位置:首页 > 蛋白库 > MPP8_MOUSE
MPP8_MOUSE
ID   MPP8_MOUSE              Reviewed;         858 AA.
AC   Q3TYA6; A6H600; Q3TWY7;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=M-phase phosphoprotein 8 {ECO:0000250|UniProtKB:Q99549};
GN   Name=Mphosph8 {ECO:0000250|UniProtKB:Q99549, ECO:0000312|MGI:MGI:1922589};
GN   Synonyms=Mpp8 {ECO:0000250|UniProtKB:Q99549};
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=Visual cortex;
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 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   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   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-85; SER-136; SER-138;
RP   THR-144; SER-267 AND SER-271, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Kidney, Lung, Pancreas, 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 expression.";
RL   Cell 143:1174-1189(2010).
RN   [7]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=23416073; DOI=10.1016/j.bbrc.2013.02.027;
RA   Nishigaki M., Kawada Y., Misaki T., Murata K., Goshima T., Hirokawa T.,
RA   Yamada C., Shimada M., Nakanishi M.;
RT   "Mitotic phosphorylation of MPP8 by cyclin-dependent kinases regulates
RT   chromatin dissociation.";
RL   Biochem. Biophys. Res. Commun. 432:654-659(2013).
RN   [8]
RP   INTERACTION WITH TASOR, AND TISSUE SPECIFICITY.
RX   PubMed=31112734; DOI=10.1016/j.yexcr.2019.05.018;
RA   Gresakova V., Novosadova V., Prochazkova M., Bhargava S., Jenickova I.,
RA   Prochazka J., Sedlacek R.;
RT   "Fam208a orchestrates interaction protein network essential for early
RT   embryonic development and cell division.";
RL   Exp. Cell Res. 382:111437-111437(2019).
CC   -!- FUNCTION: Heterochromatin component that specifically recognizes and
CC       binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes
CC       recruitment of proteins that mediate epigenetic repression. Mediates
CC       recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is
CC       recruited to genomic loci rich in H3K9me3 and is required to maintain
CC       transcriptional silencing by promoting recruitment of SETDB1, a histone
CC       methyltransferase that mediates further deposition of H3K9me3, as well
CC       as MORC2. Binds H3K9me and promotes DNA methylation by recruiting
CC       DNMT3A to target CpG sites; these can be situated within the coding
CC       region of the gene. Mediates down-regulation of CDH1 expression. Also
CC       represses L1 retrotransposons in collaboration with MORC2 and,
CC       probably, SETDB1, the silencing is dependent of repressive epigenetic
CC       modifications, such as H3K9me3 mark. Silencing events often occur
CC       within introns of transcriptionally active genes, and lead to the down-
CC       regulation of host gene expression. The HUSH complex is also involved
CC       in the silencing of unintegrated retroviral DNA by being recruited by
CC       ZNF638: some part of the retroviral DNA formed immediately after
CC       infection remains unintegrated in the host genome and is
CC       transcriptionally repressed. {ECO:0000250|UniProtKB:Q99549}.
CC   -!- SUBUNIT: Homodimer. Interacts (via chromo domain) with histone H3K9me3.
CC       Has the highest affinity for H3K9me3, and lesser affinity for H3K9me2
CC       and H3K9me1. Component of the HUSH complex; at least composed of TASOR,
CC       PPHLN1 and MPHOSPH8. Interacts with DNMT3, EHMT1 and SETDB1. Interacts
CC       with MORC2; the interaction associateS MORC2 with the HUSH complex
CC       which recruits MORC2 to heterochromatic loci. Interacts with ZNF638;
CC       leading to recruitment of the HUSH complex to unintegrated retroviral
CC       DNA (By similarity). Interacts with TASOR (PubMed:31112734).
