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MRES1_HUMAN
ID   MRES1_HUMAN             Reviewed;         240 AA.
AC   Q9P0P8; B3KRG9;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 139.
DE   RecName: Full=Mitochondrial transcription rescue factor 1 {ECO:0000303|PubMed:31226201};
DE   Flags: Precursor;
GN   Name=MTRES1 {ECO:0000312|HGNC:HGNC:17971}; Synonyms=C6orf203;
GN   ORFNames=HSPC230;
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].
RC   TISSUE=Umbilical cord blood;
RX   PubMed=11042152; DOI=10.1101/gr.140200;
RA   Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA   Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA   Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT   "Cloning and functional analysis of cDNAs with open reading frames for 300
RT   previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT   cells.";
RL   Genome Res. 10:1546-1560(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Bone marrow;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-116, AND
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-116, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106 AND SER-116, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [10]
RP   SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, MUTAGENESIS OF ARG-143; ASP-145;
RP   LYS-149; ARG-156 AND LYS-158, INTERACTION WITH POLRMT, AND INDUCTION.
RX   PubMed=31226201; DOI=10.1093/nar/gkz542;
RA   Kotrys A.V., Cysewski D., Czarnomska S.D., Pietras Z., Borowski L.S.,
RA   Dziembowski A., Szczesny R.J.;
RT   "Quantitative proteomics revealed C6orf203/MTRES1 as a factor preventing
RT   stress-induced transcription deficiency in human mitochondria.";
RL   Nucleic Acids Res. 47:7502-7517(2019).
RN   [11]
RP   FUNCTION, INTERACTION WITH MTRES1, RNA-BINDING, INTERACTION WITH
RP   MITORIBOSOMAL LARGE SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=31396629; DOI=10.1093/nar/gkz684;
RA   Gopalakrishna S., Pearce S.F., Dinan A.M., Schober F.A., Cipullo M.,
RA   Spaahr H., Khawaja A., Maffezzini C., Freyer C., Wredenberg A.,
RA   Atanassov I., Firth A.E., Rorbach J.;
RT   "C6orf203 is an RNA-binding protein involved in mitochondrial protein
RT   synthesis.";
RL   Nucleic Acids Res. 47:9386-9399(2019).
RN   [12] {ECO:0000312|PDB:7A5H}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.3 ANGSTROMS) OF 1-240 IN COMPLEX WITH
RP   MTRFR; PEPTIDYL TRNA AND MITORIBOSOMAL LARGE SUBUNIT, FUNCTION, INTERACTION
RP   WITH MTRES1, AND RNA-BINDING.
RX   PubMed=33243891; DOI=10.1126/science.abc7782;
RA   Desai N., Yang H., Chandrasekaran V., Kazi R., Minczuk M., Ramakrishnan V.;
RT   "Elongational stalling activates mitoribosome-associated quality control.";
RL   Science 370:1105-1110(2020).
CC   -!- FUNCTION: Mitochondrial RNA-binding protein involved in mitochondrial
CC       transcription regulation. Functions as a protective factor to maintain
CC       proper mitochondrial RNA level during stress. Acts at the transcription
CC       level and its protective function depends on its RNA binding ability
CC       (PubMed:31226201). Part of a mitoribosome-associated quality control
CC       pathway that prevents aberrant translation by responding to
CC       interruptions during elongation (PubMed:33243891, PubMed:31396629). As
CC       heterodimer with MTRF, ejects the unfinished nascent chain and peptidyl
CC       transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment
CC       of mitoribosome biogenesis factors to these quality control
CC       intermediates suggests additional roles for MTRES1 and MTRF during
CC       mitoribosome rescue (PubMed:33243891). {ECO:0000269|PubMed:31226201,
CC       ECO:0000269|PubMed:31396629, ECO:0000269|PubMed:33243891}.
