-395708, EBI-2339219;
CC       Q96C00; O60573: EIF4E2; NbExp=4; IntAct=EBI-395708, EBI-398610;
CC       Q96C00; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-395708, EBI-11959885;
CC       Q96C00; P60409: KRTAP10-7; NbExp=7; IntAct=EBI-395708, EBI-10172290;
CC       Q96C00; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-395708, EBI-10172052;
CC       Q96C00; P59991: KRTAP12-2; NbExp=6; IntAct=EBI-395708, EBI-10176379;
CC       Q96C00; Q14847: LASP1; NbExp=4; IntAct=EBI-395708, EBI-742828;
CC       Q96C00; Q14566: MCM6; NbExp=3; IntAct=EBI-395708, EBI-374900;
CC       Q96C00; Q99750: MDFI; NbExp=6; IntAct=EBI-395708, EBI-724076;
CC       Q96C00; Q9UBU8: MORF4L1; NbExp=4; IntAct=EBI-395708, EBI-399246;
CC       Q96C00; Q9UBU8-2: MORF4L1; NbExp=3; IntAct=EBI-395708, EBI-10288852;
CC       Q96C00; Q13526: PIN1; NbExp=6; IntAct=EBI-395708, EBI-714158;
CC       Q96C00; Q9Y237: PIN4; NbExp=4; IntAct=EBI-395708, EBI-714599;
CC       Q96C00; Q8TAD8: SNIP1; NbExp=6; IntAct=EBI-395708, EBI-749336;
CC       Q96C00; Q96C24: SYTL4; NbExp=3; IntAct=EBI-395708, EBI-747142;
CC       Q96C00; Q15560: TCEA2; NbExp=3; IntAct=EBI-395708, EBI-710310;
CC       Q96C00; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-395708, EBI-11955057;
CC       Q96C00; Q6FI91: TSPYL; NbExp=3; IntAct=EBI-395708, EBI-723389;
CC       Q96C00; Q969E8: TSR2; NbExp=6; IntAct=EBI-395708, EBI-746981;
CC       Q96C00; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-395708, EBI-10180829;
CC       Q96C00; O43167: ZBTB24; NbExp=3; IntAct=EBI-395708, EBI-744471;
CC       Q96C00; Q9HCK0: ZBTB26; NbExp=3; IntAct=EBI-395708, EBI-3918996;
CC       Q96C00; P10074: ZBTB48; NbExp=3; IntAct=EBI-395708, EBI-744864;
CC       Q96C00; Q96C00: ZBTB9; NbExp=5; IntAct=EBI-395708, EBI-395708;
CC       Q96C00; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-395708, EBI-740727;
CC       Q96C00; Q9NQZ8: ZNF71; NbExp=3; IntAct=EBI-395708, EBI-7138235;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
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DR   EMBL; AK122644; BAG53637.1; -; mRNA.
DR   EMBL; BX088650; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03739.1; -; Genomic_DNA.
DR   EMBL; BC014978; AAH14978.1; -; mRNA.
DR   CCDS; CCDS4780.1; -.
DR   RefSeq; NP_689948.1; NM_152735.3.
DR   AlphaFoldDB; Q96C00; -.
DR   SMR; Q96C00; -.
DR   BioGRID; 128736; 106.
DR   IntAct; Q96C00; 72.
DR   MINT; Q96C00; -.
DR   STRING; 9606.ENSP00000378503; -.
DR   iPTMnet; Q96C00; -.
DR   PhosphoSitePlus; Q96C00; -.
DR   BioMuta; ZBTB9; -.
DR   DMDM; 46577533; -.
DR   EPD; Q96C00; -.
DR   jPOST; Q96C00; -.
DR   MassIVE; Q96C00; -.
DR   MaxQB; Q96C00; -.
DR   PaxDb; Q96C00; -.
DR   PeptideAtlas; Q96C00; -.
DR   PRIDE; Q96C00; -.
DR   ProteomicsDB; 76137; -.
DR   Antibodypedia; 14338; 99 antibodies from 22 providers.
DR   DNASU; 221504; -.
DR   Ensembl; ENST00000395064.3; ENSP00000378503.2; ENSG00000213588.6.
