位置:首页 > 蛋白库 > EMAL1_HUMAN
EMAL1_HUMAN
ID   EMAL1_HUMAN             Reviewed;         815 AA.
AC   O00423; Q86U15; Q8N536; Q8N5C4; Q8WWL6;
DT   18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 3.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Echinoderm microtubule-associated protein-like 1;
DE            Short=EMAP-1;
DE            Short=HuEMAP-1;
GN   Name=EML1; Synonyms=EMAP1, EMAPL, EMAPL1;
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 [MRNA] (ISOFORM 1), AND VARIANT PRO-556.
RX   PubMed=9226380; DOI=10.1006/geno.1997.4779;
RA   Eudy J.D., Ma-Edmonds M., Yao S.F., Talmadge C.B., Kelley P.M.,
RA   Weston M.D., Kimberling W.J., Sumegi J.;
RT   "Isolation of a novel human homologue of the gene coding for echinoderm
RT   microtubule-associated protein (EMAP) from the Usher syndrome type 1a locus
RT   at 14q32.";
RL   Genomics 43:104-106(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-556.
RA   Gerber S., Sumegi J., Rozet J.-M., Perrault I., Ducroq D., Munnich A.,
RA   Kaplan J.;
RT   "Complete exon-intron structure of human homologue of the gene coding the
RT   echinoderm microtubule-associated protein (EMAP).";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-552
RP   AND PRO-556.
RC   TISSUE=Brain, and Uterus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-500 (ISOFORM 3).
RC   TISSUE=Fetal brain;
RA   Li W.B., Gruber C., Jessee J., Polayes D.;
RT   "Full-length cDNA libraries and normalization.";
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   TISSUE SPECIFICITY.
RX   PubMed=10521658; DOI=10.1016/s0378-1119(99)00335-2;
RA   Lepley D.M., Palange J.M., Suprenant K.A.;
RT   "Sequence and expression patterns of a human EMAP-related protein-2
RT   (HuEMAP-2).";
RL   Gene 237:343-349(1999).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP   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   [7]
RP   SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 59-LEU--ASP-61.
RX   PubMed=25740311; DOI=10.1042/bj20150039;
RA   Richards M.W., O'Regan L., Roth D., Montgomery J.M., Straube A., Fry A.M.,
RA   Bayliss R.;
RT   "Microtubule association of EML proteins and the EML4-ALK variant 3
RT   oncoprotein require an N-terminal trimerization domain.";
RL   Biochem. J. 467:529-536(2015).
RN   [8]
RP   INVOLVEMENT IN BH, VARIANTS BH ARG-225 AND ALA-243, CHARACTERIZATION OF
RP   VARIANT BH ALA-243, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=24859200; DOI=10.1038/nn.3729;
RA   Kielar M., Tuy F.P., Bizzotto S., Lebrand C., de Juan Romero C.,
RA   Poirier K., Oegema R., Mancini G.M., Bahi-Buisson N., Olaso R.,
RA   Le Moing A.G., Boutourlinsky K., Boucher D., Carpentier W., Berquin P.,
RA   Deleuze J.F., Belvindrah R., Borrell V., Welker E., Chelly J.,
RA   Croquelois A., Francis F.;
RT   "Mutations in Eml1 lead to ectopic progenitors and neuronal heterotopia in
RT   mouse and human.";
RL   Nat. Neurosci. 17:923-933(2014).
RN   [9]
RP   INVOLVEMENT IN BH, AND VARIANT BH 523-ARG--ILE-815 DEL.
RX   PubMed=28556411; DOI=10.1002/ana.24964;
RA   Shaheen R., Sebai M.A., Patel N., Ewida N., Kurdi W., Altweijri I.,
RA   Sogaty S., Almardawi E., Seidahmed M.Z., Alnemri A., Madirevula S.,
RA   Ibrahim N., Abdulwahab F., Hashem M., Al-Sheddi T., Alomar R., Alobeid E.,
RA   Sallout B., AlBaqawi B., AlAali W., Ajaji N., Lesmana H., Hopkin R.J.,
RA   Dupuis L., Mendoza-Londono R., Al Rukban H., Yoon G., Faqeih E.,
RA   Alkuraya F.S.;
RT   "The genetic landscape of familial congenital hydrocephalus.";
RL   Ann. Neurol. 81:890-897(2017).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 167-815, DOMAIN, INTERACTION WITH
RP   TUBULIN, AND MUTAGENESIS OF 59-LEU--ASP-61; ARG-192; ARG-194; TRP-547;
RP   ASN-626; GLU-627; HIS-646 AND HIS-786.