CC   -!- SUBUNIT: Monomer (PubMed:31226201). Interacts with POLRMT
CC       (PubMed:31226201). Interacts (via S4 domain) with MTRFR (via C-
CC       terminus) (PubMed:33243891, PubMed:31396629). Associates with
CC       mitoribosomal S39 large subunit, peptidyl tRNA and nascent chain
CC       (PubMed:33243891, PubMed:31396629). {ECO:0000269|PubMed:31226201,
CC       ECO:0000269|PubMed:31396629, ECO:0000269|PubMed:33243891}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:31226201, ECO:0000269|PubMed:31396629}.
CC   -!- INDUCTION: Up-regulated upon depletion of mitochondrial nucleic acids.
CC       {ECO:0000269|PubMed:31226201}.
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DR   EMBL; AF151064; AAF36150.1; -; mRNA.
DR   EMBL; AK091564; BAG52381.1; -; mRNA.
DR   EMBL; AL355586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471051; EAW48402.1; -; Genomic_DNA.
DR   EMBL; BC010899; AAH10899.1; -; mRNA.
DR   CCDS; CCDS5058.1; -.
DR   RefSeq; NP_001135940.1; NM_001142468.2.
DR   RefSeq; NP_001135942.1; NM_001142470.2.
DR   RefSeq; NP_057571.1; NM_016487.4.
DR   PDB; 7A5H; EM; 3.30 A; G=1-240.
DR   PDBsum; 7A5H; -.
DR   AlphaFoldDB; Q9P0P8; -.
DR   SMR; Q9P0P8; -.
DR   BioGRID; 119407; 292.
DR   IntAct; Q9P0P8; 24.
DR   MINT; Q9P0P8; -.
DR   STRING; 9606.ENSP00000384867; -.
DR   iPTMnet; Q9P0P8; -.
DR   PhosphoSitePlus; Q9P0P8; -.
DR   BioMuta; C6orf203; -.
DR   DMDM; 71152388; -.
DR   EPD; Q9P0P8; -.
DR   jPOST; Q9P0P8; -.
DR   MassIVE; Q9P0P8; -.
DR   MaxQB; Q9P0P8; -.
DR   PaxDb; Q9P0P8; -.
DR   PeptideAtlas; Q9P0P8; -.
DR   PRIDE; Q9P0P8; -.
DR   ProteomicsDB; 83590; -.
DR   TopDownProteomics; Q9P0P8; -.
DR   Antibodypedia; 55873; 84 antibodies from 15 providers.
DR   DNASU; 51250; -.
DR   Ensembl; ENST00000311381.8; ENSP00000310951.5; ENSG00000130349.10.
DR   Ensembl; ENST00000405204.6; ENSP00000384867.2; ENSG00000130349.10.
DR   GeneID; 51250; -.
DR   KEGG; hsa:51250; -.
DR   MANE-Select; ENST00000311381.8; ENSP00000310951.5; NM_016487.5; NP_057571.1.
DR   UCSC; uc003prq.5; human.
DR   CTD; 51250; -.
DR   GeneCards; MTRES1; -.
DR   HGNC; HGNC:17971; MTRES1.
DR   HPA; ENSG00000130349; Low tissue specificity.
DR   MIM; 618583; gene.
DR   neXtProt; NX_Q9P0P8; -.
DR   OpenTargets; ENSG00000130349; -.
DR   VEuPathDB; HostDB:ENSG00000130349; -.
DR   eggNOG; KOG4837; Eukaryota.
DR   GeneTree; ENSGT00390000009366; -.
DR   HOGENOM; CLU_076117_0_0_1; -.
DR   InParanoid; Q9P0P8; -.
DR   OMA; VHHLRFK; -.
DR   OrthoDB; 1440120at2759; -.
DR   PhylomeDB; Q9P0P8; -.
DR   PathwayCommons; Q9P0P8; -.
DR   SignaLink; Q9P0P8; -.
DR   BioGRID-ORCS; 51250; 24 hits in 1067 CRISPR screens.
DR   ChiTaRS; C6orf203; human.
DR   GenomeRNAi; 51250; -.
