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MLXPL_HUMAN
ID   MLXPL_HUMAN             Reviewed;         852 AA.
AC   Q9NP71; C5HU02; C5HU03; C5HU04; Q96E48; Q9BY03; Q9BY04; Q9BY05; Q9BY06;
AC   Q9Y2P3;
DT   23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 183.
DE   RecName: Full=Carbohydrate-responsive element-binding protein;
DE            Short=ChREBP;
DE   AltName: Full=Class D basic helix-loop-helix protein 14;
DE            Short=bHLHd14;
DE   AltName: Full=MLX interactor;
DE   AltName: Full=MLX-interacting protein-like;
DE   AltName: Full=WS basic-helix-loop-helix leucine zipper protein;
DE            Short=WS-bHLH;
DE   AltName: Full=Williams-Beuren syndrome chromosomal region 14 protein;
GN   Name=MLXIPL; Synonyms=BHLHD14, MIO, WBSCR14;
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 (ISOFORM 1), AND INVOLVEMENT IN WBS.
RX   PubMed=10780788; DOI=10.1038/sj.ejhg.5200435;
RA   de Luis O., Valero M.C., Perez Jurado L.A.;
RT   "WBSCR14, a putative transcription factor gene deleted in Williams-Beuren
RT   syndrome: complete characterisation of the human gene and the mouse
RT   ortholog.";
RL   Eur. J. Hum. Genet. 8:215-222(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND SUBUNIT.
RX   PubMed=11230181; DOI=10.1093/hmg/10.6.617;
RA   Cairo S., Merla G., Urbinati F., Ballabio A., Reymond A.;
RT   "WBSCR14, a gene mapping to the Williams-Beuren syndrome deleted region, is
RT   a new member of the Mlx transcription factor network.";
RL   Hum. Mol. Genet. 10:617-627(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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 [MRNA] OF 620-852 (ISOFORM 4).
RX   PubMed=9860302; DOI=10.1007/s004390050874;
RA   Meng X., Lu X., Li Z., Green E.D., Massa H., Trask B.J., Morris C.A.,
RA   Keating M.T.;
RT   "Complete physical map of the common deletion region in Williams syndrome
RT   and identification and characterization of three novel genes.";
RL   Hum. Genet. 103:590-599(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
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   [7]
RP   SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
RX   PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8;
RA   Hillman R.T., Green R.E., Brenner S.E.;
RT   "An unappreciated role for RNA surveillance.";
RL   Genome Biol. 5:R8.1-R8.16(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196; SER-602 AND SER-614, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-25; THR-27;
RP   SER-29; SER-602 AND SER-631, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP   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).
CC   -!- FUNCTION: Transcriptional repressor. Binds to the canonical and non-
CC       canonical E box sequences 5'-CACGTG-3' (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds DNA as a heterodimer with TCFL4/MLX.
CC       {ECO:0000269|PubMed:11230181}.
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Alpha;
CC         IsoId=Q9NP71-1; Sequence=Displayed;
CC       Name=2; Synonyms=Beta;
CC         IsoId=Q9NP71-2; Sequence=VSP_002171;
CC       Name=3; Synonyms=Gamma;
CC         IsoId=Q9NP71-3; Sequence=VSP_002170;
CC       Name=4; Synonyms=Delta;
CC         IsoId=Q9NP71-4; Sequence=VSP_002170, VSP_002171;
CC       Name=5; Synonyms=Epsilon;
CC         IsoId=Q9NP71-5; Sequence=VSP_002168, VSP_002169;
CC       Name=6;
CC         IsoId=Q9NP71-6; Sequence=VSP_002167, VSP_002172, VSP_002173;
CC   -!- TISSUE SPECIFICITY: Expressed in liver, heart, kidney, cerebellum and
CC       intestinal tissues.
CC   -!- PTM: Phosphorylation at Ser-556 by AMPK inactivates the DNA-binding
CC       activity. {ECO:0000250}.
CC   -!- DISEASE: Note=WBSCR14 is located in the Williams-Beuren syndrome (WBS)
CC       critical region. WBS results from a hemizygous deletion of several
CC       genes on chromosome 7q11.23, thought to arise as a consequence of
CC       unequal crossing over between highly homologous low-copy repeat
CC       sequences flanking the deleted region. Haploinsufficiency of WBSCR14
CC       may be the cause of certain cardiovascular and musculo-skeletal
CC       abnormalities observed in the disease. {ECO:0000269|PubMed:10780788}.