RX   PubMed=24706829; DOI=10.1073/pnas.1322892111;
RA   Richards M.W., Law E.W., Rennalls L.P., Busacca S., O'Regan L., Fry A.M.,
RA   Fennell D.A., Bayliss R.;
RT   "Crystal structure of EML1 reveals the basis for Hsp90 dependence of
RT   oncogenic EML4-ALK by disruption of an atypical beta-propeller domain.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:5195-5200(2014).
CC   -!- FUNCTION: Modulates the assembly and organization of the microtubule
CC       cytoskeleton, and probably plays a role in regulating the orientation
CC       of the mitotic spindle and the orientation of the plane of cell
CC       division. Required for normal proliferation of neuronal progenitor
CC       cells in the developing brain and for normal brain development. Does
CC       not affect neuron migration per se. {ECO:0000250|UniProtKB:Q05BC3}.
CC   -!- SUBUNIT: Homotrimer; self-association is mediated by the N-terminal
CC       coiled coil (By similarity). Does not interact with EML3
CC       (PubMed:25740311). Binds repolymerizing microtubules (PubMed:24859200).
CC       Binds unpolymerized tubulins via its WD repeat region
CC       (PubMed:24706829). Interacts with TASOR (By similarity).
CC       {ECO:0000250|UniProtKB:Q05BC3, ECO:0000250|UniProtKB:Q9HC35,
CC       ECO:0000269|PubMed:24706829, ECO:0000269|PubMed:24859200,
CC       ECO:0000269|PubMed:25740311}.
CC   -!- INTERACTION:
CC       O00423; P55212: CASP6; NbExp=3; IntAct=EBI-751327, EBI-718729;
CC       O00423; P51114: FXR1; NbExp=2; IntAct=EBI-751327, EBI-713291;
CC       O00423; Q9H9L3: ISG20L2; NbExp=3; IntAct=EBI-751327, EBI-751335;
CC       O00423; P13473-2: LAMP2; NbExp=3; IntAct=EBI-751327, EBI-21591415;
CC       O00423; P31948: STIP1; NbExp=3; IntAct=EBI-751327, EBI-1054052;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}.
CC       Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}.
CC       Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200,
CC       ECO:0000269|PubMed:25740311}. Note=Detected in cytoplasmic punctae. Co-
CC       localizes with microtubules (PubMed:24859200, PubMed:25740311).
CC       Enriched in perinuclear regions during interphase and in the region of
CC       spindle microtubules during metaphase. Enriched at the midzone during
CC       telophase and cytokinesis. Detected at growth cones in neurons (By
CC       similarity). {ECO:0000250|UniProtKB:Q05BC3,
CC       ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O00423-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=O00423-3; Sequence=VSP_024476;
CC   -!- TISSUE SPECIFICITY: Ubiquitous; expressed in most tissues with the
CC       exception of thymus and peripheral blood lymphocytes.
CC       {ECO:0000269|PubMed:10521658}.
CC   -!- DOMAIN: Contains a tandem atypical propeller in EMLs (TAPE) domain. The
CC       N-terminal beta-propeller is formed by canonical WD repeats; in
CC       contrast, the second beta-propeller contains one blade that is formed
CC       by discontinuous parts of the polypeptide chain.
CC       {ECO:0000269|PubMed:24706829}.
CC   -!- DOMAIN: The N-terminal coiled coil is required for association with
CC       microtubules. {ECO:0000269|PubMed:25740311}.
CC   -!- DISEASE: Band heterotopia (BH) [MIM:600348]: A brain malformation of
CC       the lissencephaly spectrum, resulting from disordered neuronal
CC       migration and characterized by bands of gray matter interposed in the
CC       central white matter. Disease features include severe developmental
CC       delay with intellectual disability, enlarged head circumference,
CC       periventricular and ribbon-like subcortical heterotopia, polymicrogyria
CC       and agenesis of the corpus callosum. {ECO:0000269|PubMed:24859200,
CC       ECO:0000269|PubMed:28556411}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB57824.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAD62313.1; Type=Erroneous initiation; Note=Extended 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; U97018; AAB57824.1; ALT_FRAME; mRNA.
DR   EMBL; AJ420603; CAD12600.2; -; Genomic_DNA.