DR   Pharos; Q9P0P8; Tdark.
DR   PRO; PR:Q9P0P8; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9P0P8; protein.
DR   Bgee; ENSG00000130349; Expressed in oocyte and 191 other tissues.
DR   ExpressionAtlas; Q9P0P8; baseline and differential.
DR   Genevisible; Q9P0P8; HS.
DR   GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:UniProtKB.
DR   GO; GO:0043023; F:ribosomal large subunit binding; IDA:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0000049; F:tRNA binding; IDA:UniProtKB.
DR   GO; GO:1903108; P:regulation of mitochondrial transcription; IMP:UniProtKB.
DR   GO; GO:0072344; P:rescue of stalled ribosome; IDA:UniProtKB.
DR   InterPro; IPR039167; MTRES1.
DR   PANTHER; PTHR13633; PTHR13633; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Phosphoprotein; Reference proteome;
KW   RNA-binding; Transcription; Transcription regulation; Transit peptide.
FT   TRANSIT         1..84
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000269|PubMed:31226201"
FT   CHAIN           85..240
FT                   /note="Mitochondrial transcription rescue factor 1"
FT                   /id="PRO_0000089559"
FT   DOMAIN          142..217
FT                   /note="S4 RNA-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00182,
FT                   ECO:0000269|PubMed:31396629, ECO:0000269|PubMed:33243891"
FT   REGION          95..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..124
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         106
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT   MUTAGEN         143
FT                   /note="R->A: Decreased RNA-binding; when associated with A-
FT                   145; A-149: A-156 and A-158. Does not rescue diminished
FT                   mitochondrial transcription induced by EtBr; when
FT                   associated with A-145; A-149: A-156 and A-158."
FT                   /evidence="ECO:0000269|PubMed:31226201"
FT   MUTAGEN         145
FT                   /note="D->A: Decreased RNA-binding; when associated with A-
FT                   143; A-149: A-156 and A-158. Does not rescue diminished
FT                   mitochondrial transcription induced by EtBr; when
FT                   associated with A-143; A-149: A-156 and A-158."
FT                   /evidence="ECO:0000269|PubMed:31226201"
FT   MUTAGEN         149
FT                   /note="K->A: Decreased RNA-binding; when associated with A-
FT                   143; A-145: A-156 and A-158. Does not rescue diminished
FT                   mitochondrial transcription induced by EtBr; when
FT                   associated with A-143; A-149: A-156 and A-158."
FT                   /evidence="ECO:0000269|PubMed:31226201"
FT   MUTAGEN         156
FT                   /note="R->A: Decreased RNA-binding; when associated with A-
FT                   143; A-145: A-149 and A-158. Does not rescue diminished
FT                   mitochondrial transcription induced by EtBr; when
FT                   associated with A-143; A-145: A-149 and A-158."
FT                   /evidence="ECO:0000269|PubMed:31226201"
FT   MUTAGEN         158
FT                   /note="K->A: Decreased RNA-binding; when associated with A-
FT                   143; A-145: A-149 and A-156. Does not rescue diminished
FT                   mitochondrial transcription induced by EtBr; when
FT                   associated with A-143; A-145: A-149 and A-156."
FT                   /evidence="ECO:0000269|PubMed:31226201"
SQ   SEQUENCE   240 AA;  27941 MW;  01E2DBCB11537275 CRC64;
     MAMASVKLLA GVLRKPDAWI GLWGVLRGTP SSYKLCTSWN RYLYFSSTKL RAPNYKTLFY
     NIFSLRLPGL LLSPECIFPF SVRLKSNIRS TKSTKKSLQK VDEEDSDEES HHDEMSEQEE
     ELEDDPTVVK NYKDLEKAVQ SFRYDVVLKT GLDIGRNKVE DAFYKGELRL NEEKLWKKSR
     TVKVGDTLDL LIGEDKEAGT ETVMRILLKK VFEEKTESEK YRVVLRRWKS LKLPKKRMSK
 
 
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