CC       {ECO:0000250|UniProtKB:Q99549, ECO:0000269|PubMed:31112734}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23416073}. Chromosome
CC       {ECO:0000269|PubMed:23416073}. Note=Detected on heterochromatin
CC       (PubMed:23416073). Dissociates from chromatin during interphase and
CC       early mitosis (PubMed:23416073). Detected on nucleosomes (By
CC       similarity). {ECO:0000250|UniProtKB:Q99549,
CC       ECO:0000269|PubMed:23416073}.
CC   -!- TISSUE SPECIFICITY: Expressed in the spermatogonia, spermatocytes and
CC       granular cells within the cerebellum. {ECO:0000269|PubMed:31112734}.
CC   -!- DOMAIN: The chromo domain mediates interaction with methylated 'Lys-9'
CC       of histone H3 (H3K9me), with the highest affinity for the trimethylated
CC       form (H3K9me3). {ECO:0000250|UniProtKB:Q99549}.
CC   -!- PTM: Phosphorylated in M (mitotic) phase. Phosphorylation by CDK1
CC       promotes dissociation from chromatin. {ECO:0000250|UniProtKB:Q99549}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAI45701.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK158773; BAE34657.1; -; mRNA.
DR   EMBL; AK159495; BAE35129.1; -; mRNA.
DR   EMBL; AC154731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466535; EDL36192.1; -; Genomic_DNA.
DR   EMBL; BC145700; AAI45701.1; ALT_INIT; mRNA.
DR   CCDS; CCDS49504.1; -.
DR   RefSeq; NP_076262.2; NM_023773.2.
DR   AlphaFoldDB; Q3TYA6; -.
DR   SMR; Q3TYA6; -.
DR   BioGRID; 217406; 3.
DR   STRING; 10090.ENSMUSP00000112170; -.
DR   iPTMnet; Q3TYA6; -.
DR   PhosphoSitePlus; Q3TYA6; -.
DR   EPD; Q3TYA6; -.
DR   jPOST; Q3TYA6; -.
DR   MaxQB; Q3TYA6; -.
DR   PaxDb; Q3TYA6; -.
DR   PeptideAtlas; Q3TYA6; -.
DR   PRIDE; Q3TYA6; -.
DR   ProteomicsDB; 291437; -.
DR   Antibodypedia; 22243; 103 antibodies from 29 providers.
DR   DNASU; 75339; -.
DR   Ensembl; ENSMUST00000116468; ENSMUSP00000112170; ENSMUSG00000079184.
DR   GeneID; 75339; -.
DR   KEGG; mmu:75339; -.
DR   UCSC; uc011zmc.1; mouse.
DR   CTD; 54737; -.
DR   MGI; MGI:1922589; Mphosph8.
DR   VEuPathDB; HostDB:ENSMUSG00000079184; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   eggNOG; KOG1911; Eukaryota.
DR   GeneTree; ENSGT00730000111087; -.
DR   HOGENOM; CLU_332588_0_0_1; -.
DR   InParanoid; Q3TYA6; -.
DR   OMA; FAISCEF; -.
DR   OrthoDB; 1628171at2759; -.
DR   PhylomeDB; Q3TYA6; -.
DR   TreeFam; TF106394; -.
DR   BioGRID-ORCS; 75339; 8 hits in 75 CRISPR screens.
DR   ChiTaRS; Mphosph8; mouse.
DR   PRO; PR:Q3TYA6; -.
DR   Proteomes; UP000000589; Chromosome 14.
DR   RNAct; Q3TYA6; protein.
DR   Bgee; ENSMUSG00000079184; Expressed in animal zygote and 252 other tissues.
DR   Genevisible; Q3TYA6; MM.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0000792; C:heterochromatin; ISS:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000786; C:nucleosome; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR   GO; GO:0035064; F:methylated histone binding; ISS:UniProtKB.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; ISS:UniProtKB.
DR   GO; GO:0045869; P:negative regulation of single stranded viral RNA replication via double stranded DNA intermediate; ISS:UniProtKB.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR   GO; GO:0090309; P:positive regulation of DNA methylation-dependent heterochromatin assembly; ISS:UniProtKB.
