MA651_ARATH
ID MA651_ARATH Reviewed; 587 AA.
AC Q9FLP0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=65-kDa microtubule-associated protein 1;
DE Short=AtMAP65-1;
GN Name=MAP65-1; OrderedLocusNames=At5g55230; ORFNames=MCO15.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH SH3P1.
RX PubMed=11701884; DOI=10.2307/3871590;
RA Lam B.C.-H., Sage T.L., Bianchi F., Blumwald E.;
RT "Role of SH3 domain-containing proteins in clathrin-mediated vesicle
RT trafficking in Arabidopsis.";
RL Plant Cell 13:2499-2512(2001).
RN [6]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12516862; DOI=10.1023/a:1021236307508;
RA Hussey P.J., Hawkins T.J., Igarashi H., Kaloriti D., Smertenko A.;
RT "The plant cytoskeleton: recent advances in the study of the plant
RT microtubule-associated proteins MAP-65, MAP-190 and the Xenopus MAP215-like
RT protein, MOR1.";
RL Plant Mol. Biol. 50:915-924(2002).
RN [7]
RP INTERACTION WITH MICROTUBULES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DIMERIZATION, AND MUTAGENESIS OF ALA-409 AND ALA-420.
RX PubMed=15273298; DOI=10.1105/tpc.104.023937;
RA Smertenko A.P., Chang H.-Y., Wagner V., Kaloriti D., Fenyk S., Sonobe S.,
RA Lloyd C., Hauser M.-T., Hussey P.J.;
RT "The Arabidopsis microtubule-associated protein AtMAP65-1: molecular
RT analysis of its microtubule bundling activity.";
RL Plant Cell 16:2035-2047(2004).
RN [8]
RP INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=15469496; DOI=10.1111/j.1365-313x.2004.02222.x;
RA Van Damme D., Bouget F.-Y., Van Poucke K., Inze D., Geelen D.;
RT "Molecular dissection of plant cytokinesis and phragmoplast structure: a
RT survey of GFP-tagged proteins.";
RL Plant J. 40:386-398(2004).
RN [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=15557096; DOI=10.1104/pp.104.051623;
RA Van Damme D., Van Poucke K., Boutant E., Ritzenthaler C., Inze D.,
RA Geelen D.;
RT "In vivo dynamics and differential microtubule-binding activities of MAP65
RT proteins.";
RL Plant Physiol. 136:3956-3967(2004).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=16014384; DOI=10.1242/jcs.02433;
RA Chang H.-Y., Smertenko A.P., Igarashi H., Dixon D.P., Hussey P.J.;
RT "Dynamic interaction of NtMAP65-1a with microtubules in vivo.";
RL J. Cell Sci. 118:3195-3201(2005).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF SER-503.
RX PubMed=16098102; DOI=10.1111/j.1365-313x.2005.02464.x;
RA Mao G., Chan J., Calder G., Doonan J.H., Lloyd C.W.;
RT "Modulated targeting of GFP-AtMAP65-1 to central spindle microtubules
RT during division.";
RL Plant J. 43:469-478(2005).
RN [12]
RP FUNCTION, AND SUBUNIT.
RX PubMed=15908607; DOI=10.1104/pp.104.052456;
RA Mao T., Jin L., Li H., Liu B., Yuan M.;
RT "Two microtubule-associated proteins of the Arabidopsis MAP65 family
RT function differently on microtubules.";
RL Plant Physiol. 138:654-662(2005).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-503; THR-526;
RP SER-532; SER-540; THR-543; THR-552; SER-573; SER-576 AND SER-586, SUBUNIT,
RP AND MUTAGENESIS OF SER-503; THR-526; SER-532; SER-540; THR-543; THR-552;
RP SER-573; SER-576 AND SER-586.
RX PubMed=16847052; DOI=10.1242/jcs.03051;
RA Smertenko A.P., Chang H.-Y., Sonobe S., Fenyk S.I., Weingartner M.,
RA Boegre L., Hussey P.J.;
RT "Control of the AtMAP65-1 interaction with microtubules through the cell
RT cycle.";
RL J. Cell Sci. 119:3227-3237(2006).
RN [14]
RP FUNCTION, AND INTERACTION WITH TUBULIN ALPHA-SUBUNIT.
RX PubMed=17394772; DOI=10.5483/bmbrep.2007.40.2.218;
RA Li H., Yuan M., Mao T.;
RT "AtMAP65-1 binds to tubulin dimers to promote tubulin assembly.";
RL J. Biochem. Mol. Biol. 40:218-225(2007).
RN [15]
RP SUBUNIT.