CC   -!- MISCELLANEOUS: [Isoform 5]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
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DR   EMBL; AF156673; AAF68176.1; -; Genomic_DNA.
DR   EMBL; AF156603; AAF68174.1; -; mRNA.
DR   EMBL; AF245470; AAK20935.1; -; mRNA.
DR   EMBL; AF245471; AAK20936.1; -; mRNA.
DR   EMBL; AF245472; AAK20937.1; -; mRNA.
DR   EMBL; AF245473; AAK20938.1; -; mRNA.
DR   EMBL; AF245474; AAK20939.1; -; mRNA.
DR   EMBL; FJ515858; ACS13745.1; -; Genomic_DNA.
DR   EMBL; FJ515858; ACS13746.1; -; Genomic_DNA.
DR   EMBL; FJ515858; ACS13748.1; -; Genomic_DNA.
DR   EMBL; AF056184; AAD28084.1; -; mRNA.
DR   EMBL; CH471200; EAW69660.1; -; Genomic_DNA.
DR   EMBL; CH471200; EAW69661.1; -; Genomic_DNA.
DR   EMBL; CH471200; EAW69662.1; -; Genomic_DNA.
DR   EMBL; BC012925; AAH12925.1; -; mRNA.
DR   CCDS; CCDS47605.1; -. [Q9NP71-2]
DR   CCDS; CCDS47606.1; -. [Q9NP71-3]
DR   CCDS; CCDS5553.1; -. [Q9NP71-1]
DR   CCDS; CCDS5554.1; -. [Q9NP71-4]
DR   RefSeq; NP_116569.1; NM_032951.2. [Q9NP71-1]
DR   RefSeq; NP_116570.1; NM_032952.2. [Q9NP71-2]
DR   RefSeq; NP_116571.1; NM_032953.2. [Q9NP71-3]
DR   RefSeq; NP_116572.1; NM_032954.2. [Q9NP71-4]
DR   PDB; 6MJL; X-ray; 2.50 A; A=168-176.
DR   PDB; 6YGJ; X-ray; 2.07 A; B/I=117-137.
DR   PDBsum; 6MJL; -.
DR   PDBsum; 6YGJ; -.
DR   AlphaFoldDB; Q9NP71; -.
DR   SMR; Q9NP71; -.
DR   BioGRID; 119275; 21.
DR   IntAct; Q9NP71; 6.
DR   STRING; 9606.ENSP00000320886; -.
DR   iPTMnet; Q9NP71; -.
DR   PhosphoSitePlus; Q9NP71; -.
DR   BioMuta; MLXIPL; -.
DR   DMDM; 20140871; -.
DR   jPOST; Q9NP71; -.
DR   MassIVE; Q9NP71; -.
DR   MaxQB; Q9NP71; -.
DR   PaxDb; Q9NP71; -.
DR   PeptideAtlas; Q9NP71; -.
DR   PRIDE; Q9NP71; -.
DR   ProteomicsDB; 81900; -. [Q9NP71-1]
DR   ProteomicsDB; 81901; -. [Q9NP71-2]
DR   ProteomicsDB; 81902; -. [Q9NP71-3]
DR   ProteomicsDB; 81903; -. [Q9NP71-4]
DR   ProteomicsDB; 81904; -. [Q9NP71-5]
DR   ProteomicsDB; 81905; -. [Q9NP71-6]
DR   Antibodypedia; 14346; 354 antibodies from 30 providers.
DR   DNASU; 51085; -.
DR   Ensembl; ENST00000313375.8; ENSP00000320886.3; ENSG00000009950.16. [Q9NP71-1]
DR   Ensembl; ENST00000345114.9; ENSP00000343767.5; ENSG00000009950.16. [Q9NP71-5]
DR   Ensembl; ENST00000354613.5; ENSP00000346629.1; ENSG00000009950.16. [Q9NP71-4]
DR   Ensembl; ENST00000414749.6; ENSP00000412330.2; ENSG00000009950.16. [Q9NP71-3]
DR   Ensembl; ENST00000429400.6; ENSP00000406296.2; ENSG00000009950.16. [Q9NP71-2]
DR   GeneID; 51085; -.
DR   KEGG; hsa:51085; -.
DR   MANE-Select; ENST00000313375.8; ENSP00000320886.3; NM_032951.3; NP_116569.1.