DR   EMBL; AJ428183; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428184; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428185; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428189; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428191; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428193; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428195; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428197; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ496645; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ496644; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428200; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428199; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428198; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428196; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428194; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428192; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428190; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428188; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428187; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; AJ428186; CAD12600.2; JOINED; Genomic_DNA.
DR   EMBL; BC032541; AAH32541.1; -; mRNA.
DR   EMBL; BC033043; AAH33043.1; -; mRNA.
DR   EMBL; BX247979; CAD62313.1; ALT_INIT; mRNA.
DR   CCDS; CCDS32154.1; -. [O00423-3]
DR   CCDS; CCDS32155.1; -. [O00423-1]
DR   RefSeq; NP_001008707.1; NM_001008707.1. [O00423-3]
DR   RefSeq; NP_004425.2; NM_004434.2. [O00423-1]
DR   PDB; 4CI8; X-ray; 2.60 A; A/B=167-815.
DR   PDBsum; 4CI8; -.
DR   AlphaFoldDB; O00423; -.
DR   SMR; O00423; -.
DR   BioGRID; 108324; 28.
DR   IntAct; O00423; 16.
DR   MINT; O00423; -.
DR   STRING; 9606.ENSP00000334314; -.
DR   iPTMnet; O00423; -.
DR   PhosphoSitePlus; O00423; -.
DR   BioMuta; EML1; -.
DR   CPTAC; CPTAC-1606; -.
DR   EPD; O00423; -.
DR   jPOST; O00423; -.
DR   MassIVE; O00423; -.
DR   MaxQB; O00423; -.
DR   PaxDb; O00423; -.
DR   PeptideAtlas; O00423; -.
DR   PRIDE; O00423; -.
DR   ProteomicsDB; 47880; -. [O00423-1]
DR   ProteomicsDB; 47881; -. [O00423-3]
DR   Antibodypedia; 27460; 87 antibodies from 25 providers.
DR   DNASU; 2009; -.
DR   Ensembl; ENST00000262233.11; ENSP00000262233.7; ENSG00000066629.18. [O00423-1]
DR   Ensembl; ENST00000334192.8; ENSP00000334314.4; ENSG00000066629.18. [O00423-3]
DR   GeneID; 2009; -.
DR   KEGG; hsa:2009; -.
DR   MANE-Select; ENST00000262233.11; ENSP00000262233.7; NM_004434.3; NP_004425.2.
DR   UCSC; uc001ygr.4; human. [O00423-1]
DR   CTD; 2009; -.
DR   DisGeNET; 2009; -.
DR   GeneCards; EML1; -.
DR   HGNC; HGNC:3330; EML1.
DR   HPA; ENSG00000066629; Low tissue specificity.
DR   MalaCards; EML1; -.
DR   MIM; 600348; phenotype.
DR   MIM; 602033; gene.
DR   neXtProt; NX_O00423; -.
DR   OpenTargets; ENSG00000066629; -.
DR   Orphanet; 99796; Subcortical band heterotopia.
DR   PharmGKB; PA27767; -.
DR   VEuPathDB; HostDB:ENSG00000066629; -.
DR   eggNOG; KOG2106; Eukaryota.
DR   GeneTree; ENSGT00940000153887; -.
DR   InParanoid; O00423; -.
DR   OMA; TTRDIQW; -.
DR   OrthoDB; 271572at2759; -.
DR   PhylomeDB; O00423; -.
DR   TreeFam; TF317832; -.
DR   PathwayCommons; O00423; -.
DR   SignaLink; O00423; -.
DR   BioGRID-ORCS; 2009; 8 hits in 1065 CRISPR screens.
DR   ChiTaRS; EML1; human.
DR   GeneWiki; EML1; -.
DR   GenomeRNAi; 2009; -.
DR   Pharos; O00423; Tbio.
DR   PRO; PR:O00423; -.
DR   Proteomes; UP000005640; Chromosome 14.
DR   RNAct; O00423; protein.
DR   Bgee; ENSG00000066629; Expressed in cortical plate and 193 other tissues.
DR   ExpressionAtlas; O00423; baseline and differential.
DR   Genevisible; O00423; HS.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR   GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR   GO; GO:1990023; C:mitotic spindle midzone; IEA:Ensembl.
DR   GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR   GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR   GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR   GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR   GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR   GO; GO:0007405; P:neuroblast proliferation; ISS:UniProtKB.
DR   Gene3D; 2.130.10.10; -; 2.