RX PubMed=17504815; DOI=10.1093/pcp/pcm059;
RA Li H., Mao T., Zhang Z., Yuan M.;
RT "The AtMAP65-1 cross-bridge between microtubules is formed by one dimer.";
RL Plant Cell Physiol. 48:866-874(2007).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18667529; DOI=10.1091/mbc.e08-04-0341;
RA Gaillard J., Neumann E., Van Damme D., Stoppin-Mellet V., Ebel C.,
RA Barbier E., Geelen D., Vantard M.;
RT "Two microtubule-associated proteins of Arabidopsis MAP65s promote
RT antiparallel microtubule bundling.";
RL Mol. Biol. Cell 19:4534-4544(2008).
RN [17]
RP SUBCELLULAR LOCATION.
RX PubMed=19060108; DOI=10.1105/tpc.108.063362;
RA Smertenko A.P., Kaloriti D., Chang H.-Y., Fiserova J., Opatrny Z.,
RA Hussey P.J.;
RT "The C-terminal variable region specifies the dynamic properties of
RT Arabidopsis microtubule-associated protein MAP65 isotypes.";
RL Plant Cell 20:3346-3358(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-586, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [20]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH MPK4.
RX PubMed=20215588; DOI=10.1105/tpc.109.071746;
RA Beck M., Komis G., Mueller J., Menzel D., Samaj J.;
RT "Arabidopsis homologs of nucleus- and phragmoplast-localized kinase 2 and 3
RT and mitogen-activated protein kinase 4 are essential for microtubule
RT organization.";
RL Plant Cell 22:755-771(2010).
CC -!- FUNCTION: Microtubule-associated protein that bundle and stabilize
CC adjacent microtubules (MT) of the cell cortex. Enhances MT nucleation.
CC Can also bind to tubulin dimers and promotes their polymerization.
CC Confers MT resistance to the drug propyzamide and cold conditions.
CC Plays a role in the central spindle at anaphase to early cytokinesis
CC but is not essential at the midline of the phragmoplast at later
CC stages. Represses metaphase spindle organization and the transition to
CC anaphase in dephosphorylated active form. Promotes the formation of a
CC planar network of antiparallel microtubules. May be involved in
CC stomatal movement modulation by regulating the dynamic and arrangement
CC of cortical MT. {ECO:0000269|PubMed:15557096,
CC ECO:0000269|PubMed:15908607, ECO:0000269|PubMed:16014384,
CC ECO:0000269|PubMed:16098102, ECO:0000269|PubMed:16847052,
CC ECO:0000269|PubMed:17394772, ECO:0000269|PubMed:18667529,
CC ECO:0000269|PubMed:20215588}.
CC -!- SUBUNIT: Forms dimer. Binds to MT, mostly with coaligned MT, both
CC between parallel or antiparallel, forming thick bundles. Interacts with
CC the alpha-tubulin subunit of the tubulin heterodimer. Bundles
CC polymerized MT via the formation of 25-nm crossbridges at specific
CC stages of the cell cycle (e.g. bundles microtubules in interphase,
CC anaphase and telophase but does not bind microtubules in prophase or
CC metaphase), at the plus-end, the minus-end, or along the entire length
CC of MT, and along phragmoplast MT. Interacts with SH3P1 and MPK4.
CC {ECO:0000269|PubMed:11701884, ECO:0000269|PubMed:15273298,
CC ECO:0000269|PubMed:15469496, ECO:0000269|PubMed:15557096,
CC ECO:0000269|PubMed:15908607, ECO:0000269|PubMed:16014384,
CC ECO:0000269|PubMed:16098102, ECO:0000269|PubMed:16847052,
CC ECO:0000269|PubMed:17394772, ECO:0000269|PubMed:17504815,
CC ECO:0000269|PubMed:18667529, ECO:0000269|PubMed:20215588}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, cytoskeleton,
CC spindle. Cytoplasm, cytoskeleton, phragmoplast. Cytoplasm, cell cortex.
CC Note=During interphase, binds cortical microtubules. In M-phase,
CC locates to the preprophase band. Binds the preprophase band but does
CC not accumulate at the prophase spindle microtubules that coexists
CC within the same cell. In the metaphase and anaphase, localized to
CC spindle. In the phragmoplast, concentrated at the midzone where
CC vesicles guide by MT coalesce to form the cell plate. Present in MT
CC cortical arrays. Concentrated in dots surrounding the nuclei.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FLP0-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in all organs and tissues with the
CC exception of sepals and anthers. Bound to subsets of microtubules in
CC the cells of root epidermis, hypocotyl and cotyledons (at protein
CC level). {ECO:0000269|PubMed:15273298}.