DR   GO; GO:2000812; P:regulation of barbed-end actin filament capping; IBA:GO_Central.
DR   GO; GO:0044030; P:regulation of DNA methylation; ISS:UniProtKB.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR023779; Chromodomain_CS.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF00385; Chromo; 1.
DR   SMART; SM00248; ANK; 3.
DR   SMART; SM00298; CHROMO; 1.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS00598; CHROMO_1; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
PE   1: Evidence at protein level;
KW   ANK repeat; Chromosome; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat; Transcription; Transcription regulation.
FT   CHAIN           1..858
FT                   /note="M-phase phosphoprotein 8"
FT                   /id="PRO_0000415976"
FT   DOMAIN          59..118
FT                   /note="Chromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT   REPEAT          598..627
FT                   /note="ANK 1"
FT   REPEAT          631..660
FT                   /note="ANK 2"
FT   REPEAT          664..693
FT                   /note="ANK 3"
FT   REPEAT          697..726
FT                   /note="ANK 4"
FT   REGION          18..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          80..87
FT                   /note="Histone H3K9me3 binding"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   REGION          129..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..431
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        159..175
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        284..300
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..367
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..391
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..431
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            59
FT                   /note="Interaction with histone H3K9me3"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         51
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         138
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         144
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         149
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         164
FT                   /note="Phosphoserine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         267
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         271
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         318
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         385
FT                   /note="Phosphothreonine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         392
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         400
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   MOD_RES         453
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q99549"
FT   CONFLICT        158
FT                   /note="K -> E (in Ref. 1; BAE35129)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   858 AA;  97467 MW;  17C90A836A416964 CRC64;
     MAAAAEEGMS AAALVMSVPD SIGRSPESEG VGAGDEEKDA ATKGTVAVGD SEEDGEDVFE
     VERILDMKCE GGKNLYKVRW KGYTSEDDTW EPEVHLEDCK EVLLEFRKKL AENKAKAVRK
     DIQRLSLNND IFEADSDSDQ QSDTKEDISP RKKKKKIKCK EETSPEDLRK KRTKMGKLKD
     KFKTELESTS EIIGFDVKTK KRIWEVKEEL KDSKKPKKDE IKETKELKKA NKRAEVRDLK
     IKIREDVKEN RKTKKERYIE SPLESESPND SLILEDDSED FISDNREENQ NVRSVRDKTA
     QETVQEGIFE KHLDDLISIE EDAGTRVRRK KTKPRKFEEP KEIKKLESTN AFLERRAIPK
     KQRNQDKGIS NLELNKLPSP VFAQTLKSSR LSGEEKSLKS PDLAEEEKEK KNEPKGKYQK
     RYDLDKEEKA RKEPKVLKSF KEIRNAFDLF KKTTEEKNDV LENNSKREEI SLDSKIMNDN
     KTKDKCSLKE KRNTRDETDT WAYIAAEGDQ EVSDSVCQTD ETSDGRQPVL SLGMDLQLEW
     MKLEDFQKHL DGEDEPFITT NRIPNNLLRD AVKNGDYIAV KVALNSNEEY NLDQEDSTGM
     TLVMLAAAGG QDDLLRLLIT KGAKVNGRQK NGTTALIHAA EKNFLTTVAI LLEAGAFVNV
     QQSNGETALM KACKRGNSDI VRLVIECGAD CNILSKHQNS ALYFAKQCNN VLVYELLKSH
     LETLSRVAEE TIRDYFESRL ALLEPVFPIA CHRLCEGPDF STDFNYMPPQ NMPEGSGVLL
     FIFHANFLGK DVIARLCGPC SVQAVVLNDK FQLPVFLDSH FVYSFSPVAG PNKLFIRLTE
     APFAKVKLLI GAYRVQLQ
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024