DR   InterPro; IPR005108; HELP.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   Pfam; PF03451; HELP; 1.
DR   Pfam; PF00400; WD40; 4.
DR   SMART; SM00320; WD40; 10.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 3.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Disease variant; Epilepsy; Intellectual disability; Lissencephaly;
KW   Microtubule; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..815
FT                   /note="Echinoderm microtubule-associated protein-like 1"
FT                   /id="PRO_0000050961"
FT   REPEAT          261..310
FT                   /note="WD 1"
FT   REPEAT          315..358
FT                   /note="WD 2"
FT   REPEAT          363..400
FT                   /note="WD 3"
FT   REPEAT          409..446
FT                   /note="WD 4"
FT   REPEAT          450..489
FT                   /note="WD 5"
FT   REPEAT          493..530
FT                   /note="WD 6"
FT   REPEAT          535..572
FT                   /note="WD 7"
FT   REPEAT          578..613
FT                   /note="WD 8"
FT   REPEAT          617..655
FT                   /note="WD 9"
FT   REPEAT          664..701
FT                   /note="WD 10"
FT   REPEAT          709..768
FT                   /note="WD 11"
FT   REPEAT          775..814
FT                   /note="WD 12"
FT   REGION          77..179
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          176..815
FT                   /note="Tandem atypical propeller in EMLs"
FT   COILED          31..72
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        89..108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        153..169
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         127
FT                   /note="K -> KRLNRSVSLLNACKLNRSTP (in isoform 3)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_024476"
FT   VARIANT         225
FT                   /note="W -> R (in BH; dbSNP:rs886037937)"
FT                   /evidence="ECO:0000269|PubMed:24859200"
FT                   /id="VAR_071075"
FT   VARIANT         243
FT                   /note="T -> A (in BH; decreased microtubule-binding;
FT                   dbSNP:rs886037936)"
FT                   /evidence="ECO:0000269|PubMed:24859200"
FT                   /id="VAR_071076"
FT   VARIANT         377
FT                   /note="A -> V (in dbSNP:rs34198557)"
FT                   /id="VAR_031720"
FT   VARIANT         523..815
FT                   /note="Missing (in BH)"
FT                   /evidence="ECO:0000269|PubMed:28556411"
FT                   /id="VAR_081119"
FT   VARIANT         552
FT                   /note="H -> N (in dbSNP:rs17853154)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_031721"
FT   VARIANT         556
FT                   /note="S -> P (in dbSNP:rs2250718)"
FT                   /evidence="ECO:0000269|PubMed:15489334,
FT                   ECO:0000269|PubMed:9226380, ECO:0000269|Ref.2"
FT                   /id="VAR_031722"
FT   MUTAGEN         59..61
FT                   /note="LAD->AAA: No effect on tubulin binding. Does not
FT                   disrupt self-association. Decreased association with
FT                   microtubules."
FT                   /evidence="ECO:0000269|PubMed:24706829,
FT                   ECO:0000269|PubMed:25740311"
FT   MUTAGEN         192
FT                   /note="R->S: Abolishes tubulin binding; when associated
FT                   with S-194; A-547; T-626; S-627; A-646 and A-786."
FT                   /evidence="ECO:0000269|PubMed:24706829"
FT   MUTAGEN         194
FT                   /note="R->S: Abolishes tubulin binding; when associated
FT                   with S-192; A-547; T-626; S-627; A-646 and A-786."
FT                   /evidence="ECO:0000269|PubMed:24706829"
FT   MUTAGEN         547
FT                   /note="W->A: Abolishes tubulin binding; when associated
FT                   with S-192; S-194; T-626; S-627; A-646 and A-786."
FT                   /evidence="ECO:0000269|PubMed:24706829"
FT   MUTAGEN         626
FT                   /note="N->T: Abolishes tubulin binding; when associated
FT                   with S-192; S-194; A-547; S-627; A-646 and A-786."
FT                   /evidence="ECO:0000269|PubMed:24706829"
FT   MUTAGEN         627
FT                   /note="E->S: Abolishes tubulin binding; when associated
FT                   with S-192; S-194; A-547; T-626; A-646 and A-786."
FT                   /evidence="ECO:0000269|PubMed:24706829"
FT   MUTAGEN         646
FT                   /note="H->A: Abolishes tubulin binding; when associated
FT                   with S-192; S-194; A-547; T-626; S-627 and A-786."