DR   UCSC; uc003tyk.1; human. [Q9NP71-1]
DR   CTD; 51085; -.
DR   DisGeNET; 51085; -.
DR   GeneCards; MLXIPL; -.
DR   HGNC; HGNC:12744; MLXIPL.
DR   HPA; ENSG00000009950; Tissue enriched (liver).
DR   MalaCards; MLXIPL; -.
DR   MIM; 605678; gene.
DR   neXtProt; NX_Q9NP71; -.
DR   OpenTargets; ENSG00000009950; -.
DR   Orphanet; 904; Williams syndrome.
DR   PharmGKB; PA37353; -.
DR   VEuPathDB; HostDB:ENSG00000009950; -.
DR   eggNOG; KOG3582; Eukaryota.
DR   GeneTree; ENSGT00940000159210; -.
DR   HOGENOM; CLU_007471_1_1_1; -.
DR   InParanoid; Q9NP71; -.
DR   OMA; EYHTSSM; -.
DR   OrthoDB; 388166at2759; -.
DR   PhylomeDB; Q9NP71; -.
DR   TreeFam; TF324749; -.
DR   PathwayCommons; Q9NP71; -.
DR   Reactome; R-HSA-163358; PKA-mediated phosphorylation of key metabolic factors.
DR   Reactome; R-HSA-163680; AMPK inhibits chREBP transcriptional activation activity.
DR   Reactome; R-HSA-163765; ChREBP activates metabolic gene expression.
DR   Reactome; R-HSA-163767; PP2A-mediated dephosphorylation of key metabolic factors.
DR   SignaLink; Q9NP71; -.
DR   SIGNOR; Q9NP71; -.
DR   BioGRID-ORCS; 51085; 10 hits in 1097 CRISPR screens.
DR   ChiTaRS; MLXIPL; human.
DR   GeneWiki; MLXIPL; -.
DR   GenomeRNAi; 51085; -.
DR   Pharos; Q9NP71; Tbio.
DR   PRO; PR:Q9NP71; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9NP71; protein.
DR   Bgee; ENSG00000009950; Expressed in right lobe of liver and 140 other tissues.
DR   ExpressionAtlas; Q9NP71; baseline and differential.
DR   Genevisible; Q9NP71; HS.
DR   GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR   GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR   GO; GO:0005667; C:transcription regulator complex; NAS:UniProtKB.
DR   GO; GO:0035538; F:carbohydrate response element binding; TAS:BHF-UCL.
DR   GO; GO:0003677; F:DNA binding; NAS:BHF-UCL.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; NAS:BHF-UCL.
DR   GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR   GO; GO:0046982; F:protein heterodimerization activity; IPI:BHF-UCL.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR   GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR   GO; GO:0009653; P:anatomical structure morphogenesis; TAS:ProtInc.
DR   GO; GO:0097009; P:energy homeostasis; ISS:UniProtKB.
DR   GO; GO:0055089; P:fatty acid homeostasis; ISS:UniProtKB.
DR   GO; GO:0042593; P:glucose homeostasis; ISS:BHF-UCL.
DR   GO; GO:0010255; P:glucose mediated signaling pathway; ISS:BHF-UCL.
DR   GO; GO:0090324; P:negative regulation of oxidative phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0033137; P:negative regulation of peptidyl-serine phosphorylation; IMP:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:BHF-UCL.
DR   GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; ISS:BHF-UCL.
DR   GO; GO:0045821; P:positive regulation of glycolytic process; IMP:BHF-UCL.
DR   GO; GO:0046889; P:positive regulation of lipid biosynthetic process; IMP:BHF-UCL.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:BHF-UCL.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:BHF-UCL.
DR   GO; GO:0070328; P:triglyceride homeostasis; NAS:BHF-UCL.
DR   Gene3D; 4.10.280.10; -; 1.
DR   InterPro; IPR011598; bHLH_dom.
DR   InterPro; IPR036638; HLH_DNA-bd_sf.
DR   Pfam; PF00010; HLH; 1.
DR   SMART; SM00353; HLH; 1.
DR   SUPFAM; SSF47459; SSF47459; 1.
DR   PROSITE; PS50888; BHLH; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repressor; Transcription; Transcription regulation;
KW   Williams-Beuren syndrome.
