(data stored in SCRATCH zone)

SWISSPROT: MA652_ARATH

ID   MA652_ARATH             Reviewed;         578 AA.
AC   Q8LEG3; Q9SZ16;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   11-DEC-2019, entry version 93.
DE   RecName: Full=65-kDa microtubule-associated protein 2;
DE            Short=AtMAP65-2;
GN   Name=MAP65-2; OrderedLocusNames=At4g26760; ORFNames=F10M23.100;
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=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
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;
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Wu S.Y., De Los Reyes C., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
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   [7]
RP   FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=19002591; DOI=10.1007/s11103-008-9426-1;
RA   Li H., Zeng X., Liu Z.-Q., Meng Q.-T., Yuan M., Mao T.-L.;
RT   "Arabidopsis microtubule-associated protein AtMAP65-2 acts as a microtubule
RT   stabilizer.";
RL   Plant Mol. Biol. 69:313-324(2009).
CC   -!- FUNCTION: Microtubule-associated protein that stabilize microtubules
CC       (MT). Involved in the regulation of MT organization and dynamics.
CC       Confers MT resistance to the drug propyzamide and cold conditions.
CC       {ECO:0000269|PubMed:19002591}.
CC   -!- SUBUNIT: Forms a dimer (By similarity). Binds to microtubules (MT).
CC       Bundles polymerized MT via the formation of 25-nm crossbridges with
CC       centrally located endocytic MT. {ECO:0000250,
CC       ECO:0000269|PubMed:19002591}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Cytoplasm. Cytoplasm,
CC       cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, phragmoplast.
CC       Note=During interphase, binds cortical microtubules. In M-phase,
CC       locates to the preprophase band. Decorates entire mitotic spindle
CC       during cell division. During the anaphase to telophase transition,
CC       accumulates in the midline where oppositely oriented phragmoplast MTs
CC       overlap. In the phragmoplast, colocalizes completely with the MTs.
CC   -!- SIMILARITY: Belongs to the MAP65/ASE1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB36522.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79531.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AL035440; CAB36522.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161565; CAB79531.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85249.1; -; Genomic_DNA.
DR   EMBL; AY085430; AAM62657.1; -; mRNA.
DR   EMBL; BT030366; ABO38779.1; -; mRNA.
DR   PIR; T04799; T04799.
DR   RefSeq; NP_567756.1; NM_118810.4.
DR   SMR; Q8LEG3; -.
DR   BioGrid; 14070; 1.
DR   STRING; 3702.AT4G26760.1; -.
DR   iPTMnet; Q8LEG3; -.
DR   PaxDb; Q8LEG3; -.
DR   PRIDE; Q8LEG3; -.
DR   EnsemblPlants; AT4G26760.1; AT4G26760.1; AT4G26760.
DR   GeneID; 828783; -.
DR   Gramene; AT4G26760.1; AT4G26760.1; AT4G26760.
DR   KEGG; ath:AT4G26760; -.
DR   Araport; AT4G26760; -.
DR   TAIR; locus:2116267; AT4G26760.
DR   eggNOG; KOG4302; Eukaryota.
DR   eggNOG; ENOG410YZBK; LUCA.
DR   HOGENOM; HOG000238749; -.
DR   InParanoid; Q8LEG3; -.
DR   KO; K16732; -.
DR   OMA; CYISASV; -.
DR   OrthoDB; 272248at2759; -.
DR   PhylomeDB; Q8LEG3; -.
DR   PRO; PR:Q8LEG3; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8LEG3; baseline and differential.
DR   Genevisible; Q8LEG3; AT.
DR   GO; GO:0055028; C:cortical microtubule; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005874; C:microtubule; IDA:TAIR.
DR   GO; GO:0072686; C:mitotic spindle; IDA:TAIR.
DR   GO; GO:1990023; C:mitotic spindle midzone; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0009524; C:phragmoplast; IDA:TAIR.
DR   GO; GO:0009574; C:preprophase band; IDA:TAIR.
DR   GO; GO:0005819; C:spindle; IDA:TAIR.
DR   GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR   GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IGI:TAIR.
DR   GO; GO:0000911; P:cytokinesis by cell plate formation; IGI:TAIR.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IEA:InterPro.
DR   GO; GO:0048528; P:post-embryonic root development; IGI:TAIR.
DR   InterPro; IPR007145; MAP65_Ase1_PRC1.
DR   PANTHER; PTHR19321; PTHR19321; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8LEG3.
DR   SWISS-2DPAGE; Q8LEG3.
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT   CHAIN           1..578
FT                   /note="65-kDa microtubule-associated protein 2"
FT                   /id="PRO_0000395473"
FT   COILED          64..84
FT                   /evidence="ECO:0000255"
FT   COILED          151..184
FT                   /evidence="ECO:0000255"
FT   COILED          235..257
FT                   /evidence="ECO:0000255"
FT   COILED          290..312
FT                   /evidence="ECO:0000255"
FT   COILED          461..489
FT                   /evidence="ECO:0000255"
FT   SITE            409
FT                   /note="Microtubule binding"
FT                   /evidence="ECO:0000250"
FT   SITE            420
FT                   /note="Microtubule binding"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         503
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT   MOD_RES         532
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT   MOD_RES         566
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT   MOD_RES         569
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLP0"
FT   MOD_RES         577
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9FLP0"
SQ   SEQUENCE   578 AA;  65205 MW;  A8544528EFB6C2DE CRC64;
     MAVTEAENPL LGEITCGTLL QKLQEIWDEV GESDEERDKL LLQIEEECLN VYKKKVELAA
     KSRAELLQTL SDATVELSNL TTALGEKSYI DIPDKTSGTI KEQLSAIAPA LEQLWQQKEE
     RVRAFSDVQS QIQKICEEIA GGLNNGPHVV DETDLSLKRL DDFQRKLQEL QKEKSDRLQK
     VLEFVSTVHD LCAVLRLDFL STVTEVHPSL DEANGVQTKS ISNETLARLA KTVLTLKEDK
     MQRLKKLQEL ATQLTDLWNL MDTSDEEREL FDHVTSNISA SVHEVTASGA LALDLIEQAE
     VEVDRLDQLK SSRMKEIAFK KQSELEEIYA RAHIEIKPEV VRERIMSLID AGNTEPTELL
     ADMDSQIAKA KEEAFSRKEI LDRVEKWMSA CEEESWLEDY NRDQNRYSAS RGAHLNLKRA
     EKARILVSKI TAMVDTLIAK TRAWEEENSM SFEYDGVPLL AMLDEYTMLR QEREDEKRRL
     KEQKKQQEQP HTDQESAFGS KPSPARPVSA KKPVGTRVNG GGLNETPMRR LSMNSNQNGS
     KSKRDSLNKI ASPSNIVANT KDDAASPVSR ADPVMASP
//

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