CC -!- INDUCTION: Expressed throughout the cell cycle.
CC {ECO:0000269|PubMed:15557096}.
CC -!- PTM: Basal phosphorylation at all stages of the cell cycle. MT-binding
CC properties inhibited by hyperphosphorylation mediated by CDKs and/or
CC MAPKs (e.g. ANP2, ANP3, MPK4 and MPK6) during prometaphase and
CC metaphase. {ECO:0000269|PubMed:16847052, ECO:0000269|PubMed:20215588}.
CC -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
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DR EMBL; AB010071; BAB08592.1; -; Genomic_DNA.
DR EMBL; CP002688; AED96602.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70602.1; -; Genomic_DNA.
DR EMBL; BT004641; AAO42887.1; -; mRNA.
DR EMBL; AK227916; BAE99886.1; -; mRNA.
DR RefSeq; NP_001332196.1; NM_001345120.1. [Q9FLP0-1]
DR RefSeq; NP_200334.1; NM_124905.5. [Q9FLP0-1]
DR AlphaFoldDB; Q9FLP0; -.
DR SMR; Q9FLP0; -.
DR STRING; 3702.AT5G55230.2; -.
DR iPTMnet; Q9FLP0; -.
DR PaxDb; Q9FLP0; -.
DR PRIDE; Q9FLP0; -.
DR ProteomicsDB; 238839; -. [Q9FLP0-1]
DR EnsemblPlants; AT5G55230.1; AT5G55230.1; AT5G55230. [Q9FLP0-1]
DR EnsemblPlants; AT5G55230.3; AT5G55230.3; AT5G55230. [Q9FLP0-1]
DR GeneID; 835616; -.
DR Gramene; AT5G55230.1; AT5G55230.1; AT5G55230. [Q9FLP0-1]
DR Gramene; AT5G55230.3; AT5G55230.3; AT5G55230. [Q9FLP0-1]
DR KEGG; ath:AT5G55230; -.
DR Araport; AT5G55230; -.
DR eggNOG; KOG4302; Eukaryota.
DR InParanoid; Q9FLP0; -.
DR OMA; IHVLWDR; -.
DR PhylomeDB; Q9FLP0; -.
DR PRO; PR:Q9FLP0; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FLP0; baseline and differential.
DR Genevisible; Q9FLP0; AT.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0009524; C:phragmoplast; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IBA:GO_Central.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0046983; F:protein dimerization activity; IPI:UniProtKB.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:UniProtKB.
DR GO; GO:0000911; P:cytokinesis by cell plate formation; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR InterPro; IPR007145; MAP65_Ase1_PRC1.
DR PANTHER; PTHR19321; PTHR19321; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Coiled coil; Cytoplasm;
KW Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..587
FT /note="65-kDa microtubule-associated protein 1"
FT /id="PRO_0000395472"
FT REGION 474..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 46..84
FT /evidence="ECO:0000255"
FT COILED 151..181
FT /evidence="ECO:0000255"
FT COILED 234..257
FT /evidence="ECO:0000255"
FT COILED 290..317
FT /evidence="ECO:0000255"
FT COILED 461..489
FT /evidence="ECO:0000255"
FT COMPBIAS 474..491
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 519..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 409
FT /note="Microtubule binding"
FT SITE 420
FT /note="Microtubule binding"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16847052"
FT MOD_RES 526
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16847052"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16847052"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16847052"
FT MOD_RES 543
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16847052"
FT MOD_RES 552
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16847052"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16847052"
FT MOD_RES 576
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16847052"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16847052,
FT ECO:0007744|PubMed:19245862, ECO:0007744|PubMed:19376835"
FT MUTAGEN 409
FT /note="A->D: Impaired microtubule binding."
FT /evidence="ECO:0000269|PubMed:15273298"
FT MUTAGEN 420
FT /note="A->V: Impaired microtubule binding."
FT /evidence="ECO:0000269|PubMed:15273298"
FT MUTAGEN 503
FT /note="S->A: Premature binding to microtubules traversing
FT the central region of the metaphase spindle. Impaired
FT microtubule binding and abnormal subcellular localization
FT (e.g. reduced localization in spindle midzone during
FT anaphase) leading to disturbed mitosis; when associated
FT with A-526, A-532, A-540, A-543, A-552, A-573, A-576 and A-
FT 586."