FT                   /evidence="ECO:0000269|PubMed:24706829"
FT   MUTAGEN         786
FT                   /note="H->A: Abolishes tubulin binding; when associated
FT                   with S-192; S-194; A-547; T-626; S-627 and A-646."
FT                   /evidence="ECO:0000269|PubMed:24706829"
FT   CONFLICT        93..95
FT                   /note="LRT -> FRS (in Ref. 1; AAB57824)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        106
FT                   /note="K -> I (in Ref. 1; AAB57824)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        117
FT                   /note="V -> F (in Ref. 1; AAB57824)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        120
FT                   /note="E -> D (in Ref. 1; AAB57824)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        189
FT                   /note="M -> L (in Ref. 1; AAB57824)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        464..465
FT                   /note="FA -> SP (in Ref. 1; AAB57824 and 2; CAD12600)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        499..500
FT                   /note="IP -> VS (in Ref. 4; CAD62313)"
FT                   /evidence="ECO:0000305"
FT   STRAND          179..181
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            182..185
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          186..199
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   HELIX           202..205
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          220..227
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          238..240
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          253..258
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            259..262
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          263..267
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          274..279
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          283..291
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          305..309
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            310..312
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          315..319
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            321..323
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          326..333
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          335..339
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          342..346
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          348..350
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          352..357
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   HELIX           358..360
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          362..368
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          374..379
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          386..392
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          394..401
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          404..409
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          419..426
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          432..436
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          441..444
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          449..455
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          458..461
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          463..468
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          474..478
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            479..481
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          483..487
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          493..498
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            501..503
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          505..511
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          517..521
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          526..529
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          536..539
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          546..551
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          553..562
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          565..571
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            572..575
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          576..582
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          587..592
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          596..612
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            613..615
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          618..623
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          625..627
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          629..634
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          638..645
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          650..656
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            657..660
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          661..668
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          675..681
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          687..691
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          697..700
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   HELIX           701..703
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   HELIX           710..713
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          724..726
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   TURN            727..731
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          741..747
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          749..758
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          763..768
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          772..774
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          778..780
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          789..792
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          796..802
FT                   /evidence="ECO:0007829|PDB:4CI8"
FT   STRAND          809..815
FT                   /evidence="ECO:0007829|PDB:4CI8"
SQ   SEQUENCE   815 AA;  89861 MW;  A1476F75F3537205 CRC64;
     MEDGFSSYSS LYDTSSLLQF CNDDSASAAS SMEVTDRIAS LEQRVQMQED DIQLLKSALA
     DVVRRLNITE EQQAVLNRKG PTKARPLMQT LPLRTTVNNG TVLPKKPTGS LPSPSGVRKE
     TAVPATKSNI KRTSSSERVS PGGRRESNGD SRGNRNRTGS TSSSSSGKKN SESKPKEPVF
     SAEEGYVKMF LRGRPVTMYM PKDQVDSYSL EAKVELPTKR LKLEWVYGYR GRDCRNNLYL
     LPTGETVYFI ASVVVLYNVE EQLQRHYAGH NDDVKCLAVH PDRITIATGQ VAGTSKDGKQ
     LPPHVRIWDS VTLNTLHVIG IGFFDRAVTC IAFSKSNGGT NLCAVDDSND HVLSVWDWQK
     EEKLADVKCS NEAVFAADFH PTDTNIIVTC GKSHLYFWTL EGSSLNKKQG LFEKQEKPKF
     VLCVTFSENG DTITGDSSGN ILVWGKGTNR ISYAVQGAHE GGIFALCMLR DGTLVSGGGK
     DRKLISWSGN YQKLRKTEIP EQFGPIRTVA EGKGDVILIG TTRNFVLQGT LSGDFTPITQ
     GHTDELWGLA IHASKSQFLT CGHDKHATLW DAVGHRPVWD KIIEDPAQSS GFHPSGSVVA
     VGTLTGRWFV FDTETKDLVT VHTDGNEQLS VMRYSPDGNF LAIGSHDNCI YIYGVSDNGR
     KYTRVGKCSG HSSFITHLDW SVNSQFLVSN SGDYEILYWV PSACKQVVSV ETTRDIEWAT
     YTCTLGFHVF GVWPEGSDGT DINAVCRAHE KKLLSTGDDF GKVHLFSYPC SQFRAPSHIY
     GGHSSHVTNV DFLCEDSHLI STGGKDTSIM QWRVI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024