DR   Ensembl; ENST00000414934.2; ENSP00000413557.2; ENSG00000236515.3.
DR   GeneID; 221504; -.
DR   KEGG; hsa:221504; -.
DR   MANE-Select; ENST00000395064.3; ENSP00000378503.2; NM_152735.4; NP_689948.1.
DR   UCSC; uc003oeq.4; human.
DR   CTD; 221504; -.
DR   DisGeNET; 221504; -.
DR   GeneCards; ZBTB9; -.
DR   HGNC; HGNC:28323; ZBTB9.
DR   HPA; ENSG00000213588; Low tissue specificity.
DR   neXtProt; NX_Q96C00; -.
DR   OpenTargets; ENSG00000213588; -.
DR   PharmGKB; PA134895172; -.
DR   VEuPathDB; HostDB:ENSG00000213588; -.
DR   eggNOG; KOG1721; Eukaryota.
DR   GeneTree; ENSGT00940000162408; -.
DR   HOGENOM; CLU_029118_2_0_1; -.
DR   InParanoid; Q96C00; -.
DR   OMA; KVFYIKQ; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; Q96C00; -.
DR   PathwayCommons; Q96C00; -.
DR   SignaLink; Q96C00; -.
DR   BioGRID-ORCS; 221504; 18 hits in 1116 CRISPR screens.
DR   GenomeRNAi; 221504; -.
DR   Pharos; Q96C00; Tdark.
DR   PRO; PR:Q96C00; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q96C00; protein.
DR   Bgee; ENSG00000213588; Expressed in pituitary gland and 103 other tissues.
DR   ExpressionAtlas; Q96C00; baseline and differential.
DR   Genevisible; Q96C00; HS.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   Pfam; PF00651; BTB; 1.
DR   SMART; SM00225; BTB; 1.
DR   SMART; SM00355; ZnF_C2H2; 2.
DR   SUPFAM; SSF54695; SSF54695; 1.
DR   SUPFAM; SSF57667; SSF57667; 1.
DR   PROSITE; PS50097; BTB; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Repeat; Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..473
FT                   /note="Zinc finger and BTB domain-containing protein 9"
FT                   /id="PRO_0000047723"
FT   DOMAIN          48..112
FT                   /note="BTB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00037"
FT   ZN_FING         411..433
FT                   /note="C2H2-type 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   ZN_FING         438..460
FT                   /note="C2H2-type 2; atypical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT   REGION          177..279
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        208..227
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        286
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO1); alternate"
FT                   /evidence="ECO:0007744|PubMed:25114211"
FT   CROSSLNK        286
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0007744|PubMed:25218447,
FT                   ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT                   ECO:0007744|PubMed:28112733"
FT   CROSSLNK        293
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        307
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        382
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         274
FT                   /note="A -> G (in dbSNP:rs9469425)"
FT                   /id="VAR_061981"
SQ   SEQUENCE   473 AA;  50602 MW;  2BC8041790090FD9 CRC64;
     METPTPLPPV PASPTCNPAP RTIQIEFPQH SSSLLESLNR HRLEGKFCDV SLLVQGRELR
     AHKAVLAAAS PYFHDKLLLG DAPRLTLPSV IEADAFEGLL QLIYSGRLRL PLDALPAHLL
     VASGLQMWQV VDQCSEILRE LETSGGGISA RGGNSYHALL STTSSTGGWC IRSSPFQTPV
     QSSASTESPA STESPVGGEG SELGEVLQIQ VEEEEEEEED DDDEDQGSAT LSQTPQPQRV
     SGVFPRPHGP HPLPMTATPR KLPEGESAPL ELPAPPALPP KIFYIKQEPF EPKEEISGSG
     TQPGGAKEET KVFSGGDTEG NGELGFLLPS GPGPTSGGGG PSWKPVDLHG NEILSGGGGP
     GGAGQAVHGP VKLGGTPPAD GKRFGCLCGK RFAVKPKRDR HIMLTFSLRP FGCGICNKRF
     KLKHHLTEHM KTHAGALHAC PHCGRRFRVH ACFLRHRDLC KGQGWATAHW TYK
 
 
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