FT /evidence="ECO:0000269|PubMed:16098102,
FT ECO:0000269|PubMed:16847052"
FT MUTAGEN 526
FT /note="T->A: Impaired microtubule binding and abnormal
FT subcellular localization (e.g. reduced localization in
FT spindle midzone during anaphase) leading to disturbed
FT mitosis; when associated with A-503; A-532; A-540; A-543;
FT A-552; A-573; A-576 and A-586."
FT /evidence="ECO:0000269|PubMed:16847052"
FT MUTAGEN 532
FT /note="S->A: Impaired microtubule bindingImpaired
FT microtubule binding and abnormal subcellular localization
FT (e.g. reduced localization in spindle midzone during
FT anaphase) leading to disturbed mitosis; when associated
FT with A-503; A-526; A-540; A-543; A-552; A-573; A-576 and A-
FT 586."
FT /evidence="ECO:0000269|PubMed:16847052"
FT MUTAGEN 540
FT /note="S->A: Impaired microtubule binding and abnormal
FT subcellular localization (e.g. reduced localization in
FT spindle midzone during anaphase) leading to disturbed
FT mitosis; when associated with A-503; A-526; A-532; A-543;
FT A-552; A-573; A-576 and A-586."
FT /evidence="ECO:0000269|PubMed:16847052"
FT MUTAGEN 543
FT /note="T->A: Impaired microtubule binding and abnormal
FT subcellular localization (e.g. reduced localization in
FT spindle midzone during anaphase) leading to disturbed
FT mitosis; when associated with A-503; A-526; A-532; A-540;
FT A-552; A-573; A-576 and A-586."
FT /evidence="ECO:0000269|PubMed:16847052"
FT MUTAGEN 552
FT /note="T->A: Impaired microtubule binding and abnormal
FT subcellular localization (e.g. reduced localization in
FT spindle midzone during anaphase); when associated with A-
FT 503, A- leading to disturbed mitosis, A-532; A-540; A-543;
FT A-573; A-576 and A-586."
FT /evidence="ECO:0000269|PubMed:16847052"
FT MUTAGEN 573
FT /note="S->A: Impaired microtubule binding and abnormal
FT subcellular localization (e.g. reduced localization in
FT spindle midzone during anaphase) leading to disturbed
FT mitosis; when associated with A-503; A-526; A-532; A-540;
FT A-543; A-552; A-576 and A-586."
FT /evidence="ECO:0000269|PubMed:16847052"
FT MUTAGEN 576
FT /note="S->A: Impaired microtubule binding and abnormal
FT subcellular localization (e.g. reduced localization in
FT spindle midzone during anaphase) leading to disturbed
FT mitosis; when associated with A-503; A-526; A-532; A-540;
FT A-543; A-552; A-573 and A-586."
FT /evidence="ECO:0000269|PubMed:16847052"
FT MUTAGEN 586
FT /note="S->A: Impaired microtubule binding and abnormal
FT subcellular localization (e.g. reduced localization in
FT spindle midzone during anaphase) leading to disturbed
FT mitosis; when associated with A-503; A-526; A-532; A-540;
FT A-543; A-552; A-573 and A-576."
FT /evidence="ECO:0000269|PubMed:16847052"
SQ SEQUENCE 587 AA; 65785 MW; E816218DF69558F6 CRC64;
MAVTDTESPH LGEITCGTLL EKLQEIWDEV GESDDERDKL LLQIEQECLD VYKRKVEQAA
KSRAELLQTL SDANAELSSL TMSLGDKSLV GIPDKSSGTI KEQLAAIAPA LEQLWQQKEE
RVREFSDVQS QIQKICGDIA GGLSNEVPIV DESDLSLKKL DDFQSQLQEL QKEKSDRLRK
VLEFVSTVHD LCAVLGLDFL STVTEVHPSL DEDTSVQSKS ISNETLSRLA KTVLTLKDDK
KQRLQKLQEL ATQLIDLWNL MDTPDEEREL FDHVTCNISS SVDEVTVPGA LARDLIEQAE
VEVDRLDQLK ASRMKEIAFK KQSELEEIYA RAHVEVNPES ARERIMSLID SGNVEPTELL
ADMDSQISKA KEEAFSRKDI LDRVEKWMSA CEEESWLEDY NRDQNRYSAS RGAHLNLKRA
EKARILVSKI PAMVDTLVAK TRAWEEEHSM SFAYDGVPLL AMLDEYGMLR QEREEEKRRL
REQKKVQEQP HVEQESAFST RPSPARPVSA KKTVGPRANN GGANGTHNRR LSLNANQNGS
RSTAKEAGRR ETLNRPAAPT NYVAISKEEA ASSPVSGAAD HQVPASP