FT   CHAIN           1..852
FT                   /note="Carbohydrate-responsive element-binding protein"
FT                   /id="PRO_0000127504"
FT   DOMAIN          649..703
FT                   /note="bHLH"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          54..80
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          328..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          703..724
FT                   /note="Leucine-zipper"
FT   COMPBIAS        347..365
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..505
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        564..589
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         23
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         27
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         29
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         196
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         556
FT                   /note="Phosphoserine; by AMPK"
FT                   /evidence="ECO:0000250|UniProtKB:Q8VIP2"
FT   MOD_RES         602
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163,
FT                   ECO:0007744|PubMed:24275569"
FT   MOD_RES         614
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         631
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         176..268
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002167"
FT   VAR_SEQ         558..575
FT                   /note="QETVPEFPCTFLPPTPAP -> AVNGGCQGTSAPCQALGL (in isoform
FT                   5)"
FT                   /evidence="ECO:0000303|PubMed:11230181"
FT                   /id="VSP_002168"
FT   VAR_SEQ         576..852
FT                   /note="Missing (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:11230181"
FT                   /id="VSP_002169"
FT   VAR_SEQ         647..648
FT                   /note="Missing (in isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11230181,
FT                   ECO:0000303|PubMed:9860302"
FT                   /id="VSP_002170"
FT   VAR_SEQ         687..705
FT                   /note="Missing (in isoform 2 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:11230181,
FT                   ECO:0000303|PubMed:9860302"
FT                   /id="VSP_002171"
FT   VAR_SEQ         814..815
FT                   /note="TV -> ST (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002172"
FT   VAR_SEQ         816..852
FT                   /note="Missing (in isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_002173"
FT   VARIANT         241
FT                   /note="Q -> H (in dbSNP:rs3812316)"
FT                   /id="VAR_049556"
FT   VARIANT         244
FT                   /note="D -> E (in dbSNP:rs34922362)"
FT                   /id="VAR_049557"
FT   CONFLICT        558
FT                   /note="Missing (in Ref. 6; AAH12925)"
FT                   /evidence="ECO:0000305"
FT   HELIX           120..134
FT                   /evidence="ECO:0007829|PDB:6YGJ"
SQ   SEQUENCE   852 AA;  93073 MW;  D49E5C3D7C0A72EC CRC64;
     MAGALAGLAA GLQVPRVAPS PDSDSDTDSE DPSLRRSAGG LLRSQVIHSG HFMVSSPHSD
     SLPRRRDQEG SVGPSDFGPR SIDPTLTRLF ECLSLAYSGK LVSPKWKNFK GLKLLCRDKI
     RLNNAIWRAW YIQYVKRRKS PVCGFVTPLQ GPEADAHRKP EAVVLEGNYW KRRIEVVMRE
     YHKWRIYYKK RLRKPSREDD LLAPKQAEGR WPPPEQWCKQ LFSSVVPVLL GDPEEEPGGR
     QLLDLNCFLS DISDTLFTMT QSGPSPLQLP PEDAYVGNAD MIQPDLTPLQ PSLDDFMDIS
     DFFTNSRLPQ PPMPSNFPEP PSFSPVVDSL FSSGTLGPEV PPASSAMTHL SGHSRLQARN
     SCPGPLDSSA FLSSDFLLPE DPKPRLPPPP VPPPLLHYPP PAKVPGLEPC PPPPFPPMAP
     PTALLQEEPL FSPRFPFPTV PPAPGVSPLP APAAFPPTPQ SVPSPAPTPF PIELLPLGYS
     EPAFGPCFSM PRGKPPAPSP RGQKASPPTL APATASPPTT AGSNNPCLTQ LLTAAKPEQA
     LEPPLVSSTL LRSPGSPQET VPEFPCTFLP PTPAPTPPRP PPGPATLAPS RPLLVPKAER
     LSPPAPSGSE RRLSGDLSSM PGPGTLSVRV SPPQPILSRG RPDSNKTENR RITHISAEQK
     RRFNIKLGFD TLHGLVSTLS AQPSLKVSKA TTLQKTAEYI LMLQQERAGL QEEAQQLRDE
     IEELNAAINL CQQQLPATGV PITHQRFDQM RDMFDDYVRT RTLHNWKFWV FSILIRPLFE
     SFNGMVSTAS VHTLRQTSLA WLDQYCSLPA LRPTVLNSLR QLGTSTSILT DPGRIPEQAT
     RAVTEGTLGK PL
 
 
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